{ "date": "2025-12-18", "proteins": [ { "function": "Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration (PubMed:12879005, PubMed:1480034, PubMed:2551898). Could play a role in bone osteoclastic resorption (By similarity). Cleaves KiSS1 at a Gly-|-Leu bond (PubMed:12879005). Cleaves NINJ1 to generate the Secreted ninjurin-1 form (PubMed:32883094). Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments (PubMed:1480034). Degrades fibronectin but not laminin or Pz-peptide", "gene_name": "MMP9", "glycan_count": 39, "glycosylation_sites": [ { "position": 38, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 120, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 127, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P14780", "name": "MMP-9", "organism": "Homo sapiens", "uniprot_id": "P14780" }, { "function": "Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues in association with MMP14", "gene_name": "MMP2", "glycan_count": 2, "glycosylation_sites": [ { "position": 573, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 642, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08253", "name": "MMP-2", "organism": "Homo sapiens", "uniprot_id": "P08253" }, { "function": "Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X (PubMed:1645757, PubMed:2153297, PubMed:2557822). In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity (PubMed:16807369)", "gene_name": "MMP1", "glycan_count": 48, "glycosylation_sites": [ { "position": 120, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P03956", "name": "MMP-1", "organism": "Homo sapiens", "uniprot_id": "P03956" }, { "function": "Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14. Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling. Mediates erythropoiesis in vitro; but, unlike IL3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors", "gene_name": "TIMP1", "glycan_count": 136, "glycosylation_sites": [ { "position": 53, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 101, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01033", "name": "TIMP-1", "organism": "Homo sapiens", "uniprot_id": "P01033" }, { "function": "Muscle assembly regulating factor. Mediates the antiparallel assembly of titin (TTN) molecules at the sarcomeric Z-disk", "gene_name": "TCAP", "glycan_count": 0, "glycosylation_sites": [], "id": "O15273", "name": "Galectin-7 (Gal-7)", "organism": "Homo sapiens", "uniprot_id": "O15273" }, { "function": "Gap junction protein that acts as a regulator of bladder capacity. A gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. May play a critical role in the physiology of hearing by participating in the recycling of potassium to the cochlear endolymph. Negative regulator of bladder functional capacity: acts by enhancing intercellular electrical and chemical transmission, thus sensitizing bladder muscles to cholinergic neural stimuli and causing them to contract (By similarity). May play a role in cell growth inhibition through the regulation of NOV expression and localization. Plays an essential role in gap junction communication in the ventricles (By similarity)", "gene_name": "GJA1", "glycan_count": 1, "glycosylation_sites": [], "id": "P17302", "name": "Connexin 43 (Cx43)", "organism": "Homo sapiens", "uniprot_id": "P17302" }, { "function": "Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions (PubMed:15014436, PubMed:18285447, PubMed:2430973, PubMed:6489349). Multifunctional, involved in inflammation, angiogenesis, wound healing, reactive oxygen species (ROS) signaling, nitrous oxide (NO) signaling, apoptosis, senescence, aging, cellular self-renewal, stemness, and cardiovascular and metabolic homeostasis (PubMed:10613822, PubMed:11134179, PubMed:1371676, PubMed:14568985, PubMed:24511121, PubMed:29042481, PubMed:32679764). Negatively modulates dendritic cell activation and cytokine release, as part of an autocrine feedback loop, contributing to the resolution of inflammation and immune homeostasis (PubMed:14568985). Ligand for receptor CD47 (PubMed:19004835, PubMed:8550562). Modulates nitrous oxide (NO) signaling via CD47, hence playing a role as a pressor agent, supporting blood pressure (By similarity). Plays a role in endothelial cell senescence, acting via CD47, by increasing the abundance and activation of NADPH oxidase NOX1, and so generating excess ROS (PubMed:29042481). Inhibits stem cell self-renewal, acting via CD47 signaling, probably by regulation of the stem cell transcription factors POU5F1/OCT4, SOX2, MYC/c-Myc and KLF4 (By similarity). Negatively modulates wound healing, acting via CD47 (By similarity). Ligand for receptor CD36 (PubMed:10613822, PubMed:11134179, PubMed:1371676). Involved in inducing apoptosis in podocytes in response to elevated free fatty acids, acting via CD36 (By similarity). Plays a role in suppressing angiogenesis, acting, depending on context, via CD36 or CD47 (PubMed:10613822, PubMed:11134179, PubMed:1371676, PubMed:32679764). Promotes cellular senescence in a TP53-CDKN1A-RB1 signaling-dependent manner (PubMed:29042481). Ligand for immunoglobulin-like cell surface receptor SIRPA (PubMed:24511121). Involved in ROS signaling in non-phagocytic cells, stimulating NADPH oxidase-derived ROS production, acting via interaction with SIRPA (PubMed:24511121). Plays a role in metabolic dysfunction in diet-induced obesity, perhaps acting by exacerbating adipose inflammatory activity; its effects may be mediated, at least in part, through enhanced adipocyte proliferation (By similarity). Plays a role in ER stress response, via its interaction with the activating transcription factor 6 alpha (ATF6) which produces adaptive ER stress response factors (By similarity). May be involved in age-related conditions, including metabolic dysregulation, during normal aging (PubMed:29042481, PubMed:32679764)", "gene_name": "THBS1", "glycan_count": 217, "glycosylation_sites": [ { "position": 248, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 360, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 385, "type": "C-linked (Man) tryptophan" }, { "position": 394, "type": "O-linked (Fuc...) serine" }, { "position": 438, "type": "C-linked (Man) tryptophan" }, { "position": 441, "type": "C-linked (Man) tryptophan" }, { "position": 450, "type": "O-linked (Fuc...) threonine" }, { "position": 498, "type": "C-linked (Man) tryptophan" }, { "position": 507, "type": "O-linked (Fuc...) threonine" }, { "position": 553, "type": "O-linked (Xyl) serine" }, { "position": 708, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1067, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P07996", "name": "Thrombospondin-1 (TSP-1)", "organism": "Homo sapiens", "uniprot_id": "P07996" }, { "function": "Exhibits antimicrobial activity against Gram-negative bacteria and Gram-positive bacteria, with highest activity against Gram-negative bacteria (PubMed:10837369, PubMed:9202117). Antimicrobial activity against P.aruginosa seems to be salt-sensitive and is reduced with high salt concentrations greater than 25 mM (PubMed:10837369). Also exhibits antimicrobial activity against the yeast C.albicans (PubMed:10837369, PubMed:30050988, PubMed:9202117). Permeabilizes C.albicans cell membranes via targeting plasma membrane lipid phosphatidylinositol 4,5-bisphosphate (PIP2), thereby leading to cell fragmentation and cell death (PubMed:30050988). Acts as a ligand for C-C chemokine receptor CCR6 (PubMed:10521347, PubMed:20068036). Binds to CCR6 and induces chemotactic activity of CCR6-expressing cells, such as immature dendritic cells and memory T cells (PubMed:10521347, PubMed:20068036)", "gene_name": "DEFB4A", "glycan_count": 0, "glycosylation_sites": [], "id": "O15263", "name": "Human beta-defensin 2 (HBD-2)", "organism": "Homo sapiens", "uniprot_id": "O15263" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q5UQV5", "name": "Human beta-defensin 3 (HBD-3)", "organism": "Acanthamoeba polyphaga mimivirus", "uniprot_id": "Q5UQV5" }, { "function": "Antimicrobial protein that is an integral component of the innate immune system (PubMed:14978112, PubMed:16637646, PubMed:18818205, PubMed:22879591, PubMed:9736536). Binds to bacterial lipopolysaccharides (LPS) (PubMed:16637646, PubMed:18818205). Acts via neutrophil N-formyl peptide receptors to enhance the release of CXCL2 (PubMed:22879591). Postsecretory processing generates multiple cathelicidin antimicrobial peptides with various lengths which act as a topical antimicrobial defense in sweat on skin (PubMed:14978112). The unprocessed precursor form, cathelicidin antimicrobial peptide, inhibits the growth of Gram-negative E.coli and E.aerogenes with efficiencies comparable to that of the mature peptide LL-37 (in vitro) (PubMed:9736536)", "gene_name": "CAMP", "glycan_count": 2, "glycosylation_sites": [], "id": "P49913", "name": "Cathelicidin (LL-37)", "organism": "Homo sapiens", "uniprot_id": "P49913" }, { "function": "Receptor tyrosine kinase which mediates the pleiotropic actions of insulin. Binding of insulin leads to phosphorylation of several intracellular substrates, including, insulin receptor substrates (IRS1, 2, 3, 4), SHC, GAB1, CBL and other signaling intermediates. Each of these phosphorylated proteins serve as docking proteins for other signaling proteins that contain Src-homology-2 domains (SH2 domain) that specifically recognize different phosphotyrosine residues, including the p85 regulatory subunit of PI3K and SHP2. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways: the PI3K-AKT/PKB pathway, which is responsible for most of the metabolic actions of insulin, and the Ras-MAPK pathway, which regulates expression of some genes and cooperates with the PI3K pathway to control cell growth and differentiation. Binding of the SH2 domains of PI3K to phosphotyrosines on IRS1 leads to the activation of PI3K and the generation of phosphatidylinositol-(3, 4, 5)-triphosphate (PIP3), a lipid second messenger, which activates several PIP3-dependent serine/threonine kinases, such as PDPK1 and subsequently AKT/PKB. The net effect of this pathway is to produce a translocation of the glucose transporter SLC2A4/GLUT4 from cytoplasmic vesicles to the cell membrane to facilitate glucose transport. Moreover, upon insulin stimulation, activated AKT/PKB is responsible for: anti-apoptotic effect of insulin by inducing phosphorylation of BAD; regulates the expression of gluconeogenic and lipogenic enzymes by controlling the activity of the winged helix or forkhead (FOX) class of transcription factors. Another pathway regulated by PI3K-AKT/PKB activation is mTORC1 signaling pathway which regulates cell growth and metabolism and integrates signals from insulin. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 thereby activating mTORC1 pathway. The Ras/RAF/MAP2K/MAPK pathway is mainly involved in mediating cell growth, survival and cellular differentiation of insulin. Phosphorylated IRS1 recruits GRB2/SOS complex, which triggers the activation of the Ras/RAF/MAP2K/MAPK pathway. In addition to binding insulin, the insulin receptor can bind insulin-like growth factors (IGFI and IGFII). Isoform Short has a higher affinity for IGFII binding. When present in a hybrid receptor with IGF1R, binds IGF1. PubMed:12138094 shows that hybrid receptors composed of IGF1R and INSR isoform Long are activated with a high affinity by IGF1, with low affinity by IGF2 and not significantly activated by insulin, and that hybrid receptors composed of IGF1R and INSR isoform Short are activated by IGF1, IGF2 and insulin. In contrast, PubMed:16831875 shows that hybrid receptors composed of IGF1R and INSR isoform Long and hybrid receptors composed of IGF1R and INSR isoform Short have similar binding characteristics, both bind IGF1 and have a low affinity for insulin. In adipocytes, inhibits lipolysis (By similarity)", "gene_name": "INSR", "glycan_count": 83, "glycosylation_sites": [ { "position": 43, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 52, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 105, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 138, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 242, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 282, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 322, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 364, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 424, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 445, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 541, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 633, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 651, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 698, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 769, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 782, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 920, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 933, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P06213", "name": "Insulin Receptor (IR)", "organism": "Homo sapiens", "uniprot_id": "P06213" }, { "function": "Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen response element (ERE) sequence or association with other DNA-binding transcription factors, such as AP-1/c-Jun, c-Fos, ATF-2, Sp1 and Sp3, to mediate ERE-independent signaling. Ligand binding induces a conformational change allowing subsequent or combinatorial association with multiprotein coactivator complexes through LXXLL motifs of their respective components. Mutual transrepression occurs between the estrogen receptor (ER) and NF-kappa-B in a cell-type specific manner. Decreases NF-kappa-B DNA-binding activity and inhibits NF-kappa-B-mediated transcription from the IL6 promoter and displace RELA/p65 and associated coregulators from the promoter. Recruited to the NF-kappa-B response element of the CCL2 and IL8 promoters and can displace CREBBP. Present with NF-kappa-B components RELA/p65 and NFKB1/p50 on ERE sequences. Can also act synergistically with NF-kappa-B to activate transcription involving respective recruitment adjacent response elements; the function involves CREBBP. Can activate the transcriptional activity of TFF1. Also mediates membrane-initiated estrogen signaling involving various kinase cascades. Essential for MTA1-mediated transcriptional regulation of BRCA1 and BCAS3 (PubMed:17922032). Maintains neuronal survival in response to ischemic reperfusion injury when in the presence of circulating estradiol (17-beta-estradiol/E2) (By similarity)", "gene_name": "ESR1", "glycan_count": 1, "glycosylation_sites": [ { "position": 10, "type": "O-linked (GlcNAc) serine" } ], "id": "P03372", "name": "Estrogen Receptor alpha (ER\u03b1)", "organism": "Homo sapiens", "uniprot_id": "P03372" }, { "function": "Nuclear hormone receptor. Binds estrogens with an affinity similar to that of ESR1/ER-alpha, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner (PubMed:20074560)", "gene_name": "ESR2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q92731", "name": "Estrogen Receptor beta (ER\u03b2)", "organism": "Homo sapiens", "uniprot_id": "Q92731" }, { "function": "Insulin-regulated facilitative glucose transporter, which plays a key role in removal of glucose from circulation. Response to insulin is regulated by its intracellular localization: in the absence of insulin, it is efficiently retained intracellularly within storage compartments in muscle and fat cells. Upon insulin stimulation, translocates from these compartments to the cell surface where it transports glucose from the extracellular milieu into the cell", "gene_name": "SLC2A4", "glycan_count": 0, "glycosylation_sites": [ { "position": 57, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P14672", "name": "GLUT4 (SLC2A4)", "organism": "Homo sapiens", "uniprot_id": "P14672" }, { "function": "NAD-dependent protein deacetylase that links transcriptional regulation directly to intracellular energetics and participates in the coordination of several separated cellular functions such as cell cycle, response to DNA damage, metabolism, apoptosis and autophagy (PubMed:11672523, PubMed:12006491, PubMed:14976264, PubMed:14980222, PubMed:15126506, PubMed:15152190, PubMed:15205477, PubMed:15469825, PubMed:15692560, PubMed:16079181, PubMed:16166628, PubMed:16892051, PubMed:16998810, PubMed:17283066, PubMed:17290224, PubMed:17334224, PubMed:17505061, PubMed:17612497, PubMed:17620057, PubMed:17936707, PubMed:18203716, PubMed:18296641, PubMed:18662546, PubMed:18687677, PubMed:19188449, PubMed:19220062, PubMed:19364925, PubMed:19690166, PubMed:19934257, PubMed:20097625, PubMed:20100829, PubMed:20203304, PubMed:20375098, PubMed:20620956, PubMed:20670893, PubMed:20817729, PubMed:20955178, PubMed:21149730, PubMed:21245319, PubMed:21471201, PubMed:21504832, PubMed:21555002, PubMed:21698133, PubMed:21701047, PubMed:21775285, PubMed:21807113, PubMed:21841822, PubMed:21890893, PubMed:21947282, PubMed:22274616, PubMed:22918831, PubMed:24415752, PubMed:24824780, PubMed:29681526, PubMed:29765047, PubMed:30409912). Can modulate chromatin function through deacetylation of histones and can promote alterations in the methylation of histones and DNA, leading to transcriptional repression (PubMed:15469825). Deacetylates a broad range of transcription factors and coregulators, thereby regulating target gene expression positively and negatively (PubMed:14976264, PubMed:14980222, PubMed:15152190). Serves as a sensor of the cytosolic ratio of NAD(+)/NADH which is altered by glucose deprivation and metabolic changes associated with caloric restriction (PubMed:15205477). Is essential in skeletal muscle cell differentiation and in response to low nutrients mediates the inhibitory effect on skeletal myoblast differentiation which also involves 5'-AMP-activated protein kinase (AMPK) and nicotinamide phosphoribosyltransferase (NAMPT) (By similarity). Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes (PubMed:18485871). The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus (PubMed:18485871, PubMed:21504832). Deacetylates 'Lys-266' of SUV39H1, leading to its activation (PubMed:21504832). Inhibits skeletal muscle differentiation by deacetylating PCAF and MYOD1 (PubMed:19188449). Deacetylates H2A and 'Lys-26' of H1-4 (PubMed:15469825). Deacetylates 'Lys-16' of histone H4 (in vitro). Involved in NR0B2/SHP corepression function through chromatin remodeling: Recruited to LRH1 target gene promoters by NR0B2/SHP thereby stimulating histone H3 and H4 deacetylation leading to transcriptional repression (PubMed:20375098). Proposed to contribute to genomic integrity via positive regulation of telomere length; however, reports on localization to pericentromeric heterochromatin are conflicting (By similarity). Proposed to play a role in constitutive heterochromatin (CH) formation and/or maintenance through regulation of the available pool of nuclear SUV39H1 (PubMed:15469825, PubMed:18004385). Upon oxidative/metabolic stress decreases SUV39H1 degradation by inhibiting SUV39H1 polyubiquitination by MDM2 (PubMed:18004385, PubMed:21504832). This increase in SUV39H1 levels enhances SUV39H1 turnover in CH, which in turn seems to accelerate renewal of the heterochromatin which correlates with greater genomic integrity during stress response (PubMed:18004385, PubMed:21504832). Deacetylates 'Lys-382' of p53/TP53 and impairs its ability to induce transcription-dependent proapoptotic program and modulate cell senescence (PubMed:11672523, PubMed:12006491, PubMed:22542455). Deacetylates TAF1B and thereby represses rDNA transcription by the RNA polymerase I (By similarity). Deacetylates MYC, promotes the association of MYC with MAX and decreases MYC stability leading to compromised transformational capability (PubMed:19364925, PubMed:21807113). Deacetylates FOXO3 in response to oxidative stress thereby increasing its ability to induce cell cycle arrest and resistance to oxidative stress but inhibiting FOXO3-mediated induction of apoptosis transcriptional activity; also leading to FOXO3 ubiquitination and protesomal degradation (PubMed:14976264, PubMed:14980222, PubMed:21841822). Appears to have a similar effect on MLLT7/FOXO4 in regulation of transcriptional activity and apoptosis (PubMed:15126506). Deacetylates DNMT1; thereby impairs DNMT1 methyltransferase-independent transcription repressor activity, modulates DNMT1 cell cycle regulatory function and DNMT1-mediated gene silencing (PubMed:21947282). Deacetylates RELA/NF-kappa-B p65 thereby inhibiting its transactivating potential and augments apoptosis in response to TNF-alpha (PubMed:15152190). Deacetylates HIF1A, KAT5/TIP60, RB1 and HIC1 (PubMed:17283066, PubMed:17620057, PubMed:20100829, PubMed:20620956). Deacetylates FOXO1 resulting in its nuclear retention and enhancement of its transcriptional activity leading to increased gluconeogenesis in liver (PubMed:15692560). Inhibits E2F1 transcriptional activity and apoptotic function, possibly by deacetylation (PubMed:16892051). Involved in HES1- and HEY2-mediated transcriptional repression (PubMed:12535671). In cooperation with MYCN seems to be involved in transcriptional repression of DUSP6/MAPK3 leading to MYCN stabilization by phosphorylation at 'Ser-62' (PubMed:21698133). Deacetylates MEF2D (PubMed:16166628). Required for antagonist-mediated transcription suppression of AR-dependent genes which may be linked to local deacetylation of histone H3 (PubMed:17505061). Represses HNF1A-mediated transcription (By similarity). Required for the repression of ESRRG by CREBZF (PubMed:19690166). Deacetylates NR1H3 and NR1H2 and deacetylation of NR1H3 at 'Lys-434' positively regulates transcription of NR1H3:RXR target genes, promotes NR1H3 proteasomal degradation and results in cholesterol efflux; a promoter clearing mechanism after reach round of transcription is proposed (PubMed:17936707). Involved in lipid metabolism: deacetylates LPIN1, thereby inhibiting diacylglycerol synthesis (PubMed:20817729, PubMed:29765047). Implicated in regulation of adipogenesis and fat mobilization in white adipocytes by repression of PPARG which probably involves association with NCOR1 and SMRT/NCOR2 (By similarity). Deacetylates p300/EP300 and PRMT1 (By similarity). Deacetylates ACSS2 leading to its activation, and HMGCS1 deacetylation (PubMed:21701047). Involved in liver and muscle metabolism. Through deacetylation and activation of PPARGC1A is required to activate fatty acid oxidation in skeletal muscle under low-glucose conditions and is involved in glucose homeostasis (PubMed:23142079). Involved in regulation of PPARA and fatty acid beta-oxidation in liver. Involved in positive regulation of insulin secretion in pancreatic beta cells in response to glucose; the function seems to imply transcriptional repression of UCP2. Proposed to deacetylate IRS2 thereby facilitating its insulin-induced tyrosine phosphorylation. Deacetylates SREBF1 isoform SREBP-1C thereby decreasing its stability and transactivation in lipogenic gene expression (PubMed:17290224, PubMed:20817729). Involved in DNA damage response by repressing genes which are involved in DNA repair, such as XPC and TP73, deacetylating XRCC6/Ku70, and facilitating recruitment of additional factors to sites of damaged DNA, such as SIRT1-deacetylated NBN can recruit ATM to initiate DNA repair and SIRT1-deacetylated XPA interacts with RPA2 (PubMed:15205477, PubMed:16998810, PubMed:17334224, PubMed:17612497, PubMed:20670893, PubMed:21149730). Also involved in DNA repair of DNA double-strand breaks by homologous recombination and specifically single-strand annealing independently of XRCC6/Ku70 and NBN (PubMed:15205477, PubMed:17334224, PubMed:20097625). Promotes DNA double-strand breaks by mediating deacetylation of SIRT6 (PubMed:32538779). Transcriptional suppression of XPC probably involves an E2F4:RBL2 suppressor complex and protein kinase B (AKT) signaling. Transcriptional suppression of TP73 probably involves E2F4 and PCAF. Deacetylates WRN thereby regulating its helicase and exonuclease activities and regulates WRN nuclear translocation in response to DNA damage (PubMed:18203716). Deacetylates APEX1 at 'Lys-6' and 'Lys-7' and stimulates cellular AP endonuclease activity by promoting the association of APEX1 to XRCC1 (PubMed:19934257). Catalyzes deacetylation of ERCC4/XPF, thereby impairing interaction with ERCC1 and nucleotide excision repair (NER) (PubMed:32034146). Increases p53/TP53-mediated transcription-independent apoptosis by blocking nuclear translocation of cytoplasmic p53/TP53 and probably redirecting it to mitochondria. Deacetylates XRCC6/Ku70 at 'Lys-539' and 'Lys-542' causing it to sequester BAX away from mitochondria thereby inhibiting stress-induced apoptosis. Is involved in autophagy, presumably by deacetylating ATG5, ATG7 and MAP1LC3B/ATG8 (PubMed:18296641). Deacetylates AKT1 which leads to enhanced binding of AKT1 and PDK1 to PIP3 and promotes their activation (PubMed:21775285). Proposed to play role in regulation of STK11/LBK1-dependent AMPK signaling pathways implicated in cellular senescence which seems to involve the regulation of the acetylation status of STK11/LBK1. Can deacetylate STK11/LBK1 and thereby increase its activity, cytoplasmic localization and association with STRAD; however, the relevance of such activity in normal cells is unclear (PubMed:18687677, PubMed:20203304). In endothelial cells is shown to inhibit STK11/LBK1 activity and to promote its degradation. Deacetylates SMAD7 at 'Lys-64' and 'Lys-70' thereby promoting its degradation. Deacetylates CIITA and augments its MHC class II transactivation and contributes to its stability (PubMed:21890893). Deacetylates MECOM/EVI1 (PubMed:21555002). Deacetylates PML at 'Lys-487' and this deacetylation promotes PML control of PER2 nuclear localization (PubMed:22274616). During the neurogenic transition, represses selective NOTCH1-target genes through histone deacetylation in a BCL6-dependent manner and leading to neuronal differentiation. Regulates the circadian expression of several core clock genes, including BMAL1, RORC, PER2 and CRY1 and plays a critical role in maintaining a controlled rhythmicity in histone acetylation, thereby contributing to circadian chromatin remodeling (PubMed:18662546). Deacetylates BMAL1 and histones at the circadian gene promoters in order to facilitate repression by inhibitory components of the circadian oscillator (By similarity). Deacetylates PER2, facilitating its ubiquitination and degradation by the proteasome (By similarity). Protects cardiomyocytes against palmitate-induced apoptosis (By similarity). Deacetylates XBP1 isoform 2; deacetylation decreases protein stability of XBP1 isoform 2 and inhibits its transcriptional activity (PubMed:20955178). Deacetylates PCK1 and directs its activity toward phosphoenolpyruvate production promoting gluconeogenesis (PubMed:30193097). Involved in the CCAR2-mediated regulation of PCK1 and NR1D1 (PubMed:24415752). Deacetylates CTNB1 at 'Lys-49' (PubMed:24824780). In POMC (pro-opiomelanocortin) neurons, required for leptin-induced activation of PI3K signaling (By similarity). Deacetylates SOX9; promoting SOX9 nuclear localization and transactivation activity (By similarity). Involved in the regulation of centrosome duplication: deacetylates CENATAC in G1 phase, allowing for SASS6 accumulation on the centrosome and subsequent procentriole assembly (PubMed:31722219). Deacetylates NDC80/HEC1 (PubMed:30409912). In addition to protein deacetylase activity, also acts as a protein-lysine deacylase by mediating protein delactylation, depropionylation and decrotonylation (PubMed:28497810, PubMed:38512451). Mediates depropionylation of Osterix (SP7) (By similarity). Catalyzes decrotonylation of histones; it however does not represent a major histone decrotonylase (PubMed:28497810). Mediates protein delactylation of TEAD1 and YAP1 (PubMed:38512451)", "gene_name": "SIRT1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96EB6", "name": "Sirtuin 1 (Sirt1)", "organism": "Homo sapiens", "uniprot_id": "Q96EB6" }, { "function": "AKT1 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis (PubMed:11882383, PubMed:15526160, PubMed:15861136, PubMed:21432781, PubMed:21620960, PubMed:31204173). This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates (PubMed:11882383, PubMed:15526160, PubMed:21432781, PubMed:21620960, PubMed:29343641, PubMed:31204173). Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported (PubMed:11882383, PubMed:15526160, PubMed:21432781, PubMed:21620960). AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface (By similarity). Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling (By similarity). Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport (PubMed:11994271). AKT also regulates the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity (By similarity). Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven (By similarity). AKT also regulates cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase) (PubMed:11154276). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis (PubMed:11154276). AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating the mTORC1 signaling pathway, and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1 (PubMed:12150915, PubMed:12172553). Also regulates the mTORC1 signaling pathway by catalyzing phosphorylation of CASTOR1 and DEPDC5 (PubMed:31548394, PubMed:33594058). AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation (By similarity). Part of a positive feedback loop of mTORC2 signaling by mediating phosphorylation of MAPKAP1/SIN1, promoting mTORC2 activation (By similarity). AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization (PubMed:10358075). In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319' (PubMed:10358075). FOXO3 and FOXO4 are phosphorylated on equivalent sites (PubMed:10358075). AKT has an important role in the regulation of NF-kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein) (PubMed:9829964). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1 (PubMed:9829964). AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis (By similarity). Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis (By similarity). Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P-5 activity (By similarity). The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth (By similarity). Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor 1 (IGF1) (PubMed:12176338, PubMed:12964941). AKT mediates the antiapoptotic effects of IGF1 (By similarity). Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly (PubMed:19934221). May be involved in the regulation of the placental development (By similarity). Phosphorylates STK4/MST1 at 'Thr-120' and 'Thr-387' leading to inhibition of its: kinase activity, nuclear translocation, autophosphorylation and ability to phosphorylate FOXO3 (PubMed:17726016). Phosphorylates STK3/MST2 at 'Thr-117' and 'Thr-384' leading to inhibition of its: cleavage, kinase activity, autophosphorylation at Thr-180, binding to RASSF1 and nuclear translocation (PubMed:20086174). Phosphorylates SRPK2 and enhances its kinase activity towards SRSF2 and ACIN1 and promotes its nuclear translocation (PubMed:19592491). Phosphorylates RAF1 at 'Ser-259' and negatively regulates its activity (PubMed:10576742). Phosphorylation of BAD stimulates its pro-apoptotic activity (PubMed:10926925). Phosphorylates KAT6A at 'Thr-369' and this phosphorylation inhibits the interaction of KAT6A with PML and negatively regulates its acetylation activity towards p53/TP53 (PubMed:23431171). Phosphorylates palladin (PALLD), modulating cytoskeletal organization and cell motility (PubMed:20471940). Phosphorylates prohibitin (PHB), playing an important role in cell metabolism and proliferation (PubMed:18507042). Phosphorylates CDKN1A, for which phosphorylation at 'Thr-145' induces its release from CDK2 and cytoplasmic relocalization (PubMed:16982699). These recent findings indicate that the AKT1 isoform has a more specific role in cell motility and proliferation (PubMed:16139227). Phosphorylates CLK2 thereby controlling cell survival to ionizing radiation (PubMed:20682768). Phosphorylates PCK1 at 'Ser-90', reducing the binding affinity of PCK1 to oxaloacetate and changing PCK1 into an atypical protein kinase activity using GTP as donor (PubMed:32322062). Also acts as an activator of TMEM175 potassium channel activity in response to growth factors: forms the lysoK(GF) complex together with TMEM175 and acts by promoting TMEM175 channel activation, independently of its protein kinase activity (PubMed:32228865). Acts as a regulator of mitochondrial calcium uptake by mediating phosphorylation of MICU1 in the mitochondrial intermembrane space, impairing MICU1 maturation (PubMed:30504268). Acts as an inhibitor of tRNA methylation by mediating phosphorylation of the N-terminus of METTL1, thereby inhibiting METTL1 methyltransferase activity (PubMed:15861136). In response to LPAR1 receptor pathway activation, phosphorylates Rabin8/RAB3IP which alters its activity and phosphorylates WDR44 which induces WDR44 binding to Rab11, thereby switching Rab11 vesicular function from preciliary trafficking to endocytic recycling (PubMed:31204173)", "gene_name": "AKT1", "glycan_count": 1, "glycosylation_sites": [ { "position": 126, "type": "O-linked (GlcNAc) serine; alternate" }, { "position": 129, "type": "O-linked (GlcNAc) serine; alternate" }, { "position": 305, "type": "O-linked (GlcNAc) threonine" }, { "position": 312, "type": "O-linked (GlcNAc) threonine" }, { "position": 473, "type": "O-linked (GlcNAc) serine; alternate" } ], "id": "P31749", "name": "Akt (Protein kinase B)", "organism": "Homo sapiens", "uniprot_id": "P31749" }, { "function": "Transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress (PubMed:10358076, PubMed:12228231, PubMed:15220471, PubMed:15890677, PubMed:18356527, PubMed:19221179, PubMed:20543840, PubMed:21245099). Binds to the insulin response element (IRE) with consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with consensus sequence 5'-TT[G/A]TTTAC-3' (PubMed:10358076). Activity suppressed by insulin (PubMed:10358076). Main regulator of redox balance and osteoblast numbers and controls bone mass (By similarity). Orchestrates the endocrine function of the skeleton in regulating glucose metabolism (By similarity). Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). Acts synergistically with ATF4 to suppress osteocalcin/BGLAP activity, increasing glucose levels and triggering glucose intolerance and insulin insensitivity (By similarity). Also suppresses the transcriptional activity of RUNX2, an upstream activator of osteocalcin/BGLAP (By similarity). Acts as an inhibitor of glucose sensing in pancreatic beta cells by acting as a transcription repressor and suppressing expression of PDX1 (By similarity). In hepatocytes, promotes gluconeogenesis by acting together with PPARGC1A and CEBPA to activate the expression of genes such as IGFBP1, G6PC1 and PCK1 (By similarity). Also promotes gluconeogenesis by directly promoting expression of PPARGC1A and G6PC1 (PubMed:17024043). Important regulator of cell death acting downstream of CDK1, PKB/AKT1 and STK4/MST1 (PubMed:18356527, PubMed:19221179). Promotes neural cell death (PubMed:18356527). Mediates insulin action on adipose tissue (By similarity). Regulates the expression of adipogenic genes such as PPARG during preadipocyte differentiation and, adipocyte size and adipose tissue-specific gene expression in response to excessive calorie intake (By similarity). Regulates the transcriptional activity of GADD45A and repair of nitric oxide-damaged DNA in beta-cells (By similarity). Required for the autophagic cell death induction in response to starvation or oxidative stress in a transcription-independent manner (PubMed:20543840). Mediates the function of MLIP in cardiomyocytes hypertrophy and cardiac remodeling (By similarity). Positive regulator of apoptosis in cardiac smooth muscle cells as a result of its transcriptional activation of pro-apoptotic genes (PubMed:19483080). Regulates endothelial cell (EC) viability and apoptosis in a PPIA/CYPA-dependent manner via transcription of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis (PubMed:31063815)", "gene_name": "FOXO1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q12778", "name": "FoxO1", "organism": "Homo sapiens", "uniprot_id": "Q12778" }, { "function": "G-protein coupled receptor for glucagon-like peptide 1 (GLP-1) (PubMed:19861722, PubMed:26308095, PubMed:27196125, PubMed:28514449, PubMed:7517895, PubMed:8216285, PubMed:8405712). Ligand binding triggers activation of a signaling cascade that leads to the activation of adenylyl cyclase and increased intracellular cAMP levels (PubMed:19861722, PubMed:26308095, PubMed:27196125, PubMed:28514449, PubMed:7517895, PubMed:8216285, PubMed:8405712). Plays a role in regulating insulin secretion in response to GLP-1 (By similarity)", "gene_name": "GLP1R", "glycan_count": 0, "glycosylation_sites": [ { "position": 63, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 82, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 115, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P43220", "name": "GLP1 Receptor", "organism": "Homo sapiens", "uniprot_id": "P43220" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9XTG1 (Drosophila)", "name": "O-GlcNAc Transferase (OGT)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9V3A8 (Drosophila)", "name": "O-GlcNAcase (OGA)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P13368 (Drosophila)", "name": "Mitogen Activated Protein Kinase/Extracellular signal Regulated Kinase (MAPK/ERK, rolled)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P22812 (Drosophila)", "name": "Stripe (Sr/EGR2/Krox20)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P09087 (Drosophila)", "name": "cad (Caudal)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9V3N7 (Drosophila)", "name": "Ptx1", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9V3K3 (Drosophila)", "name": "dawdle (daw)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9V3I6 (Drosophila)", "name": "cabut (cbt)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9V3J2 (Drosophila)", "name": "Irk1", "organism": "", "uniprot_id": "" }, { "function": "Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:33065002). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Subunit H is essential for V-ATPase activity, but not for the assembly of the complex (By similarity). Involved in the endocytosis mediated by clathrin-coated pits, required for the formation of endosomes (PubMed:12032142)", "gene_name": "ATP6V1H", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UI12", "name": "ATP6AP1", "organism": "Homo sapiens", "uniprot_id": "Q9UI12" }, { "function": "Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation", "gene_name": "TF", "glycan_count": 297, "glycosylation_sites": [ { "position": 51, "type": "O-linked (GalNAc...) serine" }, { "position": 432, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 491, "type": "N-linked (GlcNAc...) asparagine; atypical; partial" }, { "position": 630, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P02787", "name": "Transferrin", "organism": "Homo sapiens", "uniprot_id": "P02787" }, { "function": "Multifunctional blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane (PubMed:16150804). Copper ions provide a large number of enzymatic activites. Oxidizes highly toxic ferrous ions to the ferric state for further incorporation onto apo-transferrins, catalyzes Cu(+) oxidation and promotes the oxidation of biogenic amines such as norepinephrin and serotonin (PubMed:14623105, PubMed:4643313, PubMed:5912351). Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1 (By similarity). Has glutathione peroxidase-like activity, can remove both hydrogen peroxide and lipid hydroperoxide in the presence of thiols (PubMed:10481051). Also shows NO-oxidase and NO2 synthase activities that determine endocrine NO homeostasis (PubMed:16906150)", "gene_name": "CP", "glycan_count": 229, "glycosylation_sites": [ { "position": 138, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 358, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 397, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 588, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 762, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 926, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P00450", "name": "Ceruloplasmin", "organism": "Homo sapiens", "uniprot_id": "P00450" }, { "function": "Binds copper, nickel, and fatty acids as well as, and bilirubin less well than, serum albumin. Only a small percentage (less than 2%) of the human AFP shows estrogen-binding properties", "gene_name": "AFP", "glycan_count": 49, "glycosylation_sites": [ { "position": 251, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P02771", "name": "Alpha-fetoprotein", "organism": "Homo sapiens", "uniprot_id": "P02771" }, { "function": "Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in cytoplasmic and nuclear proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc) (PubMed:12150998, PubMed:15361863, PubMed:19451179, PubMed:20018868, PubMed:21240259, PubMed:21285374, PubMed:23103939, PubMed:26237509, PubMed:26369908, PubMed:26678539, PubMed:27713473, PubMed:37541260, PubMed:37962578). Glycosylates a large and diverse number of proteins including histone H2B, AKT1, AMPK, ATG4B, CAPRIN1, EZH2, FNIP1, GSDMD, KRT7, LMNA, LMNB1, LMNB2, RPTOR, HOXA1, PFKL, KMT2E/MLL5, MAPT/TAU, TET2, RBL2, RET, NOD2 and HCFC1 (PubMed:19451179, PubMed:20200153, PubMed:21285374, PubMed:22923583, PubMed:23353889, PubMed:24474760, PubMed:26237509, PubMed:26369908, PubMed:26678539, PubMed:27527864, PubMed:30699359, PubMed:34074792, PubMed:34667079, PubMed:37541260, PubMed:37962578). Can regulate their cellular processes via cross-talk between glycosylation and phosphorylation or by affecting proteolytic processing (PubMed:21285374). Involved in insulin resistance in muscle and adipocyte cells via glycosylating insulin signaling components and inhibiting the 'Thr-308' phosphorylation of AKT1, enhancing IRS1 phosphorylation and attenuating insulin signaling (By similarity). Involved in glycolysis regulation by mediating glycosylation of 6-phosphofructokinase PFKL, inhibiting its activity (PubMed:22923583). Plays a key role in chromatin structure by mediating O-GlcNAcylation of 'Ser-112' of histone H2B: recruited to CpG-rich transcription start sites of active genes via its interaction with TET proteins (TET1, TET2 or TET3) (PubMed:22121020, PubMed:23353889). As part of the NSL complex indirectly involved in acetylation of nucleosomal histone H4 on several lysine residues (PubMed:20018852). O-GlcNAcylation of 'Ser-75' of EZH2 increases its stability, and facilitating the formation of H3K27me3 by the PRC2/EED-EZH2 complex (PubMed:24474760). Stabilizes KMT2E/MLL5 by mediating its glycosylation, thereby preventing KMT2E/MLL5 ubiquitination (PubMed:26678539). Regulates circadian oscillation of the clock genes and glucose homeostasis in the liver (By similarity). Stabilizes clock proteins BMAL1 and CLOCK through O-glycosylation, which prevents their ubiquitination and subsequent degradation (By similarity). Promotes the CLOCK-BMAL1-mediated transcription of genes in the negative loop of the circadian clock such as PER1/2 and CRY1/2. O-glycosylates HCFC1 and regulates its proteolytic processing and transcriptional activity (PubMed:21285374, PubMed:28302723, PubMed:28584052). Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1 (PubMed:20200153). Regulates mitochondrial motility in neurons by mediating glycosylation of TRAK1 (By similarity). Promotes autophagy by mediating O-glycosylation of ATG4B (PubMed:27527864). Acts as a regulator of mTORC1 signaling by mediating O-glycosylation of RPTOR and FNIP1: O-GlcNAcylation of RPTOR in response to glucose sufficiency promotes activation of the mTORC1 complex (PubMed:30699359, PubMed:37541260)", "gene_name": "OGT", "glycan_count": 1, "glycosylation_sites": [ { "position": 3, "type": "O-linked (GlcNAc) serine; alternate" }, { "position": 4, "type": "O-linked (GlcNAc) serine; alternate" }, { "position": 399, "type": "O-linked (GlcNAc) serine; by autocatalysis" }, { "position": 10, "type": "O-linked (GlcNAc) serine" }, { "position": 12, "type": "O-linked (GlcNAc) threonine" }, { "position": 18, "type": "O-linked (GlcNAc) serine" }, { "position": 38, "type": "O-linked (GlcNAc) threonine" }, { "position": 52, "type": "O-linked (GlcNAc) serine" }, { "position": 56, "type": "O-linked (GlcNAc) serine" } ], "id": "O15294", "name": "O-GlcNAc transferase (OGT)", "organism": "Homo sapiens", "uniprot_id": "O15294" }, { "function": "Dioxygenase that plays a key role in active DNA demethylation, by catalyzing the sequential oxidation of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC), 5-formylcytosine (5fC), and 5-carboxylcytosine (5caC) (PubMed:19372391, PubMed:21496894, PubMed:21778364, PubMed:35798741). In addition to its role in DNA demethylation, plays a more general role in chromatin regulation by recruiting histone modifying protein complexes to alter histone marks and chromatin accessibility, leading to both activation and repression of gene expression (PubMed:33833093). Plays therefore a role in many biological processes, including stem cell maintenance, T- and B-cell development, inflammation regulation, genomic imprinting, neural activity or DNA repair (PubMed:31278917). Involved in the balance between pluripotency and lineage commitment of cells and plays a role in embryonic stem cells maintenance and inner cell mass cell specification. Together with QSER1, plays an essential role in the protection and maintenance of transcriptional and developmental programs to inhibit the binding of DNMT3A/3B and therefore de novo methylation (PubMed:33833093). May play a role in pancreatic beta-cell specification during development. In this context, may function as an upstream epigenetic regulator of PAX4 presumably through direct recruitment by FOXA2 to a PAX4 enhancer to preserve its unmethylated status, thereby potentiating PAX4 expression to adopt beta-cell fate during endocrine lineage commitment (PubMed:35798741). Under DNA hypomethylation conditions, such as in female meiotic germ cells, may induce epigenetic reprogramming of pericentromeric heterochromatin (PCH), the constitutive heterochromatin of pericentromeric regions. PCH forms chromocenters in the interphase nucleus and chromocenters cluster at the prophase of meiosis. In this context, may also be essential for chromocenter clustering in a catalytic activity-independent manner, possibly through the recruitment polycomb repressive complex 1 (PRC1) to the chromocenters (By similarity). During embryonic development, may be required for normal meiotic progression in oocytes and meiotic gene activation (By similarity). Binds preferentially to DNA containing cytidine-phosphate-guanosine (CpG) dinucleotides over CpH (H=A, T, and C), hemimethylated-CpG and hemimethylated-hydroxymethyl-CpG (PubMed:29276034)", "gene_name": "TET1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8NFU7", "name": "TET methylcytosine dioxygenase 1 (TET1)", "organism": "Homo sapiens", "uniprot_id": "Q8NFU7" }, { "function": "RNA-binding protein that is involved in various steps of RNA biogenesis and processing (PubMed:23519609). Preferentially binds, via its two RNA recognition motifs RRM1 and RRM2, to GU-repeats on RNA molecules predominantly localized within long introns and in the 3'UTR of mRNAs (PubMed:23519609, PubMed:24240615, PubMed:24464995). In turn, regulates the splicing of many non-coding and protein-coding RNAs including proteins involved in neuronal survival, as well as mRNAs that encode proteins relevant for neurodegenerative diseases (PubMed:21358640, PubMed:29438978). Plays a role in maintaining mitochondrial homeostasis by regulating the processing of mitochondrial transcripts (PubMed:28794432). Also regulates mRNA stability by recruiting CNOT7/CAF1 deadenylase on mRNA 3'UTR leading to poly(A) tail deadenylation and thus shortening (PubMed:30520513). In response to oxidative insult, associates with stalled ribosomes localized to stress granules (SGs) and contributes to cell survival (PubMed:19765185, PubMed:23398327). Also participates in the normal skeletal muscle formation and regeneration, forming cytoplasmic myo-granules and binding mRNAs that encode sarcomeric proteins (PubMed:30464263). Plays a role in the maintenance of the circadian clock periodicity via stabilization of the CRY1 and CRY2 proteins in a FBXL3-dependent manner (PubMed:27123980). Negatively regulates the expression of CDK6 (PubMed:19760257). Regulates the expression of HDAC6, ATG7 and VCP in a PPIA/CYPA-dependent manner (PubMed:25678563)", "gene_name": "TARDBP", "glycan_count": 1, "glycosylation_sites": [], "id": "Q13148", "name": "TAR DNA-binding protein 43 (TARDBP)", "organism": "Homo sapiens", "uniprot_id": "Q13148" }, { "function": "Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules (PubMed:12509468, PubMed:16010978, PubMed:7567451, PubMed:8264621). Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides (PubMed:8264621). May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. N6-methyladenosine (m6A) has been shown to alter the local structure in mRNAs and long non-coding RNAs (lncRNAs) via a mechanism named 'm(6)A-switch', facilitating binding of HNRNPC, leading to regulation of mRNA splicing (PubMed:25719671)", "gene_name": "HNRNPC", "glycan_count": 1, "glycosylation_sites": [], "id": "P07910", "name": "Serine/arginine-rich splicing factor 2 (SRSF2)", "organism": "Homo sapiens", "uniprot_id": "P07910" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UBB5-2", "name": "Methyl-CpG-binding domain protein 2, variant 2 (MBD2_v2)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "PRR36", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H6K5", "name": "O-GlcNAcase (OGA)", "organism": "Homo sapiens", "uniprot_id": "Q9H6K5" }, { "function": "Participates in O-mannosyl glycosylation by catalyzing the addition of N-acetylglucosamine to O-linked mannose on glycoproteins (PubMed:11709191, PubMed:27493216, PubMed:28512129). Catalyzes the synthesis of the GlcNAc(beta1-2)Man(alpha1-)O-Ser/Thr moiety on alpha-dystroglycan and other O-mannosylated proteins, providing the necessary basis for the addition of further carbohydrate moieties (PubMed:11709191, PubMed:27493216). Is specific for alpha linked terminal mannose and does not have MGAT3, MGAT4, MGAT5, MGAT7 or MGAT8 activity", "gene_name": "POMGNT1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8WZA1", "name": "POMGNT1", "organism": "Homo sapiens", "uniprot_id": "Q8WZA1" }, { "function": "Required for TCR (T-cell antigen receptor)- and pre-TCR-mediated signaling, both in mature T-cells and during their development (PubMed:23514740, PubMed:25907557). Involved in FCGR3 (low affinity immunoglobulin gamma Fc region receptor III)-mediated signaling in natural killer cells and FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Couples activation of these receptors and their associated kinases with distal intracellular events such as mobilization of intracellular calcium stores, PKC activation, MAPK activation or cytoskeletal reorganization through the recruitment of PLCG1, GRB2, GRAP2, and other signaling molecules", "gene_name": "LAT", "glycan_count": 2, "glycosylation_sites": [], "id": "O43561", "name": "alpha-dystroglycan", "organism": "Homo sapiens", "uniprot_id": "O43561" }, { "function": "Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient (PubMed:14699049, PubMed:28512129). Essentially dedicated to O-mannosylation of alpha-DAG1 and few other proteins but not of cadherins and protocaherins (PubMed:28512129)", "gene_name": "POMT2", "glycan_count": 10, "glycosylation_sites": [ { "position": 98, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 330, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 445, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 528, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 583, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UKY4", "name": "POMT2", "organism": "Homo sapiens", "uniprot_id": "Q9UKY4" }, { "function": "Beta-1,3-N-acetylgalactosaminyltransferase that synthesizes a unique carbohydrate structure, GalNAc-beta-1-3GlcNAc, on N- and O-glycans. Has no galactose nor galactosaminyl transferase activity toward any acceptor substrate. Involved in alpha-dystroglycan (DAG1) glycosylation: acts coordinately with GTDC2/POMGnT2 to synthesize a GalNAc-beta3-GlcNAc-beta-terminus at the 4-position of protein O-mannose in the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan, which is required for binding laminin G-like domain-containing extracellular proteins with high affinity", "gene_name": "B3GALNT2", "glycan_count": 1, "glycosylation_sites": [ { "position": 116, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 174, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8NCR0", "name": "B3GALNT2", "organism": "Homo sapiens", "uniprot_id": "Q8NCR0" }, { "function": "The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sarcolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization", "gene_name": "DAG1", "glycan_count": 22, "glycosylation_sites": [ { "position": 63, "type": "O-linked (GalNAc...) threonine" }, { "position": 141, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 317, "type": "O-linked (Man6P...) threonine" }, { "position": 319, "type": "O-linked (Man6P...) threonine" }, { "position": 367, "type": "O-linked (Hex...) threonine" }, { "position": 369, "type": "O-linked (Hex...) threonine" }, { "position": 372, "type": "O-linked (Hex...) threonine" }, { "position": 379, "type": "O-linked (Man6P...) threonine" }, { "position": 381, "type": "O-linked (Hex...) threonine" }, { "position": 388, "type": "O-linked (Hex...) threonine" }, { "position": 455, "type": "O-linked (GalNAc...) threonine" }, { "position": 641, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 649, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 661, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q14118", "name": "Dystroglycan", "organism": "Homo sapiens", "uniprot_id": "Q14118" }, { "function": "Anchors the extracellular matrix to the cytoskeleton via F-actin. Ligand for dystroglycan. Component of the dystrophin-associated glycoprotein complex which accumulates at the neuromuscular junction (NMJ) and at a variety of synapses in the peripheral and central nervous systems and has a structural function in stabilizing the sarcolemma. Also implicated in signaling events and synaptic transmission", "gene_name": "DMD", "glycan_count": 3, "glycosylation_sites": [], "id": "P11532", "name": "Dystrophin", "organism": "Homo sapiens", "uniprot_id": "P11532" }, { "function": "Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the extracellular matrix via the dystrophin glycoprotein complex. Plays an important role in synapse formation and in the organization of UTRN and acetylcholine receptors at the neuromuscular synapse. Binds to phosphatidylinositol 4,5-bisphosphate (By similarity)", "gene_name": "SNTA1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q13424", "name": "Alpha-syntrophin", "organism": "Homo sapiens", "uniprot_id": "Q13424" }, { "function": "Hypothalamic neuropeptide which binds to the G-protein-coupled galanin receptors (GALR1, GALR2 and GALR3). Involved in a large number of putative physiological functions in CNS homeostatic processes, including the regulation of gonadotropin-releasing hormone secretion", "gene_name": "GALP", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UBC7", "name": "Dystrobrevin", "organism": "Homo sapiens", "uniprot_id": "Q9UBC7" }, { "function": "May play a role in anchoring the cytoskeleton to the plasma membrane", "gene_name": "UTRN", "glycan_count": 2, "glycosylation_sites": [], "id": "P46939", "name": "Utrophin", "organism": "Homo sapiens", "uniprot_id": "P46939" }, { "function": "Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter. Probably has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR", "gene_name": "NOS1", "glycan_count": 1, "glycosylation_sites": [], "id": "P29475", "name": "Neuronal Nitric Oxide Synthase (nNOS)", "organism": "Homo sapiens", "uniprot_id": "P29475" }, { "function": "Integrin alpha-7/beta-1 is the primary laminin receptor on skeletal myoblasts and adult myofibers. During myogenic differentiation, it may induce changes in the shape and mobility of myoblasts, and facilitate their localization at laminin-rich sites of secondary fiber formation. It is involved in the maintenance of the myofibers cytoarchitecture as well as for their anchorage, viability and functional integrity. Isoform Alpha-7X2B and isoform Alpha-7X1B promote myoblast migration on laminin 1 and laminin 2/4, but isoform Alpha-7X1B is less active on laminin 1 (In vitro). Acts as a Schwann cell receptor for laminin-2. Acts as a receptor of COMP and mediates its effect on vascular smooth muscle cells (VSMCs) maturation (By similarity). Required to promote contractile phenotype acquisition in differentiated airway smooth muscle (ASM) cells", "gene_name": "ITGA7", "glycan_count": 8, "glycosylation_sites": [ { "position": 86, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 786, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 989, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1025, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1045, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13683", "name": "Alpha7-integrin", "organism": "Homo sapiens", "uniprot_id": "Q13683" }, { "function": "Integral component of basement membranes. Component of the glomerular basement membrane (GBM), responsible for the fixed negative electrostatic membrane charge, and which provides a barrier which is both size- and charge-selective. It serves as an attachment substrate for cells. Plays essential roles in vascularization. Critical for normal heart development and for regulating the vascular response to injury. Also required for avascular cartilage development", "gene_name": "HSPG2", "glycan_count": 183, "glycosylation_sites": [ { "position": 42, "type": "O-linked (GalNAc...) threonine" }, { "position": 65, "type": "O-linked (Xyl...) (heparan sulfate) serine" }, { "position": 71, "type": "O-linked (Xyl...) (heparan sulfate) serine" }, { "position": 76, "type": "O-linked (Xyl...) (heparan sulfate) serine" }, { "position": 89, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 554, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1755, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2121, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2995, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 3072, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3105, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3279, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3780, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3836, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3933, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 4068, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4179, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 4193, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" } ], "id": "P98160", "name": "Perlecan", "organism": "Homo sapiens", "uniprot_id": "P98160" }, { "function": "Electrogenic Na(+)-coupled sugar symporter that actively transports D-glucose or D-galactose at the plasma membrane, with a Na(+) to sugar coupling ratio of 2:1. Transporter activity is driven by a transmembrane Na(+) electrochemical gradient set by the Na(+)/K(+) pump (PubMed:20980548, PubMed:34880492, PubMed:35077764, PubMed:8563765, PubMed:37217492). Has a primary role in the transport of dietary monosaccharides from enterocytes to blood. Responsible for the absorption of D-glucose or D-galactose across the apical brush-border membrane of enterocytes, whereas basolateral exit is provided by GLUT2. Additionally, functions as a D-glucose sensor in enteroendocrine cells, triggering the secretion of the incretins GCG and GIP that control food intake and energy homeostasis (By similarity) (PubMed:8563765). Together with SGLT2, functions in reabsorption of D-glucose from glomerular filtrate, playing a nonredundant role in the S3 segment of the proximal tubules (By similarity). Transports D-glucose into endometrial epithelial cells, controlling glycogen synthesis and nutritional support for the embryo as well as the decidual transformation of endometrium prior to conception (PubMed:28974690). Acts as a water channel enabling passive water transport across the plasma membrane in response to the osmotic gradient created upon sugar and Na(+) uptake. Has high water conductivity, comparable to aquaporins, and therefore is expected to play an important role in transepithelial water permeability, especially in the small intestine", "gene_name": "SLC5A1", "glycan_count": 6, "glycosylation_sites": [ { "position": 248, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P13866", "name": "SGLT1", "organism": "Homo sapiens", "uniprot_id": "P13866" }, { "function": "Facilitative glucose transporter, which is responsible for constitutive or basal glucose uptake (PubMed:10227690, PubMed:10954735, PubMed:18245775, PubMed:19449892, PubMed:25982116, PubMed:27078104, PubMed:32860739). Has a very broad substrate specificity; can transport a wide range of aldoses including both pentoses and hexoses (PubMed:18245775, PubMed:19449892). Most important energy carrier of the brain: present at the blood-brain barrier and assures the energy-independent, facilitative transport of glucose into the brain (PubMed:10227690). In association with BSG and NXNL1, promotes retinal cone survival by increasing glucose uptake into photoreceptors (By similarity). Required for mesendoderm differentiation (By similarity)", "gene_name": "SLC2A1", "glycan_count": 9, "glycosylation_sites": [ { "position": 45, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P11166", "name": "GLUT1", "organism": "Homo sapiens", "uniprot_id": "P11166" }, { "function": "Facilitative hexose transporter that mediates the transport of glucose, fructose and galactose (PubMed:16186102, PubMed:23396969, PubMed:28083649, PubMed:8027028, PubMed:8457197). Likely mediates the bidirectional transfer of glucose across the plasma membrane of hepatocytes and is responsible for uptake of glucose by the beta cells; may comprise part of the glucose-sensing mechanism of the beta cell (PubMed:8027028). May also participate with the Na(+)/glucose cotransporter in the transcellular transport of glucose in the small intestine and kidney (PubMed:3399500). Also able to mediate the transport of dehydroascorbate (PubMed:23396969)", "gene_name": "SLC2A2", "glycan_count": 1, "glycosylation_sites": [ { "position": 62, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P11168", "name": "GLUT2", "organism": "Homo sapiens", "uniprot_id": "P11168" }, { "function": "Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis", "gene_name": "PFKM", "glycan_count": 1, "glycosylation_sites": [ { "position": 530, "type": "O-linked (GlcNAc) serine" } ], "id": "P08237", "name": "PFK1", "organism": "Homo sapiens", "uniprot_id": "P08237" }, { "function": "Catalyzes the final rate-limiting step of glycolysis by mediating the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP (PubMed:15996096, PubMed:1854723, PubMed:20847263). The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production (PubMed:15996096, PubMed:1854723, PubMed:20847263). The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival (PubMed:15996096, PubMed:1854723, PubMed:20847263)", "gene_name": "PKM", "glycan_count": 1, "glycosylation_sites": [], "id": "P14618", "name": "PKM2", "organism": "Homo sapiens", "uniprot_id": "P14618" }, { "function": "Multifunctional glycoprotein that acts as a receptor for a broad range of ligands. Ligands can be of proteinaceous nature like thrombospondin, fibronectin, collagen or amyloid-beta as well as of lipidic nature such as oxidized low-density lipoprotein (oxLDL), anionic phospholipids, long-chain fatty acids and bacterial diacylated lipopeptides. They are generally multivalent and can therefore engage multiple receptors simultaneously, the resulting formation of CD36 clusters initiates signal transduction and internalization of receptor-ligand complexes. The dependency on coreceptor signaling is strongly ligand specific. Cellular responses to these ligands are involved in angiogenesis, inflammatory response, fatty acid metabolism, taste and dietary fat processing in the intestine (Probable). Binds long-chain fatty acids and facilitates their transport into cells, thus participating in muscle lipid utilization, adipose energy storage, and gut fat absorption (By similarity) (PubMed:18353783, PubMed:21610069). Mechanistically, binding of fatty acids activates downstream kinase LYN, which phosphorylates the palmitoyltransferase ZDHHC5 and inactivates it, resulting in the subsequent depalmitoylation of CD36 and caveolar endocytosis (PubMed:32958780). In the small intestine, plays a role in proximal absorption of dietary fatty acid and cholesterol for optimal chylomicron formation, possibly through the activation of MAPK1/3 (ERK1/2) signaling pathway (By similarity) (PubMed:18753675). Involved in oral fat perception and preferences (PubMed:22240721, PubMed:25822988). Detection into the tongue of long-chain fatty acids leads to a rapid and sustained rise in flux and protein content of pancreatobiliary secretions (By similarity). In taste receptor cells, mediates the induction of an increase in intracellular calcium levels by long-chain fatty acids, leading to the activation of the gustatory neurons in the nucleus of the solitary tract (By similarity). Important factor in both ventromedial hypothalamus neuronal sensing of long-chain fatty acid and the regulation of energy and glucose homeostasis (By similarity). Receptor for thrombospondins, THBS1 and THBS2, mediating their antiangiogenic effects (By similarity). Involved in inducing apoptosis in podocytes in response to elevated free fatty acids, acting together with THBS1 (By similarity). As a coreceptor for TLR4:TLR6 heterodimer, promotes inflammation in monocytes/macrophages. Upon ligand binding, such as oxLDL or amyloid-beta 42, interacts with the heterodimer TLR4:TLR6, the complex is internalized and triggers inflammatory response, leading to NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway, as well as IL1B secretion, through the priming and activation of the NLRP3 inflammasome (By similarity) (PubMed:20037584). Selective and nonredundant sensor of microbial diacylated lipopeptide that signal via TLR2:TLR6 heterodimer, this cluster triggers signaling from the cell surface, leading to the NF-kappa-B-dependent production of TNF, via MYD88 signaling pathway and subsequently is targeted to the Golgi in a lipid-raft dependent pathway (By similarity) (PubMed:16880211)", "gene_name": "CD36", "glycan_count": 42, "glycosylation_sites": [ { "position": 79, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 102, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 134, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 163, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 205, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 220, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 235, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 247, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 321, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 417, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P16671", "name": "CD36", "organism": "Homo sapiens", "uniprot_id": "P16671" }, { "function": "Catalyzes the conversion of (3S)-hydroxy-3-methylglutaryl-CoA (HMG-CoA) to mevalonic acid, the rate-limiting step in the synthesis of cholesterol and other isoprenoids, thus plays a critical role in cellular cholesterol homeostasis (PubMed:21357570, PubMed:2991281, PubMed:36745799, PubMed:6995544). HMGCR is the main target of statins, a class of cholesterol-lowering drugs (PubMed:11349148, PubMed:18540668, PubMed:36745799)", "gene_name": "HMGCR", "glycan_count": 7, "glycosylation_sites": [ { "position": 281, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 296, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P04035", "name": "HMG-CoA reductase", "organism": "Homo sapiens", "uniprot_id": "P04035" }, { "function": "Plays a critical role in the sodium-dependent reabsorption of bile acids from the lumen of the small intestine (PubMed:7592981, PubMed:9458785, PubMed:9856990). Transports various bile acids, unconjugated or conjugated, such as cholate and taurocholate (PubMed:7592981, PubMed:9458785, PubMed:9856990). Also responsible for bile acid transport in the renal proximal tubules, a salvage mechanism that helps conserve bile acids (Probable). Works collaboratively with the Na(+)-taurocholate cotransporting polypeptide (NTCP), the organic solute transporter (OST), and the bile salt export pump (BSEP), to ensure efficacious biological recycling of bile acids during enterohepatic circulation (PubMed:33222321)", "gene_name": "SLC10A2", "glycan_count": 0, "glycosylation_sites": [ { "position": 10, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q12908", "name": "ASBT (SLC10A2)", "organism": "Homo sapiens", "uniprot_id": "Q12908" }, { "function": "Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions", "gene_name": "PMM2", "glycan_count": 2, "glycosylation_sites": [], "id": "O15305", "name": "Phosphomannomutase-2 (PMM2)", "organism": "Homo sapiens", "uniprot_id": "O15305" }, { "function": "Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for fibronectin. Alpha-4/beta-1 recognizes one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1 are receptors for lamimin. Integrin alpha-6/beta-1 (ITGA6:ITGB1) is present in oocytes and is involved in sperm-egg fusion (By similarity). Integrin alpha-4/beta-1 is a receptor for VCAM1. It recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-9/beta-1 is a receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin. Integrin alpha-3/beta-1 is a receptor for epiligrin, thrombospondin and CSPG4. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration. Integrin alpha-V/beta-1 is a receptor for vitronectin. Beta-1 integrins recognize the sequence R-G-D in a wide array of ligands. When associated with alpha-7 integrin, regulates cell adhesion and laminin matrix deposition. Involved in promoting endothelial cell motility and angiogenesis. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process and the formation of mineralized bone nodules. May be involved in up-regulation of the activity of kinases such as PKC via binding to KRT1. Together with KRT1 and RACK1, serves as a platform for SRC activation or inactivation. Plays a mechanistic adhesive role during telophase, required for the successful completion of cytokinesis. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling (PubMed:23125415, PubMed:24789099). ITGA4:ITGB1 and ITGA5:ITGB1 bind to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1 (PubMed:18635536, PubMed:25398877). ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1 (PubMed:12807887, PubMed:17158881). ITGA5:ITGB1 acts as a receptor for fibronectin FN1 and mediates R-G-D-dependent cell adhesion to FN1 (PubMed:33962943). ITGA5:ITGB1 is a receptor for IL1B and binding is essential for IL1B signaling (PubMed:29030430). ITGA5:ITGB3 is a receptor for soluble CD40LG and is required for CD40/CD40LG signaling (PubMed:31331973). Plays an important role in myoblast differentiation and fusion during skeletal myogenesis (By similarity). ITGA9:ITGB1 may play a crucial role in SVEP1/polydom-mediated myoblast cell adhesion (By similarity). Integrins ITGA9:ITGB1 and ITGA4:ITGB1 repress PRKCA-mediated L-type voltage-gated channel Ca(2+) influx and ROCK-mediated calcium sensitivity in vascular smooth muscle cells via their interaction with SVEP1, thereby inhibit vasocontraction (PubMed:35802072)", "gene_name": "ITGB1", "glycan_count": 217, "glycosylation_sites": [ { "position": 50, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 94, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 97, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 212, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 269, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 363, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 406, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 417, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 481, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 520, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 584, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 669, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P05556", "name": "Integrin \u03b21", "organism": "Homo sapiens", "uniprot_id": "P05556" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P23229/P16144", "name": "Integrin \u03b16\u03b24", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q14118 (human)", "name": "Dystroglycan", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q13683 (human)", "name": "Integrin alpha7 (Itga7)", "organism": "", "uniprot_id": "" }, { "function": "Mannosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. Catalyzes, on the cytoplasmic face of the endoplasmic reticulum, the addition of the second and third mannose residues to the dolichol-linked oligosaccharide chain, to produce Man3GlcNAc(2)-PP-dolichol core oligosaccharide. Man3GlcNAc(2)-PP-dolichol is a substrate for ALG11, the following enzyme in the biosynthetic pathway (PubMed:12684507, PubMed:35136180). While both alpha 1,3 and alpha 1,6 linkages are possible, the sequential addition of alpha 1,3 followed by alpha 1,6 is probably the preferred route (PubMed:35136180)", "gene_name": "ALG2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H553", "name": "ALG1 (\u03b21,4 mannosyltransferase)", "organism": "Homo sapiens", "uniprot_id": "Q9H553" }, { "function": "As a result of hemolysis, hemoglobin is found to accumulate in the kidney and is secreted in the urine. Haptoglobin captures, and combines with free plasma hemoglobin to allow hepatic recycling of heme iron and to prevent kidney damage. Haptoglobin also acts as an antioxidant, has antibacterial activity, and plays a role in modulating many aspects of the acute phase response. Hemoglobin/haptoglobin complexes are rapidly cleared by the macrophage CD163 scavenger receptor expressed on the surface of liver Kupfer cells through an endocytic lysosomal degradation pathway", "gene_name": "HP", "glycan_count": 299, "glycosylation_sites": [ { "position": 184, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 207, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 211, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 241, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P00738", "name": "Haptoglobin", "organism": "Homo sapiens", "uniprot_id": "P00738" }, { "function": "Inhibitor of serine proteases. Its primary target is elastase, but it also has a moderate affinity for plasmin and thrombin. Irreversibly inhibits trypsin, chymotrypsin and plasminogen activator. The aberrant form inhibits insulin-induced NO synthesis in platelets, decreases coagulation time and has proteolytic activity against insulin and plasmin", "gene_name": "SERPINA1", "glycan_count": 267, "glycosylation_sites": [ { "position": 70, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 107, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 271, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P01009", "name": "Alpha-1 antitrypsin", "organism": "Homo sapiens", "uniprot_id": "P01009" }, { "function": "Signaling adapter protein that participates in the signal transduction from two prominent receptor tyrosine kinases, insulin receptor/INSR and insulin-like growth factor I receptor/IGF1R (PubMed:7541045, PubMed:33991522, PubMed:38625937). Plays therefore an important role in development, growth, glucose homeostasis as well as lipid metabolism (PubMed:19639489). Upon phosphorylation by the insulin receptor, functions as a signaling scaffold that propagates insulin action through binding to SH2 domain-containing proteins including the p85 regulatory subunit of PI3K, NCK1, NCK2, GRB2 or SHP2 (PubMed:11171109, PubMed:8265614). Recruitment of GRB2 leads to the activation of the guanine nucleotide exchange factor SOS1 which in turn triggers the Ras/Raf/MEK/MAPK signaling cascade (By similarity). Activation of the PI3K/AKT pathway is responsible for most of insulin metabolic effects in the cell, and the Ras/Raf/MEK/MAPK is involved in the regulation of gene expression and in cooperation with the PI3K pathway regulates cell growth and differentiation. Acts a positive regulator of the Wnt/beta-catenin signaling pathway through suppression of DVL2 autophagy-mediated degradation leading to cell proliferation (PubMed:24616100)", "gene_name": "IRS1", "glycan_count": 1, "glycosylation_sites": [], "id": "P35568", "name": "IRS1", "organism": "Homo sapiens", "uniprot_id": "P35568" }, { "function": "Adapter protein which acts downstream of several membrane receptors including cytokine, antigen, hormone, cell matrix and growth factor receptors to regulate multiple signaling pathways. Regulates osteoclast differentiation mediating the TNFRSF11A/RANK signaling. In allergic response, it plays a role in mast cells activation and degranulation through PI-3-kinase regulation. Also involved in the regulation of cell proliferation and hematopoiesis", "gene_name": "GAB2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UQC2", "name": "PLC\u03b4", "organism": "Homo sapiens", "uniprot_id": "Q9UQC2" }, { "function": "Generates phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as second messengers. Has a role in several intracellular trafficking events. Functions in insulin signaling and secretion. Required for translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane and glucose uptake in response to insulin-mediated RHOQ activation. Regulates insulin secretion through two different mechanisms: involved in glucose-induced insulin secretion downstream of insulin receptor in a pathway that involves AKT1 activation and TBC1D4/AS160 phosphorylation, and participates in the late step of insulin granule exocytosis probably in insulin granule fusion. Synthesizes PtdIns3P in response to insulin signaling. Functions in clathrin-coated endocytic vesicle formation and distribution. Regulates dynamin-independent endocytosis, probably by recruiting EEA1 to internalizing vesicles. In neurosecretory cells synthesizes PtdIns3P on large dense core vesicles. Participates in calcium induced contraction of vascular smooth muscle by regulating myosin light chain (MLC) phosphorylation through a mechanism involving Rho kinase-dependent phosphorylation of the MLCP-regulatory subunit MYPT1. May play a role in the EGF signaling cascade. May be involved in mitosis and UV-induced damage response. Required for maintenance of normal renal structure and function by supporting normal podocyte function. Involved in the regulation of ciliogenesis and trafficking of ciliary components (PubMed:31034465)", "gene_name": "PIK3C2A", "glycan_count": 1, "glycosylation_sites": [], "id": "O00443", "name": "PI3K-C2\u03b1", "organism": "Homo sapiens", "uniprot_id": "O00443" }, { "function": "Non-receptor tyrosine kinase indispensable for B lymphocyte development, differentiation and signaling (PubMed:19290921). Binding of antigen to the B-cell antigen receptor (BCR) triggers signaling that ultimately leads to B-cell activation (PubMed:19290921). After BCR engagement and activation at the plasma membrane, phosphorylates PLCG2 at several sites, igniting the downstream signaling pathway through calcium mobilization, followed by activation of the protein kinase C (PKC) family members (PubMed:11606584). PLCG2 phosphorylation is performed in close cooperation with the adapter protein B-cell linker protein BLNK (PubMed:11606584). BTK acts as a platform to bring together a diverse array of signaling proteins and is implicated in cytokine receptor signaling pathways (PubMed:16517732, PubMed:17932028). Plays an important role in the function of immune cells of innate as well as adaptive immunity, as a component of the Toll-like receptors (TLR) pathway (PubMed:16517732). The TLR pathway acts as a primary surveillance system for the detection of pathogens and are crucial to the activation of host defense (PubMed:16517732). Especially, is a critical molecule in regulating TLR9 activation in splenic B-cells (PubMed:16517732, PubMed:17932028). Within the TLR pathway, induces tyrosine phosphorylation of TIRAP which leads to TIRAP degradation (PubMed:16415872). BTK also plays a critical role in transcription regulation (PubMed:19290921). Induces the activity of NF-kappa-B, which is involved in regulating the expression of hundreds of genes (PubMed:19290921). BTK is involved on the signaling pathway linking TLR8 and TLR9 to NF-kappa-B (PubMed:19290921). Acts as an activator of NLRP3 inflammasome assembly by mediating phosphorylation of NLRP3 (PubMed:34554188). Transiently phosphorylates transcription factor GTF2I on tyrosine residues in response to BCR (PubMed:9012831). GTF2I then translocates to the nucleus to bind regulatory enhancer elements to modulate gene expression (PubMed:9012831). ARID3A and NFAT are other transcriptional target of BTK (PubMed:16738337). BTK is required for the formation of functional ARID3A DNA-binding complexes (PubMed:16738337). There is however no evidence that BTK itself binds directly to DNA (PubMed:16738337). BTK has a dual role in the regulation of apoptosis (PubMed:9751072). Plays a role in STING1-mediated induction of type I interferon (IFN) response by phosphorylating DDX41 (PubMed:25704810)", "gene_name": "BTK", "glycan_count": 1, "glycosylation_sites": [], "id": "Q06187", "name": "BTK", "organism": "Homo sapiens", "uniprot_id": "Q06187" }, { "function": "Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways (PubMed:16824732). Required for correct mitotic spindle orientation and therefore progression of mitosis (By similarity). Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear (PubMed:9660833). While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking (By similarity). Confers resistance to dietary obesity (By similarity). May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane (By similarity). Part of a signaling pathway that regulates actin cytoskeleton remodeling (PubMed:11739414, PubMed:12676785). Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation (PubMed:15668240). Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling (PubMed:21624956). Regulates cell adhesion and cell spreading (PubMed:12235291). Required for HGF-mediated lamellipodium formation, cell scattering and spreading (PubMed:15735664). Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation (PubMed:17135240). Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth (By similarity). Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A) (PubMed:12690104). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems (PubMed:11016922). Involved in EGF signaling pathway (PubMed:11349134). Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3 (PubMed:11349134). Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity (PubMed:11349134). Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1 (By similarity). In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling (By similarity). Plays a role in the localization of AURKA and NEDD9/HEF1 to the basolateral membrane at interphase in polarized cysts, thereby mediates cell cycle homeostasis, cell polarization and cilia assembly (By similarity). Additionally promotion of cilia growth is also facilitated by hydrolysis of (PtdIns(3,4,5)P3) to PtdIns(3,4)P2 (By similarity). Promotes formation of apical membrane-initiation sites during the initial stages of lumen formation via Rho family-induced actin filament organization and CTNNB1 localization to cell-cell contacts (By similarity). May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6. Involved in endochondral ossification (PubMed:23273569)", "gene_name": "INPPL1", "glycan_count": 2, "glycosylation_sites": [], "id": "O15357", "name": "SHIP2", "organism": "Homo sapiens", "uniprot_id": "O15357" }, { "function": "Dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins (PubMed:9187108, PubMed:9256433, PubMed:9616126). Also functions as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring of PtdIns(3,4,5)P3/phosphatidylinositol 3,4,5-trisphosphate, PtdIns(3,4)P2/phosphatidylinositol 3,4-diphosphate and PtdIns3P/phosphatidylinositol 3-phosphate with a preference for PtdIns(3,4,5)P3 (PubMed:16824732, PubMed:26504226, PubMed:9593664, PubMed:9811831). Furthermore, this enzyme can also act as a cytosolic inositol 3-phosphatase acting on Ins(1,3,4,5,6)P5/inositol 1,3,4,5,6 pentakisphosphate and possibly Ins(1,3,4,5)P4/1D-myo-inositol 1,3,4,5-tetrakisphosphate (PubMed:11418101, PubMed:15979280). Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival (PubMed:31492966, PubMed:37279284). The unphosphorylated form cooperates with MAGI2 to suppress AKT1 activation (PubMed:11707428). In motile cells, suppresses the formation of lateral pseudopods and thereby promotes cell polarization and directed movement (PubMed:22279049). Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation (PubMed:22279049). Required for growth factor-induced epithelial cell migration; growth factor stimulation induces PTEN phosphorylation which changes its binding preference from the p85 regulatory subunit of the PI3K kinase complex to DLC1 and results in translocation of the PTEN-DLC1 complex to the posterior of migrating cells to promote RHOA activation (PubMed:26166433). Meanwhile, TNS3 switches binding preference from DLC1 to p85 and the TNS3-p85 complex translocates to the leading edge of migrating cells to activate RAC1 activation (PubMed:26166433). Plays a role as a key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation (By similarity). Involved in the regulation of synaptic function in excitatory hippocampal synapses. Recruited to the postsynaptic membrane upon NMDA receptor activation, is required for the modulation of synaptic activity during plasticity. Enhancement of lipid phosphatase activity is able to drive depression of AMPA receptor-mediated synaptic responses, activity required for NMDA receptor-dependent long-term depression (LTD) (By similarity). May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue. The nuclear monoubiquitinated form possesses greater apoptotic potential, whereas the cytoplasmic nonubiquitinated form induces less tumor suppressive ability (PubMed:10468583, PubMed:18716620)", "gene_name": "PTEN", "glycan_count": 1, "glycosylation_sites": [], "id": "P60484", "name": "PTEN", "organism": "Homo sapiens", "uniprot_id": "P60484" }, { "function": "Catalyzes the hydrolysis of ATP coupled with the transport of calcium from the cytoplasm to the extracellular space thereby maintaining intracellular calcium homeostasis (PubMed:35358416). Plays a role in blood pressure regulation through regulation of intracellular calcium concentration and nitric oxide production leading to regulation of vascular smooth muscle cells vasoconstriction. Positively regulates bone mineralization through absorption of calcium from the intestine. Plays dual roles in osteoclast differentiation and survival by regulating RANKL-induced calcium oscillations in preosteoclasts and mediating calcium extrusion in mature osteoclasts (By similarity). Regulates insulin sensitivity through calcium/calmodulin signaling pathway by regulating AKT1 activation and NOS3 activation in endothelial cells (PubMed:29104511). May play a role in synaptic transmission by modulating calcium and proton dynamics at the synaptic vesicles", "gene_name": "ATP2B1", "glycan_count": 2, "glycosylation_sites": [], "id": "P20020", "name": "PMCA1", "organism": "Homo sapiens", "uniprot_id": "P20020" }, { "function": "This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen (PubMed:12542527, PubMed:16402920). Involved in autophagy in response to starvation. Upon interaction with VMP1 and activation, controls ER-isolation membrane contacts for autophagosome formation (PubMed:28890335). Also modulates ER contacts with lipid droplets, mitochondria and endosomes (PubMed:28890335). In coordination with FLVCR2 mediates heme-stimulated switching from mitochondrial ATP synthesis to thermogenesis (By similarity)", "gene_name": "ATP2A2", "glycan_count": 1, "glycosylation_sites": [], "id": "P16615", "name": "SERCA", "organism": "Homo sapiens", "uniprot_id": "P16615" }, { "function": "Serine/threonine protein kinase which is a central regulator of cellular metabolism, growth and survival in response to hormones, growth factors, nutrients, energy and stress signals (PubMed:12087098, PubMed:12150925, PubMed:12150926, PubMed:12231510, PubMed:12718876, PubMed:14651849, PubMed:15268862, PubMed:15467718, PubMed:15545625, PubMed:15718470, PubMed:18497260, PubMed:18762023, PubMed:18925875, PubMed:20516213, PubMed:20537536, PubMed:21659604, PubMed:23429703, PubMed:23429704, PubMed:25799227, PubMed:26018084, PubMed:29150432, PubMed:29236692, PubMed:31112131, PubMed:31601708, PubMed:32561715, PubMed:34519269, PubMed:37751742). MTOR directly or indirectly regulates the phosphorylation of at least 800 proteins (PubMed:15268862, PubMed:15467718, PubMed:17517883, PubMed:18372248, PubMed:18497260, PubMed:18925875, PubMed:20516213, PubMed:21576368, PubMed:21659604, PubMed:23429704, PubMed:30171069, PubMed:29236692, PubMed:37751742). Functions as part of 2 structurally and functionally distinct signaling complexes mTORC1 and mTORC2 (mTOR complex 1 and 2) (PubMed:15268862, PubMed:15467718, PubMed:18497260, PubMed:18925875, PubMed:20516213, PubMed:21576368, PubMed:21659604, PubMed:23429704, PubMed:29424687, PubMed:29567957, PubMed:35926713). In response to nutrients, growth factors or amino acids, mTORC1 is recruited to the lysosome membrane and promotes protein, lipid and nucleotide synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis (PubMed:12087098, PubMed:12150925, PubMed:12150926, PubMed:12231510, PubMed:12718876, PubMed:14651849, PubMed:15268862, PubMed:15467718, PubMed:15545625, PubMed:15718470, PubMed:18497260, PubMed:18762023, PubMed:18925875, PubMed:20516213, PubMed:20537536, PubMed:21659604, PubMed:23429703, PubMed:23429704, PubMed:25799227, PubMed:26018084, PubMed:29150432, PubMed:29236692, PubMed:31112131, PubMed:34519269). This includes phosphorylation of EIF4EBP1 and release of its inhibition toward the elongation initiation factor 4E (eiF4E) (PubMed:24403073, PubMed:29236692). Moreover, phosphorylates and activates RPS6KB1 and RPS6KB2 that promote protein synthesis by modulating the activity of their downstream targets including ribosomal protein S6, eukaryotic translation initiation factor EIF4B, and the inhibitor of translation initiation PDCD4 (PubMed:12087098, PubMed:12150925, PubMed:18925875, PubMed:29150432, PubMed:29236692). Stimulates the pyrimidine biosynthesis pathway, both by acute regulation through RPS6KB1-mediated phosphorylation of the biosynthetic enzyme CAD, and delayed regulation, through transcriptional enhancement of the pentose phosphate pathway which produces 5-phosphoribosyl-1-pyrophosphate (PRPP), an allosteric activator of CAD at a later step in synthesis, this function is dependent on the mTORC1 complex (PubMed:23429703, PubMed:23429704). Regulates ribosome synthesis by activating RNA polymerase III-dependent transcription through phosphorylation and inhibition of MAF1 an RNA polymerase III-repressor (PubMed:20516213). Activates dormant ribosomes by mediating phosphorylation of SERBP1, leading to SERBP1 inactivation and reactivation of translation (PubMed:36691768). In parallel to protein synthesis, also regulates lipid synthesis through SREBF1/SREBP1 and LPIN1 (PubMed:23426360). To maintain energy homeostasis mTORC1 may also regulate mitochondrial biogenesis through regulation of PPARGC1A (By similarity). In the same time, mTORC1 inhibits catabolic pathways: negatively regulates autophagy through phosphorylation of ULK1 (PubMed:32561715). Under nutrient sufficiency, phosphorylates ULK1 at 'Ser-758', disrupting the interaction with AMPK and preventing activation of ULK1 (PubMed:32561715). Also prevents autophagy through phosphorylation of the autophagy inhibitor DAP (PubMed:20537536). Also prevents autophagy by phosphorylating RUBCNL/Pacer under nutrient-rich conditions (PubMed:30704899). Prevents autophagy by mediating phosphorylation of AMBRA1, thereby inhibiting AMBRA1 ability to mediate ubiquitination of ULK1 and interaction between AMBRA1 and PPP2CA (PubMed:23524951, PubMed:25438055). mTORC1 exerts a feedback control on upstream growth factor signaling that includes phosphorylation and activation of GRB10 a INSR-dependent signaling suppressor (PubMed:21659604). Among other potential targets mTORC1 may phosphorylate CLIP1 and regulate microtubules (PubMed:12231510). The mTORC1 complex is inhibited in response to starvation and amino acid depletion (PubMed:12150925, PubMed:12150926, PubMed:24403073, PubMed:31695197). The non-canonical mTORC1 complex, which acts independently of RHEB, specifically mediates phosphorylation of MiT/TFE factors MITF, TFEB and TFE3 in the presence of nutrients, promoting their cytosolic retention and inactivation (PubMed:22343943, PubMed:22576015, PubMed:22692423, PubMed:24448649, PubMed:32612235, PubMed:36608670, PubMed:36697823). Upon starvation or lysosomal stress, inhibition of mTORC1 induces dephosphorylation and nuclear translocation of TFEB and TFE3, promoting their transcription factor activity (PubMed:22343943, PubMed:22576015, PubMed:22692423, PubMed:24448649, PubMed:32612235, PubMed:36608670). The mTORC1 complex regulates pyroptosis in macrophages by promoting GSDMD oligomerization (PubMed:34289345). MTOR phosphorylates RPTOR which in turn inhibits mTORC1 (By similarity). As part of the mTORC2 complex, MTOR transduces signals from growth factors to pathways involved in proliferation, cytoskeletal organization, lipogenesis and anabolic output (PubMed:15268862, PubMed:15467718, PubMed:24670654, PubMed:29424687, PubMed:29567957, PubMed:35926713). In response to growth factors, mTORC2 phosphorylates and activates AGC protein kinase family members, including AKT (AKT1, AKT2 and AKT3), PKC (PRKCA, PRKCB and PRKCE) and SGK1 (PubMed:15268862, PubMed:15467718, PubMed:21376236, PubMed:24670654, PubMed:29424687, PubMed:29567957, PubMed:35926713). In contrast to mTORC1, mTORC2 is nutrient-insensitive (PubMed:15467718). mTORC2 plays a critical role in AKT1 activation by mediating phosphorylation of different sites depending on the context, such as 'Thr-450', 'Ser-473', 'Ser-477' or 'Thr-479', facilitating the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDPK1/PDK1 which is a prerequisite for full activation (PubMed:15718470, PubMed:21376236, PubMed:24670654, PubMed:29424687, PubMed:29567957). mTORC2 also regulates the phosphorylation of SGK1 at 'Ser-422' (PubMed:18925875). mTORC2 may regulate the actin cytoskeleton, through phosphorylation of PRKCA, PXN and activation of the Rho-type guanine nucleotide exchange factors RHOA and RAC1A or RAC1B (PubMed:15268862). The mTORC2 complex also phosphorylates various proteins involved in insulin signaling, such as FBXW8 and IGF2BP1 (By similarity). May also regulate insulin signaling by acting as a tyrosine protein kinase that catalyzes phosphorylation of IGF1R and INSR; additional evidence are however required to confirm this result in vivo (PubMed:26584640). Regulates osteoclastogenesis by adjusting the expression of CEBPB isoforms (By similarity). Plays an important regulatory role in the circadian clock function; regulates period length and rhythm amplitude of the suprachiasmatic nucleus (SCN) and liver clocks (By similarity)", "gene_name": "MTOR", "glycan_count": 3, "glycosylation_sites": [], "id": "P42345", "name": "mTOR", "organism": "Homo sapiens", "uniprot_id": "P42345" }, { "function": "Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis. ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated pro-inflammatory responses. Plays a role in the regulation of cardiovascular circadian rhythms by regulating the transcription of BMAL1 in the blood vessels (By similarity)", "gene_name": "PPARG", "glycan_count": 0, "glycosylation_sites": [ { "position": 84, "type": "O-linked (GlcNAc) threonine" } ], "id": "P37231", "name": "Peroxisome proliferator-activated receptor gamma (PPAR\u03b3)", "organism": "Homo sapiens", "uniprot_id": "P37231" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "varies by virus (e.g., P29990 for DENV-2)", "name": "NS1 (Nonstructural protein 1)", "organism": "", "uniprot_id": "" }, { "function": "Peripheral membrane component of the cis-Golgi stack that acts as a membrane skeleton that maintains the structure of the Golgi apparatus, and as a vesicle thether that facilitates vesicle fusion to the Golgi membrane (Probable) (PubMed:16489344). Required for normal protein transport from the endoplasmic reticulum to the Golgi apparatus and the cell membrane (By similarity). Together with p115/USO1 and STX5, involved in vesicle tethering and fusion at the cis-Golgi membrane to maintain the stacked and inter-connected structure of the Golgi apparatus. Plays a central role in mitotic Golgi disassembly: phosphorylation at Ser-37 by CDK1 at the onset of mitosis inhibits the interaction with p115/USO1, preventing tethering of COPI vesicles and thereby inhibiting transport through the Golgi apparatus during mitosis (By similarity). Also plays a key role in spindle pole assembly and centrosome organization (PubMed:26165940). Promotes the mitotic spindle pole assembly by activating the spindle assembly factor TPX2 to nucleate microtubules around the Golgi and capture them to couple mitotic membranes to the spindle: upon phosphorylation at the onset of mitosis, GOLGA2 interacts with importin-alpha via the nuclear localization signal region, leading to recruit importin-alpha to the Golgi membranes and liberate the spindle assembly factor TPX2 from importin-alpha. TPX2 then activates AURKA kinase and stimulates local microtubule nucleation. Upon filament assembly, nascent microtubules are further captured by GOLGA2, thus linking Golgi membranes to the spindle (PubMed:19242490, PubMed:26165940). Regulates the meiotic spindle pole assembly, probably via the same mechanism (By similarity). Also regulates the centrosome organization (PubMed:18045989, PubMed:19109421). Also required for the Golgi ribbon formation and glycosylation of membrane and secretory proteins (PubMed:16489344, PubMed:17314401)", "gene_name": "GOLGA2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q08379", "name": "GM130 (Golgi Matrix Protein 130)", "organism": "Homo sapiens", "uniprot_id": "Q08379" }, { "function": "Key structural protein of the Golgi apparatus (PubMed:33301566). The membrane cisternae of the Golgi apparatus adhere to each other to form stacks, which are aligned side by side to form the Golgi ribbon (PubMed:33301566). Acting in concert with GORASP2/GRASP55, is required for the formation and maintenance of the Golgi ribbon, and may be dispensable for the formation of stacks (PubMed:33301566). However, other studies suggest that GORASP1 plays an important role in assembly and membrane stacking of the cisternae, and in the reassembly of Golgi stacks after breakdown during mitosis (By similarity). Caspase-mediated cleavage of GORASP1 is required for fragmentation of the Golgi during apoptosis (By similarity). Also mediates, via its interaction with GOLGA2/GM130, the docking of transport vesicles with the Golgi membranes (PubMed:16489344). Mediates ER stress-induced unconventional (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell membrane (PubMed:21884936)", "gene_name": "GORASP1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9BQQ3", "name": "GRASP65", "organism": "Homo sapiens", "uniprot_id": "Q9BQQ3" }, { "function": "Key structural protein of the Golgi apparatus (PubMed:33301566). The membrane cisternae of the Golgi apparatus adhere to each other to form stacks, which are aligned side by side to form the Golgi ribbon (PubMed:33301566). Acting in concert with GORASP1/GRASP65, is required for the formation and maintenance of the Golgi ribbon, and may be dispensable for the formation of stacks (PubMed:33301566). However, other studies suggest that GORASP2 plays a role in the assembly and membrane stacking of the Golgi cisternae, and in the process by which Golgi stacks reform after breakdown during mitosis and meiosis (PubMed:10487747, PubMed:21515684, PubMed:22523075). May regulate the intracellular transport and presentation of a defined set of transmembrane proteins, such as transmembrane TGFA (PubMed:11101516). Required for normal acrosome formation during spermiogenesis and normal male fertility, probably by promoting colocalization of JAM2 and JAM3 at contact sites between germ cells and Sertoli cells (By similarity). Mediates ER stress-induced unconventional (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell membrane (PubMed:21884936, PubMed:27062250, PubMed:28067262)", "gene_name": "GORASP2", "glycan_count": 4, "glycosylation_sites": [], "id": "Q9H8Y8", "name": "GRASP55", "organism": "Homo sapiens", "uniprot_id": "Q9H8Y8" }, { "function": "Transcriptional coactivator for androgen receptor (AR) and serum response factor (SRF). Contributes to the regulation of cell adhesion, spreading and cell migration and acts as a negative regulator in integrin-mediated cell adhesion events. Suppresses the integrin-induced tyrosine phosphorylation of paxillin (PXN). May play a critical role as an adapter protein in the formation of the adhesion zone in osteoclasts. Negatively regulates B-cell antigen receptor (BCR) signaling", "gene_name": "LPXN", "glycan_count": 0, "glycosylation_sites": [], "id": "O60711", "name": "ATP7A", "organism": "Homo sapiens", "uniprot_id": "O60711" }, { "function": "Copper ion transmembrane transporter involved in the export of copper out of the cells. It is involved in copper homeostasis in the liver, where it ensures the efflux of copper from hepatocytes into the bile in response to copper overload", "gene_name": "ATP7B", "glycan_count": 1, "glycosylation_sites": [], "id": "P35670", "name": "ATP7B", "organism": "Homo sapiens", "uniprot_id": "P35670" }, { "function": "Probable metal transporter", "gene_name": "CNNM1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9NRU3", "name": "LARGE", "organism": "Homo sapiens", "uniprot_id": "Q9NRU3" }, { "function": "Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis (PubMed:25122912). Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(o) and JIP. Inhibits G(o) alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity). By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapses in axons (PubMed:17062754, PubMed:23011729). Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1", "gene_name": "APP", "glycan_count": 19, "glycosylation_sites": [ { "position": 542, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 571, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 633, "type": "O-linked (GalNAc...) threonine; partial" }, { "position": 651, "type": "O-linked (GalNAc...) threonine; partial" }, { "position": 652, "type": "O-linked (GalNAc...) threonine; partial" }, { "position": 656, "type": "O-linked (Xyl...) (chondroitin sulfate) serine; in L-APP isoforms" }, { "position": 659, "type": "O-linked (HexNAc...) threonine; partial" }, { "position": 663, "type": "O-linked (GalNAc...) threonine; partial" }, { "position": 667, "type": "O-linked (GalNAc...) serine; partial" }, { "position": 681, "type": "O-linked (HexNAc...) tyrosine; partial" } ], "id": "P05067", "name": "APP (Amyloid Precursor Protein)", "organism": "Homo sapiens", "uniprot_id": "P05067" }, { "function": "Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. The major receptor is host ACE2 (PubMed:32142651, PubMed:32155444, PubMed:33607086). When S2/S2' has been cleaved, binding to the receptor triggers direct fusion at the cell membrane (PubMed:34561887). When S2/S2' has not been cleaved, binding to the receptor results in internalization of the virus by endocytosis using host TFRC and GRM2 and leading to fusion of the virion membrane with the host endosomal membrane (PubMed:32075877, PubMed:32221306, PubMed:34903715, PubMed:36779763). Alternatively, may use NRP1/NRP2 (PubMed:33082294, PubMed:33082293) and integrin as entry receptors (PubMed:35150743). The use of NRP1/NRP2 receptors may explain the tropism of the virus in human olfactory epithelial cells, which express these molecules at high levels but ACE2 at low levels (PubMed:33082293). The stalk domain of S contains three hinges, giving the head unexpected orientational freedom (PubMed:32817270)", "gene_name": "S", "glycan_count": 379, "glycosylation_sites": [ { "position": 17, "type": "N-linked (GlcNAc...) (complex) asparagine; by host" }, { "position": 61, "type": "N-linked (GlcNAc...) (hybrid) asparagine; by host" }, { "position": 74, "type": "N-linked (GlcNAc...) (complex) asparagine; by host" }, { "position": 122, "type": "N-linked (GlcNAc...) (hybrid) asparagine; by host" }, { "position": 149, "type": "N-linked (GlcNAc...) (complex) asparagine; by host" }, { "position": 165, "type": "N-linked (GlcNAc...) (complex) asparagine; by host" }, { "position": 234, "type": "N-linked (GlcNAc...) (high mannose) asparagine; by host" }, { "position": 282, "type": "N-linked (GlcNAc...) (complex) asparagine; by host" }, { "position": 323, "type": "O-linked (GalNAc) threonine; by host" }, { "position": 325, "type": "O-linked (HexNAc...) serine; by host" }, { "position": 331, "type": "N-linked (GlcNAc...) (complex) asparagine; by host" }, { "position": 343, "type": "N-linked (GlcNAc...) (complex) asparagine; by host" }, { "position": 603, "type": "N-linked (GlcNAc...) (hybrid) asparagine; by host" }, { "position": 616, "type": "N-linked (GlcNAc...) (complex) asparagine; by host" }, { "position": 657, "type": "N-linked (GlcNAc...) (complex) asparagine; by host" }, { "position": 676, "type": "O-linked (GlcNAc...) threonine; by host GALNT1" }, { "position": 678, "type": "O-linked (GlcNAc...) threonine; by host GALNT1" }, { "position": 709, "type": "N-linked (GlcNAc...) (high mannose) asparagine; by host" }, { "position": 717, "type": "N-linked (GlcNAc...) (hybrid) asparagine; by host" }, { "position": 801, "type": "N-linked (GlcNAc...) (hybrid) asparagine; by host" }, { "position": 1074, "type": "N-linked (GlcNAc...) (hybrid) asparagine; by host" }, { "position": 1098, "type": "N-linked (GlcNAc...) (complex) asparagine; by host" }, { "position": 1134, "type": "N-linked (GlcNAc...) (complex) asparagine; by host" }, { "position": 1158, "type": "N-linked (GlcNAc...) (complex) asparagine; by host" }, { "position": 1173, "type": "N-linked (GlcNAc...) (complex) asparagine; by host" }, { "position": 1194, "type": "N-linked (GlcNAc...) (complex) asparagine; by host" } ], "id": "P0DTC2", "name": "SARS-CoV-2 Spike Protein", "organism": "Severe acute respiratory syndrome coronavirus 2", "uniprot_id": "P0DTC2" }, { "function": "Important transcription factor regulating the expression of genes involved in immune and inflammatory responses (PubMed:12048245, PubMed:1741402, PubMed:18647749, PubMed:9374525). Also plays a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis. The consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Its functional capacity is governed by protein interactions and post-translational protein modifications. During early embryogenesis, plays essential and redundant roles with CEBPA. Has a promitotic effect on many cell types such as hepatocytes and adipocytes but has an antiproliferative effect on T-cells by repressing MYC expression, facilitating differentiation along the T-helper 2 lineage. Binds to regulatory regions of several acute-phase and cytokines genes and plays a role in the regulation of acute-phase reaction and inflammation. Also plays a role in intracellular bacteria killing (By similarity). During adipogenesis, is rapidly expressed and, after activation by phosphorylation, induces CEBPA and PPARG, which turn on the series of adipocyte genes that give rise to the adipocyte phenotype. The delayed transactivation of the CEBPA and PPARG genes by CEBPB appears necessary to allow mitotic clonal expansion and thereby progression of terminal differentiation (PubMed:20829347). Essential for female reproduction because of a critical role in ovarian follicle development (By similarity). Restricts osteoclastogenesis: together with NFE2L1; represses expression of DSPP during odontoblast differentiation (By similarity)", "gene_name": "CEBPB", "glycan_count": 1, "glycosylation_sites": [ { "position": 227, "type": "O-linked (GlcNAc) serine" }, { "position": 228, "type": "O-linked (GlcNAc) serine" } ], "id": "P17676", "name": "C/EBP\u03b2", "organism": "Homo sapiens", "uniprot_id": "P17676" }, { "function": "Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism (PubMed:17307971, PubMed:17712357, PubMed:24563466, PubMed:37821951). In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation (PubMed:17307971, PubMed:17712357). AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators (PubMed:17307971, PubMed:17712357). Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively (By similarity). Promotes lipolysis of lipid droplets by mediating phosphorylation of isoform 1 of CHKA (CHKalpha2) (PubMed:34077757). Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3 (By similarity). AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160 (By similarity). Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A (PubMed:11518699, PubMed:11554766, PubMed:15866171, PubMed:17711846, PubMed:18184930). Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm (By similarity). In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription (By similarity). Acts as a key regulator of cell growth and proliferation by phosphorylating FNIP1, TSC2, RPTOR, WDR24 and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2 (PubMed:14651849, PubMed:18439900, PubMed:20160076, PubMed:21205641). Also phosphorylates and inhibits GATOR2 subunit WDR24 in response to nutrient limitation, leading to suppress glucose-mediated mTORC1 activation (PubMed:36732624). In response to energetic stress, phosphorylates FNIP1, inactivating the non-canonical mTORC1 signaling, thereby promoting nuclear translocation of TFEB and TFE3, and inducing transcription of lysosomal or autophagy genes (PubMed:37079666). In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1 (PubMed:21205641). In that process, it also activates WDR45/WIPI4 (PubMed:28561066). Phosphorylates CASP6, thereby preventing its autoprocessing and subsequent activation (PubMed:32029622). In response to nutrient limitation, phosphorylates transcription factor FOXO3 promoting FOXO3 mitochondrial import (By similarity). Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin (PubMed:17486097). AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it (By similarity). May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it (By similarity). Also has tau-protein kinase activity: in response to amyloid beta A4 protein (APP) exposure, activated by CAMKK2, leading to phosphorylation of MAPT/TAU; however the relevance of such data remains unclear in vivo (By similarity). Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1 (PubMed:12519745, PubMed:20074060). Regulates hepatic lipogenesis. Activated via SIRT3, represses sterol regulatory element-binding protein (SREBP) transcriptional activities and ATP-consuming lipogenesis to restore cellular energy balance. Upon stress, regulates mitochondrial fragmentation through phosphorylation of MTFR1L (PubMed:36367943)", "gene_name": "PRKAA1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q13131", "name": "AMPK\u03b1", "organism": "Homo sapiens", "uniprot_id": "Q13131" }, { "function": "Important adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion. Antagonizes TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. Inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. May play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex, LMW, MMW or HMW", "gene_name": "ADIPOQ", "glycan_count": 2, "glycosylation_sites": [ { "position": 21, "type": "O-linked (GalNAc...) threonine" }, { "position": 22, "type": "O-linked (GalNAc...) threonine" }, { "position": 65, "type": "O-linked (Gal...) hydroxylysine; partial" }, { "position": 68, "type": "O-linked (Gal...) hydroxylysine; partial" }, { "position": 77, "type": "O-linked (Gal...) hydroxylysine; partial" }, { "position": 101, "type": "O-linked (Gal...) hydroxylysine; partial" } ], "id": "Q15848", "name": "Adiponectin", "organism": "Homo sapiens", "uniprot_id": "Q15848" }, { "function": "Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. Plays a role in cell directional movement, orientation, cell sheet organization and Golgi complex polarization at the cell migration front (By similarity). Protects SCRIB from proteasomal degradation and facilitates its localization to intermediate filaments in a cell contact-mediated manner (By similarity)", "gene_name": "VIM", "glycan_count": 4, "glycosylation_sites": [ { "position": 7, "type": "O-linked (GlcNAc) serine; alternate" }, { "position": 33, "type": "O-linked (GlcNAc) threonine" }, { "position": 34, "type": "O-linked (GlcNAc) serine; alternate" } ], "id": "P08670", "name": "Vimentin", "organism": "Homo sapiens", "uniprot_id": "P08670" }, { "function": "Pyruvate carboxylase catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second. Catalyzes in a tissue specific manner, the initial reactions of glucose (liver, kidney) and lipid (adipose tissue, liver, brain) synthesis from pyruvate", "gene_name": "PC", "glycan_count": 1, "glycosylation_sites": [], "id": "P11498", "name": "Pyruvate carboxylase", "organism": "Homo sapiens", "uniprot_id": "P11498" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "various", "name": "Long-chain fatty acid-CoA ligase", "organism": "", "uniprot_id": "" }, { "function": "Cleaves GlcNAc but not GalNAc from O-glycosylated proteins (PubMed:11148210, PubMed:11788610, PubMed:20673219, PubMed:22365600, PubMed:24088714, PubMed:28939839, PubMed:37962578). Deglycosylates a large and diverse number of proteins, such as CRYAB, ELK1, GSDMD, LMNB1 and TAB1 (PubMed:28939839, PubMed:37962578). Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrates but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro) (PubMed:20673219). Does not bind acetyl-CoA and does not have histone acetyltransferase activity (PubMed:24088714)", "gene_name": "OGA", "glycan_count": 3, "glycosylation_sites": [], "id": "O60502", "name": "OGA", "organism": "Homo sapiens", "uniprot_id": "O60502" }, { "function": "Mitochondrial protein responsible for thermogenic respiration, a specialized capacity of brown adipose tissue and beige fat that participates in non-shivering adaptive thermogenesis to temperature and diet variations and more generally to the regulation of energy balance (By similarity). Functions as a long-chain fatty acid/LCFA and proton symporter, simultaneously transporting one LCFA and one proton through the inner mitochondrial membrane (PubMed:24196960, PubMed:28781081). However, LCFAs remaining associated with the transporter via their hydrophobic tails, it results in an apparent transport of protons activated by LCFAs. Thereby, dissipates the mitochondrial proton gradient and converts the energy of substrate oxydation into heat instead of ATP. Regulates the production of reactive oxygen species/ROS by mitochondria (By similarity)", "gene_name": "UCP1", "glycan_count": 0, "glycosylation_sites": [], "id": "P25874", "name": "UCP1", "organism": "Homo sapiens", "uniprot_id": "P25874" }, { "function": "Ca(2+)-dependent receptor for myeloid cells that binds to carbohydrates on neutrophils and monocytes. Mediates the interaction of activated endothelial cells or platelets with leukocytes. The ligand recognized is sialyl-Lewis X. Mediates rapid rolling of leukocyte rolling over vascular surfaces during the initial steps in inflammation through interaction with SELPLG. Mediates cell-cell interactions and cell adhesion via the interaction with integrin alpha-IIb/beta3 (ITGA2B:ITGB3) and integrin alpha-V/beta-3 (ITGAV:ITGB3) (PubMed:37184585)", "gene_name": "SELP", "glycan_count": 8, "glycosylation_sites": [ { "position": 54, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 98, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 180, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 212, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 219, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 411, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 460, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 518, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 665, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 716, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 723, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 741, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P16109", "name": "CD62P (P-selectin)", "organism": "Homo sapiens", "uniprot_id": "P16109" }, { "function": "Functions as a cell surface receptor for TIMP1 and plays a role in the activation of cellular signaling cascades. Plays a role in the activation of ITGB1 and integrin signaling, leading to the activation of AKT, FAK/PTK2 and MAP kinases. Promotes cell survival, reorganization of the actin cytoskeleton, cell adhesion, spreading and migration, via its role in the activation of AKT and FAK/PTK2. Plays a role in VEGFA signaling via its role in regulating the internalization of KDR/VEGFR2. Plays a role in intracellular vesicular transport processes, and is required for normal trafficking of the PMEL luminal domain that is essential for the development and maturation of melanocytes. Plays a role in the adhesion of leukocytes onto endothelial cells via its role in the regulation of SELP trafficking. May play a role in mast cell degranulation in response to Ms4a2/FceRI stimulation, but not in mast cell degranulation in response to other stimuli", "gene_name": "CD63", "glycan_count": 111, "glycosylation_sites": [ { "position": 130, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 150, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 172, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08962", "name": "CD63", "organism": "Homo sapiens", "uniprot_id": "P08962" }, { "function": "Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions (PubMed:17580308, PubMed:19342684). Tyr-690 plays a critical role in TEM and is required for efficient trafficking of PECAM1 to and from the lateral border recycling compartment (LBRC) and is also essential for the LBRC membrane to be targeted around migrating leukocytes (PubMed:19342684). Trans-homophilic interaction may play a role in endothelial cell-cell adhesion via cell junctions (PubMed:27958302). Heterophilic interaction with CD177 plays a role in transendothelial migration of neutrophils (PubMed:17580308). Homophilic ligation of PECAM1 prevents macrophage-mediated phagocytosis of neighboring viable leukocytes by transmitting a detachment signal (PubMed:12110892). Promotes macrophage-mediated phagocytosis of apoptotic leukocytes by tethering them to the phagocytic cells; PECAM1-mediated detachment signal appears to be disabled in apoptotic leukocytes (PubMed:12110892). Modulates bradykinin receptor BDKRB2 activation (PubMed:18672896). Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in endothelial cells (PubMed:18672896). Induces susceptibility to atherosclerosis (By similarity)", "gene_name": "PECAM1", "glycan_count": 84, "glycosylation_sites": [ { "position": 52, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 84, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 151, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 301, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 320, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 344, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 356, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 453, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 551, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P16284", "name": "CD31 (PECAM-1)", "organism": "Homo sapiens", "uniprot_id": "P16284" }, { "function": "Integrin alpha-2/beta-1 is a receptor for laminin, collagen, collagen C-propeptides, fibronectin and E-cadherin. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen. It is responsible for adhesion of platelets and other cells to collagens, modulation of collagen and collagenase gene expression, force generation and organization of newly synthesized extracellular matrix", "gene_name": "ITGA2", "glycan_count": 76, "glycosylation_sites": [ { "position": 105, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 112, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 343, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 432, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 460, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 475, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 699, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1057, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1074, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1081, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P17301", "name": "CD49b (Integrin alpha-2)", "organism": "Homo sapiens", "uniprot_id": "P17301" }, { "function": "Key regulator of protein phosphatase 1C (PPP1C). Mediates binding to myosin. As part of the PPP1C complex, involved in dephosphorylation of PLK1. Capable of inhibiting HIF1AN-dependent suppression of HIF1A activity", "gene_name": "PPP1R12A", "glycan_count": 2, "glycosylation_sites": [], "id": "O14974", "name": "MYPT1", "organism": "Homo sapiens", "uniprot_id": "O14974" }, { "function": "Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway (PubMed:1378832). NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets", "gene_name": "NOS3", "glycan_count": 2, "glycosylation_sites": [], "id": "P29474", "name": "eNOS", "organism": "Homo sapiens", "uniprot_id": "P29474" }, { "function": "Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3' (PubMed:24940000, PubMed:25956029). Activates the transcription of growth-related genes (PubMed:24940000, PubMed:25956029). Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis (PubMed:24940000, PubMed:25956029). Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells (By similarity). Functions with TAF6L to activate target gene expression through RNA polymerase II pause release (By similarity). Positively regulates transcription of HNRNPA1, HNRNPA2 and PTBP1 which in turn regulate splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (PubMed:20010808)", "gene_name": "MYC", "glycan_count": 1, "glycosylation_sites": [ { "position": 73, "type": "O-linked (GlcNAc) threonine; alternate" } ], "id": "P01106", "name": "c-Myc", "organism": "Homo sapiens", "uniprot_id": "P01106" }, { "function": "Heparan sulfate basal lamina glycoprotein that plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ) and directs key events in postsynaptic differentiation. Component of the AGRN-LRP4 receptor complex that induces the phosphorylation and activation of MUSK. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Calcium ions are required for maximal AChR clustering. AGRN function in neurons is highly regulated by alternative splicing, glycan binding and proteolytic processing. Modulates calcium ion homeostasis in neurons, specifically by inducing an increase in cytoplasmic calcium ions. Functions differentially in the central nervous system (CNS) by inhibiting the alpha(3)-subtype of Na+/K+-ATPase and evoking depolarization at CNS synapses. This secreted isoform forms a bridge, after release from motor neurons, to basal lamina through binding laminin via the NtA domain", "gene_name": "AGRN", "glycan_count": 122, "glycosylation_sites": [ { "position": 135, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 250, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 777, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 932, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1835, "type": "O-linked (Fuc...) serine" } ], "id": "O00468", "name": "Agrin", "organism": "Homo sapiens", "uniprot_id": "O00468" }, { "function": "Cell surface protein involved in cell-cell-interactions, exocytosis of secretory granules and regulation of signal transmission. Function is isoform-specific. Alpha-type isoforms have a long N-terminus with six laminin G-like domains and play an important role in synaptic signal transmission. Alpha-type isoforms play a role in the regulation of calcium channel activity and Ca(2+)-triggered neurotransmitter release at synapses and at neuromuscular junctions. They play an important role in Ca(2+)-triggered exocytosis of secretory granules in pituitary gland. They may affect their functions at synapses and in endocrine cells via their interactions with proteins from the exocytotic machinery. Likewise, alpha-type isoforms play a role in regulating the activity of postsynaptic NMDA receptors, a subtype of glutamate-gated ion channels. Both alpha-type and beta-type isoforms may play a role in the formation or maintenance of synaptic junctions via their interactions (via the extracellular domains) with neuroligin family members, CBLN1 or CBLN2. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses. Alpha-type isoforms were first identified as receptors for alpha-latrotoxin from spider venom", "gene_name": "NRXN1", "glycan_count": 6, "glycosylation_sites": [ { "position": 125, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 190, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 790, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1223, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1355, "type": "O-linked (Xyl...) (heparan sulfate) serine" } ], "id": "Q9ULB1", "name": "Neurexin-3\u03b1", "organism": "Homo sapiens", "uniprot_id": "Q9ULB1" }, { "function": "Component of the FERRY complex (Five-subunit Endosomal Rab5 and RNA/ribosome intermediary) (PubMed:37267905, PubMed:37267906). The FERRY complex directly interacts with mRNAs and RAB5A, and functions as a RAB5A effector involved in the localization and the distribution of specific mRNAs most likely by mediating their endosomal transport. The complex recruits mRNAs and ribosomes to early endosomes through direct mRNA-interaction (PubMed:37267905). In the complex, PPP1R21 serves as a binding hub connecting all five complex subunits and mediating the binding to mRNA and early endosomes via RAB5A (PubMed:37267906). Putative regulator of protein phosphatase 1 (PP1) activity (PubMed:19389623). May play a role in the endosomal sorting process or in endosome maturation pathway (Probable) (PubMed:30520571)", "gene_name": "PPP1R21", "glycan_count": 4, "glycosylation_sites": [], "id": "Q6ZMI0", "name": "Pikachurin", "organism": "Homo sapiens", "uniprot_id": "Q6ZMI0" }, { "function": "Acts as a scavenger receptor for acetylated low density lipoprotein. Binds to both Gram-positive and Gram-negative bacteria and may play a role in defense against bacterial infection. When inhibited in endothelial tube formation assays, there is a marked decrease in cell-cell interactions, suggesting a role in angiogenesis. Involved in the delivery of newly synthesized CHID1/SI-CLP from the biosynthetic compartment to the endosomal/lysosomal system", "gene_name": "STAB1", "glycan_count": 61, "glycosylation_sites": [ { "position": 133, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 286, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 312, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 413, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 606, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 673, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 712, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 745, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 816, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1087, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1096, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1170, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1178, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1222, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1274, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1378, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1471, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1626, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1727, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2107, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2222, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2261, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2290, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2334, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2347, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2379, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2393, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2400, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2424, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NY15", "name": "Celsr3", "organism": "Homo sapiens", "uniprot_id": "Q9NY15" }, { "function": "Protein adapter that acts as an essential executor of PIWIL4-piRNA pathway directed transposon DNA methylation and silencing in the male embryonic germ cells (PubMed:38359823). Recruited to young transposons, which are specifically marked with histone H3 trimethylated at both 'Lys-4' and 'Lys-9' (H3K4me3K9me3), via its association with SPIN1 chromatin reader, and associates with the de novo DNA methylation machinery and repressive chromatin remodeling complexes (By similarity). Following this, PIWIL4 engages with nascent transposable element transcript to direct piRNA-directed DNA methylation. Not required for piRNA biosynthesis (By similarity)", "gene_name": "SPOCD1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6ZMY3", "name": "GPR179", "organism": "Homo sapiens", "uniprot_id": "Q6ZMY3" }, { "function": "Component of a complex of multiple actin cross-linking proteins. Involved in the control of myofibril assembly and stability at the Z lines in muscle cells", "gene_name": "MYOT", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UBF9", "name": "\u03b1-dystrobrevin", "organism": "Homo sapiens", "uniprot_id": "Q9UBF9" }, { "function": "Interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. Could also bind muscle proteins such as actin to membrane complexes in muscle. May be involved not only in the filaments network, but also in the regulation of their dynamics. Structural component of muscle. Isoform 9 plays a major role in the maintenance of myofiber integrity", "gene_name": "PLEC", "glycan_count": 7, "glycosylation_sites": [], "id": "Q15149", "name": "Plectin", "organism": "Homo sapiens", "uniprot_id": "Q15149" }, { "function": "Membrane-cytoskeleton linker. May participate in the maintenance/targeting of ion channels and cell adhesion molecules at the nodes of Ranvier and axonal initial segments (PubMed:7836469). In skeletal muscle, required for costamere localization of DMD and betaDAG1 (By similarity). Regulates KCNA1 channel activity in function of dietary Mg(2+) levels, and thereby contributes to the regulation of renal Mg(2+) reabsorption (PubMed:23903368). Required for intracellular adhesion and junctional conductance in myocytes, potentially via stabilization of GJA1/CX43 protein abundance and promotion of PKP2, GJA1/CX43, and SCN5A/Nav1.5 localization to cell-cell junctions (By similarity)", "gene_name": "ANK3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q12955", "name": "Ankyrin-B", "organism": "Homo sapiens", "uniprot_id": "Q12955" }, { "function": "Serine/threonine-protein kinase (PubMed:23666762). Involved in cell polarity and microtubule dynamics regulation. Phosphorylates CRTC2/TORC2, DCX, HDAC7, KIF13B, MAP2, MAP4 and RAB11FIP2. Phosphorylates the microtubule-associated protein MAPT/TAU (PubMed:23666762). Plays a key role in cell polarity by phosphorylating the microtubule-associated proteins MAP2, MAP4 and MAPT/TAU at KXGS motifs, causing detachment from microtubules, and their disassembly. Regulates epithelial cell polarity by phosphorylating RAB11FIP2. Involved in the regulation of neuronal migration through its dual activities in regulating cellular polarity and microtubule dynamics, possibly by phosphorylating and regulating DCX. Regulates axogenesis by phosphorylating KIF13B, promoting interaction between KIF13B and 14-3-3 and inhibiting microtubule-dependent accumulation of KIF13B. Also required for neurite outgrowth and establishment of neuronal polarity. Regulates localization and activity of some histone deacetylases by mediating phosphorylation of HDAC7, promoting subsequent interaction between HDAC7 and 14-3-3 and export from the nucleus. Also acts as a positive regulator of the Wnt signaling pathway, probably by mediating phosphorylation of dishevelled proteins (DVL1, DVL2 and/or DVL3). Modulates the developmental decision to build a columnar versus a hepatic epithelial cell apparently by promoting a switch from a direct to a transcytotic mode of apical protein delivery. Essential for the asymmetric development of membrane domains of polarized epithelial cells", "gene_name": "MARK2", "glycan_count": 4, "glycosylation_sites": [], "id": "Q7KZI7", "name": "MARK2 (Par1b)", "organism": "Homo sapiens", "uniprot_id": "Q7KZI7" }, { "function": "Plays an important role in caveolae formation and organization. Essential for the formation of caveolae in all tissues (PubMed:18056712, PubMed:18191225, PubMed:19726876). Core component of the CAVIN complex which is essential for recruitment of the complex to the caveolae in presence of calveolin-1 (CAV1). Essential for normal oligomerization of CAV1. Promotes ribosomal transcriptional activity in response to metabolic challenges in the adipocytes and plays an important role in the formation of the ribosomal transcriptional loop. Dissociates transcription complexes paused by DNA-bound TTF1, thereby releasing both RNA polymerase I and pre-RNA from the template (By similarity) (PubMed:18056712, PubMed:18191225, PubMed:19726876). The caveolae biogenesis pathway is required for the secretion of proteins such as GASK1A (By similarity)", "gene_name": "CAVIN1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q6NZI2", "name": "Cavin-1", "organism": "Homo sapiens", "uniprot_id": "Q6NZI2" }, { "function": "Dipeptidyl carboxypeptidase that removes dipeptides from the C-terminus of a variety of circulating hormones, such as angiotensin I, bradykinin or enkephalins, thereby playing a key role in the regulation of blood pressure, electrolyte homeostasis or synaptic plasticity (PubMed:15615692, PubMed:20826823, PubMed:2558109, PubMed:4322742, PubMed:7523412, PubMed:7683654). Composed of two similar catalytic domains, each possessing a functional active site, with different selectivity for substrates (PubMed:10913258, PubMed:1320019, PubMed:1851160, PubMed:19773553, PubMed:7683654, PubMed:7876104). Plays a major role in the angiotensin-renin system that regulates blood pressure and sodium retention by the kidney by converting angiotensin I to angiotensin II, resulting in an increase of the vasoconstrictor activity of angiotensin (PubMed:11432860, PubMed:1851160, PubMed:19773553, PubMed:23056909, PubMed:4322742). Also able to inactivate bradykinin, a potent vasodilator, and therefore enhance the blood pressure response (PubMed:15615692, PubMed:2558109, PubMed:4322742, PubMed:6055465, PubMed:6270633, PubMed:7683654). Acts as a regulator of synaptic transmission by mediating cleavage of neuropeptide hormones, such as substance P, neurotensin or enkephalins (PubMed:15615692, PubMed:6208535, PubMed:6270633, PubMed:656131). Catalyzes degradation of different enkephalin neuropeptides (Met-enkephalin, Leu-enkephalin, Met-enkephalin-Arg-Phe and possibly Met-enkephalin-Arg-Gly-Leu) (PubMed:2982830, PubMed:6270633, PubMed:656131). Acts as a regulator of synaptic plasticity in the nucleus accumbens of the brain by mediating cleavage of Met-enkephalin-Arg-Phe, a strong ligand of Mu-type opioid receptor OPRM1, into Met-enkephalin (By similarity). Met-enkephalin-Arg-Phe cleavage by ACE decreases activation of OPRM1, leading to long-term synaptic potentiation of glutamate release (By similarity). Also acts as a regulator of hematopoietic stem cell differentiation by mediating degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) (PubMed:26403559, PubMed:7876104, PubMed:8257427, PubMed:8609242). Acts as a regulator of cannabinoid signaling pathway by mediating degradation of hemopressin, an antagonist peptide of the cannabinoid receptor CNR1 (PubMed:18077343). Involved in amyloid-beta metabolism by catalyzing degradation of Amyloid-beta protein 40 and Amyloid-beta protein 42 peptides, thereby preventing plaque formation (PubMed:11604391, PubMed:16154999, PubMed:19773553). Catalyzes cleavage of cholecystokinin (maturation of Cholecystokinin-8 and Cholecystokinin-5) and Gonadoliberin-1 (both maturation and degradation) hormones (PubMed:10336644, PubMed:2983326, PubMed:7683654, PubMed:9371719). Degradation of hemoregulatory peptide N-acetyl-SDKP (AcSDKP) and amyloid-beta proteins is mediated by the N-terminal catalytic domain, while angiotensin I and cholecystokinin cleavage is mediated by the C-terminal catalytic region (PubMed:10336644, PubMed:19773553, PubMed:7876104)", "gene_name": "ACE", "glycan_count": 124, "glycosylation_sites": [ { "position": 38, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 54, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 74, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 111, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 146, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 160, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 318, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 445, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 509, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 677, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 695, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 714, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 760, "type": "N-linked (GlcNAc...) asparagine; partial" }, { "position": 942, "type": "N-linked (GlcNAc...) asparagine; partial" }, { "position": 1191, "type": "N-linked (GlcNAc...) asparagine; partial" }, { "position": 103, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 121, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 140, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 368, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 617, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P12821", "name": "Angiotensin I-converting enzyme (ACE)", "organism": "Homo sapiens", "uniprot_id": "P12821" }, { "function": "Catalyzes the dehydration of trans-3-hydroxy-L-proline to Delta(1)-pyrroline-2-carboxylate (Pyr2C). May be required to degrade trans-3-hydroxy-L-proline from the diet and originating from the degradation of proteins such as collagen-IV that contain it", "gene_name": "L3HYPDH", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96EM0", "name": "O-GlcNAcase (OGA)", "organism": "Homo sapiens", "uniprot_id": "Q96EM0" }, { "function": "Pseudokinase that plays a key role in TNF-induced necroptosis, a programmed cell death process (PubMed:22265413, PubMed:22265414, PubMed:22421439, PubMed:24316671). Does not have protein kinase activity (PubMed:22265413, PubMed:22265414, PubMed:22421439, PubMed:24316671). Activated following phosphorylation by RIPK3, leading to homotrimerization, localization to the plasma membrane and execution of programmed necrosis characterized by calcium influx and plasma membrane damage (PubMed:22265413, PubMed:22265414, PubMed:22421439, PubMed:24316671). In addition to TNF-induced necroptosis, necroptosis can also take place in the nucleus in response to orthomyxoviruses infection: following activation by ZBP1, MLKL is phosphorylated by RIPK3 in the nucleus, triggering disruption of the nuclear envelope and leakage of cellular DNA into the cytosol.following ZBP1 activation, which senses double-stranded Z-RNA structures, nuclear RIPK3 catalyzes phosphorylation and activation of MLKL, promoting disruption of the nuclear envelope and leakage of cellular DNA into the cytosol (By similarity). Binds to highly phosphorylated inositol phosphates such as inositolhexakisphosphate (InsP6) which is essential for its necroptotic function (PubMed:29883610)", "gene_name": "MLKL", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8NB16", "name": "Mixed lineage kinase domain-like pseudokinase (MLKL)", "organism": "Homo sapiens", "uniprot_id": "Q8NB16" }, { "function": "Serine/threonine-protein kinase that activates necroptosis and apoptosis, two parallel forms of cell death (PubMed:19524512, PubMed:19524513, PubMed:22265413, PubMed:22265414, PubMed:22421439, PubMed:29883609, PubMed:32657447). Necroptosis, a programmed cell death process in response to death-inducing TNF-alpha family members, is triggered by RIPK3 following activation by ZBP1 (PubMed:19524512, PubMed:19524513, PubMed:22265413, PubMed:22265414, PubMed:22421439, PubMed:29883609, PubMed:32298652). Activated RIPK3 forms a necrosis-inducing complex and mediates phosphorylation of MLKL, promoting MLKL localization to the plasma membrane and execution of programmed necrosis characterized by calcium influx and plasma membrane damage (PubMed:19524512, PubMed:19524513, PubMed:22265413, PubMed:22265414, PubMed:22421439, PubMed:25316792, PubMed:29883609). In addition to TNF-induced necroptosis, necroptosis can also take place in the nucleus in response to orthomyxoviruses infection: following ZBP1 activation, which senses double-stranded Z-RNA structures, nuclear RIPK3 catalyzes phosphorylation and activation of MLKL, promoting disruption of the nuclear envelope and leakage of cellular DNA into the cytosol (By similarity). Also regulates apoptosis: apoptosis depends on RIPK1, FADD and CASP8, and is independent of MLKL and RIPK3 kinase activity (By similarity). Phosphorylates RIPK1: RIPK1 and RIPK3 undergo reciprocal auto- and trans-phosphorylation (PubMed:19524513). In some cell types, also able to restrict viral replication by promoting cell death-independent responses (By similarity). In response to Zika virus infection in neurons, promotes a cell death-independent pathway that restricts viral replication: together with ZBP1, promotes a death-independent transcriptional program that modifies the cellular metabolism via up-regulation expression of the enzyme ACOD1/IRG1 and production of the metabolite itaconate (By similarity). Itaconate inhibits the activity of succinate dehydrogenase, generating a metabolic state in neurons that suppresses replication of viral genomes (By similarity). RIPK3 binds to and enhances the activity of three metabolic enzymes: GLUL, GLUD1, and PYGL (PubMed:19498109). These metabolic enzymes may eventually stimulate the tricarboxylic acid cycle and oxidative phosphorylation, which could result in enhanced ROS production (PubMed:19498109)", "gene_name": "RIPK3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y572", "name": "Receptor-interacting serine/threonine-protein kinase 3 (RIPK3)", "organism": "Homo sapiens", "uniprot_id": "Q9Y572" }, { "function": "Multifunctional transcription factor in endoplasmic reticulum (ER) stress response (PubMed:15322075, PubMed:15775988, PubMed:19672300). Plays an essential role in the response to a wide variety of cell stresses and induces cell cycle arrest and apoptosis in response to ER stress (PubMed:15322075, PubMed:15775988). Plays a dual role both as an inhibitor of CCAAT/enhancer-binding protein (C/EBP) function and as an activator of other genes (By similarity). Acts as a dominant-negative regulator of C/EBP-induced transcription: dimerizes with members of the C/EBP family, impairs their association with C/EBP binding sites in the promoter regions, and inhibits the expression of C/EBP regulated genes (By similarity). Positively regulates the transcription of TRIB3, IL6, IL8, IL23, TNFRSF10B/DR5, PPP1R15A/GADD34, BBC3/PUMA, BCL2L11/BIM and ERO1L (PubMed:15775988, PubMed:17709599, PubMed:20876114, PubMed:22761832). Negatively regulates; expression of BCL2 and MYOD1, ATF4-dependent transcriptional activation of asparagine synthetase (ASNS), CEBPA-dependent transcriptional activation of hepcidin (HAMP) and CEBPB-mediated expression of peroxisome proliferator-activated receptor gamma (PPARG) (PubMed:18940792, PubMed:19672300, PubMed:20829347). Together with ATF4, mediates ER-mediated cell death by promoting expression of genes involved in cellular amino acid metabolic processes, mRNA translation and the unfolded protein response (UPR) in response to ER stress (By similarity). Inhibits the canonical Wnt signaling pathway by binding to TCF7L2/TCF4, impairing its DNA-binding properties and repressing its transcriptional activity (PubMed:16434966). Plays a regulatory role in the inflammatory response through the induction of caspase-11 (CASP4/CASP11) which induces the activation of caspase-1 (CASP1) and both these caspases increase the activation of pro-IL1B to mature IL1B which is involved in the inflammatory response (By similarity). Acts as a major regulator of postnatal neovascularization through regulation of endothelial nitric oxide synthase (NOS3)-related signaling (By similarity)", "gene_name": "DDIT3", "glycan_count": 1, "glycosylation_sites": [], "id": "P35638", "name": "CCAAT\u2013enhancer-binding protein homologous protein (CHOP)", "organism": "Homo sapiens", "uniprot_id": "P35638" }, { "function": "Molecular adapter required for selective macroautophagy (aggrephagy) by acting as a bridge between polyubiquitinated proteins and autophagosomes (PubMed:15340068, PubMed:15953362, PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22017874, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:33509017, PubMed:34471133, PubMed:34893540, PubMed:35831301, PubMed:37306101, PubMed:37802024). Promotes the recruitment of ubiquitinated cargo proteins to autophagosomes via multiple domains that bridge proteins and organelles in different steps (PubMed:16286508, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:29343546, PubMed:29507397, PubMed:34893540, PubMed:37802024). SQSTM1 first mediates the assembly and removal of ubiquitinated proteins by undergoing liquid-liquid phase separation upon binding to ubiquitinated proteins via its UBA domain, leading to the formation of insoluble cytoplasmic inclusions, known as p62 bodies (PubMed:15911346, PubMed:20168092, PubMed:22017874, PubMed:24128730, PubMed:29343546, PubMed:29507397, PubMed:31857589, PubMed:37802024). SQSTM1 then interacts with ATG8 family proteins on autophagosomes via its LIR motif, leading to p62 body recruitment to autophagosomes, followed by autophagic clearance of ubiquitinated proteins (PubMed:16286508, PubMed:17580304, PubMed:20168092, PubMed:22622177, PubMed:24128730, PubMed:28404643, PubMed:37802024). SQSTM1 is itself degraded along with its ubiquitinated cargos (PubMed:16286508, PubMed:17580304, PubMed:37802024). Also required to recruit ubiquitinated proteins to PML bodies in the nucleus (PubMed:20168092). Also involved in autophagy of peroxisomes (pexophagy) in response to reactive oxygen species (ROS) by acting as a bridge between ubiquitinated PEX5 receptor and autophagosomes (PubMed:26344566). Acts as an activator of the NFE2L2/NRF2 pathway via interaction with KEAP1: interaction inactivates the BCR(KEAP1) complex by sequestering the complex in inclusion bodies, promoting nuclear accumulation of NFE2L2/NRF2 and subsequent expression of cytoprotective genes (PubMed:20452972, PubMed:28380357, PubMed:33393215, PubMed:37306101). Promotes relocalization of 'Lys-63'-linked ubiquitinated STING1 to autophagosomes (PubMed:29496741). Involved in endosome organization by retaining vesicles in the perinuclear cloud: following ubiquitination by RNF26, attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport (PubMed:27368102, PubMed:33472082). Sequesters tensin TNS2 into cytoplasmic puncta, promoting TNS2 ubiquitination and proteasomal degradation (PubMed:25101860). May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1 (PubMed:10356400, PubMed:10747026, PubMed:11244088, PubMed:12471037, PubMed:16079148, PubMed:19931284). May play a role in titin/TTN downstream signaling in muscle cells (PubMed:15802564). Adapter that mediates the interaction between TRAF6 and CYLD (By similarity)", "gene_name": "SQSTM1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q13501", "name": "p62/SQSTM1", "organism": "Homo sapiens", "uniprot_id": "Q13501" }, { "function": "Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C-terminal phosphorylation", "gene_name": "H2AX", "glycan_count": 1, "glycosylation_sites": [], "id": "P16104", "name": "\u03b3H2AX", "organism": "Homo sapiens", "uniprot_id": "P16104" }, { "function": "Regulatory component of the cyclin D1-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition (PubMed:1827756, PubMed:1833066, PubMed:19412162, PubMed:33854235, PubMed:8114739, PubMed:8302605). Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase (PubMed:1827756, PubMed:1833066, PubMed:19412162, PubMed:8114739, PubMed:8302605). Hypophosphorylates RB1 in early G(1) phase (PubMed:1827756, PubMed:1833066, PubMed:19412162, PubMed:8114739, PubMed:8302605). Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals (PubMed:1827756, PubMed:1833066, PubMed:19412162, PubMed:8302605). Also a substrate for SMAD3, phosphorylating SMAD3 in a cell-cycle-dependent manner and repressing its transcriptional activity (PubMed:15241418). Component of the ternary complex, cyclin D1/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex (PubMed:9106657). Exhibits transcriptional corepressor activity with INSM1 on the NEUROD1 and INS promoters in a cell cycle-independent manner (PubMed:16569215, PubMed:18417529)", "gene_name": "CCND1", "glycan_count": 1, "glycosylation_sites": [], "id": "P24385", "name": "Cyclin D1", "organism": "Homo sapiens", "uniprot_id": "P24385" }, { "function": "Protein that associates with the surface of mitotic chromosomes and acts both as a chromosome repellent during early mitosis and chromosome attractant during late mitosis (PubMed:27362226, PubMed:32879492, PubMed:35513709, PubMed:39153474). Required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly (PubMed:27362226). During early mitosis, relocalizes from nucleoli to the chromosome surface where it forms extended brush structures that cover a substantial fraction of the chromosome surface (PubMed:27362226). The MKI67 brush structure prevents chromosomes from collapsing into a single chromatin mass by forming a steric and electrostatic charge barrier: the protein has a high net electrical charge and acts as a surfactant, dispersing chromosomes and enabling independent chromosome motility (PubMed:27362226). During mitotic anaphase, the MKI67 brush structure collapses and MKI67 switches from a chromosome repellent to a chromosome attractant to promote chromosome clustering and facilitate the exclusion of large cytoplasmic particles from the future nuclear space (PubMed:32879492, PubMed:39153474). Mechanistically, dephosphorylation during mitotic exit and simultaneous exposure of a conserved basic patch induce the RNA-dependent formation of a liquid-like condensed phase on the chromosome surface, promoting coalescence of neighboring chromosome surfaces and clustering of chromosomes (PubMed:39153474). Binds premature ribosomal RNAs during anaphase; promoting liquid-liquid phase separation (PubMed:28935370, PubMed:39153474). Binds DNA, with a preference for supercoiled DNA and AT-rich DNA (PubMed:10878551). Does not contribute to the internal structure of mitotic chromosomes (By similarity). May play a role in chromatin organization; it is however unclear whether it plays a direct role in chromatin organization or whether it is an indirect consequence of its function in mitotic chromosome (PubMed:24867636)", "gene_name": "MKI67", "glycan_count": 1, "glycosylation_sites": [], "id": "P46013", "name": "Ki67", "organism": "Homo sapiens", "uniprot_id": "P46013" }, { "function": "Inactive protein kinase which acts as a regulator of the integrated stress response (ISR), a process for adaptation to various stress (PubMed:15775988, PubMed:15781252). Inhibits the transcriptional activity of DDIT3/CHOP and is involved in DDIT3/CHOP-dependent cell death during ER stress (PubMed:15775988, PubMed:15781252). May play a role in programmed neuronal cell death but does not appear to affect non-neuronal cells (PubMed:15775988, PubMed:15781252). Acts as a negative feedback regulator of the ATF4-dependent transcription during the ISR: while TRIB3 expression is promoted by ATF4, TRIB3 protein interacts with ATF4 and inhibits ATF4 transcription activity (By similarity). Disrupts insulin signaling by binding directly to Akt kinases and blocking their activation (By similarity). May bind directly to and mask the 'Thr-308' phosphorylation site in AKT1 (By similarity). Interacts with the NF-kappa-B transactivator p65 RELA and inhibits its phosphorylation and thus its transcriptional activation activity (PubMed:12736262). Interacts with MAPK kinases and regulates activation of MAP kinases (PubMed:15299019). Can inhibit APOBEC3A editing of nuclear DNA (PubMed:22977230)", "gene_name": "TRIB3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96RU7", "name": "TRIB3", "organism": "Homo sapiens", "uniprot_id": "Q96RU7" }, { "function": "Stimulates glucose uptake in differentiated adipocytes via the induction of glucose transporter SLC2A1/GLUT1 expression (but not SLC2A4/GLUT4 expression). Activity requires the presence of KLB. Regulates systemic glucose homeostasis and insulin sensitivity", "gene_name": "FGF21", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NSA1", "name": "FGF21", "organism": "Homo sapiens", "uniprot_id": "Q9NSA1" }, { "function": "Transforming growth factor beta-1 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains, which constitute the regulatory and active subunit of TGF-beta-1, respectively", "gene_name": "TGFB1", "glycan_count": 17, "glycosylation_sites": [ { "position": 82, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 136, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 176, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01137", "name": "TGF-\u03b21", "organism": "Homo sapiens", "uniprot_id": "P01137" }, { "function": "Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen", "gene_name": "COL4A1", "glycan_count": 2, "glycosylation_sites": [ { "position": 126, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P02462", "name": "Collagen type IV", "organism": "Homo sapiens", "uniprot_id": "P02462" }, { "function": "Type I collagen is a member of group I collagen (fibrillar forming collagen)", "gene_name": "COL1A1", "glycan_count": 21, "glycosylation_sites": [ { "position": 265, "type": "O-linked (Gal...) hydroxylysine; alternate" }, { "position": 1108, "type": "O-linked (Gal...) hydroxylysine; alternate" }, { "position": 1365, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P02452", "name": "Collagen type I", "organism": "Homo sapiens", "uniprot_id": "P02452" }, { "function": "Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin (PubMed:3024962, PubMed:3593230, PubMed:3900070, PubMed:7989369). Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape (PubMed:3024962, PubMed:3593230, PubMed:3900070, PubMed:7989369). Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization (By similarity). Participates in the regulation of type I collagen deposition by osteoblasts (By similarity). Acts as a ligand for the LILRB4 receptor, inhibiting FCGR1A/CD64-mediated monocyte activation (PubMed:34089617)", "gene_name": "FN1", "glycan_count": 275, "glycosylation_sites": [ { "position": 279, "type": "O-linked (GalNAc...) threonine" }, { "position": 430, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 528, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 542, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 877, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1007, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 1244, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2199, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P02751", "name": "Fibronectin", "organism": "Homo sapiens", "uniprot_id": "P02751" }, { "function": "Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), EIF2B, CTNNB1/beta-catenin, APC, AXIN1, DPYSL2/CRMP2, JUN, NFATC1/NFATC, MAPT/TAU and MACF1 (PubMed:11430833, PubMed:12554650, PubMed:14690523, PubMed:16484495, PubMed:1846781, PubMed:20937854, PubMed:9072970). Requires primed phosphorylation of the majority of its substrates (PubMed:11430833, PubMed:16484495). In skeletal muscle, contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis (PubMed:8397507). May also mediate the development of insulin resistance by regulating activation of transcription factors (PubMed:8397507). Regulates protein synthesis by controlling the activity of initiation factor 2B (EIF2BE/EIF2B5) in the same manner as glycogen synthase (PubMed:8397507). In Wnt signaling, GSK3B forms a multimeric complex with APC, AXIN1 and CTNNB1/beta-catenin and phosphorylates the N-terminus of CTNNB1 leading to its degradation mediated by ubiquitin/proteasomes (PubMed:12554650). Phosphorylates JUN at sites proximal to its DNA-binding domain, thereby reducing its affinity for DNA (PubMed:1846781). Phosphorylates NFATC1/NFATC on conserved serine residues promoting NFATC1/NFATC nuclear export, shutting off NFATC1/NFATC gene regulation, and thereby opposing the action of calcineurin (PubMed:9072970). Phosphorylates MAPT/TAU on 'Thr-548', decreasing significantly MAPT/TAU ability to bind and stabilize microtubules (PubMed:14690523). MAPT/TAU is the principal component of neurofibrillary tangles in Alzheimer disease (PubMed:14690523). Plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (PubMed:20937854). Phosphorylates MACF1, inhibiting its binding to microtubules which is critical for its role in bulge stem cell migration and skin wound repair (By similarity). Probably regulates NF-kappa-B (NFKB1) at the transcriptional level and is required for the NF-kappa-B-mediated anti-apoptotic response to TNF-alpha (TNF/TNFA) (By similarity). Negatively regulates replication in pancreatic beta-cells, resulting in apoptosis, loss of beta-cells and diabetes (By similarity). Through phosphorylation of the anti-apoptotic protein MCL1, may control cell apoptosis in response to growth factors deprivation (By similarity). Phosphorylates MUC1 in breast cancer cells, decreasing the interaction of MUC1 with CTNNB1/beta-catenin (PubMed:9819408). Is necessary for the establishment of neuronal polarity and axon outgrowth (PubMed:20067585). Phosphorylates MARK2, leading to inhibition of its activity (By similarity). Phosphorylates SIK1 at 'Thr-182', leading to sustainment of its activity (PubMed:18348280). Phosphorylates ZC3HAV1 which enhances its antiviral activity (PubMed:22514281). Phosphorylates SNAI1, leading to its ubiquitination and proteasomal degradation (PubMed:15448698, PubMed:15647282, PubMed:25827072, PubMed:29059170). Phosphorylates SFPQ at 'Thr-687' upon T-cell activation (PubMed:20932480). Phosphorylates NR1D1 st 'Ser-55' and 'Ser-59' and stabilizes it by protecting it from proteasomal degradation. Regulates the circadian clock via phosphorylation of the major clock components including BMAL1, CLOCK and PER2 (PubMed:19946213, PubMed:28903391). Phosphorylates FBXL2 at 'Thr-404' and primes it for ubiquitination by the SCF(FBXO3) complex and proteasomal degradation (By similarity). Phosphorylates CLOCK AT 'Ser-427' and targets it for proteasomal degradation (PubMed:19946213). Phosphorylates BMAL1 at 'Ser-17' and 'Ser-21' and primes it for ubiquitination and proteasomal degradation (PubMed:28903391). Phosphorylates OGT at 'Ser-3' or 'Ser-4' which positively regulates its activity. Phosphorylates MYCN in neuroblastoma cells which may promote its degradation (PubMed:24391509). Regulates the circadian rhythmicity of hippocampal long-term potentiation and BMAL1 and PER2 expression (By similarity). Acts as a regulator of autophagy by mediating phosphorylation of KAT5/TIP60 under starvation conditions, activating KAT5/TIP60 acetyltransferase activity and promoting acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer (PubMed:30704899). Negatively regulates extrinsic apoptotic signaling pathway via death domain receptors. Promotes the formation of an anti-apoptotic complex, made of DDX3X, BRIC2 and GSK3B, at death receptors, including TNFRSF10B. The anti-apoptotic function is most effective with weak apoptotic signals and can be overcome by stronger stimulation (PubMed:18846110). Phosphorylates E2F1, promoting the interaction between E2F1 and USP11, stabilizing E2F1 and promoting its activity (PubMed:17050006, PubMed:28992046). Phosphorylates mTORC2 complex component RICTOR at 'Ser-1235' in response to endoplasmic stress, inhibiting mTORC2 (PubMed:21343617). Phosphorylates mTORC2 complex component RICTOR at 'Thr-1695' which facilitates FBXW7-mediated ubiquitination and subsequent degradation of RICTOR (PubMed:25897075). Phosphorylates FXR1, promoting FXR1 ubiquitination by the SCF(FBXO4) complex and FXR1 degradation by the proteasome (By similarity). Phosphorylates interleukin-22 receptor subunit IL22RA1, preventing its proteasomal degradation (By similarity)", "gene_name": "GSK3B", "glycan_count": 1, "glycosylation_sites": [], "id": "P49841", "name": "GSK-3\u03b2", "organism": "Homo sapiens", "uniprot_id": "P49841" }, { "function": "NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and RelB-p50 complexes are transcriptional activators. The NF-kappa-B p50-p50 homodimer is a transcriptional repressor, but can act as a transcriptional activator when associated with BCL3. NFKB1 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p105 and generation of p50 by a cotranslational processing. The proteasome-mediated process ensures the production of both p50 and p105 and preserves their independent function, although processing of NFKB1/p105 also appears to occur post-translationally. p50 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. In a complex with MAP3K8, NFKB1/p105 represses MAP3K8-induced MAPK signaling; active MAP3K8 is released by proteasome-dependent degradation of NFKB1/p105", "gene_name": "NFKB1", "glycan_count": 1, "glycosylation_sites": [], "id": "P19838", "name": "NF-\u03baB", "organism": "Homo sapiens", "uniprot_id": "P19838" }, { "function": "Component of the BLOC-3 complex, a complex that acts as a guanine exchange factor (GEF) for RAB32 and RAB38, promotes the exchange of GDP to GTP, converting them from an inactive GDP-bound form into an active GTP-bound form. The BLOC-3 complex plays an important role in the control of melanin production and melanosome biogenesis and promotes the membrane localization of RAB32 and RAB38 (PubMed:23084991)", "gene_name": "HPS4", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NQG7", "name": "SIDT1", "organism": "Homo sapiens", "uniprot_id": "Q9NQG7" }, { "function": "Mediates homophilic cell-cell adhesion (By similarity). Minor component of the myelin sheath. May be involved in completion and/or maintenance of the myelin sheath and in cell-cell communication", "gene_name": "MOG", "glycan_count": 0, "glycosylation_sites": [ { "position": 60, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q16653", "name": "Myelin oligodendrocyte glycoprotein (MOG)", "organism": "Homo sapiens", "uniprot_id": "Q16653" }, { "function": "B-lymphocyte-specific membrane protein that plays a role in the regulation of cellular calcium influx necessary for the development, differentiation, and activation of B-lymphocytes (PubMed:12920111, PubMed:3925015, PubMed:7684739). Functions as a store-operated calcium (SOC) channel component promoting calcium influx after activation by the B-cell receptor/BCR (PubMed:12920111, PubMed:18474602, PubMed:7684739)", "gene_name": "MS4A1", "glycan_count": 4, "glycosylation_sites": [], "id": "P11836", "name": "CD20", "organism": "Homo sapiens", "uniprot_id": "P11836" }, { "function": "Could play a role in phagocytic activities of tissue macrophages, both in intracellular lysosomal metabolism and extracellular cell-cell and cell-pathogen interactions. Binds to tissue- and organ-specific lectins or selectins, allowing homing of macrophage subsets to particular sites. Rapid recirculation of CD68 from endosomes and lysosomes to the plasma membrane may allow macrophages to crawl over selectin-bearing substrates or other cells", "gene_name": "CD68", "glycan_count": 63, "glycosylation_sites": [ { "position": 88, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 96, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 118, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 126, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 164, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 199, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 246, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 261, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 279, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P34810", "name": "CD68", "organism": "Homo sapiens", "uniprot_id": "P34810" }, { "function": "NADPH oxidase that catalyzes the generation of superoxide from molecular oxygen utilizing NADPH as an electron donor", "gene_name": "NOX1", "glycan_count": 1, "glycosylation_sites": [ { "position": 162, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 236, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y5S8", "name": "PIGA (Phosphatidylinositol glycan biosynthesis class A)", "organism": "Homo sapiens", "uniprot_id": "Q9Y5S8" }, { "function": "Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (PubMed:2294010, PubMed:23769672, PubMed:23990668, PubMed:28332555). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the EIF2AK3/PERK and ERN1/IRE1-mediated unfolded protein response (UPR) (PubMed:11907036, PubMed:1550958, PubMed:19538957, PubMed:36739529). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1 (By similarity). Also binds and inactivates EIF2AK3/PERK in unstressed cells (PubMed:11907036). Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1 and EIF2AK3/PERK, allowing their homodimerization and subsequent activation (PubMed:11907036). Plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). May function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. Appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. May also play a role in apoptosis and cell proliferation (PubMed:26045166)", "gene_name": "HSPA5", "glycan_count": 2, "glycosylation_sites": [], "id": "P11021", "name": "BiP", "organism": "Homo sapiens", "uniprot_id": "P11021" }, { "function": "Has a pivotal role in cytoprotective cellular mechanisms triggered by oxygen deprivation. Promotes HSPA5/BiP-mediated ATP nucleotide exchange and thereby activates the unfolded protein response (UPR) pathway in the presence of endoplasmic reticulum stress (By similarity). May play a role as a molecular chaperone and participate in protein folding", "gene_name": "HYOU1", "glycan_count": 145, "glycosylation_sites": [ { "position": 155, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 222, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 515, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 596, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 830, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 862, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 869, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 922, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 931, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y4L1", "name": "HYOU1", "organism": "Homo sapiens", "uniprot_id": "Q9Y4L1" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q62266 (mouse)", "name": "Agrin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q62165 (mouse)", "name": "Alpha-dystroglycan (\u03b1-DG)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9QZQ8 (mouse)", "name": "MuSK", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q60673 (mouse)", "name": "Laminin-\u03b12", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P46937 (mouse)", "name": "Yap", "organism": "", "uniprot_id": "" }, { "function": "Member of the granin protein family that regulates the biogenesis of secretory granules (PubMed:19357184). Acts as a sorting receptor for intragranular proteins including chromogranin A/CHGA (By similarity). May also play a role in angiogenesis. Promotes endothelial proliferation, migration and tube formation through MEK/ERK signaling pathway (PubMed:29154827)", "gene_name": "SCG3", "glycan_count": 21, "glycosylation_sites": [ { "position": 37, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 216, "type": "O-linked (GalNAc...) threonine" }, { "position": 231, "type": "O-linked (GalNAc...) threonine" }, { "position": 359, "type": "O-linked (GalNAc...) serine" } ], "id": "Q8WXD2", "name": "POMT2", "organism": "Homo sapiens", "uniprot_id": "Q8WXD2" }, { "function": "Acts as an activator of serum response factor (SRF)-dependent transcription possibly by inducing nuclear translocation of MKL1 or MKL2 and through a mechanism requiring Rho-actin signaling", "gene_name": "ABRA", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8N0Z2", "name": "B4GAT1", "organism": "Homo sapiens", "uniprot_id": "Q8N0Z2" }, { "function": "Catalyzes the transfer of a ribitol 5-phosphate from CDP-L-ribitol to the ribitol 5-phosphate previously attached by FKTN/fukutin to the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1) (PubMed:26923585, PubMed:27194101, PubMed:29477842, PubMed:31949166). This constitutes the second step in the formation of the ribose 5-phosphate tandem repeat which links the phosphorylated O-mannosyl trisaccharide to the ligand binding moiety composed of repeats of 3-xylosyl-alpha-1,3-glucuronic acid-beta-1 (PubMed:25279699, PubMed:26923585, PubMed:27194101, PubMed:29477842, PubMed:31949166)", "gene_name": "FKRP", "glycan_count": 3, "glycosylation_sites": [ { "position": 172, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 209, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9H9S5", "name": "FKRP", "organism": "Homo sapiens", "uniprot_id": "Q9H9S5" }, { "function": "Plasma membrane transporter mediating the uptake by cells of the water soluble vitamin B2/riboflavin that plays a key role in biochemical oxidation-reduction reactions of the carbohydrate, lipid, and amino acid metabolism (PubMed:20463145, PubMed:22864630, PubMed:23243084, PubMed:24253200, PubMed:27702554). Humans are unable to synthesize vitamin B2/riboflavin and must obtain it via intestinal absorption (PubMed:20463145). May also act as a receptor for 4-hydroxybutyrate (Probable)", "gene_name": "SLC52A2", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9HAB3", "name": "PIGN (Glycosylphosphatidylinositol ethanolamine phosphate transferase 1)", "organism": "Homo sapiens", "uniprot_id": "Q9HAB3" }, { "function": "", "gene_name": "CLN6", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NWW5", "name": "CLN6", "organism": "Homo sapiens", "uniprot_id": "Q9NWW5" }, { "function": "Plays a role of transcription factor; binds to recognition signal sequences (Rss heptamer) for somatic recombination of immunoglobulin and T-cell receptor gene segments; Also binds to the kappa-B motif of gene such as S100A4, involved in cell progression and differentiation. Kappa-B motif is a gene regulatory element found in promoters and enhancers of genes involved in immunity, inflammation, and growth and that responds to viral antigens, mitogens, and cytokines. Involvement of HIVEP3 in cell growth is strengthened by the fact that its down-regulation promotes cell cycle progression with ultimate formation of multinucleated giant cells. Strongly inhibits TNF-alpha-induced NF-kappa-B activation; Interferes with nuclear factor NF-kappa-B by several mechanisms: as transcription factor, by competing for Kappa-B motif and by repressing transcription in the nucleus; through a non transcriptional process, by inhibiting nuclear translocation of RELA by association with TRAF2, an adapter molecule in the tumor necrosis factor signaling, which blocks the formation of IKK complex. Interaction with TRAF proteins inhibits both NF-Kappa-B-mediated and c-Jun N-terminal kinase/JNK-mediated responses that include apoptosis and pro-inflammatory cytokine gene expression. Positively regulates the expression of IL2 in T-cell. Essential regulator of adult bone formation", "gene_name": "HIVEP3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q5T1R4", "name": "FA2H", "organism": "Homo sapiens", "uniprot_id": "Q5T1R4" }, { "function": "Essential for the degradation of glycogen in lysosomes (PubMed:14695532, PubMed:18429042, PubMed:1856189, PubMed:7717400). Has highest activity on alpha-1,4-linked glycosidic linkages, but can also hydrolyze alpha-1,6-linked glucans (PubMed:29061980)", "gene_name": "GAA", "glycan_count": 86, "glycosylation_sites": [ { "position": 140, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 233, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 390, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 470, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 652, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 882, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 925, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P10253", "name": "GAA", "organism": "Homo sapiens", "uniprot_id": "P10253" }, { "function": "Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells", "gene_name": "ACTA2", "glycan_count": 3, "glycosylation_sites": [], "id": "P62736", "name": "ACTA1 (Alpha-actin 1)", "organism": "Homo sapiens", "uniprot_id": "P62736" }, { "function": "This giant muscle protein may be involved in maintaining the structural integrity of sarcomeres and the membrane system associated with the myofibrils. Binds and stabilize F-actin", "gene_name": "NEB", "glycan_count": 1, "glycosylation_sites": [], "id": "P20929", "name": "NEB (Nebulin)", "organism": "Homo sapiens", "uniprot_id": "P20929" }, { "function": "Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes (PubMed:26214738). Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system (By similarity). A second ligand, the hereditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C-terminal binding site. Positively regulates T and B cell proliferation through iron uptake (PubMed:26642240). Acts as a lipid sensor that regulates mitochondrial fusion by regulating activation of the JNK pathway (PubMed:26214738). When dietary levels of stearate (C18:0) are low, promotes activation of the JNK pathway, resulting in HUWE1-mediated ubiquitination and subsequent degradation of the mitofusin MFN2 and inhibition of mitochondrial fusion (PubMed:26214738). When dietary levels of stearate (C18:0) are high, TFRC stearoylation inhibits activation of the JNK pathway and thus degradation of the mitofusin MFN2 (PubMed:26214738). Mediates uptake of NICOL1 into fibroblasts where it may regulate extracellular matrix production (By similarity)", "gene_name": "TFRC", "glycan_count": 105, "glycosylation_sites": [ { "position": 104, "type": "O-linked (GalNAc...) threonine" }, { "position": 251, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 317, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 727, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P02786", "name": "Transferrin receptor (CD71)", "organism": "Homo sapiens", "uniprot_id": "P02786" }, { "function": "Structural component of specialized membrane microdomains known as tetraspanin-enriched microdomains (TERMs), which act as platforms for receptor clustering and signaling. Essential for trafficking and compartmentalization of CD19 receptor on the surface of activated B cells (PubMed:16449649, PubMed:20237408, PubMed:27881302). Upon initial encounter with microbial pathogens, enables the assembly of CD19-CR2/CD21 and B cell receptor (BCR) complexes at signaling TERMs, lowering the threshold dose of antigen required to trigger B cell clonal expansion and antibody production (PubMed:15161911, PubMed:20237408). In T cells, facilitates the localization of CD247/CD3 zeta at antigen-induced synapses with B cells, providing for costimulation and polarization toward T helper type 2 phenotype (PubMed:22307619, PubMed:23858057, PubMed:8766544). Present in MHC class II compartments, may also play a role in antigen presentation (PubMed:8409388, PubMed:8766544). Can act both as positive and negative regulator of homotypic or heterotypic cell-cell fusion processes. Positively regulates sperm-egg fusion and may be involved in acrosome reaction (By similarity). In myoblasts, associates with CD9 and PTGFRN and inhibits myotube fusion during muscle regeneration (By similarity). In macrophages, associates with CD9 and beta-1 and beta-2 integrins, and prevents macrophage fusion into multinucleated giant cells specialized in ingesting complement-opsonized large particles (PubMed:12796480). Also prevents the fusion of mononuclear cell progenitors into osteoclasts in charge of bone resorption (By similarity). May regulate the compartmentalization of enzymatic activities. In T cells, defines the subcellular localization of dNTPase SAMHD1 and permits its degradation by the proteasome, thereby controlling intracellular dNTP levels (PubMed:28871089). Also involved in cell adhesion and motility. Positively regulates integrin-mediated adhesion of macrophages, particularly relevant for the inflammatory response in the lung (By similarity)", "gene_name": "CD81", "glycan_count": 1, "glycosylation_sites": [], "id": "P60033", "name": "CD81", "organism": "Homo sapiens", "uniprot_id": "P60033" }, { "function": "Lysosomal membrane glycoprotein which plays an important role in lysosome biogenesis, lysosomal pH regulation, autophagy and cholesterol homeostasis (PubMed:37390818). Acts as an important regulator of lysosomal lumen pH regulation by acting as a direct inhibitor of the proton channel TMEM175, facilitating lysosomal acidification for optimal hydrolase activity (PubMed:37390818). Also plays an important role in NK-cells cytotoxicity (PubMed:2022921, PubMed:23632890). Mechanistically, participates in cytotoxic granule movement to the cell surface and perforin trafficking to the lytic granule (PubMed:23632890). In addition, protects NK-cells from degranulation-associated damage induced by their own cytotoxic granule content (PubMed:23847195). Presents carbohydrate ligands to selectins (PubMed:7685349)", "gene_name": "LAMP1", "glycan_count": 335, "glycosylation_sites": [ { "position": 37, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 45, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 62, "type": "N-linked (GlcNAc...) (polylactosaminoglycan) asparagine" }, { "position": 76, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 84, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 103, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 107, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 121, "type": "N-linked (GlcNAc...) (polylactosaminoglycan) asparagine" }, { "position": 130, "type": "N-linked (GlcNAc...) (polylactosaminoglycan) asparagine" }, { "position": 165, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 181, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 197, "type": "O-linked (GalNAc...) serine; partial" }, { "position": 199, "type": "O-linked (GalNAc...) threonine" }, { "position": 200, "type": "O-linked (GalNAc...) threonine" }, { "position": 207, "type": "O-linked (GalNAc...) serine" }, { "position": 209, "type": "O-linked (GalNAc...) serine" }, { "position": 211, "type": "O-linked (GalNAc...) serine" }, { "position": 223, "type": "N-linked (GlcNAc...) (polylactosaminoglycan) asparagine" }, { "position": 228, "type": "N-linked (GlcNAc...) (polylactosaminoglycan) asparagine" }, { "position": 241, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 249, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 261, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 293, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 322, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P11279", "name": "LAMP1", "organism": "Homo sapiens", "uniprot_id": "P11279" }, { "function": "Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFC and VEGFD. Plays an essential role in the regulation of angiogenesis, vascular development, vascular permeability, and embryonic hematopoiesis. Promotes proliferation, survival, migration and differentiation of endothelial cells. Promotes reorganization of the actin cytoskeleton. Isoforms lacking a transmembrane domain, such as isoform 2 and isoform 3, may function as decoy receptors for VEGFA, VEGFC and/or VEGFD. Isoform 2 plays an important role as negative regulator of VEGFA- and VEGFC-mediated lymphangiogenesis by limiting the amount of free VEGFA and/or VEGFC and preventing their binding to FLT4. Modulates FLT1 and FLT4 signaling by forming heterodimers. Binding of vascular growth factors to isoform 1 leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, reorganization of the actin cytoskeleton and activation of PTK2/FAK1. Required for VEGFA-mediated induction of NOS2 and NOS3, leading to the production of the signaling molecule nitric oxide (NO) by endothelial cells. Phosphorylates PLCG1. Promotes phosphorylation of FYN, NCK1, NOS3, PIK3R1, PTK2/FAK1 and SRC", "gene_name": "KDR", "glycan_count": 8, "glycosylation_sites": [ { "position": 46, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 66, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 96, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 143, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 158, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 245, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 318, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 374, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 395, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 511, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 523, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 580, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 613, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 619, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 631, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 675, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 704, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 721, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P35968", "name": "VEGFR2", "organism": "Homo sapiens", "uniprot_id": "P35968" }, { "function": "Transports diphosphate-N-acetylglucosamine (UDP-GlcNAc) from the cytosol into the lumen of the Golgi apparatus, functioning as an antiporter that exchanges UDP-N-acetyl-alpha-D-glucosamine for UMP (PubMed:10393322). May supply UDP-GlcNAc as substrate for Golgi-resident glycosyltransferases that generate highly branched, multiantennary complex N-glycans and keratan sulfate (PubMed:23766508, PubMed:34981577). However, the exact role of SLC35A3 still needs to be elucidated, it could be a member of a catalytically more efficient multiprotein complex rather than function independently as a single transporter (PubMed:32938718)", "gene_name": "SLC35A3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y2D2", "name": "Slc35a1", "organism": "Homo sapiens", "uniprot_id": "Q9Y2D2" }, { "function": "Ligand-specific transporter trafficking between intracellular organelles (TGN) and the plasma membrane. Plays a role in autocrine regulation of cell growth mediated by growth regulators containing cell surface retention sequence binding (CRS). May act as a hyaluronan (HA) transporter, either mediating its uptake for catabolism within lymphatic endothelial cells themselves, or its transport into the lumen of afferent lymphatic vessels for subsequent re-uptake and degradation in lymph nodes (PubMed:10037799). Binds to pericelluar hyaluronan matrices deposited on the surface of leukocytes and facilitates cell adhesion and migration through lymphatic endothelium (PubMed:26823460)", "gene_name": "LYVE1", "glycan_count": 27, "glycosylation_sites": [ { "position": 53, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 130, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y5Y7", "name": "Lyve1", "organism": "Homo sapiens", "uniprot_id": "Q9Y5Y7" }, { "function": "Possible adhesion molecule with a role in early hematopoiesis by mediating the attachment of stem cells to the bone marrow extracellular matrix or directly to stromal cells. Could act as a scaffold for the attachment of lineage specific glycans, allowing stem cells to bind to lectins expressed by stromal cells or other marrow components. Presents carbohydrate ligands to selectins", "gene_name": "CD34", "glycan_count": 71, "glycosylation_sites": [ { "position": 36, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 51, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 55, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 85, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 107, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 126, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 142, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 194, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 249, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P28906", "name": "CD34", "organism": "Homo sapiens", "uniprot_id": "P28906" }, { "function": "E2 conjugating enzyme that catalyzes the covalent conjugation of the C-terminal Gly of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or MAP1LC3A) to the amino group of phosphatidylethanolamine (PE)-containing lipids in the membrane resulting in membrane-bound ATG8-like proteins which is one of the key steps in the development of autophagic isolation membranes during autophagosome formation (PubMed:24191030, PubMed:33446636, PubMed:37252361). Cycles back and forth between binding to ATG7 for loading with the ATG8-like proteins and binding to E3 enzyme, composed of ATG12, ATG5 and ATG16L1 to promote ATG8-like proteins lipidation (PubMed:11825910, PubMed:12207896, PubMed:12890687, PubMed:16704426, PubMed:24186333). Also plays a role as a membrane curvature sensor that facilitates LC3/GABARAP lipidation by sensing local membrane stress associated with lipid-packing defects as occurs with high molar proportions of conical lipids or strident membrane curvature (By similarity). Interacts with negatively-charged membranes promoting membrane tethering and enhancing LC3/GABARAP lipidation (PubMed:29142222). Also acts as an autocatalytic E2-like enzyme by catalyzing the conjugation of ATG12 to itself in an ATG7-dependent manner, this complex thus formed, plays a role in mitochondrial homeostasis but not in autophagy (By similarity). ATG12-ATG3 conjugation promotes late endosome to lysosome trafficking and basal autophagosome maturation via its interaction with PDCD6IP (By similarity). ATG12-ATG3 conjugate is also formed upon viccina virus infection, leading to the disruption the cellular autophagy which is not necessary for vaccinia survival and proliferation (By similarity). Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway (By similarity)", "gene_name": "ATG3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NT62", "name": "O-GlcNAcase (OGA)", "organism": "Homo sapiens", "uniprot_id": "Q9NT62" }, { "function": "May act as an oxidative stress mediator by inhibiting thioredoxin activity or by limiting its bioavailability (PubMed:17603038). Interacts with COPS5 and restores COPS5-induced suppression of CDKN1B stability, blocking the COPS5-mediated translocation of CDKN1B from the nucleus to the cytoplasm (By similarity). Functions as a transcriptional repressor, possibly by acting as a bridge molecule between transcription factors and corepressor complexes, and over-expression will induce G0/G1 cell cycle arrest (PubMed:12821938). Required for the maturation of natural killer cells (By similarity). Acts as a suppressor of tumor cell growth (PubMed:18541147). Inhibits the proteasomal degradation of DDIT4, and thereby contributes to the inhibition of the mammalian target of rapamycin complex 1 (mTORC1) (PubMed:21460850)", "gene_name": "TXNIP", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H3M7", "name": "Thioredoxin-interacting protein (TXNIP)", "organism": "Homo sapiens", "uniprot_id": "Q9H3M7" }, { "function": "Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins. Regulates the circadian expression of clock genes BMAL1 and CRY1 (By similarity). Has a role in fine tuning the metabolic fluctuations of cytosolic UDP-GlcNAc and its effects on hyaluronan synthesis that occur during tissue remodeling (PubMed:26887390)", "gene_name": "GFPT1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q06210", "name": "Glutamine:fructose-6-phosphate amidotransferase (GFAT)", "organism": "Homo sapiens", "uniprot_id": "Q06210" }, { "function": "Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells (PubMed:1508712, PubMed:8183370). Regulates cell death by controlling the mitochondrial membrane permeability (PubMed:11368354). Appears to function in a feedback loop system with caspases (PubMed:11368354). Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1) (PubMed:11368354). Also acts as an inhibitor of autophagy: interacts with BECN1 and AMBRA1 during non-starvation conditions and inhibits their autophagy function (PubMed:18570871, PubMed:20889974, PubMed:21358617). May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (PubMed:17418785)", "gene_name": "BCL2", "glycan_count": 0, "glycosylation_sites": [], "id": "P10415", "name": "Bcl2", "organism": "Homo sapiens", "uniprot_id": "P10415" }, { "function": "Plays a role in the mitochondrial apoptotic process (PubMed:10772918, PubMed:11060313, PubMed:16113678, PubMed:16199525, PubMed:18948948, PubMed:21199865, PubMed:21458670, PubMed:25609812, PubMed:36361894, PubMed:8358790, PubMed:8521816). Under normal conditions, BAX is largely cytosolic via constant retrotranslocation from mitochondria to the cytosol mediated by BCL2L1/Bcl-xL, which avoids accumulation of toxic BAX levels at the mitochondrial outer membrane (MOM) (PubMed:21458670). Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis (PubMed:10772918, PubMed:11060313, PubMed:16113678, PubMed:16199525, PubMed:18948948, PubMed:21199865, PubMed:21458670, PubMed:25609812, PubMed:8358790, PubMed:8521816). Promotes activation of CASP3, and thereby apoptosis (PubMed:10772918, PubMed:11060313, PubMed:16113678, PubMed:16199525, PubMed:18948948, PubMed:21199865, PubMed:21458670, PubMed:25609812, PubMed:8358790, PubMed:8521816)", "gene_name": "BAX", "glycan_count": 1, "glycosylation_sites": [], "id": "Q07812", "name": "Bax", "organism": "Homo sapiens", "uniprot_id": "Q07812" }, { "function": "TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:7798316, PubMed:9792688). Forms a multistranded TJP1/ZO1 condensate which elongates to form a tight junction belt, the belt is anchored at the apical cell membrane via interaction with PATJ (By similarity). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Necessary for lumenogenesis, and particularly efficient epithelial polarization and barrier formation (By similarity). Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells (PubMed:21240187). Plays an important role in podosome formation and associated function, thus regulating cell adhesion and matrix remodeling (PubMed:20930113). With TJP2 and TJP3, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity). May play a role in mediating cell morphology changes during ameloblast differentiation via its role in tight junctions (By similarity)", "gene_name": "TJP1", "glycan_count": 7, "glycosylation_sites": [], "id": "Q07157", "name": "ZO-1", "organism": "Homo sapiens", "uniprot_id": "Q07157" }, { "function": "Interconverts simultaneously and stereospecifically pyruvate and lactate with concomitant interconversion of NADH and NAD(+)", "gene_name": "LDHA", "glycan_count": 7, "glycosylation_sites": [], "id": "P00338", "name": "LDHA", "organism": "Homo sapiens", "uniprot_id": "P00338" }, { "function": "Interconverts simultaneously and stereospecifically pyruvate and lactate with concomitant interconversion of NADH and NAD(+)", "gene_name": "LDHB", "glycan_count": 1, "glycosylation_sites": [], "id": "P07195", "name": "LDHB", "organism": "Homo sapiens", "uniprot_id": "P07195" }, { "function": "Transcriptional activator which binds to the enhancer of the T-cell receptor alpha and delta genes. Binds to the consensus sequence 5'-AGATAG-3'. Required for the T-helper 2 (Th2) differentiation process following immune and inflammatory responses. Positively regulates ASB2 expression (By similarity). Coordinates macrophage transcriptional activation and UCP2-dependent metabolic reprogramming in response to IL33. Upon tissue injury, acts downstream of IL33 signaling to drive differentiation of inflammation-resolving alternatively activated macrophages", "gene_name": "GATA3", "glycan_count": 1, "glycosylation_sites": [], "id": "P23771", "name": "GATA3", "organism": "Homo sapiens", "uniprot_id": "P23771" }, { "function": "Multifunctional polyribosome-associated RNA-binding protein that plays a central role in neuronal development and synaptic plasticity through the regulation of alternative mRNA splicing, mRNA stability, mRNA dendritic transport and postsynaptic local protein synthesis of target mRNAs (PubMed:12417522, PubMed:16631377, PubMed:18653529, PubMed:19166269, PubMed:23235829, PubMed:25464849). Acts as an mRNA regulator by mediating formation of some phase-separated membraneless compartment: undergoes liquid-liquid phase separation upon binding to target mRNAs, leading to assemble mRNAs into cytoplasmic ribonucleoprotein granules that concentrate mRNAs with associated regulatory factors (PubMed:12417522, PubMed:30765518, PubMed:31439799). Plays a role in the alternative splicing of its own mRNA (PubMed:18653529). Stabilizes the scaffolding postsynaptic density protein DLG4/PSD-95 and the myelin basic protein (MBP) mRNAs in hippocampal neurons and glial cells, respectively; this stabilization is further increased in response to metabotropic glutamate receptor (mGluR) stimulation (By similarity). Plays a role in selective delivery of a subset of dendritic mRNAs to synaptic sites in response to mGluR activation in a kinesin-dependent manner (By similarity). Undergoes liquid-liquid phase separation following phosphorylation and interaction with CAPRIN1, promoting formation of cytoplasmic ribonucleoprotein granules that concentrate mRNAs with factors that inhibit translation and mediate deadenylation of target mRNAs (PubMed:31439799). Acts as a repressor of mRNA translation in synaptic regions by mediating formation of neuronal ribonucleoprotein granules and promoting recruitmtent of EIF4EBP2 (PubMed:30765518). Plays a role as a repressor of mRNA translation during the transport of dendritic mRNAs to postsynaptic dendritic spines (PubMed:11157796, PubMed:11532944, PubMed:12594214, PubMed:23235829). Component of the CYFIP1-EIF4E-FMR1 complex which blocks cap-dependent mRNA translation initiation (By similarity). Represses mRNA translation by stalling ribosomal translocation during elongation (By similarity). Reports are contradictory with regards to its ability to mediate translation inhibition of MBP mRNA in oligodendrocytes (PubMed:23891804). Also involved in the recruitment of the RNA helicase MOV10 to a subset of mRNAs and hence regulates microRNA (miRNA)-mediated translational repression by AGO2 (PubMed:14703574, PubMed:17057366, PubMed:25464849). Facilitates the assembly of miRNAs on specific target mRNAs (PubMed:17057366). Also plays a role as an activator of mRNA translation of a subset of dendritic mRNAs at synapses (PubMed:19097999, PubMed:19166269). In response to mGluR stimulation, FMR1-target mRNAs are rapidly derepressed, allowing for local translation at synapses (By similarity). Binds to a large subset of dendritic mRNAs that encode a myriad of proteins involved in pre- and postsynaptic functions (PubMed:11157796, PubMed:11719189, PubMed:12594214, PubMed:17417632, PubMed:23235829, PubMed:24448548, PubMed:7692601). Binds to 5'-ACU[GU]-3' and/or 5'-[AU]GGA-3' RNA consensus sequences within mRNA targets, mainly at coding sequence (CDS) and 3'-untranslated region (UTR) and less frequently at 5'-UTR (PubMed:23235829). Binds to intramolecular G-quadruplex structures in the 5'- or 3'-UTRs of mRNA targets (PubMed:11719189, PubMed:18579868, PubMed:25464849, PubMed:25692235). Binds to G-quadruplex structures in the 3'-UTR of its own mRNA (PubMed:11532944, PubMed:12594214, PubMed:15282548, PubMed:18653529, PubMed:7692601). Also binds to RNA ligands harboring a kissing complex (kc) structure; this binding may mediate the association of FMR1 with polyribosomes (PubMed:15805463). Binds mRNAs containing U-rich target sequences (PubMed:12927206). Binds to a triple stem-loop RNA structure, called Sod1 stem loop interacting with FMRP (SoSLIP), in the 5'-UTR region of superoxide dismutase SOD1 mRNA (PubMed:19166269). Binds to the dendritic, small non-coding brain cytoplasmic RNA 1 (BC1); which may increase the association of the CYFIP1-EIF4E-FMR1 complex to FMR1 target mRNAs at synapses (By similarity). Plays a role in mRNA nuclear export (PubMed:31753916). Specifically recognizes and binds a subset of N6-methyladenosine (m6A)-containing mRNAs, promoting their nuclear export in a XPO1/CRM1-dependent manner (PubMed:31753916). Together with export factor NXF2, is involved in the regulation of the NXF1 mRNA stability in neurons (By similarity). Associates with export factor NXF1 mRNA-containing ribonucleoprotein particles (mRNPs) in a NXF2-dependent manner (By similarity). Binds to a subset of miRNAs in the brain (PubMed:14703574, PubMed:17057366). May associate with nascent transcripts in a nuclear protein NXF1-dependent manner (PubMed:18936162). In vitro, binds to RNA homomer; preferentially on poly(G) and to a lesser extent on poly(U), but not on poly(A) or poly(C) (PubMed:12950170, PubMed:15381419, PubMed:7688265, PubMed:7781595, PubMed:8156595). Moreover, plays a role in the modulation of the sodium-activated potassium channel KCNT1 gating activity (PubMed:20512134). Negatively regulates the voltage-dependent calcium channel current density in soma and presynaptic terminals of dorsal root ganglion (DRG) neurons, and hence regulates synaptic vesicle exocytosis (By similarity). Modulates the voltage-dependent calcium channel CACNA1B expression at the plasma membrane by targeting the channels for proteasomal degradation (By similarity). Plays a role in regulation of MAP1B-dependent microtubule dynamics during neuronal development (By similarity). Has been shown to play a translation-independent role in the modulation of presynaptic action potential (AP) duration and neurotransmitter release via large-conductance calcium-activated potassium (BK) channels in hippocampal and cortical excitatory neurons (PubMed:25561520). May be involved in the control of DNA damage response (DDR) mechanisms through the regulation of ATR-dependent signaling pathways such as histone H2AX/H2A.x and BRCA1 phosphorylations (PubMed:24813610). Forms a cytoplasmic messenger ribonucleoprotein (mRNP) network by packaging long mRNAs, serving as a scaffold that recruits proteins and signaling molecules. This network facilitates signaling reactions by maintaining proximity between kinases and substrates (PubMed:39106863)", "gene_name": "FMR1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q06787", "name": "Fragile X Mental Retardation Protein (FMRP)", "organism": "Homo sapiens", "uniprot_id": "Q06787" }, { "function": "Exopeptidase which selectively removes arginine and/or lysine residues from the N-terminus of several peptide substrates including Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(-1)-Lys(0)-somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene B4 (LTB-4) (By similarity)", "gene_name": "RNPEP", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H4A4", "name": "OGA", "organism": "Homo sapiens", "uniprot_id": "Q9H4A4" }, { "function": "Transcription factor involved in osteoblastic differentiation and skeletal morphogenesis (PubMed:28505335, PubMed:28703881, PubMed:28738062). Essential for the maturation of osteoblasts and both intramembranous and endochondral ossification. CBF binds to the core site, 5'-PYGPYGGT-3', of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, osteocalcin, osteopontin, bone sialoprotein, alpha 1(I) collagen, LCK, IL-3 and GM-CSF promoters. In osteoblasts, supports transcription activation: synergizes with SPEN/MINT to enhance FGFR2-mediated activation of the osteocalcin FGF-responsive element (OCFRE) (By similarity). Inhibits KAT6B-dependent transcriptional activation", "gene_name": "RUNX2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q13950", "name": "Runx2", "organism": "Homo sapiens", "uniprot_id": "Q13950" }, { "function": "NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The heterodimeric RELA-NFKB1 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. The NF-kappa-B heterodimeric RELA-NFKB1 and RELA-REL complexes, for instance, function as transcriptional activators. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. The inhibitory effect of I-kappa-B on NF-kappa-B through retention in the cytoplasm is exerted primarily through the interaction with RELA. RELA shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappa-B complex. Besides its activity as a direct transcriptional activator, it is also able to modulate promoters accessibility to transcription factors and thereby indirectly regulate gene expression. Associates with chromatin at the NF-kappa-B promoter region via association with DDX1. Essential for cytokine gene expression in T-cells (PubMed:15790681). The NF-kappa-B homodimeric RELA-RELA complex appears to be involved in invasin-mediated activation of IL-8 expression. Key transcription factor regulating the IFN response during SARS-CoV-2 infection (PubMed:33440148)", "gene_name": "RELA", "glycan_count": 2, "glycosylation_sites": [], "id": "Q04206", "name": "NF-\u03baB p65", "organism": "Homo sapiens", "uniprot_id": "Q04206" }, { "function": "Key adapter protein that plays an essential role in JNK and NF-kappa-B activation and proinflammatory cytokines production in response to stimulation with TLRs and cytokines (PubMed:22307082, PubMed:24403530). Mechanistically, associates with the catalytic domain of MAP3K7/TAK1 to trigger MAP3K7/TAK1 autophosphorylation leading to its full activation (PubMed:10838074, PubMed:25260751, PubMed:37832545). Similarly, associates with MAPK14 and triggers its autophosphorylation and subsequent activation (PubMed:11847341, PubMed:29229647). In turn, MAPK14 phosphorylates TAB1 and inhibits MAP3K7/TAK1 activation in a feedback control mechanism (PubMed:14592977). Also plays a role in recruiting MAPK14 to the TAK1 complex for the phosphorylation of the TAB2 and TAB3 regulatory subunits (PubMed:18021073)", "gene_name": "TAB1", "glycan_count": 2, "glycosylation_sites": [ { "position": 395, "type": "O-linked (GlcNAc) serine" } ], "id": "Q15750", "name": "TAB1", "organism": "Homo sapiens", "uniprot_id": "Q15750" }, { "function": "Acts as a scavenger receptor on macrophages, which specifically binds to OxLDL (oxidized low density lipoprotein), suggesting that it may be involved in pathophysiology such as atherogenesis (By similarity). Induces a strong chemotactic response. Induces calcium mobilization. Binds to CXCR6/Bonzo", "gene_name": "CXCL16", "glycan_count": 6, "glycosylation_sites": [ { "position": 168, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9H2A7", "name": "ROCK2", "organism": "Homo sapiens", "uniprot_id": "Q9H2A7" }, { "function": "Transcription factor that plays a key role in chondrocytes differentiation and skeletal development (PubMed:24038782). Specifically binds the 5'-ACAAAG-3' DNA motif present in enhancers and super-enhancers and promotes expression of genes important for chondrogenesis, including cartilage matrix protein-coding genes COL2A1, COL4A2, COL9A1, COL11A2 and ACAN, SOX5 and SOX6 (PubMed:8640233). Also binds to some promoter regions (By similarity). Plays a central role in successive steps of chondrocyte differentiation (By similarity). Absolutely required for precartilaginous condensation, the first step in chondrogenesis during which skeletal progenitors differentiate into prechondrocytes (By similarity). Together with SOX5 and SOX6, required for overt chondrogenesis when condensed prechondrocytes differentiate into early stage chondrocytes, the second step in chondrogenesis (By similarity). Later, required to direct hypertrophic maturation and block osteoblast differentiation of growth plate chondrocytes: maintains chondrocyte columnar proliferation, delays prehypertrophy and then prevents osteoblastic differentiation of chondrocytes by lowering beta-catenin (CTNNB1) signaling and RUNX2 expression (By similarity). Also required for chondrocyte hypertrophy, both indirectly, by keeping the lineage fate of chondrocytes, and directly, by remaining present in upper hypertrophic cells and transactivating COL10A1 along with MEF2C (By similarity). Low lipid levels are the main nutritional determinant for chondrogenic commitment of skeletal progenitor cells: when lipids levels are low, FOXO (FOXO1 and FOXO3) transcription factors promote expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). Mechanistically, helps, but is not required, to remove epigenetic signatures of transcriptional repression and deposit active promoter and enhancer marks at chondrocyte-specific genes (By similarity). Acts in cooperation with the Hedgehog pathway-dependent GLI (GLI1 and GLI3) transcription factors (By similarity). In addition to cartilage development, also acts as a regulator of proliferation and differentiation in epithelial stem/progenitor cells: involved in the lung epithelium during branching morphogenesis, by balancing proliferation and differentiation and regulating the extracellular matrix (By similarity). Controls epithelial branching during kidney development (By similarity)", "gene_name": "SOX9", "glycan_count": 1, "glycosylation_sites": [], "id": "P48436", "name": "Sox9", "organism": "Homo sapiens", "uniprot_id": "P48436" }, { "function": "Transcriptional repressor which binds preferentially to the canonical E box sequence 5'-CACGTG-3' (PubMed:11095750). Downstream effector of Notch signaling required for cardiovascular development. Specifically required for the Notch-induced endocardial epithelial to mesenchymal transition, which is itself criticial for cardiac valve and septum development. May be required in conjunction with HEY2 to specify arterial cell fate or identity. Promotes maintenance of neuronal precursor cells and glial versus neuronal fate specification. Represses transcription by the cardiac transcriptional activators GATA4 and GATA6 and by the neuronal bHLH factors ASCL1/MASH1 and NEUROD4/MATH3 (PubMed:15485867). Involved in the regulation of liver cancer cells self-renewal (PubMed:25985737)", "gene_name": "HEY1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y5J3", "name": "FAM134B", "organism": "Homo sapiens", "uniprot_id": "Q9Y5J3" }, { "function": "Sialic-acid-binding immunoglobulin-like lectin (Siglec) that plays a role in mediating cell-cell interactions and in maintaining immune cells in a resting state (PubMed:10611343, PubMed:11320212, PubMed:15597323). Preferentially recognizes and binds alpha-2,3- and more avidly alpha-2,6-linked sialic acid-bearing glycans (PubMed:7718872). Upon engagement of ligands such as C1q or syalylated glycoproteins, two immunoreceptor tyrosine-based inhibitory motifs (ITIMs) located in CD33 cytoplasmic tail are phosphorylated by Src-like kinases such as LCK (PubMed:10887109, PubMed:28325905). These phosphorylations provide docking sites for the recruitment and activation of protein-tyrosine phosphatases PTPN6/SHP-1 and PTPN11/SHP-2 (PubMed:10206955, PubMed:10556798, PubMed:10887109). In turn, these phosphatases regulate downstream pathways through dephosphorylation of signaling molecules (PubMed:10206955, PubMed:10887109). One of the repressive effect of CD33 on monocyte activation requires phosphoinositide 3-kinase/PI3K (PubMed:15597323)", "gene_name": "CD33", "glycan_count": 4, "glycosylation_sites": [ { "position": 100, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 113, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 160, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 209, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 230, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P20138", "name": "CD33 (Siglec-3)", "organism": "Homo sapiens", "uniprot_id": "P20138" }, { "function": "Synthesizes cyclic ADP-ribose (cADPR), a second messenger for glucose-induced insulin secretion (PubMed:7961800, PubMed:8253715). Synthesizes the Ca(2+) mobilizer nicotinate-adenine dinucleotide phosphate, NAADP(+), from 2'-phospho-cADPR and nicotinic acid, as well as from NADP(+) and nicotinic acid. At both pH 5.0 and pH 7.4 preferentially transforms 2'-phospho-cADPR into NAADP(+), while preferentially cleaving NADP(+) to cADPR and ADPRP rather than into NADDP(+) (PubMed:16690024). Has cADPR hydrolase activity (PubMed:7961800, PubMed:8253715)", "gene_name": "CD38", "glycan_count": 24, "glycosylation_sites": [ { "position": 100, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 164, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 209, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 219, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P28907", "name": "CD38", "organism": "Homo sapiens", "uniprot_id": "P28907" }, { "function": "Transmembrane glycoprotein expressed by T-cells and natural killer (NK) cells and their precursors (PubMed:7506726). Plays a costimulatory role in T-cell activation upon binding to its ligand K12/SECTM1 (PubMed:10652336). In turn, mediates the production of cytokines such as IL-2 (PubMed:1709867). On resting NK-cells, CD7 activation results in a significant induction of interferon-gamma levels (PubMed:7506726)", "gene_name": "CD7", "glycan_count": 5, "glycosylation_sites": [ { "position": 45, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 96, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P09564", "name": "CD7", "organism": "Homo sapiens", "uniprot_id": "P09564" }, { "function": "Cell-surface receptor that plays a role in cell-cell interactions, cell adhesion and migration, helping them to sense and respond to changes in the tissue microenvironment (PubMed:16541107, PubMed:19703720, PubMed:22726066). Participates thereby in a wide variety of cellular functions including the activation, recirculation and homing of T-lymphocytes, hematopoiesis, inflammation and response to bacterial infection (PubMed:7528188). Engages, through its ectodomain, extracellular matrix components such as hyaluronan/HA, collagen, growth factors, cytokines or proteases and serves as a platform for signal transduction by assembling, via its cytoplasmic domain, protein complexes containing receptor kinases and membrane proteases (PubMed:18757307, PubMed:23589287). Such effectors include PKN2, the RhoGTPases RAC1 and RHOA, Rho-kinases and phospholipase C that coordinate signaling pathways promoting calcium mobilization and actin-mediated cytoskeleton reorganization essential for cell migration and adhesion (PubMed:15123640)", "gene_name": "CD44", "glycan_count": 81, "glycosylation_sites": [ { "position": 25, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 57, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 100, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 110, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 120, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 180, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 350, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 548, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 599, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 636, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P16070", "name": "CD44v6", "organism": "Homo sapiens", "uniprot_id": "P16070" }, { "function": "Cell surface receptor for IL3 expressed on hematopoietic progenitor cells, monocytes and B-lymphocytes that controls the production and differentiation of hematopoietic progenitor cells into lineage-restricted cells (PubMed:10527461). Ligand stimulation rapidly induces hetrodimerization with IL3RB, phosphorylation and enzyme activity of effector proteins such as JAK2 and PI3K that play a role in signaling cell proliferation and differentiation. Activation of JAK2 leads to STAT5-mediated transcriptional program (By similarity)", "gene_name": "IL3RA", "glycan_count": 1, "glycosylation_sites": [ { "position": 46, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 64, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 80, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 109, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 212, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 218, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P26951", "name": "CD123 (IL3R-\u03b1)", "organism": "Homo sapiens", "uniprot_id": "P26951" }, { "function": "C-type lectin receptor that binds carbohydrates mannose and fucose but also weakly interacts with N-acetylglucosamine (GlcNAc) in a Ca(2+)-dependent manner (PubMed:27015765). Involved in regulating immune reactivity (PubMed:10438934, PubMed:18258799). Once triggered by antigen, it is internalized by clathrin-dependent endocytosis and delivers its antigenic cargo into the antigen presentation pathway resulting in cross-priming of CD8(+) T cells. This cross-presentation and cross-priming are enhanced by TLR7 and TLR8 agonists with increased expansion of the CD8(+) T cells, high production of IFNG and TNF with reduced levels of IL4, IL5 and IL13 (PubMed:18258799, PubMed:20530286). In plasmacytoid dendritic cells, inhibits TLR9-mediated IFNA and TNF production (PubMed:18258799). May be involved via its ITIM motif (immunoreceptor tyrosine-based inhibitory motifs) in the inhibition of B-cell-receptor-mediated calcium mobilization and protein tyrosine phosphorylation (PubMed:10438934)", "gene_name": "CLEC4A", "glycan_count": 0, "glycosylation_sites": [ { "position": 185, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UMR7", "name": "CLL-1 (CLEC12A)", "organism": "Homo sapiens", "uniprot_id": "Q9UMR7" }, { "function": "Functions as a coreceptor for the B-cell antigen receptor complex (BCR) on B-lymphocytes (PubMed:29523808). Decreases the threshold for activation of downstream signaling pathways and for triggering B-cell responses to antigens (PubMed:1373518, PubMed:16672701, PubMed:2463100). Activates signaling pathways that lead to the activation of phosphatidylinositol 3-kinase and the mobilization of intracellular Ca(2+) stores (PubMed:12387743, PubMed:16672701, PubMed:9317126, PubMed:9382888). Is not required for early steps during B cell differentiation in the blood marrow (PubMed:9317126). Required for normal differentiation of B-1 cells (By similarity). Required for normal B cell differentiation and proliferation in response to antigen challenges (PubMed:1373518, PubMed:2463100). Required for normal levels of serum immunoglobulins, and for production of high-affinity antibodies in response to antigen challenge (PubMed:12387743, PubMed:16672701, PubMed:9317126)", "gene_name": "CD19", "glycan_count": 0, "glycosylation_sites": [ { "position": 86, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 125, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 138, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 181, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 265, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P15391", "name": "CD19", "organism": "Homo sapiens", "uniprot_id": "P15391" }, { "function": "Expressed at the plasma membrane of B cells, it is the ligand of the CD27 receptor which is specifically expressed at the surface of T cells (PubMed:28011863, PubMed:28011864, PubMed:8387892). The CD70-CD27 signaling pathway mediates antigen-specific T cell activation and expansion which in turn provides immune surveillance of B cells (PubMed:28011863, PubMed:28011864)", "gene_name": "CD70", "glycan_count": 16, "glycosylation_sites": [ { "position": 63, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 170, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P32970", "name": "CD70", "organism": "Homo sapiens", "uniprot_id": "P32970" }, { "function": "Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules", "gene_name": "DYNLRB1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NP97", "name": "Siglec-6", "organism": "Homo sapiens", "uniprot_id": "Q9NP97" }, { "function": "Cell adhesion glycoprotein predominantly expressed on the surface of endothelial cells that plays an important role in immune surveillance and inflammation (PubMed:31310649). Acts as a major regulator of leukocyte adhesion to the endothelium through interaction with different types of integrins (PubMed:10209034). During inflammatory responses, binds ligands on the surface of activated endothelial cells to initiate the activation of calcium channels and the plasma membrane-associated small GTPase RAC1 leading to leukocyte transendothelial migration (PubMed:22970700). Also serves as a quality-control checkpoint for entry into bone marrow by providing a 'don't-eat-me' stamping in the context of major histocompatibility complex (MHC) class-I presentation (PubMed:35210567)", "gene_name": "VCAM1", "glycan_count": 56, "glycosylation_sites": [ { "position": 273, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 365, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 417, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 463, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 531, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 561, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P19320", "name": "VCAM-1", "organism": "Homo sapiens", "uniprot_id": "P19320" }, { "function": "Tyrosine-protein kinase that acts as a cell-surface receptor for ANGPT1, ANGPT2 and ANGPT4 and regulates angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Has anti-inflammatory effects by preventing the leakage of pro-inflammatory plasma proteins and leukocytes from blood vessels. Required for normal angiogenesis and heart development during embryogenesis. Required for post-natal hematopoiesis. After birth, activates or inhibits angiogenesis, depending on the context. Inhibits angiogenesis and promotes vascular stability in quiescent vessels, where endothelial cells have tight contacts. In quiescent vessels, ANGPT1 oligomers recruit TEK to cell-cell contacts, forming complexes with TEK molecules from adjoining cells, and this leads to preferential activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascades. In migrating endothelial cells that lack cell-cell adhesions, ANGT1 recruits TEK to contacts with the extracellular matrix, leading to the formation of focal adhesion complexes, activation of PTK2/FAK and of the downstream kinases MAPK1/ERK2 and MAPK3/ERK1, and ultimately to the stimulation of sprouting angiogenesis. ANGPT1 signaling triggers receptor dimerization and autophosphorylation at specific tyrosine residues that then serve as binding sites for scaffold proteins and effectors. Signaling is modulated by ANGPT2 that has lower affinity for TEK, can promote TEK autophosphorylation in the absence of ANGPT1, but inhibits ANGPT1-mediated signaling by competing for the same binding site. Signaling is also modulated by formation of heterodimers with TIE1, and by proteolytic processing that gives rise to a soluble TEK extracellular domain. The soluble extracellular domain modulates signaling by functioning as decoy receptor for angiopoietins. TEK phosphorylates DOK2, GRB7, GRB14, PIK3R1; SHC1 and TIE1", "gene_name": "TEK", "glycan_count": 11, "glycosylation_sites": [ { "position": 140, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 158, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 399, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 438, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 464, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 560, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 596, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 649, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 691, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q02763", "name": "TEK (Tie2)", "organism": "Homo sapiens", "uniprot_id": "Q02763" }, { "function": "Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9 (PubMed:18799458, PubMed:22848640, PubMed:24808179). Binds to endosomes damaged by phagocytosis of particulate wear debris and participates in endosomal membrane stabilization, thereby limiting NLRP3 inflammasome activation (By similarity). Required for endothelial cell surface plasmin generation and may support fibrinolytic surveillance and neoangiogenesis (By similarity)", "gene_name": "ANXA2", "glycan_count": 2, "glycosylation_sites": [], "id": "P07355", "name": "ANXA2 (Annexin A2)", "organism": "Homo sapiens", "uniprot_id": "P07355" }, { "function": "Nucleotide pyrophosphatase that generates diphosphate (PPi) and functions in bone mineralization and soft tissue calcification by regulating pyrophosphate levels (By similarity). PPi inhibits bone mineralization and soft tissue calcification by binding to nascent hydroxyapatite crystals, thereby preventing further growth of these crystals (PubMed:11004006). Preferentially hydrolyzes ATP, but can also hydrolyze other nucleoside 5' triphosphates such as GTP, CTP and UTP to their corresponding monophosphates with release of pyrophosphate, as well as diadenosine polyphosphates, and also 3',5'-cAMP to AMP (PubMed:25344812, PubMed:27467858, PubMed:28011303, PubMed:35147247, PubMed:8001561). May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling (PubMed:27467858, PubMed:8001561). Inhibits ectopic joint calcification and maintains articular chondrocytes by repressing hedgehog signaling; it is however unclear whether hedgehog inhibition is direct or indirect (By similarity). Appears to modulate insulin sensitivity and function (PubMed:10615944). Also involved in melanogenesis (PubMed:28964717). Also able to hydrolyze 2',3'-cGAMP (cyclic GMP-AMP), a second messenger that activates TMEM173/STING and triggers type-I interferon production (PubMed:25344812). 2',3'-cGAMP degradation takes place in the lumen or extracellular space, and not in the cytosol where it is produced; the role of 2',3'-cGAMP hydrolysis is therefore unclear (PubMed:25344812). Not able to hydrolyze the 2',3'-cGAMP linkage isomer 3'-3'-cGAMP (PubMed:25344812)", "gene_name": "ENPP1", "glycan_count": 45, "glycosylation_sites": [ { "position": 179, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 285, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 341, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 477, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 585, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 643, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 700, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 731, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 748, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P22413", "name": "ENPP1", "organism": "Homo sapiens", "uniprot_id": "P22413" }, { "function": "May participate in forming intercisternal cross-bridges of the Golgi complex", "gene_name": "GOLGB1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q14789", "name": "GOLGB1", "organism": "Homo sapiens", "uniprot_id": "Q14789" }, { "function": "Integrins alpha-4/beta-1 (VLA-4) and alpha-4/beta-7 are receptors for fibronectin. They recognize one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. They are also receptors for VCAM1. Integrin alpha-4/beta-1 recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-4/beta-7 is also a receptor for MADCAM1. It recognizes the sequence L-D-T in MADCAM1. On activated endothelial cells integrin VLA-4 triggers homotypic aggregation for most VLA-4-positive leukocyte cell lines. It may also participate in cytolytic T-cell interactions with target cells. ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling (PubMed:23125415). ITGA4:ITGB1 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1 (PubMed:18635536, PubMed:25398877). Integrin ITGA4:ITGB1 represses PRKCA-mediated L-type voltage-gated channel Ca(2+) influx and ROCK-mediated calcium sensitivity in vascular smooth muscle cells via its interaction with SVEP1, thereby inhibiting vasocontraction (PubMed:35802072)", "gene_name": "ITGA4", "glycan_count": 25, "glycosylation_sites": [ { "position": 79, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 138, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 229, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 480, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 518, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 538, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 626, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 645, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 660, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 806, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 821, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P13612", "name": "ITGA4", "organism": "Homo sapiens", "uniprot_id": "P13612" }, { "function": "Cell surface receptor that regulates diverse cellular processes including cell proliferation, differentiation, migration, and apoptosis (PubMed:12958365, PubMed:19416857). Initiates BMP, inhibin, and TGF-beta signaling pathways by interacting with different ligands including TGFB1, BMP2, BMP5, BMP7 or GDF5 (PubMed:18184661). Alternatively, acts as a cell surface coreceptor for BMP ligands, serving to enhance ligand binding by differentially regulating BMPR1A/ALK3 and BMPR1B/ALK6 receptor trafficking (PubMed:19726563). Promotes epithelial cell adhesion, focal adhesion formation and integrin signaling during epithelial cell spreading on fibronectin (PubMed:22562249). By interacting with the scaffolding protein beta-arrestin2/ARRB2, regulates migration or actin cytoskeleton and promotes the activation of CDC42 as well as the inhibition of NF-kappa-B (PubMed:19416857, PubMed:19325136). In gonadotrope cells, acts as an inhibin A coreceptor and regulates follicle-stimulating hormone (FSH) levels and female fertility (By similarity). Plays a role in the inhibition of directed and random cell migration in epithelial cells by altering the actin cytoskeletal organization (PubMed:19416857). Participates in epithelial-mesenchymal transformation (EMT) upon binding to BMP2 or TGFB2, by activating the PAR6/SMURF1/RHOA pathway (By similarity)", "gene_name": "TGFBR3", "glycan_count": 6, "glycosylation_sites": [ { "position": 141, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 492, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 534, "type": "O-linked (Xyl...) (glycosaminoglycan) serine" }, { "position": 545, "type": "O-linked (Xyl...) (glycosaminoglycan) serine" }, { "position": 571, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 590, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 697, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q03167", "name": "TGF\u03b2R-3", "organism": "Homo sapiens", "uniprot_id": "Q03167" }, { "function": "Receptor for both interleukin 4 and interleukin 13 (PubMed:17030238). Couples to the JAK1/2/3-STAT6 pathway. The IL4 response is involved in promoting Th2 differentiation. The IL4/IL13 responses are involved in regulating IgE production and, chemokine and mucus production at sites of allergic inflammation. In certain cell types, can signal through activation of insulin receptor substrates, IRS1/IRS2", "gene_name": "IL4R", "glycan_count": 4, "glycosylation_sites": [ { "position": 53, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 98, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 128, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 134, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 176, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 209, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P24394", "name": "IL4R", "organism": "Homo sapiens", "uniprot_id": "P24394" }, { "function": "Hydro-lyase catalyzing the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L-homocysteine in a beta-replacement reaction to form L-cystathionine, the precursor of L-cysteine. This catabolic route allows the elimination of L-methionine and the toxic metabolite L-homocysteine (PubMed:20506325, PubMed:23974653, PubMed:23981774). Also involved in the production of hydrogen sulfide, a gasotransmitter with signaling and cytoprotective effects on neurons (By similarity)", "gene_name": "CBS", "glycan_count": 2, "glycosylation_sites": [], "id": "P35520", "name": "CBS", "organism": "Homo sapiens", "uniprot_id": "P35520" }, { "function": "Aquaglyceroporins form homotetrameric transmembrane channels, with each monomer independently mediating glycerol and water transport across the plasma membrane along their osmotic gradient (PubMed:10564231, PubMed:30420639, PubMed:35054513, PubMed:9514918). AQP9 is the primary route for glycerol uptake in hepatocytes, supporting hepatic gluconeogenesis (By similarity). It exhibits broad specificity and may transport various small, non-charged solutes, including carbamides, polyols, purines, and pyrimidines (PubMed:10564231). AQP9 may also facilitate hepatic urea extrusion (PubMed:10564231, PubMed:9514918). Due to its permeability to lactate, AQP9 might participate in the astrocyte-to-neuron lactate shuttle, supplying neurons with energy (PubMed:10564231, PubMed:35054513). Additionally, AQP9 is permeable to arsenite, contributing to arsenic excretion by the liver and providing partial protection against arsenic toxicity (PubMed:10564231). It is also permeable to H2O2 in vivo (PubMed:26837049). Could also be permeable to ammonium (By similarity)", "gene_name": "AQP9", "glycan_count": 0, "glycosylation_sites": [], "id": "O43315", "name": "Aquaporin-4", "organism": "Homo sapiens", "uniprot_id": "O43315" }, { "function": "", "gene_name": "NRCAM", "glycan_count": 0, "glycosylation_sites": [], "id": "Q92823-2", "name": "Neurofascin-155 (NF155)", "organism": "Homo sapiens", "uniprot_id": "Q92823-2" }, { "function": "Adhesion molecule that mediates interactions between myelinating cells and neurons by binding to neuronal sialic acid-containing gangliosides and to the glycoproteins RTN4R and RTN4RL2 (By similarity). Not required for initial myelination, but seems to play a role in the maintenance of normal axon myelination. Protects motoneurons against apoptosis, also after injury; protection against apoptosis is probably mediated via interaction with neuronal RTN4R and RTN4RL2. Required to prevent degeneration of myelinated axons in adults; this probably depends on binding to gangliosides on the axon cell membrane (By similarity). Negative regulator of neurite outgrowth; in dorsal root ganglion neurons the inhibition is mediated primarily via binding to neuronal RTN4R or RTN4RL2 and to a lesser degree via binding to neuronal gangliosides. In cerebellar granule cells the inhibition is mediated primarily via binding to neuronal gangliosides. In sensory neurons, inhibition of neurite extension depends only partially on RTN4R, RTN4RL2 and gangliosides. Inhibits axon longitudinal growth (By similarity). Inhibits axon outgrowth by binding to RTN4R (By similarity). Preferentially binds to alpha-2,3-linked sialic acid. Binds ganglioside Gt1b (By similarity)", "gene_name": "MAG", "glycan_count": 2, "glycosylation_sites": [ { "position": 99, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 106, "type": "N-linked (GlcNAc...) asparagine; partial" }, { "position": 223, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 246, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 315, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 406, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 450, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 454, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P20916", "name": "Myelin-associated glycoprotein (MAG)", "organism": "Homo sapiens", "uniprot_id": "P20916" }, { "function": "The classic group of MBP isoforms (isoform 4-isoform 14) are with PLP the most abundant protein components of the myelin membrane in the CNS. They have a role in both its formation and stabilization. The smaller isoforms might have an important role in remyelination of denuded axons in multiple sclerosis. The non-classic group of MBP isoforms (isoform 1-isoform 3/Golli-MBPs) may preferentially have a role in the early developing brain long before myelination, maybe as components of transcriptional complexes, and may also be involved in signaling pathways in T-cells and neural cells. Differential splicing events combined with optional post-translational modifications give a wide spectrum of isomers, with each of them potentially having a specialized function. Induces T-cell proliferation", "gene_name": "MBP", "glycan_count": 1, "glycosylation_sites": [], "id": "P02686", "name": "Myelin basic protein (MBP)", "organism": "Homo sapiens", "uniprot_id": "P02686" }, { "function": "Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signaling for determination of cell fate such as differentiation and survival. Plays a crucial role in the apoptosis signal transduction pathway through mitochondria-dependent caspase activation. MAP3K5/ASK1 is required for the innate immune response, which is essential for host defense against a wide range of pathogens. Mediates signal transduction of various stressors like oxidative stress as well as by receptor-mediated inflammatory signals, such as the tumor necrosis factor (TNF) or lipopolysaccharide (LPS). Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K4/SEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate p38 MAPKs and c-jun N-terminal kinases (JNKs). Both p38 MAPK and JNKs control the transcription factors activator protein-1 (AP-1)", "gene_name": "Map3k5", "glycan_count": 1, "glycosylation_sites": [], "id": "O35099", "name": "Thrombospondin-4 (Thbs4)", "organism": "Mus musculus", "uniprot_id": "O35099" }, { "function": "This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Involved in autophagy in response to starvation. Upon interaction with VMP1 and activation, controls ER-isolation membrane contacts for autophagosome formation. Also modulates ER contacts with lipid droplets, mitochondria and endosomes (By similarity). In coordination with FLVCR2 mediates heme-stimulated switching from mitochondrial ATP synthesis to thermogenesis", "gene_name": "Atp2a2", "glycan_count": 1, "glycosylation_sites": [], "id": "O55143", "name": "\u03b2-sarcoglycan", "organism": "Mus musculus", "uniprot_id": "O55143" }, { "function": "", "gene_name": "Tlx3", "glycan_count": 0, "glycosylation_sites": [], "id": "O55144", "name": "\u03b4-sarcoglycan", "organism": "Mus musculus", "uniprot_id": "O55144" }, { "function": "The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sarcolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization", "gene_name": "Dag1", "glycan_count": 7, "glycosylation_sites": [ { "position": 139, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 315, "type": "O-linked (Man6P...) threonine" }, { "position": 317, "type": "O-linked (Man6P...) threonine" }, { "position": 377, "type": "O-linked (Man6P...) threonine" }, { "position": 639, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 647, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 659, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q62165", "name": "Dystroglycan (\u03b1/\u03b2)", "organism": "Mus musculus", "uniprot_id": "Q62165" }, { "function": "Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components", "gene_name": "Lamb2", "glycan_count": 11, "glycosylation_sites": [ { "position": 251, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 371, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1086, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1250, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1309, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1349, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1500, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q61292", "name": "Laminin \u03b12 chain", "organism": "Mus musculus", "uniprot_id": "Q61292" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q61738/Q61739", "name": "Integrin \u03b17\u03b21", "organism": "", "uniprot_id": "" }, { "function": "Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin (By similarity). Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape healing, and maintenance of cell shape (By similarity). Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization (PubMed:21768292). Participates in the regulation of type I collagen deposition by osteoblasts (PubMed:21768292). Acts as a ligand for the Lilrb4a receptor, inhibiting Fcgr1/CD64-mediated monocyte activation (PubMed:34089617)", "gene_name": "Fn1", "glycan_count": 4, "glycosylation_sites": [ { "position": 430, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 528, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 542, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 876, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1006, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1243, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1290, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2198, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P11276", "name": "Fibronectin", "organism": "Mus musculus", "uniprot_id": "P11276" }, { "function": "Type I collagen is a member of group I collagen (fibrillar forming collagen)", "gene_name": "COL1A2", "glycan_count": 18, "glycosylation_sites": [ { "position": 177, "type": "O-linked (Gal...) hydroxylysine; alternate" }, { "position": 1267, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08123", "name": "Collagen III", "organism": "Homo sapiens", "uniprot_id": "P08123" }, { "function": "The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity)", "gene_name": "env", "glycan_count": 0, "glycosylation_sites": [ { "position": 127, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 143, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 498, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 557, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P03374", "name": "BLV gp51 (Env)", "organism": "Mouse mammary tumor virus (strain GR)", "uniprot_id": "P03374" }, { "function": "Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41", "gene_name": "env", "glycan_count": 0, "glycosylation_sites": [ { "position": 88, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 136, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 141, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 156, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 160, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 186, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 197, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 230, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 234, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 241, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 262, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 276, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 289, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 295, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 301, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 332, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 339, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 356, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 386, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 392, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 397, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 406, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 448, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 463, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 611, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 616, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 625, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 637, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 674, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P03375", "name": "BLV p24 (Gag)", "organism": "Human immunodeficiency virus type 1 group M subtype B (isolate BH10)", "uniprot_id": "P03375" }, { "function": "Integral membrane protein associated with integrins, which regulates different processes, such as sperm-egg fusion, platelet activation and aggregation, and cell adhesion (PubMed:14575715, PubMed:18541721, PubMed:8478605). Present at the cell surface of oocytes and plays a key role in sperm-egg fusion, possibly by organizing multiprotein complexes and the morphology of the membrane required for the fusion (By similarity). In myoblasts, associates with CD81 and PTGFRN and inhibits myotube fusion during muscle regeneration (By similarity). In macrophages, associates with CD81 and beta-1 and beta-2 integrins, and prevents macrophage fusion into multinucleated giant cells specialized in ingesting complement-opsonized large particles (PubMed:12796480). Also prevents the fusion between mononuclear cell progenitors into osteoclasts in charge of bone resorption (By similarity). Acts as a receptor for PSG17 (By similarity). Involved in platelet activation and aggregation (PubMed:18541721). Regulates paranodal junction formation (By similarity). Involved in cell adhesion, cell motility and tumor metastasis (PubMed:7511626, PubMed:8478605)", "gene_name": "CD9", "glycan_count": 1, "glycosylation_sites": [ { "position": 52, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 53, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P21926", "name": "CD9", "organism": "Homo sapiens", "uniprot_id": "P21926" }, { "function": "May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles", "gene_name": "FLOT1", "glycan_count": 1, "glycosylation_sites": [], "id": "O75955", "name": "Flotillin-1", "organism": "Homo sapiens", "uniprot_id": "O75955" }, { "function": "Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 (PubMed:24012426, PubMed:24318877, PubMed:26865365). Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation (PubMed:27708256). Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle (PubMed:27137183). Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling (PubMed:24613385). Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223). Required as a co-chaperone for optimal STUB1/CHIP ubiquitination of NFATC3 (By similarity). Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response (PubMed:9499401). Involved in the clearance of misfolded PRDM1/Blimp-1 proteins. Sequesters them in the cytoplasm and promotes their association with SYNV1/HRD1, leading to proteasomal degradation (PubMed:28842558)", "gene_name": "HSPA1A", "glycan_count": 3, "glycosylation_sites": [], "id": "P0DMV8", "name": "HSP70", "organism": "Homo sapiens", "uniprot_id": "P0DMV8" }, { "function": "Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:11274138, PubMed:12526792, PubMed:15577939, PubMed:15937123, PubMed:27353360, PubMed:29127155). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself (PubMed:29127155). Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:26991466, PubMed:27295069). Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70 (PubMed:12526792). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels (PubMed:25973397). In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues (PubMed:25973397). Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment (PubMed:25973397). Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11276205). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Mediates the association of TOMM70 with IRF3 or TBK1 in mitochondrial outer membrane which promotes host antiviral response (PubMed:20628368, PubMed:25609812)", "gene_name": "HSP90AA1", "glycan_count": 4, "glycosylation_sites": [], "id": "P07900", "name": "HSP90", "organism": "Homo sapiens", "uniprot_id": "P07900" }, { "function": "Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). Mediates IgG effector functions on monocytes triggering ADCC of virus-infected cells", "gene_name": "IGHG1", "glycan_count": 221, "glycosylation_sites": [ { "position": 180, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P01857", "name": "Immunoglobulin G1 (IgG1)", "organism": "Homo sapiens", "uniprot_id": "P01857" }, { "function": "May associate with CD21. May regulate the release of Ca(2+) from intracellular stores", "gene_name": "ANXA6", "glycan_count": 2, "glycosylation_sites": [], "id": "P08133", "name": "Annexin A6", "organism": "Homo sapiens", "uniprot_id": "P08133" }, { "function": "Multifunctional anion transporter that operates via two distinct transport mechanisms, namely proton-coupled anion cotransport and membrane potential-dependent anion transport (PubMed:15510212, PubMed:21781115, PubMed:22778404, PubMed:23889254). Electroneutral proton-coupled acidic monosaccharide symporter, with a sugar to proton stoichiometry of 1:1. Exports glucuronic acid and free sialic acid derived from sialoglycoconjugate degradation out of lysosomes, driven by outwardly directed lysosomal pH gradient. May regulate lysosome function and metabolism of sialylated conjugates that impact oligodendrocyte lineage differentiation and myelinogenesis in the central nervous system (By similarity) (PubMed:15510212, PubMed:21781115, PubMed:22778404, PubMed:23889254). Electrogenic proton-coupled nitrate symporter that transports nitrate ions across the basolateral membrane of salivary gland acinar cells, with nitrate to proton stoichiometry of 2:1. May contribute to nitrate clearance from serum by salivary glands, where it is further concentrated and secreted in the saliva (PubMed:22778404). Uses membrane potential to drive the uptake of acidic amino acids and peptides into synaptic vesicles. Responsible for synaptic vesicular storage of L-aspartate and L-glutamate in pinealocytes as well as vesicular uptake of N-acetyl-L-aspartyl-L-glutamate neuropeptide, relevant to aspartegic-associated glutamatergic neurotransmission and activation of metabotropic receptors that inhibit subsequent transmitter release (By similarity) (PubMed:21781115, PubMed:22778404, PubMed:23889254)", "gene_name": "SLC17A5", "glycan_count": 0, "glycosylation_sites": [ { "position": 71, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 77, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 95, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NRA2", "name": "Spermine synthase", "organism": "Homo sapiens", "uniprot_id": "Q9NRA2" }, { "function": "Translation elongation factor that catalyzes the GTP-dependent binding of aminoacyl-tRNA (aa-tRNA) to the A-site of ribosomes during the elongation phase of protein synthesis. Base pairing between the mRNA codon and the aa-tRNA anticodon promotes GTP hydrolysis, releasing the aa-tRNA from EEF1A1 and allowing its accommodation into the ribosome (By similarity). The growing protein chain is subsequently transferred from the P-site peptidyl tRNA to the A-site aa-tRNA, extending it by one amino acid through ribosome-catalyzed peptide bond formation (By similarity)", "gene_name": "EEF1A2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q05639", "name": "EEF1A2", "organism": "Homo sapiens", "uniprot_id": "Q05639" }, { "function": "Chromosomal protein that binds to methylated DNA. It can bind specifically to a single methyl-CpG pair. It is not influenced by sequences flanking the methyl-CpGs. Mediates transcriptional repression through interaction with histone deacetylase and the corepressor SIN3A. Binds both 5-methylcytosine (5mC) and 5-hydroxymethylcytosine (5hmC)-containing DNA, with a preference for 5-methylcytosine (5mC)", "gene_name": "MECP2", "glycan_count": 1, "glycosylation_sites": [], "id": "P51608", "name": "MECP2", "organism": "Homo sapiens", "uniprot_id": "P51608" }, { "function": "Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes (PubMed:25759469). A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues", "gene_name": "FZD2", "glycan_count": 5, "glycosylation_sites": [ { "position": 53, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 154, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q14332", "name": "FZD2", "organism": "Homo sapiens", "uniprot_id": "Q14332" }, { "function": "Transcription factor that binds specifically to the DRE (dual repressor element) and represses HTR1A gene transcription in neuronal cells. The combination of calcium and ATP specifically inactivates the binding with FRE. May play a role in the altered regulation of HTR1A associated with anxiety and major depression. Mediates HDAC-independent repression of HTR1A promoter in neuronal cell. Performs essential function in controlling functional maturation of synapses (By similarity). Plays distinct roles depending on its localization. When cytoplasmic, acts as a scaffold protein in the PI3K/PDK1/AKT pathway. Repressor of HTR1A when nuclear. In the centrosome, regulates spindle pole localization of the cohesin subunit SCC1/RAD21, thereby mediating centriole cohesion during mitosis", "gene_name": "CC2D1A", "glycan_count": 1, "glycosylation_sites": [], "id": "Q6P1N0", "name": "TANGO2", "organism": "Homo sapiens", "uniprot_id": "Q6P1N0" }, { "function": "Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids (By similarity). Able to translocate phosphatidylserine, but not phosphatidylcholine (PubMed:34403372). Phospholipid translocation also seems to be implicated in vesicle formation and in uptake of lipid signaling molecules (By similarity). Reconstituted to liposomes, the ATP8A2:TMEM30A flippase complex predominantly transports phosphatidylserine (PS) and to a lesser extent phosphatidylethanolamine (PE) (By similarity). Phospholipid translocation is not associated with a countertransport of an inorganic ion or other charged substrate from the cytoplasmic side toward the exoplasm in connection with the phosphorylation from ATP (By similarity). ATP8A2:TMEM30A may be involved in regulation of neurite outgrowth (By similarity). Proposed to function in the generation and maintenance of phospholipid asymmetry in photoreceptor disk membranes and neuronal axon membranes (By similarity). May be involved in vesicle trafficking in neuronal cells (By similarity). Required for normal visual and auditory function; involved in photoreceptor and inner ear spiral ganglion cell survival (By similarity)", "gene_name": "ATP8A2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NTI2", "name": "ATP8A2", "organism": "Homo sapiens", "uniprot_id": "Q9NTI2" }, { "function": "TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins. May be involved in the recycling of the translocation apparatus after completion of the translocation process or may function as a membrane-bound chaperone facilitating folding of translocated proteins", "gene_name": "SSR1", "glycan_count": 58, "glycosylation_sites": [ { "position": 136, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 191, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P43307", "name": "SSR4", "organism": "Homo sapiens", "uniprot_id": "P43307" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P11532 (human)", "name": "Dystrophin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q13751 (human)", "name": "Laminin alpha 2 (Merosin)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O15131 (human)", "name": "Alpha-sarcoglycan", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O00299 (human)", "name": "Beta-sarcoglycan", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O15132 (human)", "name": "Gamma-sarcoglycan", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P46939 (human)", "name": "Utrophin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02549 (human)", "name": "Spectrin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O75923 (human)", "name": "Dysferlin", "organism": "", "uniprot_id": "" }, { "function": "Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover. Cleaves all known types of alpha-mannosidic linkages", "gene_name": "MAN2B1", "glycan_count": 63, "glycosylation_sites": [ { "position": 133, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 310, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 367, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 497, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 645, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 651, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 692, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 766, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 832, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 930, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 989, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O00754", "name": "Mannosidase alpha class 2B member 1 (MAN2B1)", "organism": "Homo sapiens", "uniprot_id": "O00754" }, { "function": "Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release (PubMed:20798282, PubMed:26442590, PubMed:28288128, PubMed:30404828). Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores (PubMed:28288128, PubMed:30404828). Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis (PubMed:30404828). Also acts as a molecular chaperone in its multimeric membrane-bound state, assisting in the folding of synaptic fusion components called SNAREs (Soluble NSF Attachment Protein REceptors) at presynaptic plasma membrane in conjunction with cysteine string protein-alpha/DNAJC5 (PubMed:20798282). This chaperone activity is important to sustain normal SNARE-complex assembly during aging (PubMed:20798282). Also plays a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity (PubMed:26442590)", "gene_name": "SNCA", "glycan_count": 2, "glycosylation_sites": [], "id": "P37840", "name": "Alpha-synuclein", "organism": "Homo sapiens", "uniprot_id": "P37840" }, { "function": "Carbohydrate-binding lectin with a preference for chitin. Has no chitinase activity. May play a role in tissue remodeling and in the capacity of cells to respond to and cope with changes in their environment. Plays a role in T-helper cell type 2 (Th2) inflammatory response and IL-13-induced inflammation, regulating allergen sensitization, inflammatory cell apoptosis, dendritic cell accumulation and M2 macrophage differentiation. Facilitates invasion of pathogenic enteric bacteria into colonic mucosa and lymphoid organs. Mediates activation of AKT1 signaling pathway and subsequent IL8 production in colonic epithelial cells. Regulates antibacterial responses in lung by contributing to macrophage bacterial killing, controlling bacterial dissemination and augmenting host tolerance. Also regulates hyperoxia-induced injury, inflammation and epithelial apoptosis in lung", "gene_name": "CHI3L1", "glycan_count": 2, "glycosylation_sites": [ { "position": 60, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P36222", "name": "Chitinase-3-like protein 1 (CHI3L1)", "organism": "Homo sapiens", "uniprot_id": "P36222" }, { "function": "May be implicated in biomineralization processes. Has a function in binding of osteoblasts via the alpha(V)beta(3)-integrin", "gene_name": "OMD", "glycan_count": 8, "glycosylation_sites": [ { "position": 113, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 121, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 187, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 242, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 316, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q99983", "name": "Osteomodulin", "organism": "Homo sapiens", "uniprot_id": "Q99983" }, { "function": "Prolactin acts primarily on the mammary gland by promoting lactation", "gene_name": "PRL", "glycan_count": 0, "glycosylation_sites": [ { "position": 59, "type": "N-linked (GlcNAc...) asparagine; partial" } ], "id": "P01236", "name": "Prolactin", "organism": "Homo sapiens", "uniprot_id": "P01236" }, { "function": "Secreted polyprotein that is packaged and proteolytically processed by prohormone convertases PCSK1 and PCSK2 in a cell-type-specific manner (By similarity). VGF and peptides derived from its processing play many roles in neurogenesis and neuroplasticity associated with learning, memory, depression and chronic pain (By similarity)", "gene_name": "VGF", "glycan_count": 2, "glycosylation_sites": [], "id": "O15240", "name": "VGF nerve growth factor inducible", "organism": "Homo sapiens", "uniprot_id": "O15240" }, { "function": "APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids (PubMed:14754908, PubMed:1911868, PubMed:6860692). APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance (PubMed:14754908, PubMed:1911868, PubMed:1917954, PubMed:23620513, PubMed:2762297, PubMed:6860692, PubMed:9395455). Apolipoproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma (PubMed:2762297, PubMed:6860692, PubMed:9395455). As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL) (PubMed:1911868, PubMed:6860692). It also binds a wide range of cellular receptors including the LDL receptor/LDLR, the LDL receptor-related proteins LRP1, LRP2 and LRP8 and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles (PubMed:12950167, PubMed:1530612, PubMed:1917954, PubMed:20030366, PubMed:20303980, PubMed:2063194, PubMed:2762297, PubMed:7635945, PubMed:7768901, PubMed:8756331, PubMed:8939961). Finally, APOE also has a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells (PubMed:23676495, PubMed:7635945, PubMed:9395455, PubMed:9488694). A main function of APOE is to mediate lipoprotein clearance through the uptake of chylomicrons, VLDLs, and HDLs by hepatocytes (PubMed:1911868, PubMed:1917954, PubMed:23676495, PubMed:29516132, PubMed:9395455). APOE is also involved in the biosynthesis by the liver of VLDLs as well as their uptake by peripheral tissues ensuring the delivery of triglycerides and energy storage in muscle, heart and adipose tissues (PubMed:2762297, PubMed:29516132). By participating in the lipoprotein-mediated distribution of lipids among tissues, APOE plays a critical role in plasma and tissues lipid homeostasis (PubMed:1917954, PubMed:2762297, PubMed:29516132). APOE is also involved in two steps of reverse cholesterol transport, the HDLs-mediated transport of cholesterol from peripheral tissues to the liver, and thereby plays an important role in cholesterol homeostasis (PubMed:14754908, PubMed:23620513, PubMed:9395455). First, it is functionally associated with ABCA1 in the biogenesis of HDLs in tissues (PubMed:14754908, PubMed:23620513). Second, it is enriched in circulating HDLs and mediates their uptake by hepatocytes (PubMed:9395455). APOE also plays an important role in lipid transport in the central nervous system, regulating neuron survival and sprouting (PubMed:25173806, PubMed:8939961). APOE is also involved in innate and adaptive immune responses, controlling for instance the survival of myeloid-derived suppressor cells (By similarity). Binds to the immune cell receptor LILRB4 (PubMed:30333625). APOE may also play a role in transcription regulation through a receptor-dependent and cholesterol-independent mechanism, that activates MAP3K12 and a non-canonical MAPK signal transduction pathway that results in enhanced AP-1-mediated transcription of APP (PubMed:28111074)", "gene_name": "APOE", "glycan_count": 7, "glycosylation_sites": [ { "position": 26, "type": "O-linked (GalNAc...) threonine" }, { "position": 36, "type": "O-linked (GalNAc...) threonine" }, { "position": 93, "type": "N-linked (Glc) (glycation) lysine" }, { "position": 212, "type": "O-linked (GalNAc...) threonine" }, { "position": 307, "type": "O-linked (GalNAc...) threonine" }, { "position": 308, "type": "O-linked (GalNAc...) serine" }, { "position": 314, "type": "O-linked (GalNAc...) serine" } ], "id": "P02649", "name": "Apolipoprotein E (ApoE)", "organism": "Homo sapiens", "uniprot_id": "P02649" }, { "function": "Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moieties from glycoproteins and glycolipids. To be active, it is strictly dependent on its presence in the multienzyme complex. Appears to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage", "gene_name": "NEU1", "glycan_count": 32, "glycosylation_sites": [ { "position": 186, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 343, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 352, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q99519", "name": "NEU1", "organism": "Homo sapiens", "uniprot_id": "Q99519" }, { "function": "Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses (PubMed:10805725, PubMed:27153536, PubMed:2790960, PubMed:35538033). Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF (PubMed:12297049, PubMed:15611079, PubMed:17909029, PubMed:20837704, PubMed:27153536, PubMed:2790960, PubMed:7679104, PubMed:8144591, PubMed:9419975). Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules (PubMed:27153536). May also activate the NF-kappa-B signaling cascade (PubMed:11116146). Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling (PubMed:11602604). Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin (PubMed:11483589). Positively regulates cell migration via interaction with CCDC88A/GIV which retains EGFR at the cell membrane following ligand stimulation, promoting EGFR signaling which triggers cell migration (PubMed:20462955). Plays a role in enhancing learning and memory performance (By similarity). Plays a role in mammalian pain signaling (long-lasting hypersensitivity) (By similarity)", "gene_name": "EGFR", "glycan_count": 149, "glycosylation_sites": [ { "position": 56, "type": "N-linked (GlcNAc...) (complex) asparagine; atypical; partial" }, { "position": 73, "type": "N-linked (GlcNAc...) asparagine; atypical" }, { "position": 128, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 175, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 196, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 352, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 361, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 413, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 444, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 528, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 568, "type": "N-linked (GlcNAc...) asparagine; partial" }, { "position": 603, "type": "N-linked (GlcNAc...) asparagine; partial" }, { "position": 623, "type": "N-linked (GlcNAc...) (high mannose) asparagine" } ], "id": "P00533", "name": "EGFR", "organism": "Homo sapiens", "uniprot_id": "P00533" }, { "function": "S-adenosyl-L-methionine-dependent methyltransferase that mediates N(3)-methylcytidine modification of residue 32 of the tRNA anticodon loop of tRNA(Thr)(UGU) and tRNA(Arg)(CCU)", "gene_name": "METTL2B", "glycan_count": 1, "glycosylation_sites": [], "id": "Q6P1Q9", "name": "CD36", "organism": "Homo sapiens", "uniprot_id": "Q6P1Q9" }, { "function": "Integrin alpha-6/beta-4 is a receptor for laminin. Plays a critical structural role in the hemidesmosome of epithelial cells. Is required for the regulation of keratinocyte polarity and motility. ITGA6:ITGB4 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling (PubMed:20682778). ITGA6:ITGB4 binds to IGF1 and this binding is essential for IGF1 signaling (PubMed:22351760). ITGA6:ITGB4 binds to IGF2 and this binding is essential for IGF2 signaling (PubMed:28873464)", "gene_name": "ITGB4", "glycan_count": 18, "glycosylation_sites": [ { "position": 327, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 491, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 579, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 617, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 695, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P16144", "name": "Integrin \u03b24", "organism": "Homo sapiens", "uniprot_id": "P16144" }, { "function": "The alpha subunit has cell adhesive properties. Can act both as an adhesion and an anti-adhesion protein. May provide a protective layer on epithelial cells against bacterial and enzyme attack", "gene_name": "MUC1", "glycan_count": 42, "glycosylation_sites": [ { "position": 131, "type": "O-linked (GalNAc...) threonine" }, { "position": 139, "type": "O-linked (GalNAc...) threonine" }, { "position": 140, "type": "O-linked (GalNAc...) serine" }, { "position": 144, "type": "O-linked (GalNAc...) threonine" }, { "position": 957, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 975, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1029, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1055, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1133, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P15941", "name": "MUC1", "organism": "Homo sapiens", "uniprot_id": "P15941" }, { "function": "Transmembrane receptor that functions as a pattern recognition receptor recognizing pathogen- and damage-associated molecular patterns (PAMPs and DAMPs) to induce innate immune responses via downstream signaling pathways (PubMed:10835634, PubMed:15809303, PubMed:16622205, PubMed:17292937, PubMed:17478729, PubMed:20037584, PubMed:20711192, PubMed:23880187, PubMed:27022195, PubMed:29038465, PubMed:17803912). At the plasma membrane, cooperates with LY96 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) (PubMed:27022195). Also involved in LPS-independent inflammatory responses triggered by free fatty acids, such as palmitate, and Ni(2+) (PubMed:20711192). Mechanistically, acts via MYD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (PubMed:10835634, PubMed:21393102, PubMed:27022195, PubMed:36945827, PubMed:9237759). Alternatively, CD14-mediated TLR4 internalization via endocytosis is associated with the initiation of a MYD88-independent signaling via the TICAM1-TBK1-IRF3 axis leading to type I interferon production (PubMed:14517278). In addition to the secretion of proinflammatory cytokines, initiates the activation of NLRP3 inflammasome and formation of a positive feedback loop between autophagy and NF-kappa-B signaling cascade (PubMed:32894580). In complex with TLR6, promotes inflammation in monocytes/macrophages by associating with TLR6 and the receptor CD86 (PubMed:23880187). Upon ligand binding, such as oxLDL or amyloid-beta 42, the TLR4:TLR6 complex is internalized and triggers inflammatory response, leading to NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway (PubMed:23880187). In myeloid dendritic cells, vesicular stomatitis virus glycoprotein G but not LPS promotes the activation of IRF7, leading to type I IFN production in a CD14-dependent manner (PubMed:15265881, PubMed:23880187). Required for the migration-promoting effects of ZG16B/PAUF on pancreatic cancer cells", "gene_name": "TLR4", "glycan_count": 1, "glycosylation_sites": [ { "position": 35, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 173, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 205, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 282, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 309, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 497, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 526, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 575, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 624, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 630, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O00206", "name": "TLR4", "organism": "Homo sapiens", "uniprot_id": "O00206" }, { "function": "Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. ENAH induces the formation of F-actin rich outgrowths in fibroblasts. Acts synergistically with BAIAP2-alpha and downstream of NTN1 to promote filipodia formation (By similarity)", "gene_name": "ENAH", "glycan_count": 4, "glycosylation_sites": [], "id": "Q8N8S7", "name": "TMEM5 (RXYLT1)", "organism": "Homo sapiens", "uniprot_id": "Q8N8S7" }, { "function": "Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis", "gene_name": "CTSF", "glycan_count": 21, "glycosylation_sites": [ { "position": 160, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 195, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 367, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 378, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 440, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UBX1", "name": "FKTN", "organism": "Homo sapiens", "uniprot_id": "Q9UBX1" }, { "function": "Guanine nucleotide exchange factor (GEF) for RAP1A, RAP1B and RAP2A small GTPases that is activated by binding cAMP. Seems not to activate RAB3A. Involved in cAMP-dependent, PKA-independent exocytosis through interaction with RIMS2 (By similarity)", "gene_name": "RAPGEF4", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8WZA2", "name": "POMGNT1", "organism": "Homo sapiens", "uniprot_id": "Q8WZA2" }, { "function": "Mediates transport of gamma-aminobutyric acid (GABA) together with sodium and chloride and is responsible for the reuptake of GABA from the synapse (PubMed:30132828). The translocation of GABA, however, may also occur in the reverse direction leading to the release of GABA (By similarity). The direction and magnitude of GABA transport is a consequence of the prevailing thermodynamic conditions, determined by membrane potential and the intracellular and extracellular concentrations of Na(+), Cl(-) and GABA (By similarity). Can also mediate sodium- and chloride-dependent transport of hypotaurine but to a much lower extent as compared to GABA (By similarity)", "gene_name": "SLC6A1", "glycan_count": 1, "glycosylation_sites": [ { "position": 176, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 181, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 184, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P30531", "name": "GABA transporter 1 (GAT1)", "organism": "Homo sapiens", "uniprot_id": "P30531" }, { "function": "Associates with SLC3A2 to form a functional heterodimeric complex that translocates small and large neutral amino acids with broad specificity and a stoichiometry of 1:1. Functions as amino acid antiporter mediating the influx of extracellular essential amino acids mainly in exchange with the efflux of highly concentrated intracellular amino acids (PubMed:10391915, PubMed:11311135, PubMed:11847106, PubMed:12716892, PubMed:15081149, PubMed:15918515, PubMed:29355479, PubMed:33298890, PubMed:34848541). Has relatively symmetrical selectivities but strongly asymmetrical substrate affinities at both the intracellular and extracellular sides of the transporter (PubMed:11847106). This asymmetry allows SLC7A8 to regulate intracellular amino acid pools (mM concentrations) by exchange with external amino acids (uM concentration range), equilibrating the relative concentrations of different amino acids across the plasma membrane instead of mediating their net uptake (PubMed:10391915, PubMed:11847106). May play an essential role in the reabsorption of neutral amino acids from the epithelial cells to the bloodstream in the kidney (PubMed:12716892). Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity (PubMed:12117417). Involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane (PubMed:15769744). Imports the thyroid hormone diiodothyronine (T2) and to a smaller extent triiodothyronine (T3) but not rT 3 or thyroxine (T4) (By similarity). Mediates the uptake of L-DOPA (By similarity). May participate in auditory function (By similarity)", "gene_name": "SLC7A8", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UHI5", "name": "Creatine transporter 1 (CRT1)", "organism": "Homo sapiens", "uniprot_id": "Q9UHI5" }, { "function": "Mediates sodium- and chloride-dependent transport of dopamine (PubMed:10375632, PubMed:11093780, PubMed:1406597, PubMed:15505207, PubMed:19478460, PubMed:39112701, PubMed:39112703, PubMed:39112705, PubMed:8302271). Also mediates sodium- and chloride-dependent transport of norepinephrine (also known as noradrenaline) (By similarity). Regulator of light-dependent retinal hyaloid vessel regression, downstream of OPN5 signaling (By similarity)", "gene_name": "SLC6A3", "glycan_count": 0, "glycosylation_sites": [ { "position": 181, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 188, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 205, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q01959", "name": "Dopamine transporter (DAT)", "organism": "Homo sapiens", "uniprot_id": "Q01959" }, { "function": "Serotonin transporter that cotransports serotonin with one Na(+) ion in exchange for one K(+) ion and possibly one proton in an overall electroneutral transport cycle. Transports serotonin across the plasma membrane from the extracellular compartment to the cytosol thus limiting serotonin intercellular signaling (PubMed:10407194, PubMed:12869649, PubMed:21730057, PubMed:27049939, PubMed:27756841, PubMed:34851672). Essential for serotonin homeostasis in the central nervous system. In the developing somatosensory cortex, acts in glutamatergic neurons to control serotonin uptake and its trophic functions accounting for proper spatial organization of cortical neurons and elaboration of sensory circuits. In the mature cortex, acts primarily in brainstem raphe neurons to mediate serotonin uptake from the synaptic cleft back into the pre-synaptic terminal thus terminating serotonin signaling at the synapse (By similarity). Modulates mucosal serotonin levels in the gastrointestinal tract through uptake and clearance of serotonin in enterocytes. Required for enteric neurogenesis and gastrointestinal reflexes (By similarity). Regulates blood serotonin levels by ensuring rapid high affinity uptake of serotonin from plasma to platelets, where it is further stored in dense granules via vesicular monoamine transporters and then released upon stimulation (PubMed:17506858, PubMed:18317590). Mechanistically, the transport cycle starts with an outward-open conformation having Na1(+) and Cl(-) sites occupied. The binding of a second extracellular Na2(+) ion and serotonin substrate leads to structural changes to outward-occluded to inward-occluded to inward-open, where the Na2(+) ion and serotonin are released into the cytosol. Binding of intracellular K(+) ion induces conformational transitions to inward-occluded to outward-open and completes the cycle by releasing K(+) possibly together with a proton bound to Asp-98 into the extracellular compartment. Na1(+) and Cl(-) ions remain bound throughout the transport cycle (PubMed:10407194, PubMed:12869649, PubMed:21730057, PubMed:27049939, PubMed:27756841, PubMed:34851672). Additionally, displays serotonin-induced channel-like conductance for monovalent cations, mainly Na(+) ions. The channel activity is uncoupled from the transport cycle and may contribute to the membrane resting potential or excitability (By similarity)", "gene_name": "SLC6A4", "glycan_count": 0, "glycosylation_sites": [ { "position": 208, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 217, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P31645", "name": "Serotonin transporter (SERT)", "organism": "Homo sapiens", "uniprot_id": "P31645" }, { "function": "Potentially involved in docking of synaptic vesicles at presynaptic active zones. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm (By similarity)", "gene_name": "STX1B", "glycan_count": 1, "glycosylation_sites": [], "id": "P61266", "name": "Syntaxin-1A", "organism": "Homo sapiens", "uniprot_id": "P61266" }, { "function": "Receptor for TNFSF6/FASLG. The adapter molecule FADD recruits caspase CASP8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs CASP8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. FAS-mediated apoptosis may have a role in the induction of peripheral tolerance, in the antigen-stimulated suicide of mature T-cells, or both. The secreted isoforms 2 to 6 block apoptosis (in vitro)", "gene_name": "FAS", "glycan_count": 32, "glycosylation_sites": [ { "position": 28, "type": "O-linked (GalNAc...) threonine" }, { "position": 118, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 136, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 250, "type": "(Microbial infection) N-beta-linked (GlcNAc) arginine" } ], "id": "P25445", "name": "Fas receptor", "organism": "Homo sapiens", "uniprot_id": "P25445" }, { "function": "Receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Contributes to the induction of non-cytocidal TNF effects including anti-viral state and activation of the acid sphingomyelinase", "gene_name": "TNFRSF1A", "glycan_count": 2, "glycosylation_sites": [ { "position": 54, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 145, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 151, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 376, "type": "(Microbial infection) N-beta-linked (GlcNAc) arginine" } ], "id": "P19438", "name": "TNF receptor", "organism": "Homo sapiens", "uniprot_id": "P19438" }, { "function": "Costimulates T-cell proliferation. May regulate myeloid cell activity in a variety of tissues", "gene_name": "CD200", "glycan_count": 0, "glycosylation_sites": [ { "position": 95, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 103, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 110, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 157, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 181, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 190, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P41217", "name": "CD200", "organism": "Homo sapiens", "uniprot_id": "P41217" }, { "function": "Receptor for TNFRSF25 and TNFRSF6B. Mediates activation of NF-kappa-B. Inhibits vascular endothelial growth and angiogenesis (in vitro). Promotes activation of caspases and apoptosis", "gene_name": "TNFSF15", "glycan_count": 0, "glycosylation_sites": [ { "position": 133, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 229, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O95150", "name": "TNFSF9 (CD137L)", "organism": "Homo sapiens", "uniprot_id": "O95150" }, { "function": "Inhibitory receptor on antigen activated T-cells that plays a critical role in induction and maintenance of immune tolerance to self (PubMed:21276005, PubMed:37208329). Delivers inhibitory signals upon binding to ligands CD274/PDCD1L1 and CD273/PDCD1LG2 (PubMed:21276005). Following T-cell receptor (TCR) engagement, PDCD1 associates with CD3-TCR in the immunological synapse and directly inhibits T-cell activation (By similarity). Suppresses T-cell activation through the recruitment of PTPN11/SHP-2: following ligand-binding, PDCD1 is phosphorylated within the ITSM motif, leading to the recruitment of the protein tyrosine phosphatase PTPN11/SHP-2 that mediates dephosphorylation of key TCR proximal signaling molecules, such as ZAP70, PRKCQ/PKCtheta and CD247/CD3zeta (By similarity)", "gene_name": "PDCD1", "glycan_count": 2, "glycosylation_sites": [ { "position": 49, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 58, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 74, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 116, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q15116", "name": "PD-1", "organism": "Homo sapiens", "uniprot_id": "Q15116" }, { "function": "Plays a critical role in induction and maintenance of immune tolerance to self (PubMed:11015443, PubMed:28813410, PubMed:28813417, PubMed:31399419). As a ligand for the inhibitory receptor PDCD1/PD-1, modulates the activation threshold of T-cells and limits T-cell effector response (PubMed:11015443, PubMed:28813410, PubMed:28813417, PubMed:36727298). Through a yet unknown activating receptor, may costimulate T-cell subsets that predominantly produce interleukin-10 (IL10) (PubMed:10581077). Can also act as a transcription coactivator: in response to hypoxia, translocates into the nucleus via its interaction with phosphorylated STAT3 and promotes transcription of GSDMC, leading to pyroptosis (PubMed:32929201)", "gene_name": "CD274", "glycan_count": 1, "glycosylation_sites": [ { "position": 35, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 192, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 200, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 219, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NZQ7", "name": "PD-L1", "organism": "Homo sapiens", "uniprot_id": "Q9NZQ7" }, { "function": "Inhibitory receptor acting as a major negative regulator of T-cell responses. The affinity of CTLA4 for its natural B7 family ligands, CD80 and CD86, is considerably stronger than the affinity of their cognate stimulatory coreceptor CD28", "gene_name": "CTLA4", "glycan_count": 0, "glycosylation_sites": [ { "position": 113, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 145, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P16410", "name": "CTLA-4", "organism": "Homo sapiens", "uniprot_id": "P16410" }, { "function": "Serine/threonine-protein kinase component of the WNK1-SPAK/OSR1 kinase cascade, which acts as a key regulator of blood pressure and regulatory volume increase by promoting ion influx (PubMed:15883153, PubMed:17190791, PubMed:31656913, PubMed:34289367, PubMed:36318922). WNK1 mediates regulatory volume increase in response to hyperosmotic stress by acting as a molecular crowding sensor, which senses cell shrinkage and mediates formation of a membraneless compartment by undergoing liquid-liquid phase separation (PubMed:36318922). The membraneless compartment concentrates WNK1 with its substrates, OXSR1/OSR1 and STK39/SPAK, promoting WNK1-dependent phosphorylation and activation of downstream kinases OXSR1/OSR1 and STK39/SPAK (PubMed:15883153, PubMed:16263722, PubMed:17190791, PubMed:19739668, PubMed:21321328, PubMed:22989884, PubMed:25477473, PubMed:34289367, PubMed:36318922). Following activation, OXSR1/OSR1 and STK39/SPAK catalyze phosphorylation of ion cotransporters SLC12A1/NKCC2, SLC12A2/NKCC1, SLC12A5/KCC2 and SLC12A6/KCC3, regulating their activity (PubMed:16263722, PubMed:21321328). Phosphorylation of Na-K-Cl cotransporters SLC12A2/NKCC1 and SLC12A2/NKCC1 promote their activation and ion influx; simultaneously, phosphorylation of K-Cl cotransporters SLC12A5/KCC2 and SLC12A6/KCC3 inhibit their activity, blocking ion efflux (PubMed:19665974, PubMed:21321328). Also acts as a regulator of angiogenesis in endothelial cells via activation of OXSR1/OSR1 and STK39/SPAK: activation of OXSR1/OSR1 regulates chemotaxis and invasion, while STK39/SPAK regulates endothelial cell proliferation (PubMed:25362046). Also acts independently of the WNK1-SPAK/OSR1 kinase cascade by catalyzing phosphorylation of other substrates, such as SYT2, PCF11 and NEDD4L (PubMed:29196535). Mediates phosphorylation of SYT2, regulating SYT2 association with phospholipids and membrane-binding (By similarity). Regulates mRNA export in the nucleus by mediating phosphorylation of PCF11, thereby decreasing the association between PCF11 and POLR2A/RNA polymerase II and promoting mRNA export to the cytoplasm (PubMed:29196535). Acts as a negative regulator of autophagy (PubMed:27911840). Required for the abscission step during mitosis, independently of the WNK1-SPAK/OSR1 kinase cascade (PubMed:21220314). May also play a role in actin cytoskeletal reorganization (PubMed:10660600). Also acts as a scaffold protein independently of its protein kinase activity: negatively regulates cell membrane localization of various transporters and channels, such as SLC4A4, SLC26A6, SLC26A9, TRPV4 and CFTR (By similarity). Involved in the regulation of epithelial Na(+) channel (ENaC) by promoting activation of SGK1 in a kinase-independent manner: probably acts as a scaffold protein that promotes the recruitment of SGK1 to the mTORC2 complex in response to chloride, leading to mTORC2-dependent phosphorylation and activation of SGK1 (PubMed:36373794). Acts as an assembly factor for the ER membrane protein complex independently of its protein kinase activity: associates with EMC2 in the cytoplasm via its amphipathic alpha-helix, and prevents EMC2 ubiquitination and subsequent degradation, thereby promoting EMC2 stabilization (PubMed:33964204)", "gene_name": "WNK1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9H4A3", "name": "O-GlcNAcase (OGA)", "organism": "Homo sapiens", "uniprot_id": "Q9H4A3" }, { "function": "Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity (PubMed:21985311). The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both (PubMed:21985311, PubMed:32961270). Axonal polarity is predetermined by TAU/MAPT localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization", "gene_name": "MAPT", "glycan_count": 2, "glycosylation_sites": [ { "position": 87, "type": "N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro" }, { "position": 383, "type": "N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro" }, { "position": 467, "type": "N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro" }, { "position": 480, "type": "N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro" }, { "position": 491, "type": "N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro" }, { "position": 525, "type": "O-linked (GlcNAc) serine" }, { "position": 542, "type": "N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro" }, { "position": 551, "type": "N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro" }, { "position": 555, "type": "O-linked (GlcNAc) serine" }, { "position": 576, "type": "N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro" }, { "position": 597, "type": "N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro" }, { "position": 598, "type": "N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro" }, { "position": 664, "type": "N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro" }, { "position": 670, "type": "N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro" }, { "position": 686, "type": "N-linked (Glc) (glycation) lysine; in PHF-tau; in vitro" }, { "position": 717, "type": "O-linked (GlcNAc) serine; alternate" } ], "id": "P10636", "name": "Tau", "organism": "Homo sapiens", "uniprot_id": "P10636" }, { "function": "Multifunctional transcription factor that induces cell cycle arrest, DNA repair or apoptosis upon binding to its target DNA sequence (PubMed:11025664, PubMed:12524540, PubMed:12810724, PubMed:15186775, PubMed:15340061, PubMed:17317671, PubMed:17349958, PubMed:19556538, PubMed:20673990, PubMed:20959462, PubMed:22726440, PubMed:24051492, PubMed:24652652, PubMed:35618207, PubMed:36634798, PubMed:38653238, PubMed:9840937). Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type (PubMed:11025664, PubMed:12524540, PubMed:12810724, PubMed:15186775, PubMed:15340061, PubMed:17189187, PubMed:17317671, PubMed:17349958, PubMed:19556538, PubMed:20673990, PubMed:20959462, PubMed:22726440, PubMed:24051492, PubMed:24652652, PubMed:38653238, PubMed:9840937). Negatively regulates cell division by controlling expression of a set of genes required for this process (PubMed:11025664, PubMed:12524540, PubMed:12810724, PubMed:15186775, PubMed:15340061, PubMed:17317671, PubMed:17349958, PubMed:19556538, PubMed:20673990, PubMed:20959462, PubMed:22726440, PubMed:24051492, PubMed:24652652, PubMed:9840937). One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression (PubMed:12524540, PubMed:17189187). Its pro-apoptotic activity is activated via its interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 (PubMed:12524540). However, this activity is inhibited when the interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 is displaced by PPP1R13L/iASPP (PubMed:12524540). In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seems to have an effect on cell-cycle regulation. Implicated in Notch signaling cross-over. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Isoform 2 enhances the transactivation activity of isoform 1 from some but not all TP53-inducible promoters. Isoform 4 suppresses transactivation activity and impairs growth suppression mediated by isoform 1. Isoform 7 inhibits isoform 1-mediated apoptosis. Regulates the circadian clock by repressing CLOCK-BMAL1-mediated transcriptional activation of PER2 (PubMed:24051492)", "gene_name": "TP53", "glycan_count": 1, "glycosylation_sites": [], "id": "P04637", "name": "p53", "organism": "Homo sapiens", "uniprot_id": "P04637" }, { "function": "Transcription factor that can activate or repress transcription in response to physiological and pathological stimuli. Binds with high affinity to GC-rich motifs and regulates the expression of a large number of genes involved in a variety of processes such as cell growth, apoptosis, differentiation and immune responses. Highly regulated by post-translational modifications (phosphorylations, sumoylation, proteolytic cleavage, glycosylation and acetylation). Also binds the PDGFR-alpha G-box promoter. May have a role in modulating the cellular response to DNA damage. Implicated in chromatin remodeling. Plays an essential role in the regulation of FE65 gene expression. In complex with ATF7IP, maintains telomerase activity in cancer cells by inducing TERT and TERC gene expression. Isoform 3 is a stronger activator of transcription than isoform 1. Positively regulates the transcription of the core clock component BMAL1 (PubMed:10391891, PubMed:11371615, PubMed:11904305, PubMed:14593115, PubMed:16377629, PubMed:16478997, PubMed:16943418, PubMed:17049555, PubMed:18171990, PubMed:18199680, PubMed:18239466, PubMed:18513490, PubMed:18619531, PubMed:19193796, PubMed:20091743, PubMed:21046154, PubMed:21798247). Plays a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter. Plays a role in protecting cells against oxidative stress following brain injury by regulating the expression of RNF112 (By similarity)", "gene_name": "SP1", "glycan_count": 2, "glycosylation_sites": [ { "position": 491, "type": "O-linked (GlcNAc) serine" }, { "position": 612, "type": "O-linked (GlcNAc) serine; alternate" }, { "position": 640, "type": "O-linked (GlcNAc) threonine; alternate" }, { "position": 641, "type": "O-linked (GlcNAc) serine; alternate" }, { "position": 698, "type": "O-linked (GlcNAc) serine; alternate" }, { "position": 702, "type": "O-linked (GlcNAc) serine; alternate" } ], "id": "P08047", "name": "Sp1", "organism": "Homo sapiens", "uniprot_id": "P08047" }, { "function": "Mediates SOST-dependent inhibition of bone formation. Functions as a specific facilitator of SOST-mediated inhibition of Wnt signaling. Plays a key role in the formation and the maintenance of the neuromuscular junction (NMJ), the synapse between motor neuron and skeletal muscle. Directly binds AGRIN and recruits it to the MUSK signaling complex. Mediates the AGRIN-induced phosphorylation of MUSK, the kinase of the complex. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Alternatively, may be involved in the negative regulation of the canonical Wnt signaling pathway, being able to antagonize the LRP6-mediated activation of this pathway. More generally, has been proposed to function as a cell surface endocytic receptor binding and internalizing extracellular ligands for degradation by lysosomes. May play an essential role in the process of digit differentiation (By similarity)", "gene_name": "LRP4", "glycan_count": 7, "glycosylation_sites": [ { "position": 264, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 498, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 719, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 901, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1077, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1415, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1467, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O75096", "name": "LRP4", "organism": "Homo sapiens", "uniprot_id": "O75096" }, { "function": "Receptor tyrosine kinase which plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ), the synapse between the motor neuron and the skeletal muscle (PubMed:25537362). Recruitment of AGRIN by LRP4 to the MUSK signaling complex induces phosphorylation and activation of MUSK, the kinase of the complex. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. May regulate AChR phosphorylation and clustering through activation of ABL1 and Src family kinases which in turn regulate MUSK. DVL1 and PAK1 that form a ternary complex with MUSK are also important for MUSK-dependent regulation of AChR clustering. May positively regulate Rho family GTPases through FNTA. Mediates the phosphorylation of FNTA which promotes prenylation, recruitment to membranes and activation of RAC1 a regulator of the actin cytoskeleton and of gene expression. Other effectors of the MUSK signaling include DNAJA3 which functions downstream of MUSK. May also play a role within the central nervous system by mediating cholinergic responses, synaptic plasticity and memory formation (By similarity)", "gene_name": "MUSK", "glycan_count": 1, "glycosylation_sites": [ { "position": 222, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 338, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O15146", "name": "MuSK", "organism": "Homo sapiens", "uniprot_id": "O15146" }, { "function": "Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that regulates the response to oxidative stress by targeting NFE2L2/NRF2 for ubiquitination (PubMed:14585973, PubMed:15379550, PubMed:15572695, PubMed:15601839, PubMed:15983046, PubMed:37339955). KEAP1 acts as a key sensor of oxidative and electrophilic stress: in normal conditions, the BCR(KEAP1) complex mediates ubiquitination and degradation of NFE2L2/NRF2, a transcription factor regulating expression of many cytoprotective genes (PubMed:15601839, PubMed:16006525). In response to oxidative stress, different electrophile metabolites trigger non-enzymatic covalent modifications of highly reactive cysteine residues in KEAP1, leading to inactivate the ubiquitin ligase activity of the BCR(KEAP1) complex, promoting NFE2L2/NRF2 nuclear accumulation and expression of phase II detoxifying enzymes (PubMed:16006525, PubMed:17127771, PubMed:18251510, PubMed:19489739, PubMed:29590092). In response to selective autophagy, KEAP1 is sequestered in inclusion bodies following its interaction with SQSTM1/p62, leading to inactivation of the BCR(KEAP1) complex and activation of NFE2L2/NRF2 (PubMed:20452972). The BCR(KEAP1) complex also mediates ubiquitination of SQSTM1/p62, increasing SQSTM1/p62 sequestering activity and degradation (PubMed:28380357). The BCR(KEAP1) complex also targets BPTF and PGAM5 for ubiquitination and degradation by the proteasome (PubMed:15379550, PubMed:17046835)", "gene_name": "KEAP1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q14145", "name": "Kelch-like ECH-associated protein 1 (Keap1)", "organism": "Homo sapiens", "uniprot_id": "Q14145" }, { "function": "Transcriptional regulator with dual roles as a coactivator and corepressor. Critical downstream regulatory target in the Hippo signaling pathway, crucial for organ size control and tumor suppression by restricting proliferation and promoting apoptosis (PubMed:17974916, PubMed:18280240, PubMed:18579750, PubMed:21364637, PubMed:30447097). The Hippo signaling pathway core involves a kinase cascade featuring STK3/MST2 and STK4/MST1, along with its regulatory partner SAV1, which phosphorylates and activates LATS1/2 in complex with their regulatory protein, MOB1. This activation leads to the phosphorylation and inactivation of the YAP1 oncoprotein and WWTR1/TAZ (PubMed:18158288). Phosphorylation of YAP1 by LATS1/2 prevents its nuclear translocation, thereby regulating the expression of its target genes (PubMed:18158288, PubMed:26598551, PubMed:34404733). The transcriptional regulation of gene expression requires TEAD transcription factors and modulates cell growth, anchorage-independent growth, and induction of epithelial-mesenchymal transition (EMT) (PubMed:18579750). Plays a key role in tissue tension and 3D tissue shape by regulating the cortical actomyosin network, acting via ARHGAP18, a Rho GTPase activating protein that suppresses F-actin polymerization (PubMed:25778702). It also suppresses ciliogenesis by acting as a transcriptional corepressor of TEAD4 target genes AURKA and PLK1 (PubMed:25849865). In conjunction with WWTR1, regulates TGFB1-dependent SMAD2 and SMAD3 nuclear accumulation (By similarity). Synergizes with WBP2 to enhance PGR activity (PubMed:16772533)", "gene_name": "YAP1", "glycan_count": 2, "glycosylation_sites": [], "id": "P46937", "name": "Yes-associated protein (YAP)", "organism": "Homo sapiens", "uniprot_id": "P46937" }, { "function": "Receptor tyrosine kinase which mediates actions of insulin-like growth factor 1 (IGF1). Binds IGF1 with high affinity and IGF2 and insulin (INS) with a lower affinity. The activated IGF1R is involved in cell growth and survival control. IGF1R is crucial for tumor transformation and survival of malignant cell. Ligand binding activates the receptor kinase, leading to receptor autophosphorylation, and tyrosines phosphorylation of multiple substrates, that function as signaling adapter proteins including, the insulin-receptor substrates (IRS1/2), Shc and 14-3-3 proteins. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways: the PI3K-AKT/PKB pathway and the Ras-MAPK pathway. The result of activating the MAPK pathway is increased cellular proliferation, whereas activating the PI3K pathway inhibits apoptosis and stimulates protein synthesis. Phosphorylated IRS1 can activate the 85 kDa regulatory subunit of PI3K (PIK3R1), leading to activation of several downstream substrates, including protein AKT/PKB. AKT phosphorylation, in turn, enhances protein synthesis through mTOR activation and triggers the antiapoptotic effects of IGFIR through phosphorylation and inactivation of BAD. In parallel to PI3K-driven signaling, recruitment of Grb2/SOS by phosphorylated IRS1 or Shc leads to recruitment of Ras and activation of the ras-MAPK pathway. In addition to these two main signaling pathways IGF1R signals also through the Janus kinase/signal transducer and activator of transcription pathway (JAK/STAT). Phosphorylation of JAK proteins can lead to phosphorylation/activation of signal transducers and activators of transcription (STAT) proteins. In particular activation of STAT3, may be essential for the transforming activity of IGF1R. The JAK/STAT pathway activates gene transcription and may be responsible for the transforming activity. JNK kinases can also be activated by the IGF1R. IGF1 exerts inhibiting activities on JNK activation via phosphorylation and inhibition of MAP3K5/ASK1, which is able to directly associate with the IGF1R", "gene_name": "IGF1R", "glycan_count": 22, "glycosylation_sites": [ { "position": 51, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 102, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 135, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 244, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 314, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 417, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 438, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 534, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 607, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 622, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 640, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 747, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 756, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 764, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 900, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 913, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08069", "name": "Insulin-like growth factor-I receptor (IGFR)", "organism": "Homo sapiens", "uniprot_id": "P08069" }, { "function": "Transmembrane serine/threonine kinase forming with the TGF-beta type II serine/threonine kinase receptor, TGFBR2, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis (PubMed:33914044). The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways. For instance, TGFBR1 induces TRAF6 autoubiquitination which in turn results in MAP3K7 ubiquitination and activation to trigger apoptosis. Also regulates epithelial to mesenchymal transition through a SMAD-independent signaling pathway through PARD6A phosphorylation and activation", "gene_name": "TGFBR1", "glycan_count": 2, "glycosylation_sites": [ { "position": 45, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P36897", "name": "TGF-\u03b2 receptor (TGF-\u03b2R)", "organism": "Homo sapiens", "uniprot_id": "P36897" }, { "function": "Cell surface pattern recognition receptor that senses endogenous stress signals with a broad ligand repertoire including advanced glycation end products, S100 proteins, high-mobility group box 1 protein/HMGB1, amyloid beta/APP oligomers, nucleic acids, histones, phospholipids and glycosaminoglycans (PubMed:27572515, PubMed:28515150, PubMed:34743181, PubMed:35974093, PubMed:24081950). Advanced glycosylation end products are nonenzymatically glycosylated proteins which accumulate in vascular tissue in aging and at an accelerated rate in diabetes (PubMed:21565706). These ligands accumulate at inflammatory sites during the pathogenesis of various diseases including diabetes, vascular complications, neurodegenerative disorders and cancers, and RAGE transduces their binding into pro-inflammatory responses. Upon ligand binding, uses TIRAP and MYD88 as adapters to transduce the signal ultimately leading to the induction of inflammatory cytokines IL6, IL8 and TNFalpha through activation of NF-kappa-B (PubMed:21829704, PubMed:33436632). Interaction with S100A12 on endothelium, mononuclear phagocytes, and lymphocytes triggers cellular activation, with generation of key pro-inflammatory mediators (PubMed:19386136). Interaction with S100B after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling (By similarity). Contributes to the translocation of amyloid-beta peptide (ABPP) across the cell membrane from the extracellular to the intracellular space in cortical neurons (PubMed:19906677). ABPP-initiated RAGE signaling, especially stimulation of p38 mitogen-activated protein kinase (MAPK), has the capacity to drive a transport system delivering ABPP as a complex with RAGE to the intraneuronal space. Participates in endothelial albumin transcytosis together with HMGB1 through the RAGE/SRC/Caveolin-1 pathway, leading to endothelial hyperpermeability (PubMed:27572515). Mediates the loading of HMGB1 in extracellular vesicles (EVs) that shuttle HMGB1 to hepatocytes by transferrin-mediated endocytosis and subsequently promote hepatocyte pyroptosis by activating the NLRP3 inflammasome (PubMed:34743181). Binds to DNA and promotes extracellular hypomethylated DNA (CpG DNA) uptake by cells via the endosomal route to activate inflammatory responses (PubMed:24081950, PubMed:28515150). Mediates phagocytosis by non-professional phagocytes (NPP) and this is enhanced by binding to ligands including RNA, DNA, HMGB1 and histones (PubMed:35974093). Promotes NPP-mediated phagocytosis of Saccharomyces cerevisiae spores by binding to RNA attached to the spore wall (PubMed:35974093). Also promotes NPP-mediated phagocytosis of apoptotic cells (PubMed:35974093). Following DNA damage, recruited to DNA double-strand break sites where it colocalizes with the MRN repair complex via interaction with double-strand break repair protein MRE11 (By similarity). Enhances the endonuclease activity of MRE11, promoting the end resection of damaged DNA (By similarity). Promotes DNA damage repair in trophoblasts which enhances trophoblast invasion and contributes to placental development and maintenance (PubMed:33918759). Protects cells from DNA replication stress by localizing to damaged replication forks where it stabilizes the MCM2-7 complex and promotes faithful progression of the replication fork (PubMed:36807739). Mediates the production of reactive oxygen species (ROS) in human endothelial cells (PubMed:25401185)", "gene_name": "AGER", "glycan_count": 0, "glycosylation_sites": [ { "position": 25, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 81, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q15109", "name": "Receptor for AGEs (RAGE)", "organism": "Homo sapiens", "uniprot_id": "Q15109" }, { "function": "Negative regulator of bone growth that acts through inhibition of Wnt signaling and bone formation", "gene_name": "SOST", "glycan_count": 0, "glycosylation_sites": [ { "position": 53, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 175, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9BQB4", "name": "Sclerostin", "organism": "Homo sapiens", "uniprot_id": "Q9BQB4" }, { "function": "Coats the epithelia of the intestines and other mucus membrane-containing organs to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces (PubMed:17058067, PubMed:19432394, PubMed:33031746). Major constituent of the colon mucus, which is mainly formed by large polymeric networks of MUC2 secreted by goblet cells that cover the exposed surfaces of intestine (PubMed:19432394, PubMed:33031746). MUC2 networks form hydrogels that guard the underlying epithelium from pathogens and other hazardous matter entering from the outside world, while permitting nutrient absorption and gas exchange (PubMed:33031746, PubMed:36206754). Acts as a divalent copper chaperone that protects intestinal cells from copper toxicity and facilitates nutritional copper unptake into cells (PubMed:36206754). Binds both Cu(2+) and its reduced form, Cu(1+), at two juxtaposed binding sites: Cu(2+), once reduced to Cu(1+) by vitamin C (ascorbate) or other dietary antioxidants, transits to the other binding site (PubMed:36206754). MUC2-bound Cu(1+) is protected from oxidation in aerobic environments, and can be released for nutritional delivery to cells (PubMed:36206754). Mucin gels store antimicrobial molecules that participate in innate immunity (PubMed:33031746). Mucin glycoproteins also house and feed the microbiome, lubricate tissue surfaces, and may facilitate the removal of contaminants and waste products from the body (PubMed:33031746). Goblet cells synthesize two forms of MUC2 mucin that differ in branched chain O-glycosylation and the site of production in the colon: a (1) 'thick' mucus that wraps the microbiota to form fecal pellets is produced in the proximal, ascending colon (By similarity). 'Thick' mucus transits along the descending colon and is lubricated by a (2) 'thin' MUC2 mucus produced in the distal colon which adheres to the 'thick' mucus (By similarity)", "gene_name": "MUC2", "glycan_count": 55, "glycosylation_sites": [ { "position": 163, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 423, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 670, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 770, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 894, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1139, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1154, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1215, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1230, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1246, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1266, "type": "O-linked (GalNAc) threonine" }, { "position": 1267, "type": "O-linked (GalNAc) threonine" }, { "position": 1269, "type": "O-linked (GalNAc) threonine" }, { "position": 1270, "type": "O-linked (GalNAc) threonine" }, { "position": 1272, "type": "O-linked (GalNAc) threonine" }, { "position": 1275, "type": "O-linked (GalNAc) threonine" }, { "position": 1276, "type": "O-linked (GalNAc) threonine" }, { "position": 1281, "type": "O-linked (GalNAc) threonine" }, { "position": 1282, "type": "O-linked (GalNAc) threonine" }, { "position": 1287, "type": "O-linked (GalNAc) threonine" }, { "position": 1291, "type": "O-linked (GalNAc) serine" }, { "position": 1292, "type": "O-linked (GalNAc) serine" }, { "position": 1293, "type": "O-linked (GalNAc) threonine" }, { "position": 1296, "type": "O-linked (GalNAc) serine" }, { "position": 1297, "type": "O-linked (GalNAc) threonine" }, { "position": 1787, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1820, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4449, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4461, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4472, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4483, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4532, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4548, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4612, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4726, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4737, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4862, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4897, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4991, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4998, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5065, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5080, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5129, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5148, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5179, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q02817", "name": "Mucin 2", "organism": "Homo sapiens", "uniprot_id": "Q02817" }, { "function": "Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively (PubMed:11724794, PubMed:3170585). Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate (PubMed:11724794, PubMed:3170585). Modulates the organization and assembly of the cytoskeleton (By similarity). Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (By similarity). Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes (PubMed:23071094). Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation (PubMed:23071094). Also plays a role in innate immunity by promoting TNF-induced NF-kappa-B activation and type I interferon production, via interaction with TRAF2 and TRAF3, respectively (PubMed:23332158, PubMed:27387501). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis (By similarity). Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity)", "gene_name": "GAPDH", "glycan_count": 20, "glycosylation_sites": [ { "position": 197, "type": "(Microbial infection) N-beta-linked (GlcNAc) arginine" }, { "position": 200, "type": "(Microbial infection) N-beta-linked (GlcNAc) arginine" } ], "id": "P04406", "name": "GAPDH", "organism": "Homo sapiens", "uniprot_id": "P04406" }, { "function": "Multifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair and genome stability (PubMed:33147444). Proposed to be an universal biosensor for nucleic acids. Promotes host inflammatory response to sterile and infectious signals and is involved in the coordination and integration of innate and adaptive immune responses. In the cytoplasm functions as a sensor and/or chaperone for immunogenic nucleic acids implicating the activation of TLR9-mediated immune responses, and mediates autophagy. Acts as a danger-associated molecular pattern (DAMP) molecule that amplifies immune responses during tissue injury (PubMed:27362237). Released to the extracellular environment can bind DNA, nucleosomes, IL-1 beta, CXCL12, AGER isoform 2/sRAGE, lipopolysaccharide (LPS) and lipoteichoic acid (LTA), and activates cells through engagement of multiple surface receptors (PubMed:34743181). In the extracellular compartment fully reduced HMGB1 (released by necrosis) acts as a chemokine, disulfide HMGB1 (actively secreted) as a cytokine, and sulfonyl HMGB1 (released from apoptotic cells) promotes immunological tolerance (PubMed:23446148, PubMed:23519706, PubMed:23994764, PubMed:25048472). Has proangiogdenic activity (By similarity). May be involved in platelet activation (By similarity). Binds to phosphatidylserine and phosphatidylethanolamide (By similarity). Bound to RAGE mediates signaling for neuronal outgrowth (By similarity). May play a role in accumulation of expanded polyglutamine (polyQ) proteins such as huntingtin (HTT) or TBP (PubMed:23303669, PubMed:25549101)", "gene_name": "HMGB1", "glycan_count": 4, "glycosylation_sites": [], "id": "P09429", "name": "HMGB1", "organism": "Homo sapiens", "uniprot_id": "P09429" }, { "function": "Functions as a transcription factor during endoplasmic reticulum (ER) stress by regulating the unfolded protein response (UPR). Required for cardiac myogenesis and hepatogenesis during embryonic development, and the development of secretory tissues such as exocrine pancreas and salivary gland (By similarity). Involved in terminal differentiation of B lymphocytes to plasma cells and production of immunoglobulins (PubMed:11460154). Modulates the cellular response to ER stress in a PIK3R-dependent manner (PubMed:20348923). Binds to the cis-acting X box present in the promoter regions of major histocompatibility complex class II genes (PubMed:8349596). Involved in VEGF-induced endothelial cell (EC) proliferation and retinal blood vessel formation during embryonic development but also for angiogenesis in adult tissues under ischemic conditions. Also functions as a major regulator of the UPR in obesity-induced insulin resistance and type 2 diabetes for the management of obesity and diabetes prevention (By similarity)", "gene_name": "XBP1", "glycan_count": 0, "glycosylation_sites": [], "id": "P17861", "name": "XBP1", "organism": "Homo sapiens", "uniprot_id": "P17861" }, { "function": "Self-ligand receptor of the signaling lymphocytic activation molecule (SLAM) family. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. Triggers cytolytic activity only in natural killer cells (NK) expressing high surface densities of natural cytotoxicity receptors (PubMed:11489943, PubMed:16920955). Positive signaling in NK cells implicates phosphorylation of VAV1. NK cell activation seems to depend on SH2D1B and not on SH2D1A (PubMed:16920955). In conjunction with SLAMF1 controls the transition between positive selection and the subsequent expansion and differentiation of the thymocytic natural killer T (NKT) cell lineage (By similarity). Promotes T-cell differentiation into a helper T-cell Th17 phenotype leading to increased IL-17 secretion; the costimulatory activity requires SH2D1A (PubMed:16920955, PubMed:22184727). Promotes recruitment of RORC to the IL-17 promoter (PubMed:22989874). In conjunction with SLAMF1 and CD84/SLAMF5 may be a negative regulator of the humoral immune response. In the absence of SH2D1A/SAP can transmit negative signals to CD4(+) T-cells and NKT cells. Negatively regulates germinal center formation by inhibiting T-cell:B-cell adhesion; the function probably implicates increased association with PTPN6/SHP-1 via ITSMs in absence of SH2D1A/SAP. However, reported to be involved in maintaining B-cell tolerance in germinal centers and in preventing autoimmunity (By similarity)", "gene_name": "SLAMF6", "glycan_count": 1, "glycosylation_sites": [ { "position": 58, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 87, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 137, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 144, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 161, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 178, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 203, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q96DU3", "name": "SLAMF6", "organism": "Homo sapiens", "uniprot_id": "Q96DU3" }, { "function": "Transfers sialic acid from CMP-sialic acid to galactose-containing acceptor substrates. In B lymphocytes, generates neuraminidase-sensitive lymphocyte cell-surface differentiation antigens, such as CDw75, HB-6 and CD76 (PubMed:1730763)", "gene_name": "ST6GAL1", "glycan_count": 3, "glycosylation_sites": [ { "position": 149, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 161, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P15907", "name": "ST6GAL1", "organism": "Homo sapiens", "uniprot_id": "P15907" }, { "function": "Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class II molecule:peptide complex. The antigens presented by class II peptides are derived from extracellular proteins while class I peptides are derived from cytosolic proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class II presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of T-helper cells. In other cells such as macrophages or NK cells, plays a role in differentiation/activation, cytokine expression and cell migration in a TCR/LCK-independent pathway. Participates in the development of T-helper cells in the thymus and triggers the differentiation of monocytes into functional mature macrophages", "gene_name": "CD4", "glycan_count": 58, "glycosylation_sites": [ { "position": 296, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 325, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01730", "name": "CD4", "organism": "Homo sapiens", "uniprot_id": "P01730" }, { "function": "Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs). Mediates the association between the ESCRT-0 and ESCRT-I complex. Required for completion of cytokinesis; the function requires CEP55. May be involved in cell growth and differentiation. Acts as a negative growth regulator. Involved in the budding of many viruses through an interaction with viral proteins that contain a late-budding motif P-[ST]-A-P. This interaction is essential for viral particle budding of numerous retroviruses. Required for the exosomal release of SDCBP, CD63 and syndecan (PubMed:22660413). It may also play a role in the extracellular release of microvesicles that differ from the exosomes (PubMed:22315426)", "gene_name": "TSG101", "glycan_count": 1, "glycosylation_sites": [], "id": "Q99816", "name": "TSG101", "organism": "Homo sapiens", "uniprot_id": "Q99816" }, { "function": "Could be a melanogenic enzyme", "gene_name": "GPNMB", "glycan_count": 211, "glycosylation_sites": [ { "position": 93, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 134, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 146, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 200, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 249, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 275, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 296, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 300, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 306, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 312, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 459, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 467, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q14956", "name": "Glycoprotein Non-Metastatic Melanoma Protein B (GPNMB)", "organism": "Homo sapiens", "uniprot_id": "Q14956" }, { "function": "", "gene_name": "CD44", "glycan_count": 0, "glycosylation_sites": [], "id": "P16070-9", "name": "CD44v9", "organism": "Homo sapiens", "uniprot_id": "P16070-9" }, { "function": "May act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for providing immunological barrier as a first line of defense against mucosal infection. Plays a role in embryonic stem cells proliferation and differentiation. Up-regulates the expression of FABP5, MYC and cyclins A and E", "gene_name": "EPCAM", "glycan_count": 65, "glycosylation_sites": [ { "position": 74, "type": "N-linked (GlcNAc...) asparagine; partial" }, { "position": 111, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 198, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P16422", "name": "EpCAM", "organism": "Homo sapiens", "uniprot_id": "P16422" }, { "function": "Acute phase-regulated receptor involved in clearance and endocytosis of hemoglobin/haptoglobin complexes by macrophages and may thereby protect tissues from free hemoglobin-mediated oxidative damage. May play a role in the uptake and recycling of iron, via endocytosis of hemoglobin/haptoglobin and subsequent breakdown of heme. Binds hemoglobin/haptoglobin complexes in a calcium-dependent and pH-dependent manner. Exhibits a higher affinity for complexes of hemoglobin and multimeric haptoglobin of HP*1F phenotype than for complexes of hemoglobin and dimeric haptoglobin of HP*1S phenotype. Induces a cascade of intracellular signals that involves tyrosine kinase-dependent calcium mobilization, inositol triphosphate production and secretion of IL6 and CSF1. Isoform 3 exhibits the higher capacity for ligand endocytosis and the more pronounced surface expression when expressed in cells", "gene_name": "CD163", "glycan_count": 74, "glycosylation_sites": [ { "position": 105, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 140, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 767, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1027, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q86VB7", "name": "CD163", "organism": "Homo sapiens", "uniprot_id": "Q86VB7" }, { "function": "May play a role in cell differentiation, proliferation and apoptosis (PubMed:24556617). Binds cholesterol in cholesterol-containing plasma membrane microdomains and may play a role in the organization of the apical plasma membrane in epithelial cells. During early retinal development acts as a key regulator of disk morphogenesis. Involved in regulation of MAPK and Akt signaling pathways. In neuroblastoma cells suppresses cell differentiation such as neurite outgrowth in a RET-dependent manner (PubMed:20818439)", "gene_name": "PROM1", "glycan_count": 40, "glycosylation_sites": [ { "position": 220, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 274, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 395, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 414, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 548, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 580, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 729, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 730, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O43490", "name": "PROM1", "organism": "Homo sapiens", "uniprot_id": "O43490" }, { "function": "Catalyzes alpha(1->3) linkage of fucosyl moiety transferred from GDP-beta-L-fucose to N-acetyl glucosamine (GlcNAc) within type 2 lactosamine (LacNAc, Gal-beta(1->4)GlcNAc) glycan attached to N- or O-linked glycoproteins (PubMed:1702034, PubMed:1716630, PubMed:29593094). Robustly fucosylates nonsialylated distal LacNAc unit of the polylactosamine chain to form Lewis X antigen (CD15), a glycan determinant known to mediate important cellular functions in development and immunity. Fucosylates with lower efficiency sialylated LacNAc acceptors to form sialyl Lewis X and 6-sulfo sialyl Lewis X determinants that serve as recognition epitopes for C-type lectins (PubMed:1716630, PubMed:29593094). Together with FUT7 contributes to SELE, SELL and SELP selectin ligand biosynthesis and selectin-dependent lymphocyte homing, leukocyte migration and blood leukocyte homeostasis (By similarity). In a cell type specific manner, may also fucosylate the internal LacNAc unit of the polylactosamine chain to form VIM-2 antigen that serves as recognition epitope for SELE (PubMed:11278338, PubMed:1716630)", "gene_name": "FUT4", "glycan_count": 3, "glycosylation_sites": [ { "position": 216, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 315, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P22083", "name": "FUT4", "organism": "Homo sapiens", "uniprot_id": "P22083" }, { "function": "Heterodimer with SLC3A2, that functions as an antiporter by mediating the exchange of extracellular anionic L-cystine and intracellular L-glutamate across the cellular plasma membrane (PubMed:11133847, PubMed:11417227, PubMed:14722095, PubMed:15151999, PubMed:34880232, PubMed:35245456, PubMed:35352032). Provides L-cystine for the maintenance of the redox balance between extracellular L-cystine and L-cysteine and for the maintenance of the intracellular levels of glutathione that is essential for cells protection from oxidative stress (By similarity). The transport is sodium-independent, electroneutral with a stoichiometry of 1:1, and is drove by the high intracellular concentration of L-glutamate and the intracellular reduction of L-cystine (PubMed:11133847, PubMed:11417227). In addition, mediates the import of L-kynurenine leading to anti-ferroptotic signaling propagation required to maintain L-cystine and glutathione homeostasis (PubMed:35245456). Moreover, mediates N-acetyl-L-cysteine uptake into the placenta leading to subsequently down-regulation of pathways associated with oxidative stress, inflammation and apoptosis (PubMed:34120018). In vitro can also transport L-aspartate (PubMed:11417227). May participate in astrocyte and meningeal cell proliferation during development and can provide neuroprotection by promoting glutathione synthesis and delivery from non-neuronal cells such as astrocytes and meningeal cells to immature neurons (By similarity). Controls the production of pheomelanin pigment directly (By similarity)", "gene_name": "SLC7A11", "glycan_count": 1, "glycosylation_sites": [ { "position": 314, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UPY5", "name": "SLC7A11", "organism": "Homo sapiens", "uniprot_id": "Q9UPY5" }, { "function": "Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver", "gene_name": "INS", "glycan_count": 0, "glycosylation_sites": [], "id": "P01308", "name": "Insulin", "organism": "Homo sapiens", "uniprot_id": "P01308" }, { "function": "Biosynthesis of L-glutamate from L-aspartate or L-cysteine (PubMed:21900944). Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involved in hepatic glucose synthesis during development and in adipocyte glyceroneogenesis. Using L-cysteine as substrate, regulates levels of mercaptopyruvate, an important source of hydrogen sulfide. Mercaptopyruvate is converted into H(2)S via the action of 3-mercaptopyruvate sulfurtransferase (3MST). Hydrogen sulfide is an important synaptic modulator and neuroprotectant in the brain. In addition, catalyzes (2S)-2-aminobutanoate, a by-product in the cysteine biosynthesis pathway (PubMed:27827456)", "gene_name": "GOT1", "glycan_count": 1, "glycosylation_sites": [], "id": "P17174", "name": "Aspartate aminotransferase (AST)", "organism": "Homo sapiens", "uniprot_id": "P17174" }, { "function": "Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate. Participates in cellular nitrogen metabolism and also in liver gluconeogenesis starting with precursors transported from skeletal muscles (By similarity)", "gene_name": "GPT", "glycan_count": 0, "glycosylation_sites": [], "id": "P24298", "name": "Alanine aminotransferase (ALT)", "organism": "Homo sapiens", "uniprot_id": "P24298" }, { "function": "Catalyzes the deacylation of cholesteryl ester core lipids of endocytosed low density lipoproteins to generate free fatty acids and cholesterol (PubMed:15269241, PubMed:1718995, PubMed:7204383, PubMed:8112342, PubMed:9633819). Hydrolyzes triglycerides (1,2,3-triacylglycerol) and diglycerides (such as 1,2-diacylglycerol and 1,3-diacylglycerol) with preference for the acyl moieties at the sn-1 or sn-3 positions (PubMed:7204383, PubMed:8112342)", "gene_name": "LIPA", "glycan_count": 46, "glycosylation_sites": [ { "position": 36, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 72, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 101, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 161, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 273, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 321, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P38571", "name": "Lysosomal acid lipase (LIPA/LAL)", "organism": "Homo sapiens", "uniprot_id": "P38571" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01308-2", "name": "C-peptide", "organism": "", "uniprot_id": "" }, { "function": "Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing. Activates coagulation factor XI (F11); activation is promoted by the contact with negatively charged surfaces (PubMed:2019570, PubMed:21976677). Triggers the production of pro-inflammatory cytokines, such as MCP-1/CCL2 and IL8/CXCL8, in endothelial cells (PubMed:30568593, PubMed:9780208)", "gene_name": "F2", "glycan_count": 100, "glycosylation_sites": [ { "position": 121, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 143, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 416, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P00734", "name": "Prothrombin", "organism": "Homo sapiens", "uniprot_id": "P00734" }, { "function": "Major transport protein for glucocorticoids and progestins in the blood of almost all vertebrate species", "gene_name": "SERPINA6", "glycan_count": 79, "glycosylation_sites": [ { "position": 31, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 96, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 176, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 260, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 330, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 369, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08185", "name": "Cortisol-binding globulin", "organism": "Homo sapiens", "uniprot_id": "P08185" }, { "function": "Receptor for the thyroid-stimulating hormone (TSH) or thyrotropin (PubMed:11847099, PubMed:12045258). Also acts as a receptor for the heterodimeric glycoprotein hormone (GPHA2:GPHB5) or thyrostimulin (PubMed:12045258). The activity of this receptor is mediated by G proteins which activate adenylate cyclase (PubMed:11847099). Plays a central role in controlling thyroid cell metabolism (By similarity)", "gene_name": "TSHR", "glycan_count": 3, "glycosylation_sites": [ { "position": 77, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 99, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 113, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 177, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 198, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 302, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P16473", "name": "Thyroid Stimulating Hormone Receptor (TSHR)", "organism": "Homo sapiens", "uniprot_id": "P16473" }, { "function": "Alkaline phosphatase that metabolizes various phosphate compounds and plays a key role in skeletal mineralization and adaptive thermogenesis (PubMed:12162492, PubMed:23688511, PubMed:25982064). Has broad substrate specificity and can hydrolyze a considerable variety of compounds: however, only a few substrates, such as diphosphate (inorganic pyrophosphate; PPi), pyridoxal 5'-phosphate (PLP) and N-phosphocreatine are natural substrates (PubMed:12162492, PubMed:2220817). Plays an essential role in skeletal and dental mineralization via its ability to hydrolyze extracellular diphosphate, a potent mineralization inhibitor, to phosphate: it thereby promotes hydroxyapatite crystal formation and increases inorganic phosphate concentration (PubMed:23688511, PubMed:25982064). Acts in a non-redundant manner with PHOSPHO1 in skeletal mineralization: while PHOSPHO1 mediates the initiation of hydroxyapatite crystallization in the matrix vesicles (MVs), ALPL/TNAP catalyzes the spread of hydroxyapatite crystallization in the extracellular matrix (By similarity). Also promotes dephosphorylation of osteopontin (SSP1), an inhibitor of hydroxyapatite crystallization in its phosphorylated state; it is however unclear whether ALPL/TNAP mediates SSP1 dephosphorylation via a direct or indirect manner (By similarity). Catalyzes dephosphorylation of PLP to pyridoxal (PL), the transportable form of vitamin B6, in order to provide a sufficient amount of PLP in the brain, an essential cofactor for enzymes catalyzing the synthesis of diverse neurotransmitters (PubMed:20049532, PubMed:2220817). Additionally, also able to mediate ATP degradation in a stepwise manner to adenosine, thereby regulating the availability of ligands for purinergic receptors (By similarity). Also capable of dephosphorylating microbial products, such as lipopolysaccharides (LPS) as well as other phosphorylated small-molecules, such as poly-inosine:cytosine (poly I:C) (PubMed:28448526). Acts as a key regulator of adaptive thermogenesis as part of the futile creatine cycle: localizes to the mitochondria of thermogenic fat cells and acts by mediating hydrolysis of N-phosphocreatine to initiate a futile cycle of creatine dephosphorylation and phosphorylation (By similarity). During the futile creatine cycle, creatine and N-phosphocreatine are in a futile cycle, which dissipates the high energy charge of N-phosphocreatine as heat without performing any mechanical or chemical work (By similarity)", "gene_name": "ALPL", "glycan_count": 38, "glycosylation_sites": [ { "position": 140, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 230, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 271, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 303, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 430, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P05186", "name": "Alkaline phosphatase (ALP)", "organism": "Homo sapiens", "uniprot_id": "P05186" }, { "function": "The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. May be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. Stimulates glucose transport in bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also with regard to enhancing glucose uptake. May play a role in synapse maturation (PubMed:21076856, PubMed:24132240). Ca(2+)-dependent exocytosis of IGF1 is required for sensory perception of smell in the olfactory bulb (By similarity). Acts as a ligand for IGF1R. Binds to the alpha subunit of IGF1R, leading to the activation of the intrinsic tyrosine kinase activity which autophosphorylates tyrosine residues in the beta subunit thus initiating a cascade of down-stream signaling events leading to activation of the PI3K-AKT/PKB and the Ras-MAPK pathways. Binds to integrins ITGAV:ITGB3 and ITGA6:ITGB4. Its binding to integrins and subsequent ternary complex formation with integrins and IGFR1 are essential for IGF1 signaling. Induces the phosphorylation and activation of IGFR1, MAPK3/ERK1, MAPK1/ERK2 and AKT1 (PubMed:19578119, PubMed:22351760, PubMed:23243309, PubMed:23696648). As part of the MAPK/ERK signaling pathway, acts as a negative regulator of apoptosis in cardiomyocytes via promotion of STUB1/CHIP-mediated ubiquitination and degradation of ICER-type isoforms of CREM (By similarity)", "gene_name": "IGF1", "glycan_count": 0, "glycosylation_sites": [], "id": "P05019", "name": "Insulin-like growth factor-1 (IGF-1)", "organism": "Homo sapiens", "uniprot_id": "P05019" }, { "function": "Multifunctional protein that plays a critical role in regulating the availability of IGFs such as IGF1 and IGF2 to their receptors and thereby regulates IGF-mediated cellular processes including proliferation, differentiation, and apoptosis in a cell-type specific manner (PubMed:10874028, PubMed:19556345). Also exhibits IGF-independent antiproliferative and apoptotic effects mediated by its receptor TMEM219/IGFBP-3R (PubMed:20353938). Inhibits the positive effect of humanin on insulin sensitivity (PubMed:19623253). Promotes testicular germ cell apoptosis (PubMed:19952275). Acts via LRP-1/alpha2M receptor, also known as TGF-beta type V receptor, to mediate cell growth inhibition independent of IGF1 (PubMed:9252371). Mechanistically, induces serine-specific dephosphorylation of IRS1 or IRS2 upon ligation to its receptor, leading to the inhibitory cascade (PubMed:15371331). In the nucleus, interacts with transcription factors such as retinoid X receptor-alpha/RXRA to regulate transcriptional signaling and apoptosis (PubMed:10874028)", "gene_name": "IGFBP3", "glycan_count": 28, "glycosylation_sites": [ { "position": 116, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 136, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 199, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P17936", "name": "IGF binding protein 3 (IGFBP3)", "organism": "Homo sapiens", "uniprot_id": "P17936" }, { "function": "Receptor for interleukin-11 (IL11). The receptor systems for IL6, LIF, OSM, CNTF, IL11 and CT1 can utilize IL6ST for initiating signal transmission. The IL11/IL11RA/IL6ST complex may be involved in the control of proliferation and/or differentiation of skeletogenic progenitor or other mesenchymal cells (Probable). Essential for the normal development of craniofacial bones and teeth. Restricts suture fusion and tooth number", "gene_name": "IL11RA", "glycan_count": 2, "glycosylation_sites": [ { "position": 127, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 194, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q14626", "name": "Acid-labile subunit (ALS)", "organism": "Homo sapiens", "uniprot_id": "Q14626" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Not mentioned", "name": "Glycoprotein Non-Metastatic Melanoma Protein B (GPNMB)", "organism": "", "uniprot_id": "" }, { "function": "Catalyzes the electroneutral exchange or flux of physiologically important metabolites such as dicarboxylates (malonate, malate, succinate), inorganic sulfur-containing anions, and phosphate, across mitochondrial inner membrane (PubMed:29211846). Plays an important role in gluconeogenesis, fatty acid metabolism, urea synthesis, and sulfur metabolism, particularly in liver, by supplying the substrates for the different metabolic processes. Regulates fatty acid release from adipocytes, and contributes to systemic insulin sensitivity (By similarity)", "gene_name": "SLC25A10", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UBX3", "name": "Fukutin (FKTN)", "organism": "Homo sapiens", "uniprot_id": "Q9UBX3" }, { "function": "Component of clathrin-coated vesicles (PubMed:15758025). Component of the aftiphilin/p200/gamma-synergin complex, which plays roles in AP1G1/AP-1-mediated protein trafficking including the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes (PubMed:15758025)", "gene_name": "HEATR5B", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9P2D3", "name": "LARGE1", "organism": "Homo sapiens", "uniprot_id": "Q9P2D3" }, { "function": "Calcium-regulated non-lysosomal thiol-protease. Proteolytically cleaves CTBP1 at 'His-409'. Mediates, with UTP25, the proteasome-independent degradation of p53/TP53 (PubMed:23357851, PubMed:27657329)", "gene_name": "CAPN3", "glycan_count": 2, "glycosylation_sites": [], "id": "P20807", "name": "Calpain-3 (CAPN3)", "organism": "Homo sapiens", "uniprot_id": "P20807" }, { "function": "Key calcium ion sensor involved in the Ca(2+)-triggered synaptic vesicle-plasma membrane fusion. Plays a role in the sarcolemma repair mechanism of both skeletal muscle and cardiomyocytes that permits rapid resealing of membranes disrupted by mechanical stress (By similarity)", "gene_name": "DYSF", "glycan_count": 1, "glycosylation_sites": [], "id": "O75923", "name": "Dysferlin (DYSF)", "organism": "Homo sapiens", "uniprot_id": "O75923" }, { "function": "Catalytic subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (PubMed:19167329, PubMed:31296534, PubMed:31831667, PubMed:39509507). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER) (PubMed:19167329, PubMed:31296534, PubMed:31831667, PubMed:39509507). All subunits are required for a maximal enzyme activity. This subunit contains the active site and the acceptor peptide and donor lipid-linked oligosaccharide (LLO) binding pockets (PubMed:19167329, PubMed:31296534, PubMed:31831667, PubMed:39509507). STT3B is present in a small subset of OST complexes (OST-B) and mediates both cotranslational and post-translational N-glycosylation of target proteins: STT3B-containing complexes are required for efficient post-translational glycosylation and while they are less competent than STT3A-containing complexes for cotranslational glycosylation, they have the ability to mediate glycosylation of some nascent sites that are not accessible for STT3A (PubMed:19167329, PubMed:22607976, PubMed:31296534, PubMed:39509507). STT3B-containing complexes also act post-translationally and mediate modification of skipped glycosylation sites in unfolded proteins (PubMed:19167329, PubMed:22607976, PubMed:39509507). Plays a role in ER-associated degradation (ERAD) pathway that mediates ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins by mediating N-glycosylation of unfolded proteins, which are then recognized by the ERAD pathway and targeted for degradation (PubMed:19167329, PubMed:22607976). Mediates glycosylation of the disease variant AMYL-TTR 'Asp-38' of TTR at 'Asn-118', leading to its degradation (PubMed:19167329, PubMed:22607976)", "gene_name": "STT3B", "glycan_count": 47, "glycosylation_sites": [ { "position": 616, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 623, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 627, "type": "N-linked (GlcNAc...) (high mannose) asparagine" }, { "position": 641, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8TCJ2", "name": "STT3A", "organism": "Homo sapiens", "uniprot_id": "Q8TCJ2" }, { "function": "Component of triglyceride-rich very low density lipoproteins (VLDL) and high density lipoproteins (HDL) in plasma (PubMed:18201179, PubMed:22510806). Plays a multifaceted role in triglyceride homeostasis (PubMed:18201179, PubMed:22510806). Intracellularly, promotes hepatic very low density lipoprotein 1 (VLDL1) assembly and secretion; extracellularly, attenuates hydrolysis and clearance of triglyceride-rich lipoproteins (TRLs) (PubMed:18201179, PubMed:22510806). Impairs the lipolysis of TRLs by inhibiting lipoprotein lipase and the hepatic uptake of TRLs by remnant receptors (PubMed:18201179, PubMed:22510806). Formed of several curved helices connected via semiflexible hinges, so that it can wrap tightly around the curved micelle surface and easily adapt to the different diameters of its natural binding partners (PubMed:18408013)", "gene_name": "APOC3", "glycan_count": 10, "glycosylation_sites": [ { "position": 94, "type": "O-linked (GalNAc...) threonine" } ], "id": "P02656", "name": "Apolipoprotein CIII", "organism": "Homo sapiens", "uniprot_id": "P02656" }, { "function": "Exo-alpha-sialidase that catalyzes the hydrolytic cleavage of the terminal sialic acid (N-acetylneuraminic acid, Neu5Ac) of a glycan moiety in the catabolism of glycolipids, glycoproteins and oligosacharides (PubMed:14613940, PubMed:22228546). Recognizes sialyl linkage positions of the glycan moiety as well as the supramolecular organization of the sialoglycoconjugate. Displays preference for alpha-(2->3)-sialylated GD1a and GT1B gangliosides over alpha-(2->8)-sialylated GD1b, in both monomeric forms and micelles. Hydrolyzes monomeric GM1 ganglioside, but has no activity toward the miscellar form (PubMed:14613940). Has lower sialidase activity for glycoproteins such as fetuin and TF/transferrin that carry a mixture of alpha-(2->3) and alpha-(2->6)-sialyl linkages. Cleaves milk oligosaccharide alpha-(2->3)-sialyllactose, but is inactive toward alpha-(2->6)-sialyllactose isomer. Has no activity toward colominic acid, a homomer of alpha-(2->8)-linked Neu5Ac residues (PubMed:14613940)", "gene_name": "NEU2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y3R4", "name": "SIAT7A (ST6GalNAc I)", "organism": "Homo sapiens", "uniprot_id": "Q9Y3R4" }, { "function": "Transcription factor; can act both as activator and as repressor. Binds the 5'-CACCC-3' core sequence. Binds to the promoter region of its own gene and can activate its own transcription. Regulates the expression of key transcription factors during embryonic development. Plays an important role in maintaining embryonic stem cells, and in preventing their differentiation. Required for establishing the barrier function of the skin and for postnatal maturation and maintenance of the ocular surface. Involved in the differentiation of epithelial cells and may also function in skeletal and kidney development. Contributes to the down-regulation of p53/TP53 transcription", "gene_name": "KLF4", "glycan_count": 1, "glycosylation_sites": [], "id": "O43474", "name": "KLF4", "organism": "Homo sapiens", "uniprot_id": "O43474" }, { "function": "Plays a role in embryonic morphogenesis; it is involved in the regulation of endochondral skeleton formation, and the development of retinal pigment epithelium (RPE), photoreceptors and periocular tissues (By similarity)", "gene_name": "IHH", "glycan_count": 0, "glycosylation_sites": [ { "position": 282, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q14623", "name": "Laminin-211", "organism": "Homo sapiens", "uniprot_id": "Q14623" }, { "function": "Potential calcium-dependent cell-adhesion protein", "gene_name": "PCDH10", "glycan_count": 1, "glycosylation_sites": [ { "position": 273, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 557, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9P2E7", "name": "LARGE1", "organism": "Homo sapiens", "uniprot_id": "Q9P2E7" }, { "function": "Ubiquitous endoprotease within constitutive secretory pathways capable of cleavage at the RX(K/R)R consensus motif (PubMed:11799113, PubMed:1629222, PubMed:1713771, PubMed:2251280, PubMed:24666235, PubMed:25974265, PubMed:7592877, PubMed:7690548, PubMed:9130696). Mediates processing of TGFB1, an essential step in TGF-beta-1 activation (PubMed:7737999). Converts through proteolytic cleavage the non-functional Brain natriuretic factor prohormone into its active hormone BNP(1-32) (PubMed:20489134, PubMed:21763278). By mediating processing of accessory subunit ATP6AP1/Ac45 of the V-ATPase, regulates the acidification of dense-core secretory granules in islets of Langerhans cells (By similarity)", "gene_name": "FURIN", "glycan_count": 0, "glycosylation_sites": [ { "position": 387, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 440, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 553, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P09958", "name": "PACE (Furin)", "organism": "Homo sapiens", "uniprot_id": "P09958" }, { "function": "Cytokine that binds to TNFRSF3/LTBR. Binding to the decoy receptor TNFRSF6B modulates its effects. Acts as a ligand for TNFRSF14/HVEM (PubMed:10754304, PubMed:9462508). Upon binding to TNFRSF14/HVEM, delivers costimulatory signals to T cells, leading to T cell proliferation and IFNG production (PubMed:10754304)", "gene_name": "TNFSF14", "glycan_count": 0, "glycosylation_sites": [ { "position": 102, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O43557", "name": "Alpha-dystroglycan (\u03b1-DG)", "organism": "Homo sapiens", "uniprot_id": "O43557" }, { "function": "Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components", "gene_name": "LAMB3", "glycan_count": 5, "glycosylation_sites": [ { "position": 220, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 604, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 810, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13751", "name": "Laminin \u03b12", "organism": "Homo sapiens", "uniprot_id": "Q13751" }, { "function": "Catalyzes the hydrolysis of GTP and utilizes this energy to mediate vesicle scission at plasma membrane during endocytosis and filament remodeling at many actin structures during organization of the actin cytoskeleton (PubMed:15731758, PubMed:19605363, PubMed:19623537, PubMed:33713620, PubMed:34744632). Plays an important role in vesicular trafficking processes, namely clathrin-mediated endocytosis (CME), exocytic and clathrin-coated vesicle from the trans-Golgi network, and PDGF stimulated macropinocytosis (PubMed:15731758, PubMed:19623537, PubMed:33713620). During vesicular trafficking process, associates to the membrane, through lipid binding, and self-assembles into ring-like structure through oligomerization to form a helical polymer around the vesicle membrane and leading to vesicle scission (PubMed:17636067, PubMed:34744632, PubMed:36445308). Plays a role in organization of the actin cytoskeleton by mediating arrangement of stress fibers and actin bundles in podocytes (By similarity). During organization of the actin cytoskeleton, self-assembles into ring-like structure that directly bundles actin filaments to form typical membrane tubules decorated with dynamin spiral polymers (By similarity). Self-assembly increases GTPase activity and the GTP hydrolysis causes the rapid depolymerization of dynamin spiral polymers, and results in dispersion of actin bundles (By similarity). Remodels, through its interaction with CTTN, bundled actin filaments in a GTPase-dependent manner and plays a role in orchestrating the global actomyosin cytoskeleton (PubMed:19605363). The interaction with CTTN stabilizes the interaction of DNM2 and actin filaments and stimulates the intrinsic GTPase activity that results in actin filament-barbed ends and increases the sensitivity of filaments in bundles to the actin depolymerizing factor, CFL1 (By similarity). Plays a role in the autophagy process, by participating in the formation of ATG9A vesicles destined for the autophagosomes through its interaction with SNX18 (PubMed:29437695), by mediating recycling endosome scission leading to autophagosome release through MAP1LC3B interaction (PubMed:29437695, PubMed:32315611). Also regulates maturation of apoptotic cell corpse-containing phagosomes by recruiting PIK3C3 to the phagosome membrane (By similarity). Also plays a role in cytokinesis (By similarity). May participate in centrosome cohesion through its interaction with TUBG1 (By similarity). Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones (By similarity). Involved in membrane tubulation (PubMed:24135484)", "gene_name": "DNM2", "glycan_count": 2, "glycosylation_sites": [], "id": "P50570", "name": "Dynamin-2 (Dyn2)", "organism": "Homo sapiens", "uniprot_id": "P50570" }, { "function": "The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs (PubMed:18984161, PubMed:9845364). Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core) (PubMed:18984161). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP (PubMed:18984161). To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate (PubMed:18984161). Within the SMN complex, SMN1 acts as a structural backbone and together with GEMIN2 it gathers the Sm complex subunits (PubMed:17178713, PubMed:21816274, PubMed:22101937). Binding of snRNA inside 5Sm ultimately triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP (PubMed:31799625). Ensures the correct splicing of U12 intron-containing genes that may be important for normal motor and proprioceptive neurons development (PubMed:23063131). Also required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination (PubMed:26700805). May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs)", "gene_name": "SMN1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q16637", "name": "SMN protein", "organism": "Homo sapiens", "uniprot_id": "Q16637" }, { "function": "Non-receptor serine/threonine protein kinase which is necessary for the maintenance of skeletal muscle structure and function. May play a role in myocyte differentiation and survival by regulating the integrity of the nuclear envelope and the expression of muscle-specific genes. May also phosphorylate PPP1R12A and inhibit the myosin phosphatase activity to regulate myosin phosphorylation. Also critical to the modulation of cardiac contractility and to the maintenance of proper cardiac conduction activity probably through the regulation of cellular calcium homeostasis. Phosphorylates PLN, a regulator of calcium pumps and may regulate sarcoplasmic reticulum calcium uptake in myocytes. May also phosphorylate FXYD1/PLM which is able to induce chloride currents. May also play a role in synaptic plasticity", "gene_name": "DMPK", "glycan_count": 0, "glycosylation_sites": [], "id": "Q09013", "name": "DMPK", "organism": "Homo sapiens", "uniprot_id": "Q09013" }, { "function": "Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate (PubMed:20477940, PubMed:26690923, PubMed:28032905, PubMed:28424515, PubMed:7521911, PubMed:8123008). Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion (PubMed:20477940). Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport (PubMed:20477940). Plays a redundant role in the rapid removal of released glutamate from the synaptic cleft, which is essential for terminating the postsynaptic action of glutamate (By similarity)", "gene_name": "SLC1A3", "glycan_count": 4, "glycosylation_sites": [], "id": "P43003", "name": "GLT1 (EAAT2)", "organism": "Homo sapiens", "uniprot_id": "P43003" }, { "function": "May be responsible for potassium buffering action of glial cells in the brain (By similarity). Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it (PubMed:8995301). Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages (PubMed:8995301). The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium and cesium (PubMed:8995301). In the kidney, together with KCNJ16, mediates basolateral K(+) recycling in distal tubules; this process is critical for Na(+) reabsorption at the tubules (PubMed:24561201)", "gene_name": "KCNJ10", "glycan_count": 0, "glycosylation_sites": [], "id": "P78508", "name": "Kir4.1", "organism": "Homo sapiens", "uniprot_id": "P78508" }, { "function": "Forms a water-specific channel (PubMed:19383790, PubMed:7559426, PubMed:8601457). Plays an important role in brain water homeostasis (PubMed:37143309). It is involved in glymphatic solute transport and is required for a normal rate of water exchange across the blood brain interface. Required for normal levels of cerebrospinal fluid influx into the brain cortex and parenchyma along paravascular spaces that surround penetrating arteries, and for normal drainage of interstitial fluid along paravenous drainage pathways. Thereby, it is required for normal clearance of solutes from the brain interstitial fluid, including soluble beta-amyloid peptides derived from APP. Plays a redundant role in urinary water homeostasis and urinary concentrating ability (By similarity)", "gene_name": "AQP4", "glycan_count": 0, "glycosylation_sites": [ { "position": 153, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 206, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P55087", "name": "Aquaporin-4 (AQP4)", "organism": "Homo sapiens", "uniprot_id": "P55087" }, { "function": "Epithelial and hemopoietic transmembrane mucin that may play a role in cell signaling", "gene_name": "Muc13", "glycan_count": 0, "glycosylation_sites": [ { "position": 266, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 316, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 397, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P19467", "name": "Gamma-glutamyl transferase (GGT)", "organism": "Mus musculus", "uniprot_id": "P19467" }, { "function": "Gel-forming mucin that is thought to contribute to the lubricating and viscoelastic properties of whole saliva and cervical mucus", "gene_name": "MUC5B", "glycan_count": 47, "glycosylation_sites": [ { "position": 145, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 201, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 254, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 401, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 515, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 805, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 929, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1276, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1292, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1340, "type": "C-linked (Man) tryptophan" }, { "position": 1509, "type": "C-linked (Man) tryptophan" }, { "position": 1556, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1774, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1790, "type": "C-linked (Man) tryptophan" }, { "position": 2320, "type": "C-linked (Man) tryptophan" }, { "position": 2749, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2877, "type": "C-linked (Man) tryptophan" }, { "position": 3449, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3577, "type": "C-linked (Man) tryptophan" }, { "position": 4006, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4134, "type": "C-linked (Man) tryptophan" }, { "position": 4804, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4960, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5017, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5024, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5046, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5096, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5111, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5215, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5486, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5526, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5565, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5566, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5602, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5612, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5663, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5677, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5721, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9HC84", "name": "MUC5B", "organism": "Homo sapiens", "uniprot_id": "Q9HC84" }, { "function": "Thought to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces", "gene_name": "MUC16", "glycan_count": 23, "glycosylation_sites": [ { "position": 139, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 434, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 787, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 930, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 957, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1375, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1633, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1840, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1877, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1890, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2345, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2375, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2737, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3085, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3178, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3501, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4220, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4498, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4606, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4613, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4624, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4861, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5096, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5131, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5228, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5320, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5394, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5470, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5689, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5863, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 6088, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 6732, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 6859, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 6961, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 8029, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 8055, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 8324, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 8618, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 8684, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 8913, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 9202, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 9493, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 9785, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 10075, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 10173, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 10510, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 10700, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 10749, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 11053, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 11224, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 11263, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 11367, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 11594, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 12079, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 12100, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 12116, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 12168, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 12235, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 12272, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 12393, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 12414, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 12430, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 12549, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 12570, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 12586, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 12704, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 12725, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 12741, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 12824, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 12860, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 12881, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 12897, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 13016, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 13037, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 13053, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 13172, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 13193, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 13328, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 13349, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 13365, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 13484, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 13505, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 13521, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 13640, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 13661, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 13733, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 13744, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 13796, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 13816, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 13832, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 13929, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 13950, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 14080, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 14100, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 14195, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 14212, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 14254, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 14287, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 14326, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 14363, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 14417, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 14423, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8WXI7", "name": "MUC16", "organism": "Homo sapiens", "uniprot_id": "Q8WXI7" }, { "function": "Cell surface receptor implicated in modulating innate and adaptive immune responses. Generally accepted to have an inhibiting function. Reports on stimulating functions suggest that the activity may be influenced by the cellular context and/or the respective ligand (PubMed:24825777). Regulates macrophage activation (PubMed:11823861). Inhibits T-helper type 1 lymphocyte (Th1)-mediated auto- and alloimmune responses and promotes immunological tolerance (PubMed:14556005). In CD8+ cells attenuates TCR-induced signaling, specifically by blocking NF-kappaB and NFAT promoter activities resulting in the loss of IL-2 secretion. The function may implicate its association with LCK proposed to impair phosphorylation of TCR subunits, and/or LGALS9-dependent recruitment of PTPRC to the immunological synapse (PubMed:24337741, PubMed:26492563). In contrast, shown to activate TCR-induced signaling in T-cells probably implicating ZAP70, LCP2, LCK and FYN (By similarity). Expressed on Treg cells can inhibit Th17 cell responses (PubMed:24838857). Receptor for LGALS9 (PubMed:16286920, PubMed:24337741). Binding to LGALS9 is believed to result in suppression of T-cell responses; the resulting apoptosis of antigen-specific cells may implicate HAVCR2 phosphorylation and disruption of its association with BAG6. Binding to LGALS9 is proposed to be involved in innate immune response to intracellular pathogens. Expressed on Th1 cells interacts with LGALS9 expressed on Mycobacterium tuberculosis-infected macrophages to stimulate antibactericidal activity including IL-1 beta secretion and to restrict intracellular bacterial growth (By similarity). However, the function as receptor for LGALS9 has been challenged (PubMed:23555261). Also reported to enhance CD8+ T-cell responses to an acute infection such as by Listeria monocytogenes (By similarity). Receptor for phosphatidylserine (PtSer); PtSer-binding is calcium-dependent. May recognize PtSer on apoptotic cells leading to their phagocytosis. Mediates the engulfment of apoptotic cells by dendritic cells. Expressed on T-cells, promotes conjugation but not engulfment of apoptotic cells. Expressed on dendritic cells (DCs) positively regulates innate immune response and in synergy with Toll-like receptors promotes secretion of TNF-alpha. In tumor-imfiltrating DCs suppresses nucleic acid-mediated innate immune repsonse by interaction with HMGB1 and interfering with nucleic acid-sensing and trafficking of nucleid acids to endosomes (By similarity). Expressed on natural killer (NK) cells acts as a coreceptor to enhance IFN-gamma production in response to LGALS9 (PubMed:22323453). In contrast, shown to suppress NK cell-mediated cytotoxicity (PubMed:22383801). Negatively regulates NK cell function in LPS-induced endotoxic shock (By similarity)", "gene_name": "HAVCR2", "glycan_count": 5, "glycosylation_sites": [ { "position": 145, "type": "O-linked (GalNAc...) threonine" }, { "position": 172, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8TDQ0", "name": "TIM-3", "organism": "Homo sapiens", "uniprot_id": "Q8TDQ0" }, { "function": "Phosphatidylserine receptor that plays different role in immune response including phagocytosis of apoptotic cells and T-cell regulation. Controls T-cell activation in a bimodal fashion, decreasing the activation of naive T-cells by inducing cell cycle arrest, while increasing proliferation of activated T-cells by activating AKT1 and ERK1/2 phosphorylations and subsequent signaling pathways (By similarity). Also plays a role in efferocytosis which is the process by which apoptotic cells are removed by phagocytic cells (PubMed:32703939, PubMed:34067457). Mechanistically, promotes the engulfment of apoptotic cells or exogenous particles by securing them to phagocytes through direct binding to phosphatidylserine present on apoptotic cells, while other engulfment receptors such as MERTK efficiently recognize apoptotic cells and mediate their ingestion (PubMed:32640697). Additionally, promotes autophagy process by suppressing NLRP3 inflammasome activity via activation of LKB1/PRKAA1 pathway in a phosphatidylserine-dependent mechanism (By similarity)", "gene_name": "TIMD4", "glycan_count": 0, "glycosylation_sites": [ { "position": 291, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q96H15", "name": "TIM-4", "organism": "Homo sapiens", "uniprot_id": "Q96H15" }, { "function": "Plays a role in boundary lubrication within articulating joints. Prevents protein deposition onto cartilage from synovial fluid by controlling adhesion-dependent synovial growth and inhibiting the adhesion of synovial cells to the cartilage surface", "gene_name": "PRG4", "glycan_count": 23, "glycosylation_sites": [ { "position": 123, "type": "O-linked (GalNAc...) serine" }, { "position": 136, "type": "O-linked (GalNAc...) serine" }, { "position": 206, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 240, "type": "O-linked (GalNAc...) threonine" }, { "position": 253, "type": "O-linked (GalNAc...) threonine" }, { "position": 277, "type": "O-linked (GalNAc...) threonine" }, { "position": 291, "type": "O-linked (GalNAc...) threonine" }, { "position": 305, "type": "O-linked (GalNAc...) threonine" }, { "position": 306, "type": "O-linked (GalNAc...) serine" }, { "position": 310, "type": "O-linked (GalNAc...) threonine" }, { "position": 317, "type": "O-linked (GalNAc...) serine" }, { "position": 324, "type": "O-linked (GalNAc...) threonine" }, { "position": 332, "type": "O-linked (GalNAc...) threonine" }, { "position": 338, "type": "O-linked (GalNAc...) threonine" }, { "position": 367, "type": "O-linked (GalNAc...) threonine" }, { "position": 373, "type": "O-linked (GalNAc...) serine" }, { "position": 376, "type": "O-linked (GalNAc...) threonine" }, { "position": 384, "type": "O-linked (GalNAc...) threonine" }, { "position": 385, "type": "O-linked (GalNAc...) threonine" }, { "position": 388, "type": "O-linked (GalNAc...) serine" }, { "position": 391, "type": "O-linked (GalNAc...) threonine" }, { "position": 399, "type": "O-linked (GalNAc...) threonine" }, { "position": 400, "type": "O-linked (GalNAc...) threonine" }, { "position": 407, "type": "O-linked (GalNAc...) threonine" }, { "position": 408, "type": "O-linked (GalNAc...) threonine" }, { "position": 415, "type": "O-linked (GalNAc...) threonine" }, { "position": 423, "type": "O-linked (GalNAc...) threonine" }, { "position": 427, "type": "O-linked (GalNAc...) serine" }, { "position": 430, "type": "O-linked (GalNAc...) threonine" }, { "position": 438, "type": "O-linked (GalNAc...) threonine" }, { "position": 439, "type": "O-linked (GalNAc...) threonine" }, { "position": 446, "type": "O-linked (GalNAc...) threonine" }, { "position": 447, "type": "O-linked (GalNAc...) threonine" }, { "position": 454, "type": "O-linked (GalNAc...) threonine" }, { "position": 455, "type": "O-linked (GalNAc...) threonine" }, { "position": 477, "type": "O-linked (GalNAc...) threonine" }, { "position": 478, "type": "O-linked (GalNAc...) threonine" }, { "position": 485, "type": "O-linked (GalNAc...) threonine" }, { "position": 493, "type": "O-linked (GalNAc...) threonine" }, { "position": 494, "type": "O-linked (GalNAc...) threonine" }, { "position": 501, "type": "O-linked (GalNAc...) threonine" }, { "position": 502, "type": "O-linked (GalNAc...) threonine" }, { "position": 509, "type": "O-linked (GalNAc...) threonine" }, { "position": 525, "type": "O-linked (GalNAc...) threonine" }, { "position": 529, "type": "O-linked (GalNAc...) serine" }, { "position": 532, "type": "O-linked (GalNAc...) threonine" }, { "position": 540, "type": "O-linked (GalNAc...) threonine" }, { "position": 541, "type": "O-linked (GalNAc...) threonine" }, { "position": 553, "type": "O-linked (GalNAc...) serine" }, { "position": 555, "type": "O-linked (GalNAc...) threonine" }, { "position": 563, "type": "O-linked (GalNAc...) threonine" }, { "position": 564, "type": "O-linked (GalNAc...) threonine" }, { "position": 571, "type": "O-linked (GalNAc...) threonine" }, { "position": 572, "type": "O-linked (GalNAc...) threonine" }, { "position": 579, "type": "O-linked (GalNAc...) threonine" }, { "position": 580, "type": "O-linked (GalNAc...) threonine" }, { "position": 587, "type": "O-linked (GalNAc...) threonine" }, { "position": 588, "type": "O-linked (GalNAc...) threonine" }, { "position": 595, "type": "O-linked (GalNAc...) threonine" }, { "position": 603, "type": "O-linked (GalNAc...) threonine" }, { "position": 604, "type": "O-linked (GalNAc...) threonine" }, { "position": 611, "type": "O-linked (GalNAc...) threonine" }, { "position": 612, "type": "O-linked (GalNAc...) threonine" }, { "position": 616, "type": "O-linked (GalNAc...) threonine" }, { "position": 619, "type": "O-linked (GalNAc...) threonine" }, { "position": 627, "type": "O-linked (GalNAc...) threonine" }, { "position": 676, "type": "O-linked (GalNAc...) threonine" }, { "position": 683, "type": "O-linked (GalNAc...) threonine" }, { "position": 684, "type": "O-linked (GalNAc...) threonine" }, { "position": 691, "type": "O-linked (GalNAc...) threonine" }, { "position": 692, "type": "O-linked (GalNAc...) threonine" }, { "position": 699, "type": "O-linked (GalNAc...) threonine" }, { "position": 700, "type": "O-linked (GalNAc...) threonine" }, { "position": 704, "type": "O-linked (GalNAc...) threonine" }, { "position": 707, "type": "O-linked (GalNAc...) threonine" }, { "position": 723, "type": "O-linked (GalNAc...) threonine" }, { "position": 724, "type": "O-linked (GalNAc...) threonine" }, { "position": 736, "type": "O-linked (GalNAc...) threonine" }, { "position": 768, "type": "O-linked (GalNAc...) threonine" }, { "position": 769, "type": "O-linked (GalNAc...) threonine" }, { "position": 776, "type": "O-linked (GalNAc...) threonine" }, { "position": 777, "type": "O-linked (GalNAc...) threonine" }, { "position": 792, "type": "O-linked (GalNAc...) threonine" }, { "position": 793, "type": "O-linked (GalNAc...) threonine" }, { "position": 805, "type": "O-linked (GalNAc...) threonine" }, { "position": 812, "type": "O-linked (GalNAc...) serine" }, { "position": 829, "type": "O-linked (GalNAc...) threonine" }, { "position": 837, "type": "O-linked (GalNAc...) threonine" }, { "position": 838, "type": "O-linked (GalNAc...) threonine" }, { "position": 892, "type": "O-linked (GalNAc...) serine" }, { "position": 900, "type": "O-linked (GalNAc...) threonine" }, { "position": 930, "type": "O-linked (GalNAc...) threonine" }, { "position": 931, "type": "O-linked (GalNAc...) threonine" }, { "position": 962, "type": "O-linked (GalNAc...) serine" }, { "position": 963, "type": "O-linked (GalNAc...) threonine" }, { "position": 968, "type": "O-linked (GalNAc...) threonine" }, { "position": 975, "type": "O-linked (GalNAc...) threonine" }, { "position": 978, "type": "O-linked (GalNAc...) threonine" }, { "position": 979, "type": "O-linked (GalNAc...) threonine" }, { "position": 980, "type": "O-linked (GalNAc...) threonine" }, { "position": 1039, "type": "O-linked (GalNAc...) threonine" }, { "position": 1159, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1161, "type": "O-linked (GalNAc...) threonine" } ], "id": "Q92954", "name": "Lubricin", "organism": "Homo sapiens", "uniprot_id": "Q92954" }, { "function": "Catalytic subunit of the glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex that catalyzes the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol and participates in the first step of GPI biosynthesis", "gene_name": "PIGA", "glycan_count": 0, "glycosylation_sites": [ { "position": 467, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P37287", "name": "PIGA", "organism": "Homo sapiens", "uniprot_id": "P37287" }, { "function": "Glycosaminoglycans biosynthesis (PubMed:25893793). Involved in forming the linkage tetrasaccharide present in heparan sulfate and chondroitin sulfate. Transfers a glucuronic acid moiety from the uridine diphosphate-glucuronic acid (UDP-GlcUA) to the common linkage region trisaccharide Gal-beta-1,3-Gal-beta-1,4-Xyl covalently bound to a Ser residue at the glycosaminylglycan attachment site of proteoglycans. Can also play a role in the biosynthesis of l2/HNK-1 carbohydrate epitope on glycoproteins. Shows strict specificity for Gal-beta-1,3-Gal-beta-1,4-Xyl, exhibiting negligible incorporation into other galactoside substrates including Galbeta1-3Gal beta1-O-benzyl, Galbeta1-4GlcNAc and Galbeta1-4Glc. Stimulates 2-phosphoxylose phosphatase activity of PXYLP1 in presence of uridine diphosphate-glucuronic acid (UDP-GlcUA) during completion of linkage region formation (PubMed:24425863)", "gene_name": "B3GAT3", "glycan_count": 2, "glycosylation_sites": [ { "position": 300, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O94766", "name": "B3GAT3", "organism": "Homo sapiens", "uniprot_id": "O94766" }, { "function": "Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1F gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, and by benzothiazepines. Activates at more negative voltages and does not undergo calcium-dependent inactivation (CDI), due to incoming calcium ions, during depolarization", "gene_name": "CACNA1F", "glycan_count": 0, "glycosylation_sites": [ { "position": 295, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O43901", "name": "B4GALT7", "organism": "Homo sapiens", "uniprot_id": "O60840" }, { "function": "Accessory component of the STT3B-containing form of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains (PubMed:31831667). Involved in N-glycosylation of STT3B-dependent substrates (PubMed:31831667). Specifically required for the glycosylation of a subset of acceptor sites that are near cysteine residues; in this function seems to act redundantly with TUSC3. In its oxidized form proposed to form transient mixed disulfides with a glycoprotein substrate to facilitate access of STT3B to the unmodified acceptor site. Also has oxidoreductase-independent functions in the STT3B-containing OST complex possibly involving substrate recognition. Could indirectly play a role in Mg(2+) transport in epithelial cells (Probable)", "gene_name": "MAGT1", "glycan_count": 2, "glycosylation_sites": [ { "position": 71, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9H0U3", "name": "CCDC115", "organism": "Homo sapiens", "uniprot_id": "Q9H0U3" }, { "function": "Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. Probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region. Involved in O-linked glycosylation of APOC-III, ANGPTL3 and PLTP. It participates in the regulation of HDL-C metabolism (PubMed:27508872, PubMed:32293671)", "gene_name": "GALNT2", "glycan_count": 3, "glycosylation_sites": [ { "position": 29, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" } ], "id": "Q10471", "name": "GALNT2", "organism": "Homo sapiens", "uniprot_id": "Q10471" }, { "function": "Binds to various kinds of negatively charged substances such as heparin, phospholipids, and dextran sulfate. May prevent activation of the intrinsic blood coagulation cascade by binding to phospholipids on the surface of damaged cells", "gene_name": "APOH", "glycan_count": 141, "glycosylation_sites": [ { "position": 33, "type": "O-linked (GalNAc...) threonine" }, { "position": 149, "type": "O-linked (GalNAc...) threonine" }, { "position": 162, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 183, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 193, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 253, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P02749", "name": "Beta-2 glycoprotein 1", "organism": "Homo sapiens", "uniprot_id": "P02749" }, { "function": "Precursor of non-enzymatic components of the classical, alternative, lectin and GZMK complement pathways, which consist in a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system", "gene_name": "C3", "glycan_count": 98, "glycosylation_sites": [ { "position": 85, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 939, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1617, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01024", "name": "Complement component C3", "organism": "Homo sapiens", "uniprot_id": "P01024" }, { "function": "Precursor of non-enzymatic components of the classical, lectin and GZMK complement pathways, which consist in a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system", "gene_name": "C4A", "glycan_count": 47, "glycosylation_sites": [ { "position": 226, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 862, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1244, "type": "O-linked (GalNAc...) threonine" }, { "position": 1328, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 1391, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P0C0L4", "name": "Complement component C4", "organism": "Homo sapiens", "uniprot_id": "P0C0L4" }, { "function": "Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268)", "gene_name": "IGHM", "glycan_count": 202, "glycosylation_sites": [ { "position": 46, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 209, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 272, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 279, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 440, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01871", "name": "Immunoglobulin M (IgM)", "organism": "Homo sapiens", "uniprot_id": "P01871" }, { "function": "Functions as a transport protein in the blood stream. Binds various ligands in the interior of its beta-barrel domain. Also binds synthetic drugs and influences their distribution and availability in the body. Appears to function in modulating the activity of the immune system during the acute-phase reaction", "gene_name": "ORM1", "glycan_count": 239, "glycosylation_sites": [ { "position": 33, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 56, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 72, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 93, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 103, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P02763", "name": "Alpha-1-acid glycoprotein (AGP)", "organism": "Homo sapiens", "uniprot_id": "P02763" }, { "function": "Displays several functions associated with host defense: it promotes agglutination, bacterial capsular swelling, phagocytosis and complement fixation through its calcium-dependent binding to phosphorylcholine. Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells", "gene_name": "CRP", "glycan_count": 0, "glycosylation_sites": [], "id": "P02741", "name": "C-reactive protein (CRP)", "organism": "Homo sapiens", "uniprot_id": "P02741" }, { "function": "Cell-surface glycoprotein having a role in immunoadhesion. Mediates in the adhesion of blood neutrophils in cytokine-activated endothelium through interaction with SELPLG/PSGL1. May have a role in capillary morphogenesis", "gene_name": "SELE", "glycan_count": 0, "glycosylation_sites": [ { "position": 25, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 145, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 160, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 179, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 199, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 203, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 265, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 312, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 332, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 503, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 527, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P16581", "name": "E-selectin", "organism": "Homo sapiens", "uniprot_id": "P16581" }, { "function": "RNA-binding protein that binds to misfolded non-coding RNAs, pre-5S rRNA, and several small cytoplasmic RNA molecules known as Y RNAs (PubMed:18056422, PubMed:26382853). Binds to endogenous Alu retroelements which are induced by type I interferon and stimulate porinflammatory cytokine secretion (PubMed:26382853). Regulates the expression of Alu retroelements as well as inflammatory genes (PubMed:26382853). May play roles in cilia formation and/or maintenance (By similarity)", "gene_name": "RO60", "glycan_count": 2, "glycosylation_sites": [], "id": "P10155", "name": "SS-A (Ro) antigen", "organism": "Homo sapiens", "uniprot_id": "P10155" }, { "function": "Iodination and coupling of the hormonogenic tyrosines in thyroglobulin to yield the thyroid hormones T(3) and T(4)", "gene_name": "TPO", "glycan_count": 1, "glycosylation_sites": [ { "position": 129, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 307, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 342, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 569, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P07202", "name": "Anti-TPO (thyroid peroxidase)", "organism": "Homo sapiens", "uniprot_id": "P07202" }, { "function": "Serine protease inhibitor, which acrs as a regulator of the classical complement pathway (PubMed:10946292, PubMed:11527969, PubMed:3458172, PubMed:6416294). Forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases (PubMed:10946292, PubMed:3458172, PubMed:6416294). May also regulate blood coagulation, fibrinolysis and the generation of kinins (PubMed:8495195). Very efficient inhibitor of FXIIa. Inhibits chymotrypsin and kallikrein (PubMed:8495195)", "gene_name": "SERPING1", "glycan_count": 180, "glycosylation_sites": [ { "position": 25, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 47, "type": "O-linked (GalNAc...) threonine" }, { "position": 48, "type": "O-linked (GalNAc...) threonine" }, { "position": 64, "type": "O-linked (GalNAc...) serine" }, { "position": 69, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 71, "type": "O-linked (GalNAc...) threonine" }, { "position": 81, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 83, "type": "O-linked (GalNAc...) threonine" }, { "position": 88, "type": "O-linked (GalNAc...) threonine" }, { "position": 92, "type": "O-linked (GalNAc...) threonine" }, { "position": 96, "type": "O-linked (GalNAc...) threonine" }, { "position": 238, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 253, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 272, "type": "N-linked (GlcNAc...) asparagine; in variant TA" }, { "position": 352, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P05155", "name": "C1 esterase inhibitor", "organism": "Homo sapiens", "uniprot_id": "P05155" }, { "function": "Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs (Probable). Its main function is the regulation of the colloidal osmotic pressure of blood (Probable). Major zinc transporter in plasma, typically binds about 80% of all plasma zinc (PubMed:19021548). Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (By similarity). The shared binding site between zinc and calcium at residue Asp-273 suggests a crosstalk between zinc and calcium transport in the blood (By similarity). The rank order of affinity is zinc > calcium > magnesium (By similarity). Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli (PubMed:6234017). Does not prevent iron uptake by the bacterial siderophore aerobactin (PubMed:6234017)", "gene_name": "ALB", "glycan_count": 8, "glycosylation_sites": [ { "position": 36, "type": "N-linked (Glc) (glycation) lysine" }, { "position": 75, "type": "N-linked (Glc) (glycation) lysine; in vitro" }, { "position": 161, "type": "N-linked (Glc) (glycation) lysine; in vitro" }, { "position": 186, "type": "N-linked (Glc) (glycation) lysine; in vitro" }, { "position": 223, "type": "N-linked (Glc) (glycation) lysine; in vitro" }, { "position": 249, "type": "N-linked (Glc) (glycation) lysine; in vitro" }, { "position": 257, "type": "N-linked (Glc) (glycation) lysine" }, { "position": 300, "type": "N-linked (Glc) (glycation) lysine; in vitro" }, { "position": 305, "type": "N-linked (Glc) (glycation) lysine" }, { "position": 337, "type": "N-linked (Glc) (glycation) lysine; in vitro" }, { "position": 341, "type": "N-linked (Glc) (glycation) lysine" }, { "position": 342, "type": "N-linked (GlcNAc...) asparagine; in variant Redhill" }, { "position": 347, "type": "N-linked (Glc) (glycation) lysine; in vitro" }, { "position": 375, "type": "N-linked (Glc) (glycation) lysine" }, { "position": 402, "type": "N-linked (Glc) (glycation) lysine; in vitro" }, { "position": 437, "type": "N-linked (Glc) (glycation) lysine; in vitro" }, { "position": 463, "type": "N-linked (Glc) (glycation) lysine" }, { "position": 468, "type": "N-linked (Glc) (glycation) lysine; in vitro" }, { "position": 518, "type": "N-linked (GlcNAc...) asparagine; in variant Casebrook" }, { "position": 549, "type": "N-linked (Glc) (glycation) lysine" }, { "position": 558, "type": "N-linked (Glc) (glycation) lysine; alternate" }, { "position": 560, "type": "N-linked (Glc) (glycation) lysine; in vitro" }, { "position": 569, "type": "N-linked (Glc) (glycation) lysine; in vitro" }, { "position": 597, "type": "N-linked (Glc) (glycation) lysine; in vitro" } ], "id": "P02768", "name": "Albumin", "organism": "Homo sapiens", "uniprot_id": "P02768" }, { "function": "Cooperates with p53/TP53 in the negative regulatory pathway of cell growth by modulating p53-dependent transcriptional activation. Implicated as a tumor suppressor gene", "gene_name": "ING1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UK53", "name": "Protein O-mannosyl-transferase 1 (POMT1)", "organism": "Homo sapiens", "uniprot_id": "Q9UK53" }, { "function": "", "gene_name": "ADAMTSL1", "glycan_count": 4, "glycosylation_sites": [ { "position": 39, "type": "C-linked (Man) tryptophan" }, { "position": 42, "type": "C-linked (Man) tryptophan" }, { "position": 48, "type": "O-linked (Fuc...) threonine" }, { "position": 251, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 312, "type": "O-linked (Fuc...) threonine" }, { "position": 391, "type": "O-linked (Fuc...) serine" }, { "position": 451, "type": "O-linked (Fuc...) threonine" } ], "id": "Q8N6G6", "name": "Protein O-linked mannose N-acetylglucosaminyltransferase 2 (POMGNT2)", "organism": "Homo sapiens", "uniprot_id": "Q8N6G6" }, { "function": "", "gene_name": "CDRT15", "glycan_count": 0, "glycosylation_sites": [], "id": "Q96T59", "name": "GDP-mannose pyrophosphorylase B (GMPPB)", "organism": "Homo sapiens", "uniprot_id": "Q96T59" }, { "function": "Involved in endoplasmic reticulum-associated degradation (ERAD). Accelerates the glycoprotein ERAD by proteasomes, by catalyzing mannose trimming from Man8GlcNAc2 to Man7GlcNAc2 in the N-glycans (PubMed:25092655). May also participate in mannose trimming from all glycoproteins and not just misfolded ones targeted to ERAD (PubMed:34143952). May have alpha 1,2-mannosidase activity (By similarity)", "gene_name": "EDEM3", "glycan_count": 11, "glycosylation_sites": [ { "position": 118, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 195, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 504, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 511, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 810, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 814, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 900, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9BZQ6", "name": "CRPPA (ISPD)", "organism": "Homo sapiens", "uniprot_id": "Q9BZQ6" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9V3S6 (Drosophila)", "name": "Dystroglycan (DG)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9V3S7 (Drosophila)", "name": "Neurexin (DNRX)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9V3S8 (Drosophila)", "name": "Rotated Abdomen (RT, POMT1 homolog)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9V3S9 (Drosophila)", "name": "Twisted (TW, POMT2 homolog)", "organism": "", "uniprot_id": "" }, { "function": "Binds DNA as a heterodimer with MLX/TCFL4 and activates transcription. Binds to the canonical E box sequence 5'-CACGTG-3'. Plays a role in transcriptional activation of glycolytic target genes. Involved in glucose-responsive gene regulation (By similarity). Regulates transcription in response to changes in cellular carbohydrate abundance such as occurs during fasting to feeding metabolic transition. Refeeding stimulates MLXIPL/ChREBP transcription factor, leading to increased BCKDK to PPM1K expression ratio, phosphorylation and activation of ACLY that ultimately results in the generation of malonyl-CoA and oxaloacetate immediate substrates of de novo lipogenesis and gluconeogenesis, respectively (By similarity)", "gene_name": "MLXIPL", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NP71", "name": "CREB3", "organism": "Homo sapiens", "uniprot_id": "Q9NP71" }, { "function": "Precursor of the transcription factor form (Processed cyclic AMP-responsive element-binding protein 3-like protein 1), which is embedded in the endoplasmic reticulum membrane with N-terminal DNA-binding and transcription activation domains oriented toward the cytosolic face of the membrane (PubMed:12054625, PubMed:16417584, PubMed:25310401). In response to ER stress or DNA damage, transported to the Golgi, where it is cleaved in a site-specific manner by resident proteases S1P/MBTPS1 and S2P/MBTPS2. The released N-terminal cytosolic domain is translocated to the nucleus where it activates transcription of specific target genes involved in the cell-cycle progression inhibition (PubMed:12054625, PubMed:21767813, PubMed:25310401)", "gene_name": "CREB3L1", "glycan_count": 4, "glycosylation_sites": [ { "position": 492, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 513, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q96BA8", "name": "CREB3L3", "organism": "Homo sapiens", "uniprot_id": "Q96BA8" }, { "function": "May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons", "gene_name": "APOA4", "glycan_count": 2, "glycosylation_sites": [], "id": "P06727", "name": "ApoA-IV", "organism": "Homo sapiens", "uniprot_id": "P06727" }, { "function": "Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. May also function as a calcium-dependent lectin", "gene_name": "APCS", "glycan_count": 17, "glycosylation_sites": [ { "position": 51, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P02743", "name": "SAP (Serum Amyloid P)", "organism": "Homo sapiens", "uniprot_id": "P02743" }, { "function": "Catalyzes the activation of N-acetylneuraminic acid (NeuNAc) to cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-NeuNAc), a substrate required for the addition of sialic acid. Has some activity toward NeuNAc, N-glycolylneuraminic acid (Neu5Gc) or 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN)", "gene_name": "CMAS", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8NFW8", "name": "CREB3L4", "organism": "Homo sapiens", "uniprot_id": "Q8NFW8" }, { "function": "Binds to TEK/TIE2, modulating ANGPT1 signaling. Can induce tyrosine phosphorylation of TEK/TIE2. Promotes endothelial cell survival, migration and angiogenesis", "gene_name": "ANGPT4", "glycan_count": 0, "glycosylation_sites": [ { "position": 96, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 126, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 140, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 158, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 247, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 274, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 311, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 337, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 427, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y264", "name": "ANGPTL3", "organism": "Homo sapiens", "uniprot_id": "Q9Y264" }, { "function": "Plays a major role in cholesterol homeostasis (PubMed:22095670). Critical for the uptake of cholesterol across the plasma membrane of the intestinal enterocyte (PubMed:22095670). Involved in plant sterol absorption, it transports sitosterol, although at lower rates than cholesterol (By similarity). Is the direct molecular target of ezetimibe, a drug that inhibits cholesterol absorption and is approved for the treatment of hypercholesterolemia (PubMed:15928087). May have a function in the transport of multiple lipids and their homeostasis, thereby influencing lipid metabolism regulation (PubMed:15671032). May be involved in caveolin trafficking from the plasma membrane (By similarity). In addition, acts as a negative regulator of NPC2 and down-regulates its expression and secretion by inhibiting its maturation and accelerating its degradation (PubMed:22095670)", "gene_name": "NPC1L1", "glycan_count": 1, "glycosylation_sites": [ { "position": 54, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 132, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 138, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 244, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 416, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 431, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 464, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 479, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 497, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 506, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 626, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UHC9", "name": "NPC1L1", "organism": "Homo sapiens", "uniprot_id": "Q9UHC9" }, { "function": "Epithelial ion channel that plays an important role in the regulation of epithelial ion and water transport and fluid homeostasis (PubMed:26823428). Mediates the transport of chloride ions across the cell membrane (PubMed:10792060, PubMed:11524016, PubMed:11707463, PubMed:12519745, PubMed:12529365, PubMed:12588899, PubMed:12727866, PubMed:15010471, PubMed:17036051, PubMed:1712898, PubMed:17182731, PubMed:19398555, PubMed:19621064, PubMed:22178883, PubMed:25330774, PubMed:26846474, PubMed:28087700, PubMed:8910473, PubMed:9804160). Possesses an intrinsic ATPase activity and utilizes ATP to gate its channel; the passive flow of anions through the channel is gated by cycles of ATP binding and hydrolysis by the ATP-binding domains (PubMed:11524016, PubMed:15284228, PubMed:26627831, PubMed:8910473). The ion channel is also permeable to HCO(3)(-); selectivity depends on the extracellular chloride concentration (PubMed:15010471, PubMed:19019741). In vitro, mediates ATP-dependent glutathione flux (PubMed:12727866). Exerts its function also by modulating the activity of other ion channels and transporters (PubMed:12403779, PubMed:22121115, PubMed:22178883, PubMed:27941075). Plays an important role in airway fluid homeostasis (PubMed:16645176, PubMed:19621064, PubMed:26823428). Contributes to the regulation of the pH and the ion content of the airway surface fluid layer and thereby plays an important role in defense against pathogens (PubMed:14668433, PubMed:16645176, PubMed:26823428). Modulates the activity of the epithelial sodium channel (ENaC) complex, in part by regulating the cell surface expression of the ENaC complex (PubMed:17182731, PubMed:17434346, PubMed:27941075). Inhibits the activity of the ENaC channel containing subunits SCNN1A, SCNN1B and SCNN1G (PubMed:17182731). Inhibits the activity of the ENaC channel containing subunits SCNN1D, SCNN1B and SCNN1G, but not of the ENaC channel containing subunits SCNN1A, SCNN1B and SCNN1G (PubMed:17182731, PubMed:27941075). May regulate bicarbonate secretion and salvage in epithelial cells by regulating the transporter SLC4A7 (PubMed:12403779). Can inhibit the chloride channel activity of ANO1 (PubMed:22178883). Plays a role in the chloride and bicarbonate homeostasis during sperm epididymal maturation and capacitation (PubMed:19923167, PubMed:27714810, PubMed:29393851)", "gene_name": "CFTR", "glycan_count": 0, "glycosylation_sites": [ { "position": 894, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 900, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P13569", "name": "Cystic Fibrosis Transmembrane Conductance Regulator (CFTR)", "organism": "Homo sapiens", "uniprot_id": "P13569" }, { "function": "May play a role in microtubule-mediated transport or vesicle function", "gene_name": "HTT", "glycan_count": 4, "glycosylation_sites": [], "id": "P42858", "name": "Huntingtin", "organism": "Homo sapiens", "uniprot_id": "P42858" }, { "function": "Destroys radicals which are normally produced within the cells and which are toxic to biological systems", "gene_name": "SOD1", "glycan_count": 3, "glycosylation_sites": [], "id": "P00441", "name": "Superoxide dismutase 1 (SOD1)", "organism": "Homo sapiens", "uniprot_id": "P00441" }, { "function": "Chromatin-binding factor that repress Notch signaling in the absence of Notch intracellular domain by acting as a CBF1 corepressor. Binds to the HEY promoter and might assist, along with NCOR2, RBPJ-mediated repression. Binds RNA in vitro. May be involved in RNA metabolism (PubMed:21475249). In concert with CIC and ATXN1L, involved in brain development (By similarity)", "gene_name": "ATXN1", "glycan_count": 1, "glycosylation_sites": [], "id": "P54253", "name": "Ataxin-1", "organism": "Homo sapiens", "uniprot_id": "P54253" }, { "function": "Deubiquitinating enzyme involved in protein homeostasis maintenance, transcription, cytoskeleton regulation, myogenesis and degradation of misfolded chaperone substrates (PubMed:12297501, PubMed:16118278, PubMed:17696782, PubMed:23625928, PubMed:28445460, PubMed:33157014). Binds long polyubiquitin chains and trims them, while it has weak or no activity against chains of 4 or less ubiquitins (PubMed:17696782). Involved in degradation of misfolded chaperone substrates via its interaction with STUB1/CHIP: recruited to monoubiquitinated STUB1/CHIP, and restricts the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension (By similarity). Interacts with key regulators of transcription and represses transcription: acts as a histone-binding protein that regulates transcription (PubMed:12297501). Acts as a negative regulator of mTORC1 signaling in response to amino acid deprivation by mediating deubiquitination of RHEB, thereby promoting RHEB inactivation by the TSC-TBC complex (PubMed:33157014). Regulates autophagy via the deubiquitination of 'Lys-402' of BECN1 leading to the stabilization of BECN1 (PubMed:28445460)", "gene_name": "ATXN3", "glycan_count": 1, "glycosylation_sites": [], "id": "P54252", "name": "Ataxin-3", "organism": "Homo sapiens", "uniprot_id": "P54252" }, { "function": "Acts as a component of the SAGA (aka STAGA) transcription coactivator-HAT complex (PubMed:15932940, PubMed:18206972). Mediates the interaction of SAGA complex with the CRX and is involved in CRX-dependent gene activation (PubMed:15932940, PubMed:18206972). Probably involved in tethering the deubiquitination module within the SAGA complex (PubMed:24493646). Necessary for microtubule cytoskeleton stabilization (PubMed:22100762). Involved in neurodegeneration (PubMed:9288099)", "gene_name": "ATXN7", "glycan_count": 2, "glycosylation_sites": [], "id": "O15265", "name": "Ataxin-7", "organism": "Homo sapiens", "uniprot_id": "O15265" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8A789", "name": "Bacteroides thetaiotaomicron sulfatase BT1636", "organism": "Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)", "uniprot_id": "Q8A789" }, { "function": "Catalyzes the first and rate limiting step of the catabolism of the essential amino acid tryptophan along the kynurenine pathway (PubMed:17671174). Involved in the peripheral immune tolerance, contributing to maintain homeostasis by preventing autoimmunity or immunopathology that would result from uncontrolled and overreacting immune responses (PubMed:25691885). Tryptophan shortage inhibits T lymphocytes division and accumulation of tryptophan catabolites induces T-cell apoptosis and differentiation of regulatory T-cells (PubMed:25691885). Acts as a suppressor of anti-tumor immunity (PubMed:14502282, PubMed:23103127, PubMed:25157255, PubMed:25691885). Limits the growth of intracellular pathogens by depriving tryptophan (PubMed:25691885). Protects the fetus from maternal immune rejection (PubMed:25691885)", "gene_name": "IDO1", "glycan_count": 0, "glycosylation_sites": [], "id": "P14902", "name": "Indoleamine 2,3-dioxygenase (IDO)", "organism": "Homo sapiens", "uniprot_id": "P14902" }, { "function": "Cytokine produced by activated CD4-positive helper T-cells and to a lesser extend activated CD8-positive T-cells and natural killer (NK) cells that plays pivotal roles in the immune response and tolerance (PubMed:6438535). Binds to a receptor complex composed of either the high-affinity trimeric IL-2R (IL2RA/CD25, IL2RB/CD122 and IL2RG/CD132) or the low-affinity dimeric IL-2R (IL2RB and IL2RG) (PubMed:16293754, PubMed:16477002). Interaction with the receptor leads to oligomerization and conformation changes in the IL-2R subunits resulting in downstream signaling starting with phosphorylation of JAK1 and JAK3 (PubMed:7973659). In turn, JAK1 and JAK3 phosphorylate the receptor to form a docking site leading to the phosphorylation of several substrates including STAT5 (PubMed:8580378). This process leads to activation of several pathways including STAT, phosphoinositide-3-kinase/PI3K and mitogen-activated protein kinase/MAPK pathways (PubMed:25142963). Functions as a T-cell growth factor and can increase NK-cell cytolytic activity as well (PubMed:6608729). Promotes strong proliferation of activated B-cells and subsequently immunoglobulin production (PubMed:6438535). Plays a pivotal role in regulating the adaptive immune system by controlling the survival and proliferation of regulatory T-cells, which are required for the maintenance of immune tolerance. Moreover, participates in the differentiation and homeostasis of effector T-cell subsets, including Th1, Th2, Th17 as well as memory CD8-positive T-cells", "gene_name": "IL2", "glycan_count": 20, "glycosylation_sites": [ { "position": 23, "type": "O-linked (GalNAc...) threonine" } ], "id": "P60568", "name": "Interleukin-2 (IL-2)", "organism": "Homo sapiens", "uniprot_id": "P60568" }, { "function": "Receptor for interleukin-2. The receptor is involved in the regulation of immune tolerance by controlling regulatory T cells (TREGs) activity. TREGs suppress the activation and expansion of autoreactive T-cells", "gene_name": "IL2RA", "glycan_count": 3, "glycosylation_sites": [ { "position": 70, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 89, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 218, "type": "O-linked (GalNAc...) threonine" }, { "position": 224, "type": "O-linked (GalNAc...) threonine" }, { "position": 229, "type": "O-linked (GalNAc...) threonine" }, { "position": 237, "type": "O-linked (GalNAc...) threonine" } ], "id": "P01589", "name": "IL-2 receptor alpha chain (CD25)", "organism": "Homo sapiens", "uniprot_id": "P01589" }, { "function": "Cell surface glycoprotein involved in various biological processes including angiogenesis, immune response modulation, and tissue remodeling and repair. Participates in pericyte proliferation through positive modulation of the PDGF receptor signaling pathway (PubMed:20484976). Acts as a scaffold for factor X, triggering allosteric changes and the spatial re-alignment of factor X with the TF-factor VIIa complex, thereby enhancing coagulation activation. Modulates the insulin signaling pathway by interacting with insulin receptor/INSR and by diminishing its capacity to be autophosphorylated in response to insulin. Also regulates LPS-induced inflammatory response in macrophages by favoring the production of proinflammatory cytokines. In human, negatively regulates T-cell proliferation compared with stromal cells where it increases proliferation (PubMed:21466550)", "gene_name": "CD248", "glycan_count": 5, "glycosylation_sites": [ { "position": 60, "type": "O-linked (GalNAc...) threonine" }, { "position": 401, "type": "O-linked (GalNAc...) threonine" }, { "position": 428, "type": "O-linked (GalNAc...) threonine" }, { "position": 448, "type": "O-linked (GalNAc...) threonine" }, { "position": 456, "type": "O-linked (GalNAc...) threonine" }, { "position": 459, "type": "O-linked (GalNAc...) threonine" }, { "position": 472, "type": "O-linked (GalNAc...) threonine" }, { "position": 519, "type": "O-linked (GalNAc...) threonine" }, { "position": 541, "type": "O-linked (GalNAc...) threonine" }, { "position": 543, "type": "O-linked (GalNAc...) threonine" }, { "position": 544, "type": "O-linked (GalNAc...) threonine" }, { "position": 545, "type": "O-linked (GalNAc...) threonine" }, { "position": 587, "type": "O-linked (GalNAc...) threonine" }, { "position": 593, "type": "O-linked (GalNAc...) threonine" }, { "position": 594, "type": "O-linked (GalNAc...) threonine" }, { "position": 595, "type": "O-linked (GalNAc...) threonine" }, { "position": 598, "type": "O-linked (GalNAc...) serine" }, { "position": 601, "type": "O-linked (GalNAc...) serine" }, { "position": 612, "type": "O-linked (GalNAc...) threonine" }, { "position": 619, "type": "O-linked (GalNAc...) threonine" }, { "position": 623, "type": "O-linked (GalNAc...) serine" }, { "position": 625, "type": "O-linked (GalNAc...) serine" }, { "position": 627, "type": "O-linked (GalNAc...) threonine" }, { "position": 630, "type": "O-linked (GalNAc...) threonine" }, { "position": 631, "type": "O-linked (GalNAc...) serine" }, { "position": 636, "type": "O-linked (GalNAc...) threonine" }, { "position": 640, "type": "O-linked (GalNAc...) serine" } ], "id": "Q9HCU0", "name": "VISTA", "organism": "Homo sapiens", "uniprot_id": "Q9HCU0" }, { "function": "Lymphocyte activation gene 3 protein: Inhibitory receptor on antigen activated T-cells (PubMed:20421648, PubMed:7805750, PubMed:8647185). Delivers inhibitory signals upon binding to ligands, such as FGL1 (By similarity). FGL1 constitutes a major ligand of LAG3 and is responsible for LAG3 T-cell inhibitory function (By similarity). Following TCR engagement, LAG3 associates with CD3-TCR in the immunological synapse and directly inhibits T-cell activation (By similarity). May inhibit antigen-specific T-cell activation in synergy with PDCD1/PD-1, possibly by acting as a coreceptor for PDCD1/PD-1 (By similarity). Negatively regulates the proliferation, activation, effector function and homeostasis of both CD8(+) and CD4(+) T-cells (PubMed:20421648, PubMed:7805750, PubMed:8647185). Also mediates immune tolerance: constitutively expressed on a subset of regulatory T-cells (Tregs) and contributes to their suppressive function (By similarity). Also acts as a negative regulator of plasmacytoid dendritic cell (pDCs) activation (By similarity). Binds MHC class II (MHC-II); the precise role of MHC-II-binding is however unclear (PubMed:8647185)", "gene_name": "LAG3", "glycan_count": 1, "glycosylation_sites": [ { "position": 188, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 250, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 256, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 343, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P18627", "name": "LAG-3", "organism": "Homo sapiens", "uniprot_id": "P18627" }, { "function": "Transcription factor that plays an important role in cellular development and cell survival (PubMed:7862533). Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3' (PubMed:17716689, PubMed:25258363, PubMed:7862533). Regulates the expression of numerous target genes, including EPO. Plays an essential role for development of the urogenital system. It has a tumor suppressor as well as an oncogenic role in tumor formation. Function may be isoform-specific: isoforms lacking the KTS motif may act as transcription factors (PubMed:15520190). Isoforms containing the KTS motif may bind mRNA and play a role in mRNA metabolism or splicing (PubMed:16934801). Isoform 1 has lower affinity for DNA, and can bind RNA (PubMed:19123921)", "gene_name": "WT1", "glycan_count": 0, "glycosylation_sites": [], "id": "P19544", "name": "WT1", "organism": "Homo sapiens", "uniprot_id": "P19544" }, { "function": "Plays a role in viral genome replication by driving entry of quiescent cells into the cell cycle. Stimulation of progression from G1 to S phase allows the virus to efficiently use the cellular DNA replicating machinery to achieve viral genome replication. E7 protein has both transforming and trans-activating activities. Induces the disassembly of the E2F1 transcription factor from RB1, with subsequent transcriptional activation of E2F1-regulated S-phase genes. Interferes with host histone deacetylation mediated by HDAC1 and HDAC2, leading to transcription activation. Also plays a role in the inhibition of both antiviral and antiproliferative functions of host interferon alpha. Interaction with host TMEM173/STING impairs the ability of TMEM173/STING to sense cytosolic DNA and promote the production of type I interferon (IFN-alpha and IFN-beta)", "gene_name": "E7", "glycan_count": 0, "glycosylation_sites": [], "id": "P03129", "name": "HPV E7", "organism": "Human papillomavirus type 16", "uniprot_id": "P03129" }, { "function": "Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then rotates around the intact phosphodiester bond on the opposing strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity). Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. Involved in the circadian transcription of the core circadian clock component BMAL1 by altering the chromatin structure around the ROR response elements (ROREs) on the BMAL1 promoter", "gene_name": "TOP1", "glycan_count": 3, "glycosylation_sites": [], "id": "P11387", "name": "Topoisomerase I (TOP1)", "organism": "Homo sapiens", "uniprot_id": "P11387" }, { "function": "Interacts with centromeric heterochromatin in chromosomes and binds to a specific 17 bp subset of alphoid satellite DNA, called the CENP-B box (PubMed:11726497). May organize arrays of centromere satellite DNA into a higher-order structure which then directs centromere formation and kinetochore assembly in mammalian chromosomes (Probable)", "gene_name": "CENPB", "glycan_count": 0, "glycosylation_sites": [], "id": "P07199", "name": "Centromere protein B (CENP-B)", "organism": "Homo sapiens", "uniprot_id": "P07199" }, { "function": "Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). Ig alpha is the major immunoglobulin class in body secretions (PubMed:2241915)", "gene_name": "IGHA1", "glycan_count": 148, "glycosylation_sites": [ { "position": 105, "type": "O-linked (GalNAc...) serine" }, { "position": 106, "type": "O-linked (GalNAc...) threonine" }, { "position": 109, "type": "O-linked (GalNAc...) threonine" }, { "position": 111, "type": "O-linked (GalNAc...) serine" }, { "position": 113, "type": "O-linked (GalNAc...) serine" }, { "position": 114, "type": "O-linked (GalNAc...) threonine" }, { "position": 117, "type": "O-linked (GalNAc...) threonine" }, { "position": 119, "type": "O-linked (GalNAc...) serine" }, { "position": 121, "type": "O-linked (GalNAc...) serine" }, { "position": 144, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 340, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P01876", "name": "Immunoglobulin A (IgA)", "organism": "Homo sapiens", "uniprot_id": "P01876" }, { "function": "Part of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that greatly enhance PMN microbicidal activity (PubMed:9922160). Mediates the proteolytic cleavage of alpha-1-microglobulin to form t-alpha-1-microglobulin, which potently inhibits oxidation of low-density lipoprotein particles and limits vascular damage (PubMed:25698971)", "gene_name": "MPO", "glycan_count": 77, "glycosylation_sites": [ { "position": 139, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 323, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 355, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 391, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 483, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 729, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P05164", "name": "Myeloperoxidase (MPO)", "organism": "Homo sapiens", "uniprot_id": "P05164" }, { "function": "Serine protease that degrades elastin, fibronectin, laminin, vitronectin, and collagen types I, III, and IV (in vitro) (PubMed:2033050, PubMed:28240246, PubMed:3198760). By cleaving and activating receptor F2RL1/PAR-2, enhances endothelial cell barrier function and thus vascular integrity during neutrophil transendothelial migration (PubMed:23202369). Plays a role in neutrophil transendothelial migration, probably when associated with CD177 (PubMed:22266279). Triggers inflammatory processes in neutrophils by interacting with ADGRG3 upstream of F2RL1/PAR2 activation (PubMed:36302784)", "gene_name": "PRTN3", "glycan_count": 1, "glycosylation_sites": [ { "position": 129, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 174, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P24158", "name": "Proteinase 3 (PR3)", "organism": "Homo sapiens", "uniprot_id": "P24158" }, { "function": "Responsible for the origin of replication (oriP) dependent replication and maintenance of viral episomes during latent infection (PubMed:15479791, PubMed:2996781). EBNA1 dimer interacts with the DS (dyad symmetry) element within the origin of replication oriP and with a host mitotic chromosome to initiate viral DNA replication during latency (PubMed:24067969, PubMed:2996781, PubMed:31142669, PubMed:8551585). EBNA1 binding to DS recruits the host origin recognition complex (ORC) (PubMed:12953058). Governs the faithful mitotic segregation of the viral episomes by binding both the FR (family of repeats) element within oriP and the host mitotic chromosomes (PubMed:11172042, PubMed:15479791, PubMed:24067969). Forms a cell cycle-dependent tyrosine-dependent DNA cross-link and single-strand cleavage at oriP required for terminating replication and maintaining viral episomes (PubMed:33482082). Counteracts the stabilization of host p53/TP53 by host USP7, thereby decreasing apoptosis and increasing host cell survival (PubMed:15808506). Induces degradation of host PML through the ubiquitin-proteasome system, which promotes lytic reactivation and may impair the host cell DNA repair (PubMed:18833293). Increases the association of CK2 with PML proteins which increases the phosphorylation of PML proteins by CK2, triggering the polyubiquitylation and degradation of PML (PubMed:20719947). Displays inhibitory effects on a SUMO2-modified complex that includes STUB1, KAP1 and USP7 (PubMed:32176739). This inhibitory effect possibly participates to the maintenance of latency linked to PML silencing (PubMed:32176739)", "gene_name": "EBNA1", "glycan_count": 0, "glycosylation_sites": [], "id": "P03211", "name": "Epstein\u2013Barr nuclear antigen 1 (EBNA-1)", "organism": "Epstein-Barr virus (strain B95-8)", "uniprot_id": "P03211" }, { "function": "Contactins mediate cell surface interactions during nervous system development. Involved in the formation of paranodal axo-glial junctions in myelinated peripheral nerves and in the signaling between axons and myelinating glial cells via its association with CNTNAP1. Participates in oligodendrocytes generation by acting as a ligand of NOTCH1. Its association with NOTCH1 promotes NOTCH1 activation through the released notch intracellular domain (NICD) and subsequent translocation to the nucleus. Interaction with TNR induces a repulsion of neurons and an inhibition of neurite outgrowth (By similarity)", "gene_name": "CNTN1", "glycan_count": 21, "glycosylation_sites": [ { "position": 208, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 258, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 338, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 457, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 473, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 494, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 521, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 591, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 933, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q12860", "name": "Contactin-1 (CNTN1)", "organism": "Homo sapiens", "uniprot_id": "Q12860" }, { "function": "Plays a role in endocytosis and/or membrane trafficking at the trans-Golgi network (TGN) (PubMed:15758025). May act by linking the adapter protein complex AP-1 to other proteins (Probable). Component of clathrin-coated vesicles (PubMed:15758025). Component of the aftiphilin/p200/gamma-synergin complex, which plays roles in AP1G1/AP-1-mediated protein trafficking including the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes (PubMed:15758025)", "gene_name": "SYNRG", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UMZ2", "name": "Neurofascin-155 (NF155)", "organism": "Homo sapiens", "uniprot_id": "Q9UMZ2" }, { "function": "Required for gap junction formation (Probable). Required, with CNTNAP1, for radial and longitudinal organization of myelinated axons. Plays a role in the formation of functional distinct domains critical for saltatory conduction of nerve impulses in myelinated nerve fibers. Demarcates the juxtaparanodal region of the axo-glial junction", "gene_name": "CNTNAP2", "glycan_count": 0, "glycosylation_sites": [ { "position": 289, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 346, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 363, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 379, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 436, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 506, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 507, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 546, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 630, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 735, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1116, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1198, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UHC6", "name": "Contactin-associated protein 1 (Caspr1)", "organism": "Homo sapiens", "uniprot_id": "Q9UHC6" }, { "function": "ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). During leukocyte trans-endothelial migration, ICAM1 engagement promotes the assembly of endothelial apical cups through ARHGEF26/SGEF and RHOG activation", "gene_name": "ICAM1", "glycan_count": 111, "glycosylation_sites": [ { "position": 130, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 145, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 183, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 202, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 267, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 296, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 385, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 406, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P05362", "name": "ICAM-1", "organism": "Homo sapiens", "uniprot_id": "P05362" }, { "function": "Catalyzes the aldol cleavage of fructose 1,6-biphosphate to form two triosephosphates dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate in glycolysis as well as the reverse stereospecific aldol addition reaction in gluconeogenesis. In fructolysis, metabolizes fructose 1-phosphate derived from the phosphorylation of dietary fructose by fructokinase into dihydroxyacetone phosphate and D-glyceraldehyde (PubMed:10970798, PubMed:12205126, PubMed:20848650). Acts as an adapter independently of its enzymatic activity, exerts a tumor suppressor role by stabilizing the ternary complex with G6PD and TP53 to inhibit G6PD activity and keep oxidative pentose phosphate metabolism in check (PubMed:35122041)", "gene_name": "ALDOB", "glycan_count": 1, "glycosylation_sites": [], "id": "P05062", "name": "Aldolase B", "organism": "Homo sapiens", "uniprot_id": "P05062" }, { "function": "Isomerase that catalyzes the interconversion of fructose-6-P and mannose-6-P and has a critical role in the supply of D-mannose derivatives required for many eukaryotic glycosylation reactions", "gene_name": "MPI", "glycan_count": 1, "glycosylation_sites": [], "id": "P34949", "name": "Mannose phosphate isomerase (MPI)", "organism": "Homo sapiens", "uniprot_id": "P34949" }, { "function": "Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). As a member of the malate-aspartate shuttle, it has a key role in the intracellular NAD(H) redox balance. Is important for metabolite exchange between mitochondria and cytosol, and for amino acid metabolism. Facilitates cellular uptake of long-chain free fatty acids", "gene_name": "GOT2", "glycan_count": 1, "glycosylation_sites": [], "id": "P00505", "name": "Aspartate Aminotransferase (AST)", "organism": "Homo sapiens", "uniprot_id": "P00505" }, { "function": "Involved in oxygen transport from the lung to the various peripheral tissues", "gene_name": "HBA1", "glycan_count": 1, "glycosylation_sites": [ { "position": 8, "type": "N-linked (Glc) (glycation) lysine; alternate" }, { "position": 17, "type": "N-linked (Glc) (glycation) lysine; alternate" }, { "position": 41, "type": "N-linked (Glc) (glycation) lysine; alternate" }, { "position": 62, "type": "N-linked (Glc) (glycation) lysine" } ], "id": "P69905", "name": "Hemoglobin A1c (HbA1c)", "organism": "Homo sapiens", "uniprot_id": "P69905" }, { "function": "May be considered as a candidate tumor suppressor gene for brain, lung, esophageal, gastric, and colorectal cancers. May play roles in mucosal defense system, cellular immune defense and epithelial differentiation. May play a role as an opsonin receptor for SFTPD and SPAR in macrophage tissues throughout the body, including epithelial cells lining the gastrointestinal tract. May play a role in liver regeneration. May be an important factor in fate decision and differentiation of transit-amplifying ductular (oval) cells within the hepatic lineage. Required for terminal differentiation of columnar epithelial cells during early embryogenesis. May function as a binding protein in saliva for the regulation of taste sensation. Binds to HIV-1 envelope protein and has been shown to both inhibit and facilitate viral transmission. Displays a broad calcium-dependent binding spectrum against both Gram-positive and Gram-negative bacteria, suggesting a role in defense against bacterial pathogens. Binds to a range of poly-sulfated and poly-phosphorylated ligands which may explain its broad bacterial-binding specificity. Inhibits cytoinvasion of S.enterica. Associates with the actin cytoskeleton and is involved in its remodeling during regulated exocytosis. Interacts with pancreatic zymogens in a pH-dependent manner and may act as a Golgi cargo receptor in the regulated secretory pathway of the pancreatic acinar cell", "gene_name": "DMBT1", "glycan_count": 1, "glycosylation_sites": [ { "position": 566, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 737, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1712, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1745, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1818, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1832, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1842, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1889, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1998, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2120, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2188, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2233, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2240, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2256, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UGM3", "name": "DMBT1 (gp340)", "organism": "Homo sapiens", "uniprot_id": "Q9UGM3" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P05067 (fragment)", "name": "A\u03b2 (Amyloid Beta Peptide)", "organism": "", "uniprot_id": "" }, { "function": "Transmembrane metalloprotease which mediates the ectodomain shedding of a myriad of transmembrane proteins, including adhesion proteins, growth factor precursors and cytokines being essential for development and tissue homeostasis (PubMed:11786905, PubMed:12475894, PubMed:20592283, PubMed:24990881, PubMed:26686862, PubMed:28600292, PubMed:31792032). Associates with six members of the tetraspanin superfamily TspanC8 which regulate its exit from the endoplasmic reticulum and its substrate selectivity (PubMed:26686862, PubMed:28600292, PubMed:31792032, PubMed:34739841, PubMed:37516108). Cleaves the membrane-bound precursor of TNF-alpha at '76-Ala-|-Val-77' to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface (PubMed:20592283). Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2, CD44, CDH2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP) (PubMed:11786905, PubMed:26686862, PubMed:29224781, PubMed:34739841). Contributes to the normal cleavage of the cellular prion protein (PubMed:11477090). Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity (PubMed:12475894). Also controls the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis (By similarity). Required for the development of type 1 transitional B cells into marginal zone B cells, probably by cleaving Notch (By similarity). Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form (PubMed:17557115). Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B (PubMed:19114711, PubMed:21288900). Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3 (By similarity). Mediates the proteolytic cleavage of IL6R and IL11RA, leading to the release of secreted forms of IL6R and IL11RA (PubMed:26876177). Enhances the cleavage of CHL1 by BACE1 (By similarity). Cleaves NRCAM (By similarity). Cleaves TREM2, resulting in shedding of the TREM2 ectodomain (PubMed:24990881). Involved in the development and maturation of glomerular and coronary vasculature (By similarity). During development of the cochlear organ of Corti, promotes pillar cell separation by forming a ternary complex with CADH1 and EPHA4 and cleaving CADH1 at adherens junctions (By similarity). May regulate the EFNA5-EPHA3 signaling (PubMed:16239146). Regulates leukocyte transmigration as a sheddase for the adherens junction protein VE-cadherin/CDH5 in endothelial cells (PubMed:28600292)", "gene_name": "ADAM10", "glycan_count": 58, "glycosylation_sites": [ { "position": 267, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 278, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 439, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 551, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O14672", "name": "ADAM10 (A Disintegrin and Metalloproteinase Domain 10)", "organism": "Homo sapiens", "uniprot_id": "O14672" }, { "function": "Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase (PubMed:10656250, PubMed:10677483, PubMed:20354142). Cleaves CHL1 (By similarity)", "gene_name": "BACE1", "glycan_count": 36, "glycosylation_sites": [ { "position": 153, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 172, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 223, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 354, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P56817", "name": "BACE1 (Beta-secretase 1)", "organism": "Homo sapiens", "uniprot_id": "P56817" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P08514/P05106", "name": "ITGA2B/ITGB3 (Glycoprotein IIb/IIIa)", "organism": "", "uniprot_id": "" }, { "function": "GP-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to the A1 domain of vWF, which is already bound to the subendothelium", "gene_name": "GP1BA", "glycan_count": 24, "glycosylation_sites": [ { "position": 37, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 175, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 308, "type": "O-linked (GalNAc...) threonine" }, { "position": 316, "type": "O-linked (GalNAc...) threonine" }, { "position": 320, "type": "O-linked (GalNAc...) threonine" }, { "position": 321, "type": "O-linked (GalNAc...) threonine" }, { "position": 328, "type": "O-linked (GalNAc...) serine" }, { "position": 331, "type": "O-linked (GalNAc...) threonine" }, { "position": 340, "type": "O-linked (GalNAc...) serine" }, { "position": 341, "type": "O-linked (GalNAc...) serine" }, { "position": 345, "type": "O-linked (GalNAc...) threonine" }, { "position": 353, "type": "O-linked (GalNAc...) threonine" }, { "position": 354, "type": "O-linked (GalNAc...) threonine" }, { "position": 360, "type": "O-linked (GalNAc...) threonine" }, { "position": 364, "type": "O-linked (GalNAc...) threonine" }, { "position": 369, "type": "O-linked (GalNAc...) serine" }, { "position": 371, "type": "O-linked (GalNAc...) threonine" }, { "position": 373, "type": "O-linked (GalNAc...) serine" }, { "position": 379, "type": "O-linked (GalNAc...) threonine" }, { "position": 380, "type": "O-linked (GalNAc...) threonine" }, { "position": 383, "type": "O-linked (GalNAc...) threonine" }, { "position": 385, "type": "O-linked (GalNAc...) serine" }, { "position": 387, "type": "O-linked (GalNAc...) threonine" }, { "position": 388, "type": "O-linked (GalNAc...) threonine" }, { "position": 389, "type": "O-linked (GalNAc...) serine" }, { "position": 400, "type": "O-linked (GalNAc...) threonine" }, { "position": 401, "type": "O-linked (GalNAc...) threonine" }, { "position": 405, "type": "O-linked (GalNAc...) threonine" }, { "position": 453, "type": "O-linked (GalNAc...) threonine" }, { "position": 457, "type": "O-linked (GalNAc...) threonine" }, { "position": 460, "type": "O-linked (GalNAc...) threonine" }, { "position": 461, "type": "O-linked (GalNAc...) serine" }, { "position": 463, "type": "O-linked (GalNAc...) threonine" }, { "position": 467, "type": "O-linked (GalNAc...) serine" }, { "position": 469, "type": "O-linked (GalNAc...) threonine" }, { "position": 473, "type": "O-linked (GalNAc...) threonine" }, { "position": 477, "type": "O-linked (GalNAc...) threonine" }, { "position": 480, "type": "O-linked (GalNAc...) threonine" }, { "position": 481, "type": "O-linked (GalNAc...) threonine" }, { "position": 482, "type": "O-linked (GalNAc...) threonine" }, { "position": 486, "type": "O-linked (GalNAc...) serine" }, { "position": 490, "type": "O-linked (GalNAc...) serine" }, { "position": 491, "type": "O-linked (GalNAc...) threonine" }, { "position": 494, "type": "O-linked (GalNAc...) threonine" } ], "id": "P07359", "name": "GPIBA (Glycoprotein Ib alpha)", "organism": "Homo sapiens", "uniprot_id": "P07359" }, { "function": "Receptor for adenosine (By similarity). The activity of this receptor is mediated by G proteins which activate adenylyl cyclase (By similarity)", "gene_name": "ADORA2A", "glycan_count": 0, "glycosylation_sites": [ { "position": 154, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P29274", "name": "ADORA2A (Adenosine A2a receptor)", "organism": "Homo sapiens", "uniprot_id": "P29274" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02468 (LAMA1)", "name": "Laminin", "organism": "", "uniprot_id": "" }, { "function": "Cytokine that promotes the proliferation, survival and differentiation of monocytes and macrophages. Promotes the release of pro-inflammatory chemokines, and thereby plays an important role in innate immunity and in inflammatory processes. Plays an important role in the regulation of osteoclast proliferation and differentiation, and in the regulation of bone resorption. Signaling via CSF1R and its downstream effectors stimulates phosphorylation of MAPK1/ERK2 AND MAPK3/ERK1", "gene_name": "IL34", "glycan_count": 3, "glycosylation_sites": [ { "position": 76, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6ZMJ4", "name": "IL-34", "organism": "Homo sapiens", "uniprot_id": "Q6ZMJ4" }, { "function": "Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19", "gene_name": "TIMP2", "glycan_count": 0, "glycosylation_sites": [], "id": "P16035", "name": "TIMP-2", "organism": "Homo sapiens", "uniprot_id": "P16035" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02462 (COL4A1)", "name": "Collagen IV", "organism": "", "uniprot_id": "" }, { "function": "Mitochondrial outer membrane GTPase that mediates mitochondrial clustering and fusion (PubMed:11181170, PubMed:11950885, PubMed:19889647, PubMed:26214738, PubMed:28114303). Mitochondria are highly dynamic organelles, and their morphology is determined by the equilibrium between mitochondrial fusion and fission events (PubMed:28114303). Overexpression induces the formation of mitochondrial networks (PubMed:28114303). Membrane clustering requires GTPase activity and may involve a major rearrangement of the coiled coil domains (Probable). Plays a central role in mitochondrial metabolism and may be associated with obesity and/or apoptosis processes (By similarity). Plays an important role in the regulation of vascular smooth muscle cell proliferation (By similarity). Involved in the clearance of damaged mitochondria via selective autophagy (mitophagy) (PubMed:23620051). Is required for PRKN recruitment to dysfunctional mitochondria (PubMed:23620051). Involved in the control of unfolded protein response (UPR) upon ER stress including activation of apoptosis and autophagy during ER stress (By similarity). Acts as an upstream regulator of EIF2AK3 and suppresses EIF2AK3 activation under basal conditions (By similarity)", "gene_name": "MFN2", "glycan_count": 0, "glycosylation_sites": [], "id": "O95140", "name": "MFN2", "organism": "Homo sapiens", "uniprot_id": "O95140" }, { "function": "Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade (PubMed:15140129, PubMed:15853774). AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa (PubMed:15140129). Its inhibitory activity is greatly enhanced in the presence of heparin", "gene_name": "SERPINC1", "glycan_count": 111, "glycosylation_sites": [ { "position": 128, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 167, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 187, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 224, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01008", "name": "Antithrombin III (AT III)", "organism": "Homo sapiens", "uniprot_id": "P01008" }, { "function": "Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids (PubMed:25618265). Exerts a protective effect on the endothelial cell barrier function (PubMed:25651845)", "gene_name": "PROC", "glycan_count": 56, "glycosylation_sites": [ { "position": 19, "type": "O-linked (GalNAc...) threonine" }, { "position": 139, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 290, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 355, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 371, "type": "N-linked (GlcNAc...) asparagine; atypical; partial" } ], "id": "P04070", "name": "Protein C", "organism": "Homo sapiens", "uniprot_id": "P04070" }, { "function": "Anticoagulant plasma protein; it is a cofactor to activated protein C in the degradation of coagulation factors Va and VIIIa. It helps to prevent coagulation and stimulating fibrinolysis", "gene_name": "PROS1", "glycan_count": 5, "glycosylation_sites": [ { "position": 499, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 509, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 530, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P07225", "name": "Protein S", "organism": "Homo sapiens", "uniprot_id": "P07225" }, { "function": "Central regulator of hemostasis. It serves as a critical cofactor for the prothrombinase activity of factor Xa that results in the activation of prothrombin to thrombin", "gene_name": "F5", "glycan_count": 77, "glycosylation_sites": [ { "position": 51, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 55, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 239, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 297, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 382, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 460, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 468, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 554, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 741, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 752, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 760, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 776, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 782, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 805, "type": "O-linked (GalNAc...) threonine" }, { "position": 821, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 938, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 977, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1074, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1083, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1103, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1106, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1479, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1499, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1559, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1703, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2010, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2209, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P12259", "name": "Coagulation Factor V", "organism": "Homo sapiens", "uniprot_id": "P12259" }, { "function": "Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa also converts factor IX to factor IXa in the presence of tissue factor and calcium (PubMed:271951)", "gene_name": "F7", "glycan_count": 18, "glycosylation_sites": [ { "position": 112, "type": "O-linked (Glc...) serine; alternate" }, { "position": 112, "type": "O-linked (Xyl...) serine; alternate" }, { "position": 120, "type": "O-linked (Fuc) serine" }, { "position": 205, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 382, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08709", "name": "Coagulation Factor VII", "organism": "Homo sapiens", "uniprot_id": "P08709" }, { "function": "Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa", "gene_name": "F9", "glycan_count": 37, "glycosylation_sites": [ { "position": 85, "type": "O-linked (GalNAc...) threonine" }, { "position": 99, "type": "O-linked (Glc...) serine" }, { "position": 107, "type": "O-linked (Fuc...) serine" }, { "position": 203, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 205, "type": "O-linked (GalNAc...) threonine; alternate" }, { "position": 213, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 215, "type": "O-linked (GalNAc...) threonine" }, { "position": 225, "type": "O-linked (GalNAc...) threonine" } ], "id": "P00740", "name": "Coagulation Factor IX", "organism": "Homo sapiens", "uniprot_id": "P00740" }, { "function": "Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting (PubMed:22409427). Factor Xa activates pro-inflammatory signaling pathways in a protease-activated receptor (PAR)-dependent manner (PubMed:24041930, PubMed:30568593, PubMed:34831181, PubMed:18202198). Up-regulates expression of protease-activated receptors (PARs) F2R, F2RL1 and F2RL2 in dermal microvascular endothelial cells (PubMed:35738824). Triggers the production of pro-inflammatory cytokines, such as MCP-1/CCL2 and IL6, in cardiac fibroblasts and umbilical vein endothelial cells in PAR-1/F2R-dependent manner (PubMed:30568593, PubMed:34831181). Triggers the production of pro-inflammatory cytokines, such as MCP-1/CCL2, IL6, TNF-alpha/TNF, IL-1beta/IL1B, IL8/CXCL8 and IL18, in endothelial cells and atrial tissues (PubMed:24041930, PubMed:35738824, PubMed:9780208). Induces expression of adhesion molecules, such as ICAM1, VCAM1 and SELE, in endothelial cells and atrial tissues (PubMed:24041930, PubMed:35738824, PubMed:9780208). Increases expression of phosphorylated ERK1/2 in dermal microvascular endothelial cells and atrial tissues (PubMed:24041930, PubMed:35738824). Triggers activation of the transcription factor NF-kappa-B in dermal microvascular endothelial cells and atrial tissues (PubMed:24041930, PubMed:35738824). Activates pro-inflammatory and pro-fibrotic responses in dermal fibroblasts and enhances wound healing probably via PAR-2/F2RL1-dependent mechanism (PubMed:18202198). Activates barrier protective signaling responses in endothelial cells in PAR-2/F2RL1-dependent manner; the activity depends on the cleavage of PAR-2/F2RL1 by factor Xa (PubMed:22409427). Up-regulates expression of plasminogen activator inhibitor 1 (SERPINE1) in atrial tissues (PubMed:24041930)", "gene_name": "F10", "glycan_count": 35, "glycosylation_sites": [ { "position": 199, "type": "O-linked (GalNAc...) threonine" }, { "position": 211, "type": "O-linked (GalNAc...) threonine" }, { "position": 221, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 231, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P00742", "name": "Coagulation Factor X", "organism": "Homo sapiens", "uniprot_id": "P00742" }, { "function": "Factor XI triggers the middle phase of the intrinsic pathway of blood coagulation by activating factor IX", "gene_name": "F11", "glycan_count": 43, "glycosylation_sites": [ { "position": 90, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 126, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 163, "type": "N-linked (GlcNAc...) (complex) asparagine; atypical" }, { "position": 450, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 491, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P03951", "name": "Coagulation Factor XI", "organism": "Homo sapiens", "uniprot_id": "P03951" }, { "function": "Translocates drugs and phospholipids across the membrane (PubMed:2897240, PubMed:35970996, PubMed:8898203, PubMed:9038218, PubMed:35507548). Catalyzes the flop of phospholipids from the cytoplasmic to the exoplasmic leaflet of the apical membrane. Participates mainly to the flop of phosphatidylcholine, phosphatidylethanolamine, beta-D-glucosylceramides and sphingomyelins (PubMed:8898203). Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells (PubMed:2897240, PubMed:35970996, PubMed:9038218)", "gene_name": "ABCB1", "glycan_count": 4, "glycosylation_sites": [ { "position": 91, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 94, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 99, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08183", "name": "P-glycoprotein (p-gp)", "organism": "Homo sapiens", "uniprot_id": "P08183" }, { "function": "Broad substrate specificity ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes a wide variety of physiological compounds, dietary toxins and xenobiotics from cells (PubMed:11306452, PubMed:12958161, PubMed:19506252, PubMed:20705604, PubMed:28554189, PubMed:30405239, PubMed:31003562). Involved in porphyrin homeostasis, mediating the export of protoporphyrin IX (PPIX) from both mitochondria to cytosol and cytosol to extracellular space, it also functions in the cellular export of heme (PubMed:20705604, PubMed:23189181). Also mediates the efflux of sphingosine-1-P from cells (PubMed:20110355). Acts as a urate exporter functioning in both renal and extrarenal urate excretion (PubMed:19506252, PubMed:20368174, PubMed:22132962, PubMed:31003562, PubMed:36749388). In kidney, it also functions as a physiological exporter of the uremic toxin indoxyl sulfate (By similarity). Also involved in the excretion of steroids like estrone 3-sulfate/E1S, 3beta-sulfooxy-androst-5-en-17-one/DHEAS, and other sulfate conjugates (PubMed:12682043, PubMed:28554189, PubMed:30405239). Mediates the secretion of the riboflavin and biotin vitamins into milk (By similarity). Extrudes pheophorbide a, a phototoxic porphyrin catabolite of chlorophyll, reducing its bioavailability (By similarity). Plays an important role in the exclusion of xenobiotics from the brain (Probable). It confers to cells a resistance to multiple drugs and other xenobiotics including mitoxantrone, pheophorbide, camptothecin, methotrexate, azidothymidine, and the anthracyclines daunorubicin and doxorubicin, through the control of their efflux (PubMed:11306452, PubMed:12477054, PubMed:15670731, PubMed:18056989, PubMed:31254042). In placenta, it limits the penetration of drugs from the maternal plasma into the fetus (By similarity). May play a role in early stem cell self-renewal by blocking differentiation (By similarity). In inflammatory macrophages, exports itaconate from the cytosol to the extracellular compartment and limits the activation of TFEB-dependent lysosome biogenesis involved in antibacterial innate immune response", "gene_name": "ABCG2", "glycan_count": 0, "glycosylation_sites": [ { "position": 596, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UNQ0", "name": "Breast Cancer Resistant Protein (BCRP)", "organism": "Homo sapiens", "uniprot_id": "Q9UNQ0" }, { "function": "Mediates export of organic anions and drugs from the cytoplasm (PubMed:10064732, PubMed:11114332, PubMed:16230346, PubMed:7961706, PubMed:9281595). Mediates ATP-dependent transport of glutathione and glutathione conjugates, leukotriene C4, estradiol-17-beta-o-glucuronide, methotrexate, antiviral drugs and other xenobiotics (PubMed:10064732, PubMed:11114332, PubMed:16230346, PubMed:7961706, PubMed:9281595). Confers resistance to anticancer drugs by decreasing accumulation of drug in cells, and by mediating ATP- and GSH-dependent drug export (PubMed:9281595). Hydrolyzes ATP with low efficiency (PubMed:16230346). Catalyzes the export of sphingosine 1-phosphate from mast cells independently of their degranulation (PubMed:17050692). Participates in inflammatory response by allowing export of leukotriene C4 from leukotriene C4-synthesizing cells (By similarity). Mediates ATP-dependent, GSH-independent cyclic GMP-AMP (cGAMP) export (PubMed:36070769). Thus, by limiting intracellular cGAMP concentrations negatively regulates the cGAS-STING pathway (PubMed:36070769). Exports S-geranylgeranyl-glutathione (GGG) in lymphoid cells and stromal compartments of lymphoid organs. ABCC1 (via extracellular transport) with GGT5 (via GGG catabolism) establish GGG gradients within lymphoid tissues to position P2RY8-positive lymphocytes at germinal centers in lymphoid follicles and restrict their chemotactic transmigration from blood vessels to the bone marrow parenchyma (By similarity). Mediates basolateral export of GSH-conjugated R- and S-prostaglandin A2 diastereomers in polarized epithelial cells (PubMed:9426231)", "gene_name": "ABCC1", "glycan_count": 2, "glycosylation_sites": [ { "position": 19, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 23, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1006, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P33527", "name": "Multidrug Resistant Protein 1 (MRP-1)", "organism": "Homo sapiens", "uniprot_id": "P33527" }, { "function": "Functions as extracellular chaperone that prevents aggregation of non native proteins (PubMed:11123922, PubMed:19535339). Prevents stress-induced aggregation of blood plasma proteins (PubMed:11123922, PubMed:12176985, PubMed:17260971, PubMed:19996109). Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro) (PubMed:12047389, PubMed:17407782, PubMed:17412999). Does not require ATP (PubMed:11123922). Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70 (PubMed:11123922). Does not refold proteins by itself (PubMed:11123922). Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation (PubMed:21505792). Protects cells against apoptosis and against cytolysis by complement: inhibits assembly of the complement membrane attack complex (MAC) by preventing polymerization of C9 pore component of the MAC complex (PubMed:2780565, PubMed:1903064, PubMed:2601725, PubMed:2721499, PubMed:1551440, PubMed:9200695, PubMed:34667172). Intracellular forms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:20068069). Promotes proteasomal degradation of COMMD1 and IKBKB (PubMed:20068069). Modulates NF-kappa-B transcriptional activity (PubMed:12882985). A mitochondrial form suppresses BAX-dependent release of cytochrome c into the cytoplasm and inhibit apoptosis (PubMed:16113678, PubMed:17689225). Plays a role in the regulation of cell proliferation (PubMed:19137541). An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5 (PubMed:22689054). Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (PubMed:24073260). Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity)", "gene_name": "CLU", "glycan_count": 295, "glycosylation_sites": [ { "position": 86, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 103, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 145, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 291, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 354, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 374, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P10909", "name": "Clusterin", "organism": "Homo sapiens", "uniprot_id": "P10909" }, { "function": "Glucosylceramidase that catalyzes, within the lysosomal compartment, the hydrolysis of glucosylceramides/GlcCers (such as beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine) into free ceramides (such as N-acylsphing-4-enine) and glucose (PubMed:15916907, PubMed:24211208, PubMed:32144204, PubMed:9201993). Plays a central role in the degradation of complex lipids and the turnover of cellular membranes (PubMed:27378698). Through the production of ceramides, participates in the PKC-activated salvage pathway of ceramide formation (PubMed:19279011). Catalyzes the glucosylation of cholesterol, through a transglucosylation reaction where glucose is transferred from GlcCer to cholesterol (PubMed:24211208, PubMed:26724485, PubMed:32144204). GlcCer containing mono-unsaturated fatty acids (such as beta-D-glucosyl-N-(9Z-octadecenoyl)-sphing-4-enine) are preferred as glucose donors for cholesterol glucosylation when compared with GlcCer containing same chain length of saturated fatty acids (such as beta-D-glucosyl-N-octadecanoyl-sphing-4-enine) (PubMed:24211208). Under specific conditions, may alternatively catalyze the reverse reaction, transferring glucose from cholesteryl 3-beta-D-glucoside to ceramide (Probable) (PubMed:26724485). Can also hydrolyze cholesteryl 3-beta-D-glucoside producing glucose and cholesterol (PubMed:24211208, PubMed:26724485). Catalyzes the hydrolysis of galactosylceramides/GalCers (such as beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine), as well as the transfer of galactose between GalCers and cholesterol in vitro, but with lower activity than with GlcCers (PubMed:32144204). Contrary to GlcCer and GalCer, xylosylceramide/XylCer (such as beta-D-xyosyl-(1<->1')-N-acylsphing-4-enine) is not a good substrate for hydrolysis, however it is a good xylose donor for transxylosylation activity to form cholesteryl 3-beta-D-xyloside (PubMed:33361282)", "gene_name": "GBA1", "glycan_count": 36, "glycosylation_sites": [ { "position": 58, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 98, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 185, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 309, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 501, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P04062", "name": "GBA", "organism": "Homo sapiens", "uniprot_id": "P04062" }, { "function": "Is a key player in the control of plasma membrane curvature, membrane shaping and membrane remodeling. Required in muscle cells for the formation of T-tubules, tubular invaginations of the plasma membrane that function in depolarization-contraction coupling (PubMed:24755653). Is a negative regulator of endocytosis (By similarity). Is also involved in the regulation of intracellular vesicles sorting, modulation of BACE1 trafficking and the control of amyloid-beta production (PubMed:27179792). In neuronal circuits, endocytosis regulation may influence the internalization of PHF-tau aggregates (By similarity). May be involved in the regulation of MYC activity and the control cell proliferation (PubMed:8782822). Has actin bundling activity and stabilizes actin filaments against depolymerization in vitro (PubMed:28893863)", "gene_name": "BIN1", "glycan_count": 1, "glycosylation_sites": [], "id": "O00499", "name": "BIN1", "organism": "Homo sapiens", "uniprot_id": "O00499" }, { "function": "Endoplasmic reticulum (ER)-anchored autophagy regulator which mediates ER delivery into lysosomes through sequestration into autophagosomes (PubMed:26040720, PubMed:31930741, PubMed:34338405). Promotes membrane remodeling and ER scission via its membrane bending capacity and targets the fragments into autophagosomes via interaction with ATG8 family proteins (PubMed:26040720, PubMed:31930741, PubMed:34338405). Active under basal conditions (PubMed:34338405). Required for collagen quality control in a LIR motif-dependent manner (By similarity). Required for long-term survival of nociceptive and autonomic ganglion neurons (PubMed:19838196, PubMed:26040720)", "gene_name": "RETREG1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H6L5", "name": "TMEM175", "organism": "Homo sapiens", "uniprot_id": "Q9H6L5" }, { "function": "The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. It is a crucial enzyme in transmembrane signaling", "gene_name": "PLCG2", "glycan_count": 1, "glycosylation_sites": [], "id": "P16885", "name": "PLCG2", "organism": "Homo sapiens", "uniprot_id": "P16885" }, { "function": "Deubiquitinase that mediates deubiquitination of target proteins such as BECN1, MITF, SKP2 and USP10 and is involved in various processes such as autophagy, endoplasmic reticulum-associated degradation (ERAD), cell cycle progression or DNA damage response (PubMed:21571647, PubMed:32772043, PubMed:33592542). Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. Alternatively, forms with NEDD4 a deubiquitination complex, which subsequently stabilizes VPS34 to promote autophagy (PubMed:32101753). Also deubiquitinates USP10, an essential regulator of p53/TP53 stability. In turn, PIK3C3/VPS34-containing complexes regulate USP13 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Recruited by nuclear UFD1 and mediates deubiquitination of SKP2, thereby regulating endoplasmic reticulum-associated degradation (ERAD). Also regulates ERAD through the deubiquitination of UBL4A a component of the BAG6/BAT3 complex. Mediates stabilization of SIAH2 independently of deubiquitinase activity: binds ubiquitinated SIAH2 and acts by impairing SIAH2 autoubiquitination. Regulates the cell cycle progression by stabilizing cell cycle proteins such as SKP2 and AURKB (PubMed:32772043). In addition, plays an important role in maintaining genomic stability and in DNA replication checkpoint activation via regulation of RAP80 and TOPBP1 (PubMed:33592542). Deubiquitinates the multifunctional protein HMGB1 and subsequently drives its nucleocytoplasmic localization and its secretion (PubMed:36585612). Positively regulates type I and type II interferon signalings by deubiquitinating STAT1 but negatively regulates antiviral response by deubiquitinating STING1 (PubMed:23940278, PubMed:28534493)", "gene_name": "USP13", "glycan_count": 1, "glycosylation_sites": [], "id": "Q92995", "name": "USP13", "organism": "Homo sapiens", "uniprot_id": "Q92995" }, { "function": "Forms a receptor signaling complex with TYROBP which mediates signaling and cell activation following ligand binding (PubMed:10799849). Acts as a receptor for amyloid-beta protein 42, a cleavage product of the amyloid-beta precursor protein APP, and mediates its uptake and degradation by microglia (PubMed:27477018, PubMed:29518356). Binding to amyloid-beta 42 mediates microglial activation, proliferation, migration, apoptosis and expression of pro-inflammatory cytokines, such as IL6R and CCL3, and the anti-inflammatory cytokine ARG1 (By similarity). Acts as a receptor for lipoprotein particles such as LDL, VLDL, and HDL and for apolipoproteins such as APOA1, APOA2, APOB, APOE, APOE2, APOE3, APOE4, and CLU and enhances their uptake in microglia (PubMed:27477018). Binds phospholipids (preferably anionic lipids) such as phosphatidylserine, phosphatidylethanolamine, phosphatidylglycerol and sphingomyelin (PubMed:29794134). Regulates microglial proliferation by acting as an upstream regulator of the Wnt/beta-catenin signaling cascade (By similarity). Required for microglial phagocytosis of apoptotic neurons (PubMed:24990881). Also required for microglial activation and phagocytosis of myelin debris after neuronal injury and of neuronal synapses during synapse elimination in the developing brain (By similarity). Regulates microglial chemotaxis and process outgrowth, and also the microglial response to oxidative stress and lipopolysaccharide (By similarity). It suppresses PI3K and NF-kappa-B signaling in response to lipopolysaccharide; thus promoting phagocytosis, suppressing pro-inflammatory cytokine and nitric oxide production, inhibiting apoptosis and increasing expression of IL10 and TGFB (By similarity). During oxidative stress, it promotes anti-apoptotic NF-kappa-B signaling and ERK signaling (By similarity). Plays a role in microglial MTOR activation and metabolism (By similarity). Regulates age-related changes in microglial numbers (PubMed:29752066). Triggers activation of the immune responses in macrophages and dendritic cells (PubMed:10799849). Mediates cytokine-induced formation of multinucleated giant cells which are formed by the fusion of macrophages (By similarity). In dendritic cells, receptor of SEMA6D with PLEXNA1 as coreceptor and mediates up-regulation of chemokine receptor CCR7 and dendritic cell maturation and survival (PubMed:11602640). Involved in the positive regulation of osteoclast differentiation (PubMed:12925681)", "gene_name": "TREM2", "glycan_count": 0, "glycosylation_sites": [ { "position": 20, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 79, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NZC2", "name": "TREM2", "organism": "Homo sapiens", "uniprot_id": "Q9NZC2" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P62158", "name": "CALM (Calmodulin)", "organism": "", "uniprot_id": "P62158" }, { "function": "Adapter protein which non-covalently associates with activating receptors found on the surface of a variety of immune cells to mediate signaling and cell activation following ligand binding by the receptors (PubMed:10604985, PubMed:9490415, PubMed:9655483). TYROBP is tyrosine-phosphorylated in the ITAM domain following ligand binding by the associated receptors which leads to activation of additional tyrosine kinases and subsequent cell activation (PubMed:9490415). Also has an inhibitory role in some cells (PubMed:21727189). Non-covalently associates with activating receptors of the CD300 family to mediate cell activation (PubMed:15557162, PubMed:16920917, PubMed:17928527, PubMed:26221034). Also mediates cell activation through association with activating receptors of the CD200R family (By similarity). Required for neutrophil activation mediated by integrin (By similarity). Required for the activation of myeloid cells mediated by the CLEC5A/MDL1 receptor (PubMed:10449773). Associates with natural killer (NK) cell receptors such as KIR2DS2 and the KLRD1/KLRC2 heterodimer to mediate NK cell activation (PubMed:23715743, PubMed:9490415, PubMed:9655483). Also enhances trafficking and cell surface expression of NK cell receptors KIR2DS1, KIR2DS2 and KIR2DS4 and ensures their stability at the cell surface (PubMed:23715743). Associates with SIRPB1 to mediate activation of myeloid cells such as monocytes and dendritic cells (PubMed:10604985). Associates with TREM1 to mediate activation of neutrophils and monocytes (PubMed:10799849). Associates with TREM2 on monocyte-derived dendritic cells to mediate up-regulation of chemokine receptor CCR7 and dendritic cell maturation and survival (PubMed:11602640). Association with TREM2 mediates cytokine-induced formation of multinucleated giant cells which are formed by the fusion of macrophages (PubMed:18957693). Stabilizes the TREM2 C-terminal fragment (TREM2-CTF) produced by TREM2 ectodomain shedding which suppresses the release of pro-inflammatory cytokines (PubMed:25957402). In microglia, required with TREM2 for phagocytosis of apoptotic neurons (By similarity). Required with ITGAM/CD11B in microglia to control production of microglial superoxide ions which promote the neuronal apoptosis that occurs during brain development (By similarity). Promotes pro-inflammatory responses in microglia following nerve injury which accelerates degeneration of injured neurons (By similarity). Positively regulates the expression of the IRAK3/IRAK-M kinase and IL10 production by liver dendritic cells and inhibits their T cell allostimulatory ability (By similarity). Negatively regulates B cell proliferation (PubMed:21727189). Required for CSF1-mediated osteoclast cytoskeletal organization (By similarity). Positively regulates multinucleation during osteoclast development (By similarity)", "gene_name": "TYROBP", "glycan_count": 0, "glycosylation_sites": [], "id": "O43914", "name": "DAP12", "organism": "Homo sapiens", "uniprot_id": "O43914" }, { "function": "", "gene_name": "SPATC1L", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H0A9", "name": "TMEM59", "organism": "Homo sapiens", "uniprot_id": "Q9H0A9" }, { "function": "Accessory component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation also seems to be implicated in vesicle formation and in uptake of lipid signaling molecules. The beta subunit may assist in binding of the phospholipid substrate. Required for the proper folding, assembly and ER to Golgi exit of the ATP8A2:TMEM30A flippase complex. ATP8A2:TMEM30A may be involved in regulation of neurite outgrowth, and, reconstituted to liposomes, predomiminantly transports phosphatidylserine (PS) and to a lesser extent phosphatidylethanolamine (PE). The ATP8A1:TMEM30A flippase complex seems to play a role in regulation of cell migration probably involving flippase-mediated translocation of phosphatidylethanolamine (PE) at the plasma membrane. Required for the formation of the ATP8A2, ATP8B1 and ATP8B2 P-type ATPAse intermediate phosphoenzymes. Involved in uptake of platelet-activating factor (PAF), synthetic drug alkylphospholipid edelfosine, and, probably in association with ATP8B1, of perifosine. Also mediates the export of alpha subunits ATP8A1, ATP8B1, ATP8B2, ATP8B4, ATP10A, ATP10B, ATP10D, ATP11A, ATP11B and ATP11C from the ER to other membrane localizations", "gene_name": "TMEM30A", "glycan_count": 36, "glycosylation_sites": [ { "position": 107, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 180, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 190, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 294, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NV96", "name": "NUS1 (Nogo-B receptor, NgBR)", "organism": "Homo sapiens", "uniprot_id": "Q9NV96" }, { "function": "Plays a role in intracellular protein trafficking and degradation (PubMed:11707463, PubMed:14570915, PubMed:15358775). May regulate CFTR chloride currents and acid-induced ASIC3 currents by modulating cell surface expression of both channels (By similarity). May also regulate the intracellular trafficking of the ADR1B receptor (PubMed:15358775). May play a role in autophagy (By similarity). Together with MARCHF2 mediates the ubiquitination and lysosomal degradation of CFTR (PubMed:23818989). Overexpression results in CFTR intracellular retention and lysosomaldegradation in the lysosomes (PubMed:11707463, PubMed:14570915)", "gene_name": "GOPC", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9HD26", "name": "GOPC", "organism": "Homo sapiens", "uniprot_id": "Q9HD26" }, { "function": "Receptor tyrosine kinase (RTK) that plays a role in epithelial cell differentiation and regionalization of the proximal epididymal epithelium. NELL2 is an endogenous ligand for ROS1. Upon endogenous stimulation by NELL2, ROS1 activates the intracellular signaling pathway and triggers epididymal epithelial differentiation and subsequent sperm maturation (By similarity). May activate several downstream signaling pathways related to cell differentiation, proliferation, growth and survival including the PI3 kinase-mTOR signaling pathway. Mediates the phosphorylation of PTPN11, an activator of this pathway. May also phosphorylate and activate the transcription factor STAT3 to control anchorage-independent cell growth. Mediates the phosphorylation and the activation of VAV3, a guanine nucleotide exchange factor regulating cell morphology. May activate other downstream signaling proteins including AKT1, MAPK1, MAPK3, IRS1 and PLCG2", "gene_name": "ROS1", "glycan_count": 1, "glycosylation_sites": [ { "position": 52, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 114, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 123, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 324, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 352, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 396, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 471, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 607, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 628, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 706, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 714, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 732, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 939, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 961, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1015, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1087, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1090, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1095, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1211, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1272, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1330, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1458, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1461, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1474, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1499, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1565, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1669, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1715, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1738, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1808, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08922", "name": "ROS1", "organism": "Homo sapiens", "uniprot_id": "P08922" }, { "function": "Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation. Impairs regulatory T-cells (Treg) function in individuals with rheumatoid arthritis via FOXP3 dephosphorylation. Up-regulates the expression of protein phosphatase 1 (PP1), which dephosphorylates the key 'Ser-418' residue of FOXP3, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208). Key mediator of cell death in the anticancer action of BCG-stimulated neutrophils in combination with DIABLO/SMAC mimetic in the RT4v6 bladder cancer cell line (PubMed:16829952, PubMed:22517918, PubMed:23396208). Induces insulin resistance in adipocytes via inhibition of insulin-induced IRS1 tyrosine phosphorylation and insulin-induced glucose uptake. Induces GKAP42 protein degradation in adipocytes which is partially responsible for TNF-induced insulin resistance (By similarity). Plays a role in angiogenesis by inducing VEGF production synergistically with IL1B and IL6 (PubMed:12794819). Promotes osteoclastogenesis and therefore mediates bone resorption (By similarity)", "gene_name": "TNF", "glycan_count": 5, "glycosylation_sites": [ { "position": 80, "type": "O-linked (GalNAc...) serine; in soluble form" } ], "id": "P01375", "name": "Tumor necrosis factor-alpha (TNF-\u03b1)", "organism": "Homo sapiens", "uniprot_id": "P01375" }, { "function": "Cytokine with a wide variety of biological functions in immunity, tissue regeneration, and metabolism. Binds to IL6R, then the complex associates to the signaling subunit IL6ST/gp130 to trigger the intracellular IL6-signaling pathway (Probable). The interaction with the membrane-bound IL6R and IL6ST stimulates 'classic signaling', whereas the binding of IL6 and soluble IL6R to IL6ST stimulates 'trans-signaling'. Alternatively, 'cluster signaling' occurs when membrane-bound IL6:IL6R complexes on transmitter cells activate IL6ST receptors on neighboring receiver cells (Probable)", "gene_name": "IL6", "glycan_count": 0, "glycosylation_sites": [ { "position": 73, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P05231", "name": "Interleukin-6 (IL-6)", "organism": "Homo sapiens", "uniprot_id": "P05231" }, { "function": "Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4), and some other non-histone substrates (PubMed:21030595, PubMed:21444723, PubMed:23911289, PubMed:25301942, PubMed:28167758, PubMed:28497810, PubMed:32404892, PubMed:22230954). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (PubMed:23911289). Histone deacetylases act via the formation of large multiprotein complexes, such as N-Cor repressor complex, which activate the histone deacetylase activity (PubMed:23911289, PubMed:22230954). Participates in the BCL6 transcriptional repressor activity by deacetylating the H3 'Lys-27' (H3K27) on enhancer elements, antagonizing EP300 acetyltransferase activity and repressing proximal gene expression (PubMed:23911289). Acts as a molecular chaperone for shuttling phosphorylated NR2C1 to PML bodies for sumoylation (By similarity). Contributes, together with XBP1 isoform 1, to the activation of NFE2L2-mediated HMOX1 transcription factor gene expression in a PI(3)K/mTORC2/Akt-dependent signaling pathway leading to endothelial cell (EC) survival under disturbed flow/oxidative stress (PubMed:25190803). Regulates both the transcriptional activation and repression phases of the circadian clock in a deacetylase activity-independent manner (By similarity). During the activation phase, promotes the accumulation of ubiquitinated BMAL1 at the E-boxes and during the repression phase, blocks FBXL3-mediated CRY1/2 ubiquitination and promotes the interaction of CRY1 and BMAL1 (By similarity). The NCOR1-HDAC3 complex regulates the circadian expression of the core clock gene BMAL1 and the genes involved in lipid metabolism in the liver (By similarity). Also functions as a deacetylase for non-histone targets, such as KAT5, MEF2D, MAPK14, RARA and STAT3 (PubMed:15653507, PubMed:21030595, PubMed:21444723, PubMed:25301942, PubMed:28167758). Serves as a corepressor of RARA, mediating its deacetylation and repression, leading to inhibition of RARE DNA element binding (PubMed:28167758). In association with RARA, plays a role in the repression of microRNA-10a and thereby in the inflammatory response (PubMed:28167758). In addition to protein deacetylase activity, also acts as a protein-lysine deacylase by recognizing other acyl groups: catalyzes removal of (2E)-butenoyl (crotonyl), lactoyl (lactyl) and 2-hydroxyisobutanoyl (2-hydroxyisobutyryl) acyl groups from lysine residues, leading to protein decrotonylation, delactylation and de-2-hydroxyisobutyrylation, respectively (PubMed:28497810, PubMed:29192674, PubMed:34608293, PubMed:35044827). Catalyzes decrotonylation of MAPRE1/EB1 (PubMed:34608293). Mediates delactylation NBN/NBS1, thereby inhibiting DNA double-strand breaks (DSBs) via homologous recombination (HR) (PubMed:38961290)", "gene_name": "HDAC3", "glycan_count": 2, "glycosylation_sites": [], "id": "O15379", "name": "Histone deacetylase 3 (HDAC3)", "organism": "Homo sapiens", "uniprot_id": "O15379" }, { "function": "Binds to disheveled (Dvl) and Rho, and mediates Wnt-induced Dvl-Rho complex formation. May play a role as a scaffolding protein to recruit Rho-GDP and Rho-GEF, thereby enhancing Rho-GTP formation. Can direct nucleation and elongation of new actin filaments. Involved in building functional cilia (PubMed:16630611, PubMed:17482208). Involved in the organization of the subapical actin network in multiciliated epithelial cells (By similarity). Together with DAAM2, required for myocardial maturation and sarcomere assembly (By similarity). During cell division, may regulate RHOA activation that signals spindle orientation and chromosomal segregation", "gene_name": "DAAM1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y4D1", "name": "TGN46", "organism": "Homo sapiens", "uniprot_id": "Q9Y4D1" }, { "function": "Lysosomal membrane glycoprotein which plays an important role in lysosome biogenesis, lysosomal pH regulation and autophagy (PubMed:11082038, PubMed:18644871, PubMed:24880125, PubMed:27628032, PubMed:36586411, PubMed:37390818, PubMed:8662539). Acts as an important regulator of lysosomal lumen pH regulation by acting as a direct inhibitor of the proton channel TMEM175, facilitating lysosomal acidification for optimal hydrolase activity (PubMed:37390818). Plays an important role in chaperone-mediated autophagy, a process that mediates lysosomal degradation of proteins in response to various stresses and as part of the normal turnover of proteins with a long biological half-live (PubMed:11082038, PubMed:18644871, PubMed:24880125, PubMed:27628032, PubMed:36586411, PubMed:8662539). Functions by binding target proteins, such as GAPDH, NLRP3 and MLLT11, and targeting them for lysosomal degradation (PubMed:11082038, PubMed:18644871, PubMed:24880125, PubMed:36586411, PubMed:8662539). In the chaperone-mediated autophagy, acts downstream of chaperones, such as HSPA8/HSC70, which recognize and bind substrate proteins and mediate their recruitment to lysosomes, where target proteins bind LAMP2 (PubMed:36586411). Plays a role in lysosomal protein degradation in response to starvation (By similarity). Required for the fusion of autophagosomes with lysosomes during autophagy (PubMed:27628032). Cells that lack LAMP2 express normal levels of VAMP8, but fail to accumulate STX17 on autophagosomes, which is the most likely explanation for the lack of fusion between autophagosomes and lysosomes (PubMed:27628032). Required for normal degradation of the contents of autophagosomes (PubMed:27628032). Required for efficient MHC class II-mediated presentation of exogenous antigens via its function in lysosomal protein degradation; antigenic peptides generated by proteases in the endosomal/lysosomal compartment are captured by nascent MHC II subunits (PubMed:15894275, PubMed:20518820). Is not required for efficient MHC class II-mediated presentation of endogenous antigens (PubMed:20518820)", "gene_name": "LAMP2", "glycan_count": 313, "glycosylation_sites": [ { "position": 32, "type": "N-linked (GlcNAc...) (polylactosaminoglycan) asparagine" }, { "position": 38, "type": "N-linked (GlcNAc...) (polylactosaminoglycan) asparagine" }, { "position": 49, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 58, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 75, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 101, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 123, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 179, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 195, "type": "O-linked (GalNAc...) serine" }, { "position": 196, "type": "O-linked (GalNAc...) threonine" }, { "position": 200, "type": "O-linked (GalNAc...) threonine" }, { "position": 203, "type": "O-linked (GalNAc...) threonine" }, { "position": 204, "type": "O-linked (GalNAc...) threonine" }, { "position": 207, "type": "O-linked (GalNAc...) serine; partial" }, { "position": 209, "type": "O-linked (GalNAc...) threonine; partial" }, { "position": 210, "type": "O-linked (GalNAc...) threonine" }, { "position": 211, "type": "O-linked (GalNAc...) threonine" }, { "position": 213, "type": "O-linked (GalNAc...) threonine; partial" }, { "position": 229, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 242, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 257, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 275, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 300, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 307, "type": "N-linked (GlcNAc...) (polylactosaminoglycan) asparagine" }, { "position": 317, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 356, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P13473", "name": "LAMP2", "organism": "Homo sapiens", "uniprot_id": "P13473" }, { "function": "Glycosyltransferase that generates the core 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins (PubMed:11677243). Plays a central role in many processes, such as angiogenesis, thrombopoiesis and kidney homeostasis development (By similarity)", "gene_name": "C1GALT1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NS00", "name": "C1GALT1", "organism": "Homo sapiens", "uniprot_id": "Q9NS00" }, { "function": "May regulate calcium-dependent activities in the endoplasmic reticulum lumen or post-ER compartment", "gene_name": "SDF4", "glycan_count": 3, "glycosylation_sites": [ { "position": 40, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9BRK5", "name": "Cab45", "organism": "Homo sapiens", "uniprot_id": "Q9BRK5" }, { "function": "Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells. CDH23 is required for establishing and/or maintaining the proper organization of the stereocilia bundle of hair cells in the cochlea and the vestibule during late embryonic/early postnatal development. It is part of the functional network formed by USH1C, USH1G, CDH23 and MYO7A that mediates mechanotransduction in cochlear hair cells. Required for normal hearing", "gene_name": "CDH23", "glycan_count": 4, "glycosylation_sites": [ { "position": 155, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 206, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 349, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 393, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 434, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 466, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 472, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 652, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 694, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 765, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 810, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 827, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 941, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1001, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1018, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1171, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1282, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1315, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1473, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1534, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1651, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1667, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1818, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1857, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1889, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1902, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2013, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2050, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2129, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2168, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2195, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2263, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2357, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2369, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2616, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2749, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2808, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2877, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2896, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2941, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2981, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9H251", "name": "GPR39", "organism": "Homo sapiens", "uniprot_id": "Q9H251" }, { "function": "Secreted protein that acts as a key regulator of lysosomal function and as a growth factor involved in inflammation, wound healing and cell proliferation (PubMed:12526812, PubMed:18378771, PubMed:28073925, PubMed:28453791, PubMed:28541286). Regulates protein trafficking to lysosomes, and also the activity of lysosomal enzymes (PubMed:28453791, PubMed:28541286). Also facilitates the acidification of lysosomes, causing degradation of mature CTSD by CTSB (PubMed:28073925). In addition, functions as a wound-related growth factor that acts directly on dermal fibroblasts and endothelial cells to promote division, migration and the formation of capillary-like tubule structures (By similarity). Also promotes epithelial cell proliferation by blocking TNF-mediated neutrophil activation preventing release of oxidants and proteases (PubMed:12526812). Moreover, modulates inflammation in neurons by preserving neurons survival, axonal outgrowth and neuronal integrity (PubMed:18378771)", "gene_name": "GRN", "glycan_count": 31, "glycosylation_sites": [ { "position": 118, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 236, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 265, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 368, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 530, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P28799", "name": "Progranulin (PGRN)", "organism": "Homo sapiens", "uniprot_id": "P28799" }, { "function": "Functions as a sorting receptor in the Golgi compartment and as a clearance receptor on the cell surface. Required for protein transport from the Golgi apparatus to the lysosomes by a pathway that is independent of the mannose-6-phosphate receptor (M6PR). Lysosomal proteins bind specifically to the receptor in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelysosomal compartment where the low pH mediates the dissociation of the complex (PubMed:16787399). The receptor is then recycled back to the Golgi for another round of trafficking through its binding to the retromer. Also required for protein transport from the Golgi apparatus to the endosomes. Promotes neuronal apoptosis by mediating endocytosis of the proapoptotic precursor forms of BDNF (proBDNF) and NGFB (proNGFB). Also acts as a receptor for neurotensin. May promote mineralization of the extracellular matrix during osteogenic differentiation by scavenging extracellular LPL. Probably required in adipocytes for the formation of specialized storage vesicles containing the glucose transporter SLC2A4/GLUT4 (GLUT4 storage vesicles, or GSVs). These vesicles provide a stable pool of SLC2A4 and confer increased responsiveness to insulin. May also mediate transport from the endoplasmic reticulum to the Golgi", "gene_name": "SORT1", "glycan_count": 71, "glycosylation_sites": [ { "position": 98, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 162, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 274, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 406, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 582, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 684, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q99523", "name": "Sortilin (SORT1)", "organism": "Homo sapiens", "uniprot_id": "Q99523" }, { "function": "Hormone involved in the regulation of erythrocyte proliferation and differentiation and the maintenance of a physiological level of circulating erythrocyte mass (PubMed:28283061). Binds to EPOR leading to EPOR dimerization and JAK2 activation thereby activating specific downstream effectors, including STAT1 and STAT3 (PubMed:9774108)", "gene_name": "EPO", "glycan_count": 208, "glycosylation_sites": [ { "position": 51, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 65, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 110, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 153, "type": "O-linked (GalNAc...) serine" } ], "id": "P01588", "name": "Erythropoietin (EPO)", "organism": "Homo sapiens", "uniprot_id": "P01588" }, { "function": "Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). As a member of the malate-aspartate shuttle, it has a key role in the intracellular NAD(H) redox balance. Is important for metabolite exchange between mitochondria and cytosol, and for amino acid metabolism. Facilitates cellular uptake of long-chain free fatty acids", "gene_name": "Got2", "glycan_count": 1, "glycosylation_sites": [], "id": "P05202", "name": "Alanine aminotransferase (ALT)", "organism": "Mus musculus", "uniprot_id": "P05202" }, { "function": "Integrin alpha-X/beta-2 is a receptor for fibrinogen. It recognizes the sequence G-P-R in fibrinogen. It mediates cell-cell interaction during inflammatory responses. It is especially important in monocyte adhesion and chemotaxis", "gene_name": "ITGAX", "glycan_count": 28, "glycosylation_sites": [ { "position": 61, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 89, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 392, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 697, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 735, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 899, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 939, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1050, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P20702", "name": "Itgax (CD11c)", "organism": "Homo sapiens", "uniprot_id": "P20702" }, { "function": "Lectin that functions as a pattern recognizing receptor (PRR) specific for beta-1,3-linked and beta-1,6-linked glucans, which constitute cell wall constituents from pathogenic bacteria and fungi (PubMed:11567029, PubMed:12423684). Necessary for the TLR2-mediated inflammatory response and activation of NF-kappa-B: upon beta-glucan binding, recruits SYK via its ITAM motif and promotes a signaling cascade that activates some CARD domain-BCL10-MALT1 (CBM) signalosomes, leading to the activation of NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways which stimulate expression of genes encoding pro-inflammatory cytokines and chemokines (By similarity). Enhances cytokine production in macrophages and dendritic cells (By similarity). Mediates production of reactive oxygen species in the cell (By similarity). Mediates phagocytosis of C.albicans conidia (PubMed:17230442). Binds T-cells in a way that does not involve their surface glycans and plays a role in T-cell activation. Stimulates T-cell proliferation. Induces phosphorylation of SCIMP after binding beta-glucans (By similarity)", "gene_name": "CLEC7A", "glycan_count": 2, "glycosylation_sites": [ { "position": 91, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9BXN2", "name": "Clec7a (Dectin-1)", "organism": "Homo sapiens", "uniprot_id": "Q9BXN2" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q05316", "name": "Cd68", "organism": "", "uniprot_id": "Q05316" }, { "function": "Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents", "gene_name": "LYZ", "glycan_count": 1, "glycosylation_sites": [], "id": "P61626", "name": "Lyz2", "organism": "Homo sapiens", "uniprot_id": "P61626" }, { "function": "High affinity inhibitor for cathepsin L, cathepsin L2 (cathepsin V), and legumain (PubMed:30425301). Involved in the regulation of epidermal cornification, and hair follicle morphogenesis and maintenance (PubMed:30425301)", "gene_name": "CST6", "glycan_count": 1, "glycosylation_sites": [ { "position": 137, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q15828", "name": "Cst7", "organism": "Homo sapiens", "uniprot_id": "Q15828" }, { "function": "Constitutively active G-protein coupled receptor that maintains high 3'-5'-cyclic adenosine monophosphate (cAMP) levels that a plays a role in serveral processes including meiotic arrest in oocytes or neuronal development via activation of numerous intracellular signaling pathways. Acts as an essential activator of thermogenic adipocytes and drives thermogenesis via its intrinsic G(s)-coupling activity without the requirement of a ligand (PubMed:34048700). Has a potential role in modulating a number of brain functions, including behavioral responses to stress (By similarity), amyloid-beta peptide generation in neurons (By similarity). Stimulates neurite outgrowth in cerebellar granular neurons modulated via PKA, ERK, and most strongly PI3K-mediated signaling pathways (By similarity)", "gene_name": "GPR3", "glycan_count": 0, "glycosylation_sites": [ { "position": 20, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P46089", "name": "GPR3", "organism": "Homo sapiens", "uniprot_id": "P46089" }, { "function": "Although its physiological function is unclear, it can inhibit neutrophil cathepsin G and mast cell chymase, both of which can convert angiotensin-1 to the active angiotensin-2", "gene_name": "SERPINA3", "glycan_count": 192, "glycosylation_sites": [ { "position": 33, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 93, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 106, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 127, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 186, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 271, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01011", "name": "SERPINA3", "organism": "Homo sapiens", "uniprot_id": "P01011" }, { "function": "Plays essential roles in both eye and limb development. Probable regulator of osteoblast differentiation", "gene_name": "SMOC1", "glycan_count": 9, "glycosylation_sites": [ { "position": 214, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 374, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9H4F8", "name": "SMOC1", "organism": "Homo sapiens", "uniprot_id": "Q9H4F8" }, { "function": "May be involved in mediating uptake of synaptic material during synapse remodeling or in mediating the synaptic clustering of AMPA glutamate receptors at a subset of excitatory synapses", "gene_name": "NPTX1", "glycan_count": 1, "glycosylation_sites": [ { "position": 154, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 193, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q15818", "name": "NPTX2", "organism": "Homo sapiens", "uniprot_id": "Q15818" }, { "function": "Catalyzes the reversible conversion of beta-D-fructose 1,6-bisphosphate (FBP) into two triose phosphate and plays a key role in glycolysis and gluconeogenesis (PubMed:14766013). In addition, may also function as scaffolding protein (By similarity)", "gene_name": "ALDOA", "glycan_count": 1, "glycosylation_sites": [], "id": "P04075", "name": "ALDOA", "organism": "Homo sapiens", "uniprot_id": "P04075" }, { "function": "Substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control, DNA damage response and translesion DNA synthesis. The DCX(DTL) complex, also named CRL4(CDT2) complex, mediates the polyubiquitination and subsequent degradation of CDT1, CDKN1A/p21(CIP1), FBH1, KMT5A and SDE2 (PubMed:16861906, PubMed:16949367, PubMed:16964240, PubMed:17085480, PubMed:18703516, PubMed:18794347, PubMed:18794348, PubMed:19332548, PubMed:20129063, PubMed:23478441, PubMed:23478445, PubMed:23677613, PubMed:27906959). CDT1 degradation in response to DNA damage is necessary to ensure proper cell cycle regulation of DNA replication (PubMed:16861906, PubMed:16949367, PubMed:17085480). CDKN1A/p21(CIP1) degradation during S phase or following UV irradiation is essential to control replication licensing (PubMed:18794348, PubMed:19332548). KMT5A degradation is also important for a proper regulation of mechanisms such as TGF-beta signaling, cell cycle progression, DNA repair and cell migration (PubMed:23478445). Most substrates require their interaction with PCNA for their polyubiquitination: substrates interact with PCNA via their PIP-box, and those containing the 'K+4' motif in the PIP box, recruit the DCX(DTL) complex, leading to their degradation. In undamaged proliferating cells, the DCX(DTL) complex also promotes the 'Lys-164' monoubiquitination of PCNA, thereby being involved in PCNA-dependent translesion DNA synthesis (PubMed:20129063, PubMed:23478441, PubMed:23478445, PubMed:23677613). The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1 (PubMed:26431207)", "gene_name": "DTL", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9NZJ0", "name": "GPR3", "organism": "Homo sapiens", "uniprot_id": "Q9NZJ0" }, { "function": "GFAP, a class-III intermediate filament, is a cell-specific marker that, during the development of the central nervous system, distinguishes astrocytes from other glial cells", "gene_name": "GFAP", "glycan_count": 1, "glycosylation_sites": [], "id": "P14136", "name": "GFAP", "organism": "Homo sapiens", "uniprot_id": "P14136" }, { "function": "Potent pro-inflammatory cytokine (PubMed:10653850, PubMed:12794819, PubMed:28331908, PubMed:3920526). Initially discovered as the major endogenous pyrogen, induces prostaglandin synthesis, neutrophil influx and activation, T-cell activation and cytokine production, B-cell activation and antibody production, and fibroblast proliferation and collagen production (PubMed:3920526). Promotes Th17 differentiation of T-cells. Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T-helper 1 (Th1) cells (PubMed:10653850). Plays a role in angiogenesis by inducing VEGF production synergistically with TNF and IL6 (PubMed:12794819). Involved in transduction of inflammation downstream of pyroptosis: its mature form is specifically released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore (PubMed:33377178, PubMed:33883744). Acts as a sensor of S.pyogenes infection in skin: cleaved and activated by pyogenes SpeB protease, leading to an inflammatory response that prevents bacterial growth during invasive skin infection (PubMed:28331908)", "gene_name": "IL1B", "glycan_count": 0, "glycosylation_sites": [], "id": "P01584", "name": "IL-1\u03b2", "organism": "Homo sapiens", "uniprot_id": "P01584" }, { "function": "Homodimeric cytokine expressed predominantly by T-lymphocytes and NK cells that plays an important role in the survival, differentiation, and chemotaxis of eosinophils (PubMed:2653458, PubMed:9010276). Also acts on activated and resting B-cells to induce immunoglobulin production, growth, and differentiation (By similarity). Mechanistically, exerts its biological effects through a receptor composed of IL5RA subunit and the cytokine receptor common subunit beta/CSF2RB (PubMed:1495999, PubMed:22528658). Binding to the receptor leads to activation of various kinases including LYN, SYK and JAK2 and thereby propagates signals through the RAS-MAPK and JAK-STAT5 pathways respectively (PubMed:7613138)", "gene_name": "IL5", "glycan_count": 0, "glycosylation_sites": [ { "position": 22, "type": "O-linked (GalNAc...) threonine" }, { "position": 47, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P05113", "name": "IL-5", "organism": "Homo sapiens", "uniprot_id": "P05113" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NZJ7/Q9NZJ6", "name": "Chil3/5", "organism": "", "uniprot_id": "" }, { "function": "Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone", "gene_name": "Ndufa7", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Z1P6", "name": "Ccl6", "organism": "Mus musculus", "uniprot_id": "Q9Z1P6" }, { "function": "May be involved in the control of cytoskeleton formation by regulating actin polymerization", "gene_name": "Kank3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Z1P7", "name": "Ccl9", "organism": "Mus musculus", "uniprot_id": "Q9Z1P7" }, { "function": "Scaffold protein of the presynaptic cytomatrix at the active zone (CAZ) which is the place in the synapse where neurotransmitter is released (PubMed:19812333). After synthesis, participates in the formation of Golgi-derived membranous organelles termed Piccolo-Bassoon transport vesicles (PTVs) that are transported along axons to sites of nascent synaptic contacts (By similarity). At the presynaptic active zone, regulates the spatial organization of synaptic vesicle cluster, the protein complexes that execute membrane fusion and compensatory endocytosis (By similarity). Organizes as well the readily releasable pool of synaptic vesicles and safeguards a fraction of them to be not immediately available for action potential-induced release (By similarity). Also functions in processes other than assembly such as the regulation of specific presynaptic protein ubiquitination by interacting with SIAH1 or the regulation of presynaptic autophagy (By similarity) (PubMed:28231469). Also mediates synapse to nucleus communication leading to reconfiguration of gene expression by associating with the transcriptional corepressor CTBP1 and by subsequently reducing the size of its pool available for nuclear import (By similarity)", "gene_name": "Pclo", "glycan_count": 2, "glycosylation_sites": [ { "position": 2686, "type": "O-linked (GlcNAc) threonine" }, { "position": 2960, "type": "O-linked (GlcNAc) serine" } ], "id": "Q9QYX7", "name": "Cxcl9", "organism": "Mus musculus", "uniprot_id": "Q9QYX7" }, { "function": "Plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. Required for normal ear development", "gene_name": "FGF3", "glycan_count": 0, "glycosylation_sites": [ { "position": 65, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P11487", "name": "Fgf3", "organism": "Homo sapiens", "uniprot_id": "P11487" }, { "function": "Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions and is involved in various processes including cellular proliferation, migration, adhesion and attachment, inflammatory response to CNS injury, regulation of vascular inflammation and adaptive responses of the heart to pressure overload and in myocardial function and remodeling. Binds to structural extracellular matrix (ECM) proteins and modulates the ECM in response to tissue damage, contributing to cardioprotective and adaptive ECM remodeling. Plays a role in ER stress response, via its interaction with the activating transcription factor 6 alpha (ATF6) which produces adaptive ER stress response factors and protects myocardium from pressure overload. May contribute to spinal presynaptic hypersensitivity and neuropathic pain states after peripheral nerve injury. May play a role in regulating protective astrogenesis from the subventricular zone (SVZ) niche after injury in a NOTCH1-dependent manner", "gene_name": "Thbs4", "glycan_count": 1, "glycosylation_sites": [ { "position": 614, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 650, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 943, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Z1T2", "name": "Pdgfd", "organism": "Mus musculus", "uniprot_id": "Q9Z1T2" }, { "function": "May function as an adapter protein or regulator of Ras signaling pathways, in synaptic junctions", "gene_name": "Cnksr2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Z1T4", "name": "Vegfd", "organism": "Rattus norvegicus", "uniprot_id": "Q9Z1T4" }, { "function": "Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway", "gene_name": "VTN", "glycan_count": 169, "glycosylation_sites": [ { "position": 86, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 169, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 242, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P04004", "name": "Vitronectin", "organism": "Homo sapiens", "uniprot_id": "P04004" }, { "function": "Specifically phosphorylates the agonist-occupied form of the beta-adrenergic and closely related receptors, probably inducing a desensitization of them (PubMed:19715378). Key regulator of LPAR1 signaling (PubMed:19306925). Competes with RALA for binding to LPAR1 thus affecting the signaling properties of the receptor (PubMed:19306925). Desensitizes LPAR1 and LPAR2 in a phosphorylation-independent manner (PubMed:19306925). Positively regulates ciliary smoothened (SMO)-dependent Hedgehog (Hh) signaling pathway by facilitating the trafficking of SMO into the cilium and the stimulation of SMO activity (By similarity). Inhibits relaxation of airway smooth muscle in response to blue light (PubMed:30284927)", "gene_name": "GRK2", "glycan_count": 0, "glycosylation_sites": [], "id": "P25098", "name": "GPCR kinase 2 (GRK2)", "organism": "Homo sapiens", "uniprot_id": "P25098" }, { "function": "Functions in regulating agonist-mediated G-protein coupled receptor (GPCR) signaling by mediating both receptor desensitization and resensitization processes. During homologous desensitization, beta-arrestins bind to the GPRK-phosphorylated receptor and sterically preclude its coupling to the cognate G-protein; the binding appears to require additional receptor determinants exposed only in the active receptor conformation. The beta-arrestins target many receptors for internalization by acting as endocytic adapters (CLASPs, clathrin-associated sorting proteins) and recruiting the GPRCs to the adapter protein 2 complex 2 (AP-2) in clathrin-coated pits (CCPs). However, the extent of beta-arrestin involvement appears to vary significantly depending on the receptor, agonist and cell type. Internalized arrestin-receptor complexes traffic to intracellular endosomes, where they remain uncoupled from G-proteins. Two different modes of arrestin-mediated internalization occur. Class A receptors, like ADRB2, OPRM1, ENDRA, D1AR and ADRA1B dissociate from beta-arrestin at or near the plasma membrane and undergo rapid recycling. Class B receptors, like AVPR2, AGTR1, NTSR1, TRHR and TACR1 internalize as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptors, for extended periods of time. Receptor resensitization then requires that receptor-bound arrestin is removed so that the receptor can be dephosphorylated and returned to the plasma membrane. Mediates endocytosis of CCR7 following ligation of CCL19 but not CCL21. Involved in internalization of P2RY1, P2RY4, P2RY6 and P2RY11 and ATP-stimulated internalization of P2RY2. Involved in phosphorylation-dependent internalization of OPRD1 and subsequent recycling or degradation. Involved in ubiquitination of IGF1R. Beta-arrestins function as multivalent adapter proteins that can switch the GPCR from a G-protein signaling mode that transmits short-lived signals from the plasma membrane via small molecule second messengers and ion channels to a beta-arrestin signaling mode that transmits a distinct set of signals that are initiated as the receptor internalizes and transits the intracellular compartment. Acts as a signaling scaffold for MAPK pathways such as MAPK1/3 (ERK1/2) and MAPK10 (JNK3). ERK1/2 and JNK3 activated by the beta-arrestin scaffold are largely excluded from the nucleus and confined to cytoplasmic locations such as endocytic vesicles, also called beta-arrestin signalosomes. Acts as a signaling scaffold for the AKT1 pathway. GPCRs for which the beta-arrestin-mediated signaling relies on both ARRB1 and ARRB2 (codependent regulation) include ADRB2, F2RL1 and PTH1R. For some GPCRs the beta-arrestin-mediated signaling relies on either ARRB1 or ARRB2 and is inhibited by the other respective beta-arrestin form (reciprocal regulation). Increases ERK1/2 signaling in AGTR1- and AVPR2-mediated activation (reciprocal regulation). Involved in CCR7-mediated ERK1/2 signaling involving ligand CCL19. Is involved in type-1A angiotensin II receptor/AGTR1-mediated ERK activity. Is involved in type-1A angiotensin II receptor/AGTR1-mediated MAPK10 activity. Is involved in dopamine-stimulated AKT1 activity in the striatum by disrupting the association of AKT1 with its negative regulator PP2A. Involved in AGTR1-mediated chemotaxis. Appears to function as signaling scaffold involved in regulation of MIP-1-beta-stimulated CCR5-dependent chemotaxis. Involved in attenuation of NF-kappa-B-dependent transcription in response to GPCR or cytokine stimulation by interacting with and stabilizing CHUK. Suppresses UV-induced NF-kappa-B-dependent activation by interacting with CHUK. The function is promoted by stimulation of ADRB2 and dephosphorylation of ARRB2. Involved in p53/TP53-mediated apoptosis by regulating MDM2 and reducing the MDM2-mediated degradation of p53/TP53. May serve as nuclear messenger for GPCRs. Upon stimulation of OR1D2, may be involved in regulation of gene expression during the early processes of fertilization. Also involved in regulation of receptors other than GPCRs. Involved in endocytosis of TGFBR2 and TGFBR3 and down-regulates TGF-beta signaling such as NF-kappa-B activation. Involved in endocytosis of low-density lipoprotein receptor/LDLR. Involved in endocytosis of smoothened homolog/Smo, which also requires GRK2. Involved in endocytosis of SLC9A5. Involved in endocytosis of ENG and subsequent TGF-beta-mediated ERK activation and migration of epithelial cells. Involved in Toll-like receptor and IL-1 receptor signaling through the interaction with TRAF6 which prevents TRAF6 autoubiquitination and oligomerization required for activation of NF-kappa-B and JUN (PubMed:26839314). Involved in insulin resistance by acting as insulin-induced signaling scaffold for SRC, AKT1 and INSR. Involved in regulation of inhibitory signaling of natural killer cells by recruiting PTPN6 and PTPN11 to KIR2DL1. Involved in IL8-mediated granule release in neutrophils. Involved in the internalization of the atypical chemokine receptor ACKR3. Acts as an adapter protein coupling FFAR4 receptor to specific downstream signaling pathways, as well as mediating receptor endocytosis (PubMed:22282525, PubMed:23809162). During the activation step of NLRP3 inflammasome, directly associates with NLRP3 leading to inhibition of pro-inflammatory cytokine release and inhibition of inflammation (PubMed:23809162)", "gene_name": "ARRB2", "glycan_count": 1, "glycosylation_sites": [], "id": "P32121", "name": "\u03b2-arrestin 2", "organism": "Homo sapiens", "uniprot_id": "P32121" }, { "function": "Plays a role in the control of regulated secretion in neural and endocrine cells, enhancing selectively low-frequency neurotransmission. Positively regulates vesicle fusion by maintaining the readily releasable pool of secretory vesicles (By similarity)", "gene_name": "SV2A", "glycan_count": 2, "glycosylation_sites": [ { "position": 498, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 548, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 573, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q7L0J3", "name": "Synaptic vesicle glycoprotein 2A (SV2A)", "organism": "Homo sapiens", "uniprot_id": "Q7L0J3" }, { "function": "Chemotactic for B-lymphocytes but not for T-lymphocytes, monocytes and neutrophils. Does not induce calcium release in B-lymphocytes. Binds to BLR1/CXCR5", "gene_name": "CXCL13", "glycan_count": 0, "glycosylation_sites": [], "id": "O43927", "name": "Chemokine (C-X-C motif) ligand 13", "organism": "Homo sapiens", "uniprot_id": "O43927" }, { "function": "Neurofilaments usually contain three intermediate filament proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of neuronal caliber. May additionally cooperate with the neuronal intermediate filament proteins PRPH and INA to form neuronal filamentous networks (By similarity)", "gene_name": "NEFL", "glycan_count": 1, "glycosylation_sites": [ { "position": 21, "type": "O-linked (GlcNAc) threonine" }, { "position": 27, "type": "O-linked (GlcNAc) serine" } ], "id": "P07196", "name": "Neurofilament light chain", "organism": "Homo sapiens", "uniprot_id": "P07196" }, { "function": "As an inhibitor of cysteine proteinases, this protein is thought to serve an important physiological role as a local regulator of this enzyme activity", "gene_name": "CST3", "glycan_count": 0, "glycosylation_sites": [], "id": "P01034", "name": "CST3 (Cystatin C)", "organism": "Homo sapiens", "uniprot_id": "P01034" }, { "function": "Degrades chitin, chitotriose and chitobiose. May participate in the defense against nematodes and other pathogens. Isoform 3 has no enzymatic activity", "gene_name": "CHIT1", "glycan_count": 1, "glycosylation_sites": [ { "position": 100, "type": "N-linked (GlcNAc...) asparagine; in variant S-102" } ], "id": "Q13231", "name": "CHIT1 (Chitotriosidase-1)", "organism": "Homo sapiens", "uniprot_id": "Q13231" }, { "function": "FABPs are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters", "gene_name": "FABP3", "glycan_count": 0, "glycosylation_sites": [], "id": "P05413", "name": "FABP3 (Fatty acid-binding protein 3)", "organism": "Homo sapiens", "uniprot_id": "P05413" }, { "function": "Catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein) (PubMed:10206644, PubMed:10545183, PubMed:10593990, PubMed:10811883, PubMed:10899933, PubMed:12679784, PubMed:12740439, PubMed:15274632, PubMed:20460383, PubMed:25043039, PubMed:26280335, PubMed:28269784, PubMed:30598546, PubMed:30630874). Requires the presence of the other members of the gamma-secretase complex for protease activity (PubMed:15274632, PubMed:25043039, PubMed:26280335, PubMed:30598546, PubMed:30630874). Plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins, and by regulating cytosolic CTNNB1 levels (PubMed:10593990, PubMed:10811883, PubMed:10899933, PubMed:9738936). Stimulates cell-cell adhesion via its interaction with CDH1; this stabilizes the complexes between CDH1 (E-cadherin) and its interaction partners CTNNB1 (beta-catenin), CTNND1 and JUP (gamma-catenin) (PubMed:11953314). Under conditions of apoptosis or calcium influx, cleaves CDH1 (PubMed:11953314). This promotes the disassembly of the complexes between CDH1 and CTNND1, JUP and CTNNB1, increases the pool of cytoplasmic CTNNB1, and thereby negatively regulates Wnt signaling (PubMed:11953314, PubMed:9738936). Required for normal embryonic brain and skeleton development, and for normal angiogenesis (By similarity). Mediates the proteolytic cleavage of EphB2/CTF1 into EphB2/CTF2 (PubMed:17428795, PubMed:28269784). The holoprotein functions as a calcium-leak channel that allows the passive movement of calcium from endoplasmic reticulum to cytosol and is therefore involved in calcium homeostasis (PubMed:16959576, PubMed:25394380). Involved in the regulation of neurite outgrowth (PubMed:15004326, PubMed:20460383). Is a regulator of presynaptic facilitation, spike transmission and synaptic vesicles replenishment in a process that depends on gamma-secretase activity. It acts through the control of SYT7 presynaptic expression (By similarity)", "gene_name": "PSEN1", "glycan_count": 0, "glycosylation_sites": [], "id": "P49768", "name": "Presenilin-1 (PSEN1)", "organism": "Homo sapiens", "uniprot_id": "P49768" }, { "function": "Negatively regulates periodontal ligament (PDL) differentiation and mineralization to ensure that the PDL is not ossified and to maintain homeostasis of the tooth-supporting system. Inhibits BMP2-induced cytodifferentiation of PDL cells by preventing its binding to BMPR1B/BMP type-1B receptor, resulting in inhibition of BMP-dependent activation of SMAD proteins (By similarity). Critical regulator of TGF-beta in articular cartilage and plays an essential role in cartilage homeostasis and osteoarthritis (OA) pathogenesis. Negatively regulates chondrogenesis in the articular cartilage by blocking the TGF-beta/receptor interaction on the cell surface and inhibiting the canonical TGF-beta/Smad signal. Binds calcium and plays a role in osteoblast-driven collagen biomineralization activity", "gene_name": "ASPN", "glycan_count": 124, "glycosylation_sites": [ { "position": 55, "type": "O-linked (GalNAc...) serine" }, { "position": 282, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9BXN1", "name": "CRTAC1", "organism": "Homo sapiens", "uniprot_id": "Q9BXN1" }, { "function": "Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding growth factor GAS6 and which is thus regulating many physiological processes including cell survival, cell proliferation, migration and differentiation. Ligand binding at the cell surface induces dimerization and autophosphorylation of AXL. Following activation by ligand, AXL binds and induces tyrosine phosphorylation of PI3-kinase subunits PIK3R1, PIK3R2 and PIK3R3; but also GRB2, PLCG1, LCK and PTPN11. Other downstream substrate candidates for AXL are CBL, NCK2, SOCS1 and TNS2. Recruitment of GRB2 and phosphatidylinositol 3 kinase regulatory subunits by AXL leads to the downstream activation of the AKT kinase. GAS6/AXL signaling plays a role in various processes such as endothelial cell survival during acidification by preventing apoptosis, optimal cytokine signaling during human natural killer cell development, hepatic regeneration, gonadotropin-releasing hormone neuron survival and migration, platelet activation, or regulation of thrombotic responses. Also plays an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response", "gene_name": "AXL", "glycan_count": 14, "glycosylation_sites": [ { "position": 43, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 157, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 198, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 339, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 345, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 401, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P30530", "name": "AXL", "organism": "Homo sapiens", "uniprot_id": "P30530" }, { "function": "Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7 and MMP-9", "gene_name": "TIMP4", "glycan_count": 0, "glycosylation_sites": [], "id": "Q99727", "name": "TIMP4", "organism": "Homo sapiens", "uniprot_id": "Q99727" }, { "function": "Neurofilaments usually contain three intermediate filament proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of neuronal caliber. NEFH has an important function in mature axons that is not subserved by the two smaller NF proteins. May additionally cooperate with the neuronal intermediate filament proteins PRPH and INA to form neuronal filamentous networks (By similarity)", "gene_name": "NEFH", "glycan_count": 1, "glycosylation_sites": [], "id": "P12036", "name": "NfL", "organism": "Homo sapiens", "uniprot_id": "P12036" }, { "function": "Metalloproteinase with a rather broad substrate specificity that can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates different molecules including growth factors, plasminogen or other matrix metalloproteinases such as MMP9 (PubMed:11029580, PubMed:1371271). Once released into the extracellular matrix (ECM), the inactive pro-enzyme is activated by the plasmin cascade signaling pathway (PubMed:2383557). Also acts intracellularly (PubMed:22265821). For example, in dopaminergic neurons, gets activated by the serine protease HTRA2 upon stress and plays a pivotal role in DA neuronal degeneration by mediating microglial activation and alpha-synuclein/SNCA cleavage (PubMed:21330369). In addition, plays a role in immune response and possesses antiviral activity against various viruses such as vesicular stomatitis virus, influenza A virus (H1N1) and human herpes virus 1 (PubMed:35940311). Mechanistically, translocates from the cytoplasm into the cell nucleus upon virus infection to influence NF-kappa-B activities (PubMed:35940311)", "gene_name": "MMP3", "glycan_count": 1, "glycosylation_sites": [], "id": "P08254", "name": "MMP3", "organism": "Homo sapiens", "uniprot_id": "P08254" }, { "function": "Serine protease which exhibits a preference for Arg over Lys in the substrate P1 position and for Ser or Pro in the P2 position. Shows activity against amyloid precursor protein, myelin basic protein, gelatin, casein and extracellular matrix proteins such as fibronectin, laminin, vitronectin and collagen. Degrades alpha-synuclein and prevents its polymerization, indicating that it may be involved in the pathogenesis of Parkinson disease and other synucleinopathies. May be involved in regulation of axon outgrowth following spinal cord injury. Tumor cells treated with a neutralizing KLK6 antibody migrate less than control cells, suggesting a role in invasion and metastasis", "gene_name": "KLK6", "glycan_count": 18, "glycosylation_sites": [ { "position": 134, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q92876", "name": "Kallikrein-6 (neurosin)", "organism": "Homo sapiens", "uniprot_id": "Q92876" }, { "function": "May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex", "gene_name": "DCAF4", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y4P5", "name": "TRAPPC11", "organism": "Homo sapiens", "uniprot_id": "Q8WV16" }, { "function": "May play a role in vesicular transport from endoplasmic reticulum to Golgi", "gene_name": "TRAPPC3", "glycan_count": 0, "glycosylation_sites": [], "id": "O43617", "name": "TRAPPC2", "organism": "Homo sapiens", "uniprot_id": "O43617" }, { "function": "Acts as a mitochondrial iron-sulfur (Fe-S) cluster assembly factor that facilitates (Fe-S) cluster insertion into a subset of mitochondrial proteins (By similarity). Probably acts together with the monothiol glutaredoxin GLRX5 (PubMed:27532772). May protect cells against oxidative stress (PubMed:22746225)", "gene_name": "BOLA1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9Y3E2", "name": "TRAPPC4", "organism": "Homo sapiens", "uniprot_id": "Q9Y3E2" }, { "function": "Plays a role in primary cilia formation (PubMed:26365339). May act as a downstream effector of HOXC8 possibly by transducing or transmitting extracellular information required for axial skeletal patterning during development (By similarity). May be involved in cartilage and bone development (By similarity). May play a role in the differentiation of cranial neural crest cells (By similarity)", "gene_name": "TAPT1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6NXT6", "name": "TRAPPC9", "organism": "Homo sapiens", "uniprot_id": "Q6NXT6" }, { "function": "Enhances DNA synthesis and may play a role in cell proliferation", "gene_name": "HDGFL3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y3E1", "name": "TRAPPC10", "organism": "Homo sapiens", "uniprot_id": "Q9Y3E1" }, { "function": "Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex. Its ability to bind ubiquitin probably plays a role in endosomal sorting of ubiquitinated cargo proteins by ESCRT complexes. The ESCRT-II complex may also play a role in transcription regulation, possibly via its interaction with ELL. Binds phosphoinosides such as PtdIns(3,4,5)P3", "gene_name": "VPS36", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y3E3", "name": "TRAPPC2L", "organism": "Homo sapiens", "uniprot_id": "Q86VN1" }, { "function": "Potential role in vesicular protein trafficking, mainly in the early secretory pathway. Contributes to the coupled localization of TMED2 and TMED10 in the cis-Golgi network", "gene_name": "TMED3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y3Q3", "name": "TRAPPC3", "organism": "Homo sapiens", "uniprot_id": "Q9Y3Q3" }, { "function": "Binds double-stranded RNA (regardless of the sequence) and tubulin. May play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site", "gene_name": "STAU1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y3Q2", "name": "TRAPPC6B", "organism": "Homo sapiens", "uniprot_id": "O95793" }, { "function": "Functions as a guanine nucleotide exchange factor (GEF), which activates Rap and Ras family of small GTPases by exchanging bound GDP for free GTP in a cAMP-dependent manner. Serves as a link between cell surface receptors and Rap/Ras GTPases in intracellular signaling cascades. Also acts as an effector for Rap1 by direct association with Rap1-GTP thereby leading to the amplification of Rap1-mediated signaling. Shows weak activity on HRAS. It is controversial whether RAPGEF2 binds cAMP and cGMP (PubMed:23800469, PubMed:10801446) or not (PubMed:10548487, PubMed:10608844, PubMed:11359771). Its binding to ligand-activated beta-1 adrenergic receptor ADRB1 leads to the Ras activation through the G(s)-alpha signaling pathway. Involved in the cAMP-induced Ras and Erk1/2 signaling pathway that leads to sustained inhibition of long term melanogenesis by reducing dendrite extension and melanin synthesis. Also provides inhibitory signals for cell proliferation of melanoma cells and promotes their apoptosis in a cAMP-independent nanner. Regulates cAMP-induced neuritogenesis by mediating the Rap1/B-Raf/ERK signaling through a pathway that is independent on both PKA and RAPGEF3/RAPGEF4. Involved in neuron migration and in the formation of the major forebrain fiber connections forming the corpus callosum, the anterior commissure and the hippocampal commissure during brain development. Involved in neuronal growth factor (NGF)-induced sustained activation of Rap1 at late endosomes and in brain-derived neurotrophic factor (BDNF)-induced axon outgrowth of hippocampal neurons. Plays a role in the regulation of embryonic blood vessel formation and in the establishment of basal junction integrity and endothelial barrier function. May be involved in the regulation of the vascular endothelial growth factor receptor KDR and cadherin CDH5 expression at allantois endothelial cell-cell junctions", "gene_name": "RAPGEF2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y4G8", "name": "TRAPPC14 (MAP11)", "organism": "Homo sapiens", "uniprot_id": "Q9Y4G8" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y4P6", "name": "TRAPPC12", "organism": "", "uniprot_id": "Q9Y4P6" }, { "function": "", "gene_name": "G6E", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UKT1", "name": "FKRP", "organism": "Homo sapiens", "uniprot_id": "Q9UKT1" }, { "function": "Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:2188730, PubMed:22431096, PubMed:2344612, PubMed:23666920, PubMed:24741066, PubMed:31434876, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:24741066, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamin A and C also regulate matrix stiffness by conferring nuclear mechanical properties (PubMed:23990565, PubMed:25127216). The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively (PubMed:2188730, PubMed:2344612). Lamin A and C are present in equal amounts in the lamina of mammals (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:31548606). Also invoved in DNA repair: recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends (PubMed:31548606). Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation (PubMed:10080180, PubMed:10814726, PubMed:11799477, PubMed:18551513, PubMed:22431096). Required for osteoblastogenesis and bone formation (PubMed:12075506, PubMed:15317753, PubMed:18611980). Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone (PubMed:10587585). Required for cardiac homeostasis (PubMed:10580070, PubMed:12927431, PubMed:18611980, PubMed:23666920)", "gene_name": "LMNA", "glycan_count": 2, "glycosylation_sites": [ { "position": 625, "type": "O-linked (GlcNAc) serine" }, { "position": 628, "type": "O-linked (GlcNAc) serine" } ], "id": "P02545", "name": "LMNA", "organism": "Homo sapiens", "uniprot_id": "P02545" }, { "function": "Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells", "gene_name": "ACTA1", "glycan_count": 1, "glycosylation_sites": [], "id": "P68133", "name": "ACTA1", "organism": "Homo sapiens", "uniprot_id": "P68133" }, { "function": "Cytosolic calcium-activated calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytosol and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules (PubMed:11741831, PubMed:16163667, PubMed:18268335, PubMed:18650434, PubMed:26115329). Repeated very high-level exercise increases the open probability of the channel and leads to Ca(2+) leaking into the cytoplasm (PubMed:18268335). Can also mediate the release of Ca(2+) from intracellular stores in neurons, and may thereby promote prolonged Ca(2+) signaling in the brain. Required for normal embryonic development of muscle fibers and skeletal muscle. Required for normal heart morphogenesis, skin development and ossification during embryogenesis (By similarity)", "gene_name": "RYR1", "glycan_count": 2, "glycosylation_sites": [], "id": "P21817", "name": "RYR1", "organism": "Homo sapiens", "uniprot_id": "P21817" }, { "function": "Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in interferon response and anterograde Golgi to endosome transport. The BCR(KLHL20) E3 ubiquitin ligase complex mediates the ubiquitination of DAPK1, leading to its degradation by the proteasome, thereby acting as a negative regulator of apoptosis (PubMed:20389280). The BCR(KLHL20) E3 ubiquitin ligase complex also specifically mediates 'Lys-33'-linked ubiquitination (PubMed:24768539). Involved in anterograde Golgi to endosome transport by mediating 'Lys-33'-linked ubiquitination of CORO7, promoting interaction between CORO7 and EPS15, thereby facilitating actin polymerization and post-Golgi trafficking (PubMed:24768539). Also acts as a regulator of endothelial migration during angiogenesis by controlling the activation of Rho GTPases. The BCR(KLHL20) E3 ubiquitin ligase complex acts as a regulator of neurite outgrowth by mediating ubiquitination and degradation of PDZ-RhoGEF/ARHGEF11 (PubMed:21670212). In case of tumor, the BCR(KLHL20) E3 ubiquitin ligase complex is involved in tumor hypoxia: following hypoxia, the BCR(KLHL20)complex mediates ubiquitination and degradation of PML, potentiating HIF-1 signaling and cancer progression (PubMed:21840486)", "gene_name": "KLHL20", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y2M5", "name": "KLHL40", "organism": "Homo sapiens", "uniprot_id": "Q9Y2M5" }, { "function": "Involved in the regulation of mitochondrial distribution and morphology (PubMed:17349998, PubMed:28544275, PubMed:28554942). Required for mitochondrial fusion and mitochondrial network formation (PubMed:28544275, PubMed:28554942)", "gene_name": "MSTO1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9BUK6", "name": "MSTO1", "organism": "Homo sapiens", "uniprot_id": "Q9BUK6" }, { "function": "Atlastin-1 (ATL1) is a membrane-anchored GTPase that mediates the GTP-dependent fusion of endoplasmic reticulum (ER) membranes, maintaining the continuous ER network. It facilitates the formation of three-way junctions where ER tubules intersect (PubMed:14506257, PubMed:18270207, PubMed:19665976, PubMed:27619977, PubMed:34817557, PubMed:38509071). Two atlastin-1 on neighboring ER tubules bind GTP and form loose homodimers through the GB1/RHD3-type G domains and 3HB regions. Upon GTP hydrolysis, the 3HB regions tighten, pulling the membranes together to drive their fusion. After fusion, the homodimer disassembles upon release of inorganic phosphate (Pi). Subsequently, GDP dissociates, resetting the monomers to a conformation ready for a new fusion cycle (PubMed:14506257, PubMed:21220294, PubMed:21368113, PubMed:23334294, PubMed:38509071). May also regulate more or less directly Golgi biogenesis (PubMed:17321752). Indirectly regulates axonal development (By similarity)", "gene_name": "ATL1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8WXF7", "name": "ATL1", "organism": "Homo sapiens", "uniprot_id": "Q8WXF7" }, { "function": "Catalytic subunit of the UDP-N-acetylglucosamine transferase complex that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. On the cytoplasmic face of the endoplasmic reticulum, the dimeric ALG13/ALG14 complex catalyzes the second step of dolichol pyrophosphate biosynthesis, transferring a beta1,4-linked N-acetylglucosamine (GlcNAc) from UDP-GlcNAc to GlcNAc-pyrophosphatedolichol (Gn-PDol) to produce N,N'-diacetylchitobiosyl diphosphodolichol. N,N'-diacetylchitobiosyl diphosphodolichol is a substrate for ALG1, the following enzyme in the biosynthetic pathway", "gene_name": "ALG13", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NP73", "name": "ALG13", "organism": "Homo sapiens", "uniprot_id": "Q9NP73" }, { "function": "Intracellular cholesterol transporter which acts in concert with NPC2 and plays an important role in the egress of cholesterol from the endosomal/lysosomal compartment (PubMed:10821832, PubMed:12554680, PubMed:18772377, PubMed:27238017, PubMed:9211849, PubMed:9927649). Unesterified cholesterol that has been released from LDLs in the lumen of the late endosomes/lysosomes is transferred by NPC2 to the cholesterol-binding pocket in the N-terminal domain of NPC1 (PubMed:18772377, PubMed:19563754, PubMed:27238017, PubMed:27378690, PubMed:28784760, PubMed:9211849, PubMed:9927649). Cholesterol binds to NPC1 with the hydroxyl group buried in the binding pocket (PubMed:19563754). Binds oxysterol with higher affinity than cholesterol. May play a role in vesicular trafficking in glia, a process that may be crucial for maintaining the structural and functional integrity of nerve terminals (Probable). Inhibits cholesterol-mediated mTORC1 activation throught its interaction with SLC38A9 (PubMed:28336668)", "gene_name": "NPC1", "glycan_count": 34, "glycosylation_sites": [ { "position": 70, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 122, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 135, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 158, "type": "N-linked (GlcNAc...) asparagine; atypical" }, { "position": 185, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 222, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 452, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 459, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 478, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 524, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 557, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 572, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 598, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 916, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 931, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 961, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 968, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1064, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1072, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O15118", "name": "NPC1", "organism": "Homo sapiens", "uniprot_id": "O15118" }, { "function": "Intracellular cholesterol transporter which acts in concert with NPC1 and plays an important role in the egress of cholesterol from the lysosomal compartment (PubMed:11125141, PubMed:15937921, PubMed:17018531, PubMed:18772377, PubMed:29580834). Unesterified cholesterol that has been released from LDLs in the lumen of the late endosomes/lysosomes is transferred by NPC2 to the cholesterol-binding pocket in the N-terminal domain of NPC1 (PubMed:17018531, PubMed:18772377, PubMed:27238017). May bind and mobilize cholesterol that is associated with membranes (PubMed:18823126). NPC2 binds cholesterol with a 1:1 stoichiometry (PubMed:17018531). Can bind a variety of sterols, including lathosterol, desmosterol and the plant sterols stigmasterol and beta-sitosterol (PubMed:17018531). The secreted form of NCP2 regulates biliary cholesterol secretion via stimulation of ABCG5/ABCG8-mediated cholesterol transport (By similarity)", "gene_name": "NPC2", "glycan_count": 32, "glycosylation_sites": [ { "position": 58, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 135, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P61916", "name": "NPC2", "organism": "Homo sapiens", "uniprot_id": "P61916" }, { "function": "Required for cytokinesis (PubMed:16040610). Essential for the structural integrity of the cleavage furrow and for completion of cleavage furrow ingression. Plays a role in bleb assembly during metaphase and anaphase of mitosis (PubMed:23870127). May play a significant role in podocyte cell migration (PubMed:24676636)", "gene_name": "ANLN", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NQW6", "name": "CLN5", "organism": "Homo sapiens", "uniprot_id": "Q9NQW6" }, { "function": "Acid protease active in intracellular protein breakdown. Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation (PubMed:27333034). Involved in the pathogenesis of several diseases such as breast cancer and possibly Alzheimer disease", "gene_name": "CTSD", "glycan_count": 116, "glycosylation_sites": [ { "position": 63, "type": "O-linked (GalNAc...) threonine" }, { "position": 134, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 263, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P07339", "name": "CLN10 (Cathepsin D)", "organism": "Homo sapiens", "uniprot_id": "P07339" }, { "function": "Lysosomal enzyme involved in the degradation pathway of dermatan sulfate and heparan sulfate", "gene_name": "IDS", "glycan_count": 9, "glycosylation_sites": [ { "position": 115, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 144, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 246, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 280, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 325, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 513, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 537, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P22304", "name": "IDS (Iduronate 2-sulfatase)", "organism": "Homo sapiens", "uniprot_id": "P22304" }, { "function": "", "gene_name": "IDUA", "glycan_count": 17, "glycosylation_sites": [ { "position": 110, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 190, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 336, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 372, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 415, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 451, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P35475", "name": "IDUA (Alpha-L-iduronidase)", "organism": "Homo sapiens", "uniprot_id": "P35475" }, { "function": "Catalyzes a step in lysosomal heparan sulfate degradation", "gene_name": "SGSH", "glycan_count": 12, "glycosylation_sites": [ { "position": 41, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 142, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 151, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 264, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 413, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P51688", "name": "SGSH (N-sulfoglucosamine sulfohydrolase)", "organism": "Homo sapiens", "uniprot_id": "P51688" }, { "function": "Histone methyltransferase that catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) via a non-processive mechanism. Part of chromatin remodeling machinery predominantly forms H3K4me1 and H3K4me2 methylation marks at active chromatin sites where transcription and DNA repair take place (PubMed:17707229, PubMed:25561738). Likely plays a redundant role with KMT2C in enriching H3K4me1 marks on primed and active enhancer elements (PubMed:24081332). Plays a central role in beta-globin locus transcription regulation by being recruited by NFE2 (PubMed:17707229). Plays an important role in controlling bulk H3K4me during oocyte growth and preimplantation development (By similarity). Required during the transcriptionally active period of oocyte growth for the establishment and/or maintenance of bulk H3K4 trimethylation (H3K4me3), global transcriptional silencing that preceeds resumption of meiosis, oocyte survival and normal zygotic genome activation (By similarity)", "gene_name": "KMT2B", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UMN6", "name": "NAGLU (Alpha-N-acetylglucosaminidase)", "organism": "Homo sapiens", "uniprot_id": "Q9UMN6" }, { "function": "NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins (PubMed:21908771, PubMed:22076378, PubMed:24703693, PubMed:29180469). Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation and deglutarylation of CPS1, thereby increasing CPS1 activity in response to elevated NAD levels during fasting (PubMed:22076378, PubMed:24703693). Activates SOD1 by mediating its desuccinylation, leading to reduced reactive oxygen species (PubMed:24140062). Activates SHMT2 by mediating its desuccinylation (PubMed:29180469). Modulates ketogenesis through the desuccinylation and activation of HMGCS2 (By similarity). Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. Can deacetylate cytochrome c (CYCS) and a number of other proteins in vitro such as UOX", "gene_name": "SIRT5", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y6E6", "name": "Angiopoietin-like protein 4", "organism": "Homo sapiens", "uniprot_id": "Q9NXA8" }, { "function": "Acts in part as a hepatokine that is involved in regulation of lipid and glucose metabolism (PubMed:11788823, PubMed:12909640, PubMed:23661675, PubMed:25495645). Proposed to play a role in the trafficking of energy substrates to either storage or oxidative tissues in response to food intake (By similarity). Has a stimulatory effect on plasma triglycerides (TG), which is achieved by suppressing plasma TG clearance via inhibition of LPL activity. The inhibition of LPL activity appears to be an indirect mechanism involving recruitment of proprotein convertases PCSK6 and FURIN to LPL leading to cleavage and dissociation of LPL from the cell surface; the function does not require ANGPTL3 proteolytic cleavage but seems to be mediated by the N-terminal domain, and is not inhibited by GPIHBP1 (PubMed:12097324, PubMed:19318355, PubMed:20581395). Can inhibit endothelial lipase, causing increased plasma levels of high density lipoprotein (HDL) cholesterol and phospholipids (PubMed:17110602, PubMed:19028676). Can bind to adipocytes to activate lipolysis, releasing free fatty acids and glycerol (PubMed:12565906). Suppresses LPL specifically in oxidative tissues which is required to route very low density lipoprotein (VLDL)-TG to white adipose tissue (WAT) for storage in response to food; the function may involve cooperation with circulating, liver-derived ANGPTL8 and ANGPTL4 expression in WAT (By similarity). Contributes to lower plasma levels of low density lipoprotein (LDL)-cholesterol by a mechanism that is independent of the canonical pathway implicating APOE and LDLR. May stimulate hypothalamic LPL activity (By similarity)", "gene_name": "ANGPTL3", "glycan_count": 16, "glycosylation_sites": [ { "position": 115, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 226, "type": "O-linked (GalNAc) threonine" }, { "position": 296, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 357, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y5C1", "name": "Angiopoietin-like protein 3", "organism": "Homo sapiens", "uniprot_id": "Q9Y5C1" }, { "function": "Induces sprouting in endothelial cells through an autocrine and paracrine action", "gene_name": "ANGPTL2", "glycan_count": 54, "glycosylation_sites": [ { "position": 164, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 192, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UKU9", "name": "Angiopoietin-like protein 2", "organism": "Homo sapiens", "uniprot_id": "Q9UKU9" }, { "function": "Hormone that acts as a blood lipid regulator by regulating serum triglyceride levels (PubMed:22569073, PubMed:22809513, PubMed:23150577). May be involved in the metabolic transition between fasting and refeeding: required to direct fatty acids to adipose tissue for storage in the fed state (By similarity)", "gene_name": "ANGPTL8", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6UXH0", "name": "Angiopoietin-like protein 8", "organism": "Homo sapiens", "uniprot_id": "Q6UXH0" }, { "function": "Required for normal Golgi function (PubMed:19536132, PubMed:30290151). Plays a role in SNARE-pin assembly and Golgi-to-ER retrograde transport via its interaction with SCFD1 (PubMed:19536132)", "gene_name": "COG4", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H9E3", "name": "COG4", "organism": "Homo sapiens", "uniprot_id": "Q9H9E3" }, { "function": "Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix", "gene_name": "SGCD", "glycan_count": 10, "glycosylation_sites": [ { "position": 60, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 108, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 284, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q92629", "name": "Delta-sarcoglycan (SGCD)", "organism": "Homo sapiens", "uniprot_id": "Q92629" }, { "function": "Major component of the vertebrate myofibrillar M band. Binds myosin, titin, and light meromyosin. This binding is dose dependent", "gene_name": "MYOM2", "glycan_count": 1, "glycosylation_sites": [], "id": "P54296", "name": "Myomesin-2 (MYOM2)", "organism": "Homo sapiens", "uniprot_id": "P54296" }, { "function": "Myozenins may serve as intracellular binding proteins involved in linking Z line proteins such as alpha-actinin, gamma-filamin, TCAP/telethonin, LDB3/ZASP and localizing calcineurin signaling to the sarcomere. Plays an important role in the modulation of calcineurin signaling. May play a role in myofibrillogenesis", "gene_name": "MYOZ2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NPC6", "name": "Myozenin-2 (MYOZ2)", "organism": "Homo sapiens", "uniprot_id": "Q9NPC6" }, { "function": "E3 ubiquitin-protein ligase that regulates several biological processes through the ubiquitin-mediated proteasomal degradation of various target proteins. Mediates 'Lys-48'-linked polyubiquitination of PRR5L and its subsequent proteasomal degradation thereby indirectly regulating cell migration through the mTORC2 complex. Ubiquitinates the caspases CASP8 and CASP10, promoting their proteasomal degradation, to negatively regulate cell death downstream of death domain receptors in the extrinsic pathway of apoptosis. Negatively regulates the tumor necrosis factor-mediated signaling pathway through targeting of RIPK1 to ubiquitin-mediated proteasomal degradation. Negatively regulates p53/TP53 through its direct ubiquitination and targeting to proteasomal degradation. Indirectly, may also negatively regulate p53/TP53 through ubiquitination and degradation of SFN. May also play a role in endocytic recycling", "gene_name": "RFFL", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8WZ73", "name": "E3 ubiquitin-protein ligase rififylin (RFFL)", "organism": "Homo sapiens", "uniprot_id": "Q8WZ73" }, { "function": "", "gene_name": "CALR", "glycan_count": 0, "glycosylation_sites": [], "id": "A0A7P0T861", "name": "Calreticulin", "organism": "Homo sapiens", "uniprot_id": "A0A7P0T861" }, { "function": "Plays an adhesive role by integrating collagen bundles. It is probably associated with the surface of interstitial collagen fibrils via COL1. The COL2 domain may then serve as a rigid arm which sticks out from the fibril and protrudes the large N-terminal globular domain into the extracellular space, where it might interact with other matrix molecules or cell surface receptors (By similarity)", "gene_name": "COL14A1", "glycan_count": 107, "glycosylation_sites": [ { "position": 94, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 137, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 372, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1384, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1388, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1476, "type": "O-linked (Gal...) hydroxylysine; alternate" }, { "position": 1485, "type": "O-linked (Gal...) hydroxylysine; partial" }, { "position": 1523, "type": "O-linked (Gal...) hydroxylysine; partial" }, { "position": 1526, "type": "O-linked (Gal...) hydroxylysine; partial" }, { "position": 1601, "type": "O-linked (Gal...) hydroxylysine; alternate" }, { "position": 1698, "type": "O-linked (Gal...) hydroxylysine; alternate" }, { "position": 1701, "type": "O-linked (Gal...) hydroxylysine; alternate" } ], "id": "Q05707", "name": "Collagen alpha-1(XIV) chain (COL14A1)", "organism": "Homo sapiens", "uniprot_id": "Q05707" }, { "function": "", "gene_name": "XPO1", "glycan_count": 0, "glycosylation_sites": [], "id": "A0A7I2V2S3", "name": "Exportin-1 (XPO1)", "organism": "Homo sapiens", "uniprot_id": "A0A7I2V2S3" }, { "function": "", "gene_name": "TPM3", "glycan_count": 0, "glycosylation_sites": [], "id": "P06753-5", "name": "Tropomyosin alpha-3 chain (TPM3)", "organism": "Homo sapiens", "uniprot_id": "P06753-5" }, { "function": "Essential for the organization of sarcomeric actin thin filaments in skeletal muscle (PubMed:25250574). Increases the rate of actin polymerization (PubMed:25250574)", "gene_name": "LMOD3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q0VAK6", "name": "Leiomodin-3 (LMOD3)", "organism": "Homo sapiens", "uniprot_id": "Q0VAK6" }, { "function": "K(+) channel that conducts voltage-dependent outward rectifying currents upon membrane depolarization. Voltage sensing is coupled to K(+) electrochemical gradient in an 'ion flux gating' mode where outward but not inward ion flow opens the gate. Converts to voltage-independent 'leak' conductance mode upon stimulation by various stimuli including mechanical membrane stretch, acidic pH, heat and lipids. Reversibly converts between a voltage-insensitive K(+) 'leak' channel and a voltage-dependent outward rectifying K(+) channel in a phosphorylation-dependent manner (By similarity) (PubMed:10321245, PubMed:10784345, PubMed:11319556, PubMed:23169818, PubMed:30573346, PubMed:38605031). Homo- and heterodimerizes to form functional channels with distinct regulatory and gating properties (By similarity). In trigeminal ganglia sensory neurons, the heterodimer of KCNK2/TREK-1 and KCNK18/TRESK inhibits neuronal firing and neurogenic inflammation by stabilizing the resting membrane potential at K(+) equilibrium potential as well as by regulating the threshold of action potentials and the spike frequency (By similarity). At trigeminal A-beta afferent nerves, the heterodimer of KCNK2/TREK-1 and KCNK4/TRAAK is mostly coexpressed at nodes of Ranvier where it conducts voltage-independent mechanosensitive and thermosensitive currents, allowing rapid action potential repolarization, high speed and high frequence saltatory conduction on myelinated nerves to ensure prompt sensory responses (By similarity). In hippocampal astrocytes, the heterodimer of KCNK2/TREK-1 and KCNK1/TWIK-1 allows passive K(+) conductance under basal conditions, but changes ion selectivity and becomes permeable to L-glutamate and Cl(-) ions upon binding to G-protein subunit GNG4 in stimulated astrocytes. Mediates rapid L-glutamate release in response to activation of G-protein-coupled receptors, such as F2R and CNR1 (By similarity). In hippocampal pyramidal neurons, the homodimer of KCNK2/TREK-1 contributes to gamma-aminobutyric acid (GABA) B-induced slow inhibitory postsynaptic potential. Associates with AKAP5 and Gs-protein-coupled receptor B2AR at postsynaptic dense bodies and converts to a leak channel no longer sensitive to stimulation by arachidonic acid, acidic pH or mechanical stress, nor inhibited by Gq-coupled receptors but still under the negative control of Gs-coupled receptors (By similarity). Permeable to other monovalent cations such as Rb(+) and Cs(+) (By similarity)", "gene_name": "KCNK2", "glycan_count": 1, "glycosylation_sites": [ { "position": 110, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 134, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O95069", "name": "KCC2 (SLC12A5)", "organism": "Homo sapiens", "uniprot_id": "O95069" }, { "function": "A cytochrome P450 monooxygenase involved in the metabolism of sterols, steroid hormones, retinoids and fatty acids (PubMed:10681376, PubMed:11093772, PubMed:11555828, PubMed:12865317, PubMed:14559847, PubMed:15373842, PubMed:15764715, PubMed:19965576, PubMed:20702771, PubMed:21490593, PubMed:21576599). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds (PubMed:12865317, PubMed:14559847, PubMed:15373842, PubMed:15764715, PubMed:21490593, PubMed:21576599, PubMed:2732228). Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2, as well as D-ring hydroxylated E1 and E2 at the C-16 position (PubMed:11555828, PubMed:12865317, PubMed:14559847). Plays a role in the metabolism of androgens, particularly in oxidative deactivation of testosterone (PubMed:15373842, PubMed:15764715, PubMed:22773874, PubMed:2732228). Metabolizes testosterone to less biologically active 2beta- and 6beta-hydroxytestosterones (PubMed:15373842, PubMed:15764715, PubMed:2732228). Contributes to the formation of hydroxycholesterols (oxysterols), particularly A-ring hydroxylated cholesterol at the C-4beta position, and side chain hydroxylated cholesterol at the C-25 position, likely contributing to cholesterol degradation and bile acid biosynthesis (PubMed:21576599). Catalyzes bisallylic hydroxylation of polyunsaturated fatty acids (PUFA) (PubMed:9435160). Catalyzes the epoxidation of double bonds of PUFA with a preference for the last double bond (PubMed:19965576). Metabolizes endocannabinoid arachidonoylethanolamide (anandamide) to 8,9-, 11,12-, and 14,15-epoxyeicosatrienoic acid ethanolamides (EpETrE-EAs), potentially modulating endocannabinoid system signaling (PubMed:20702771). Plays a role in the metabolism of retinoids. Displays high catalytic activity for oxidation of all-trans-retinol to all-trans-retinal, a rate-limiting step for the biosynthesis of all-trans-retinoic acid (atRA) (PubMed:10681376). Further metabolizes atRA toward 4-hydroxyretinoate and may play a role in hepatic atRA clearance (PubMed:11093772). Responsible for oxidative metabolism of xenobiotics. Acts as a 2-exo-monooxygenase for plant lipid 1,8-cineole (eucalyptol) (PubMed:11159812). Metabolizes the majority of the administered drugs. Catalyzes sulfoxidation of the anthelmintics albendazole and fenbendazole (PubMed:10759686). Hydroxylates antimalarial drug quinine (PubMed:8968357). Acts as a 1,4-cineole 2-exo-monooxygenase (PubMed:11695850). Also involved in vitamin D catabolism and calcium homeostasis. Catalyzes the inactivation of the active hormone calcitriol (1-alpha,25-dihydroxyvitamin D(3)) (PubMed:29461981)", "gene_name": "CYP3A4", "glycan_count": 0, "glycosylation_sites": [], "id": "P08684", "name": "Cytochrome P450 3A (CYP3A)", "organism": "Homo sapiens", "uniprot_id": "P08684" }, { "function": "UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile (PubMed:12181437, PubMed:15472229, PubMed:18004206, PubMed:18004212, PubMed:18719240, PubMed:19830808, PubMed:23288867, PubMed:15231852, PubMed:21422672, PubMed:38211441). Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds (PubMed:12181437, PubMed:18004206, PubMed:18004212). Catalyzes the glucuronidation of endogenous estrogen hormones such as estradiol, estrone and estriol (PubMed:15472229, PubMed:18719240, PubMed:23288867). Involved in the glucuronidation of bilirubin, a degradation product occurring in the normal catabolic pathway that breaks down heme in vertebrates (PubMed:17187418, PubMed:18004206, PubMed:19830808, PubMed:24525562). Involved in the glucuronidation of arachidonic acid (AA) and AA-derived eicosanoids including 15-HETE, 20-HETE, PGB1 and F2-isoprostane (8-iso-PGF2alpha) (PubMed:15231852, PubMed:38211441). Involved in the glucuronidation of the phytochemical ferulic acid at the phenolic or the carboxylic acid group (PubMed:21422672). Also catalyzes the glucuronidation the isoflavones genistein, daidzein, glycitein, formononetin, biochanin A and prunetin, which are phytoestrogens with anticancer and cardiovascular properties (PubMed:18052087, PubMed:19545173). Involved in the glucuronidation of the AGTR1 angiotensin receptor antagonist losartan, a drug which can inhibit the effect of angiotensin II (PubMed:18674515). Involved in the biotransformation of 7-ethyl-10-hydroxycamptothecin (SN-38), the pharmacologically active metabolite of the anticancer drug irinotecan (PubMed:12181437, PubMed:18004212, PubMed:20610558)", "gene_name": "UGT1A1", "glycan_count": 3, "glycosylation_sites": [ { "position": 102, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 295, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 347, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P22309", "name": "UDP-glucuronosyltransferase 1A1 (UGT1A1)", "organism": "Homo sapiens", "uniprot_id": "P22309" }, { "function": "Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41", "gene_name": "env", "glycan_count": 0, "glycosylation_sites": [ { "position": 88, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 136, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 141, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 156, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 160, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 186, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 197, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 230, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 234, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 241, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 262, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 276, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 289, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 295, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 301, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 332, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 339, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 356, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 386, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 392, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 397, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 406, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 448, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 463, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 611, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 616, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 624, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 637, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 674, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P04578", "name": "HIV-1 gp120", "organism": "Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)", "uniprot_id": "P04578" }, { "function": "Pro-inflammatory cytokine that is involved in a wide variety of processes such as chemotaxis, differentiation, and activation of peripheral immune cells, regulation of cell growth, apoptosis and modulation of angiostatic effects (PubMed:11157474, PubMed:22652417, PubMed:7540647). Plays thereby an important role during viral infections by stimulating the activation and migration of immune cells to the infected sites (By similarity). Mechanistically, binding of CXCL10 to the CXCR3 receptor activates G protein-mediated signaling and results in downstream activation of phospholipase C-dependent pathway, an increase in intracellular calcium production and actin reorganization (PubMed:12750173, PubMed:19151743). In turn, recruitment of activated Th1 lymphocytes occurs at sites of inflammation (PubMed:12663757, PubMed:12750173). Activation of the CXCL10/CXCR3 axis also plays an important role in neurons in response to brain injury for activating microglia, the resident macrophage population of the central nervous system, and directing them to the lesion site. This recruitment is an essential element for neuronal reorganization (By similarity)", "gene_name": "CXCL10", "glycan_count": 0, "glycosylation_sites": [], "id": "P02778", "name": "CXCL10", "organism": "Homo sapiens", "uniprot_id": "P02778" }, { "function": "Major immune regulatory cytokine that acts on many cells of the immune system where it has profound anti-inflammatory functions, limiting excessive tissue disruption caused by inflammation. Mechanistically, IL10 binds to its heterotetrameric receptor comprising IL10RA and IL10RB leading to JAK1 and STAT2-mediated phosphorylation of STAT3 (PubMed:16982608). In turn, STAT3 translocates to the nucleus where it drives expression of anti-inflammatory mediators (PubMed:18025162). Targets antigen-presenting cells (APCs) such as macrophages and monocytes and inhibits their release of pro-inflammatory cytokines including granulocyte-macrophage colony-stimulating factor /GM-CSF, granulocyte colony-stimulating factor/G-CSF, IL-1 alpha, IL-1 beta, IL-6, IL-8 and TNF-alpha (PubMed:11564774, PubMed:1940799, PubMed:7512027). Also interferes with antigen presentation by reducing the expression of MHC-class II and co-stimulatory molecules, thereby inhibiting their ability to induce T cell activation (PubMed:8144879). In addition, controls the inflammatory response of macrophages by reprogramming essential metabolic pathways including mTOR signaling (By similarity)", "gene_name": "IL10", "glycan_count": 0, "glycosylation_sites": [ { "position": 134, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P22301", "name": "IL-10", "organism": "Homo sapiens", "uniprot_id": "P22301" }, { "function": "Chemotactic factor that mediates inflammatory response by attracting neutrophils, basophils, and T-cells to clear pathogens and protect the host from infection (PubMed:18692776, PubMed:7636208). Also plays an important role in neutrophil activation (PubMed:2145175, PubMed:9623510). Released in response to an inflammatory stimulus, exerts its effect by binding to the G-protein-coupled receptors CXCR1 and CXCR2, primarily found in neutrophils, monocytes and endothelial cells (PubMed:1840701, PubMed:1891716). G-protein heterotrimer (alpha, beta, gamma subunits) constitutively binds to CXCR1/CXCR2 receptor and activation by IL8 leads to beta and gamma subunits release from Galpha (GNAI2 in neutrophils) and activation of several downstream signaling pathways including PI3K and MAPK pathways (PubMed:11971003, PubMed:8662698)", "gene_name": "CXCL8", "glycan_count": 0, "glycosylation_sites": [], "id": "P10145", "name": "IL-8", "organism": "Homo sapiens", "uniprot_id": "P10145" }, { "function": "Acts as a ligand for C-C chemokine receptor CCR2 (PubMed:10529171, PubMed:10587439, PubMed:9837883). Signals through binding and activation of CCR2 and induces a strong chemotactic response and mobilization of intracellular calcium ions (PubMed:10587439, PubMed:9837883). Exhibits a chemotactic activity for monocytes and basophils but not neutrophils or eosinophils (PubMed:8195247, PubMed:8627182, PubMed:9792674). May be involved in the recruitment of monocytes into the arterial wall during the disease process of atherosclerosis (PubMed:8107690)", "gene_name": "CCL2", "glycan_count": 0, "glycosylation_sites": [ { "position": 37, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P13500", "name": "CCL2", "organism": "Homo sapiens", "uniprot_id": "P13500" }, { "function": "Subunit of heteromeric glycine-gated chloride channels (PubMed:14551753, PubMed:23994010, PubMed:25730860, PubMed:37821459). Plays an important role in the down-regulation of neuronal excitability (PubMed:8298642, PubMed:9009272). Contributes to the generation of inhibitory postsynaptic currents (PubMed:25445488). Channel activity is potentiated by ethanol (PubMed:25973519). Potentiation of channel activity by intoxicating levels of ethanol contribute to the sedative effects of ethanol (By similarity)", "gene_name": "GLRA1", "glycan_count": 0, "glycosylation_sites": [ { "position": 66, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P23415", "name": "GLRA1 (Glycine Receptor Alpha 1)", "organism": "Homo sapiens", "uniprot_id": "P23415" }, { "function": "", "gene_name": "SLC6A16", "glycan_count": 0, "glycosylation_sites": [ { "position": 229, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9GZN6", "name": "SLC6A5 (Glycine Transporter 2)", "organism": "Homo sapiens", "uniprot_id": "Q9GZN6" }, { "function": "Subunit of heteromeric glycine-gated chloride channels (PubMed:11929858, PubMed:15302677, PubMed:16144831, PubMed:22715885, PubMed:23238346, PubMed:25445488, PubMed:34473954, PubMed:8717357). Plays an important role in the down-regulation of neuronal excitability (PubMed:11929858, PubMed:23238346). Contributes to the generation of inhibitory postsynaptic currents (PubMed:25445488)", "gene_name": "GLRB", "glycan_count": 1, "glycosylation_sites": [ { "position": 54, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 242, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P48167", "name": "GLRB (Glycine Receptor Beta)", "organism": "Homo sapiens", "uniprot_id": "P48167" }, { "function": "Microtubule-associated protein involved in membrane protein-cytoskeleton interactions. It is thought to anchor the inhibitory glycine receptor (GLYR) to subsynaptic microtubules (By similarity). Acts as a major instructive molecule at inhibitory synapses, where it also clusters GABA type A receptors (PubMed:25025157, PubMed:26613940)", "gene_name": "GPHN", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NQX3", "name": "GPHN (Gephyrin)", "organism": "Homo sapiens", "uniprot_id": "Q9NQX3" }, { "function": "As a major component of focal adhesion plaques that links integrin to the actin cytoskeleton, may play an important role in cell adhesion. Recruits PIP5K1C to focal adhesion plaques and strongly activates its kinase activity (By similarity)", "gene_name": "TLN2", "glycan_count": 3, "glycosylation_sites": [], "id": "Q9Y4G6", "name": "ARHGEF9 (Collybistin)", "organism": "Homo sapiens", "uniprot_id": "Q9Y4G6" }, { "function": "Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. In the lumen of the endoplasmic reticulum, adds the second glucose residue from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide intermediate Glc(1)Man(9)GlcNAc(2)-PP-Dol to produce Glc(2)Man(9)GlcNAc(2)-PP-Dol. Glc(2)Man(9)GlcNAc(2)-PP-Dol is a substrate for ALG10, the following enzyme in the biosynthetic pathway (PubMed:12480927, PubMed:15235028). Required for PKD1/Polycystin-1 maturation and localization to the plasma membrane of the primary cilia (By similarity)", "gene_name": "ALG8", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9BVK2", "name": "ALG1 (Asparagine-linked glycosylation 1)", "organism": "Homo sapiens", "uniprot_id": "Q9BVK2" }, { "function": "", "gene_name": "DMD", "glycan_count": 0, "glycosylation_sites": [], "id": "P11532-7", "name": "Dystrophin (Dp140)", "organism": "Homo sapiens", "uniprot_id": "P11532-7" }, { "function": "", "gene_name": "DMD", "glycan_count": 0, "glycosylation_sites": [], "id": "P11532-8", "name": "Dystrophin (Dp71)", "organism": "Homo sapiens", "uniprot_id": "P11532-8" }, { "function": "Cell surface protein involved in cell-cell-interactions via its interactions with neurexin family members. Plays a role in synapse function and synaptic signal transmission, and probably mediates its effects by recruiting and clustering other synaptic proteins. May promote the initial formation of synapses, but is not essential for this. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses. Required to maintain wakefulness quality and normal synchrony of cerebral cortex activity during wakefulness and sleep (By similarity). The protein is involved in nervous system development", "gene_name": "NLGN1", "glycan_count": 2, "glycosylation_sites": [ { "position": 109, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 323, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 363, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 567, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 703, "type": "O-linked (GalNAc...) serine" }, { "position": 706, "type": "O-linked (GalNAc...) serine" } ], "id": "Q8N2Q7", "name": "Neuroligin-2 (NLGN2)", "organism": "Homo sapiens", "uniprot_id": "Q8N2Q7" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O43557 (alpha), Q14118 (beta)", "name": "Dystroglycan (alpha/beta)", "organism": "", "uniprot_id": "" }, { "function": "Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Involved in the organization of the laminar architecture of cerebral cortex. It is probably required for the integrity of the basement membrane/glia limitans that serves as an anchor point for the endfeet of radial glial cells and as a physical barrier to migrating neurons. Radial glial cells play a central role in cerebral cortical development, where they act both as the proliferative unit of the cerebral cortex and a scaffold for neurons migrating toward the pial surface", "gene_name": "LAMB1", "glycan_count": 135, "glycosylation_sites": [ { "position": 120, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 356, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 519, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 677, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1041, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1195, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1279, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1336, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1343, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1487, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1542, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P07942", "name": "Laminin-2", "organism": "Homo sapiens", "uniprot_id": "P07942" }, { "function": "This protein is a cell adhesion molecule involved in neuron-neuron adhesion, neurite fasciculation, outgrowth of neurites, etc", "gene_name": "NCAM1", "glycan_count": 26, "glycosylation_sites": [ { "position": 222, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 315, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 347, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 433, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 459, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 488, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P13591", "name": "Neural Cell Adhesion Molecule (NCAM)", "organism": "Homo sapiens", "uniprot_id": "P13591" }, { "function": "Important signaling molecule that activates signaling cascades downstream of NTRK2 (PubMed:11152678). During development, promotes the survival and differentiation of selected neuronal populations of the peripheral and central nervous systems. Participates in axonal growth, pathfinding and in the modulation of dendritic growth and morphology. Major regulator of synaptic transmission and plasticity at adult synapses in many regions of the CNS. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (LTP), long-term depression (LTD), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability", "gene_name": "BDNF", "glycan_count": 1, "glycosylation_sites": [ { "position": 121, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P23560", "name": "Brain-derived neurotrophic factor (BDNF)", "organism": "Homo sapiens", "uniprot_id": "P23560" }, { "function": "Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate (By similarity)", "gene_name": "OXCT2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9BYC2", "name": "CMP-N-acetylneuraminic acid hydroxylase (CMAH)", "organism": "Homo sapiens", "uniprot_id": "Q9BYC2" }, { "function": "May play a role in carrying and orienting carbohydrate, as well as having a more specific role", "gene_name": "CD52", "glycan_count": 0, "glycosylation_sites": [ { "position": 27, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 40, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P31358", "name": "CD52", "organism": "Homo sapiens", "uniprot_id": "P31358" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "various (e.g., LAMA1: Q16363)", "name": "Laminin", "organism": "", "uniprot_id": "" }, { "function": "Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin", "gene_name": "TUBB1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H4B7", "name": "Fukutin", "organism": "Homo sapiens", "uniprot_id": "Q9H4B7" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UKY4/Q9Y2B2", "name": "Protein O-linked mannose N-acetylglucosaminyltransferase 1/2 (POMT1/2)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "CLRN3", "glycan_count": 0, "glycosylation_sites": [ { "position": 83, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8NCR9", "name": "POGLUT1", "organism": "Homo sapiens", "uniprot_id": "Q8NCR9" }, { "function": "Extracellular matrix serine protease secreted by pioneer neurons that plays a role in layering of neurons in the cerebral cortex and cerebellum by coordinating cell positioning during neurodevelopment. Regulates microtubule function in neurons and neuronal migration. Binding to the extracellular domains of lipoprotein receptors VLDLR and LRP8/APOER2 induces tyrosine phosphorylation of DAB1 and modulation of TAU phosphorylation. Affects migration of sympathetic preganglionic neurons in the spinal cord, where it seems to act as a barrier to neuronal migration. Enzymatic activity is important for the modulation of cell adhesion", "gene_name": "RELN", "glycan_count": 21, "glycosylation_sites": [ { "position": 140, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 257, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 289, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 305, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 628, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1266, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1599, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1749, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1920, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2144, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2268, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2316, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2568, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2961, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3015, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3072, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3184, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3411, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3438, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P78509", "name": "Reelin", "organism": "Homo sapiens", "uniprot_id": "P78509" }, { "function": "Cell surface receptor for Reelin (RELN) and apolipoprotein E (apoE)-containing ligands (PubMed:12899622, PubMed:12950167, PubMed:20223215, PubMed:30873003). LRP8 participates in transmitting the extracellular Reelin signal to intracellular signaling processes, by binding to DAB1 on its cytoplasmic tail (By similarity). Reelin acts via both the VLDL receptor (VLDLR) and LRP8 to regulate DAB1 tyrosine phosphorylation and microtubule function in neurons (By similarity). LRP8 has higher affinity for Reelin than VLDLR (By similarity). LRP8 is thus a key component of the Reelin pathway which governs neuronal layering of the forebrain during embryonic brain development (By similarity). Binds the endoplasmic reticulum resident receptor-associated protein (RAP) (By similarity). Binds dimers of beta 2-glycoprotein I and may be involved in the suppression of platelet aggregation in the vasculature (PubMed:12807892). Highly expressed in the initial segment of the epididymis, where it affects the functional expression of clusterin and phospholipid hydroperoxide glutathione peroxidase (PHGPx), two proteins required for sperm maturation (By similarity). May also function as an endocytic receptor (By similarity). Not required for endocytic uptake of SEPP1 in the kidney which is mediated by LRP2 (By similarity). Together with its ligand, apolipoprotein E (apoE), may indirectly play a role in the suppression of the innate immune response by controlling the survival of myeloid-derived suppressor cells (By similarity)", "gene_name": "LRP8", "glycan_count": 7, "glycosylation_sites": [ { "position": 176, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 441, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 518, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 538, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 772, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 807, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q14114", "name": "ApoER2 (LRP8)", "organism": "Homo sapiens", "uniprot_id": "Q14114" }, { "function": "Multifunctional cell surface receptor that binds VLDL and transports it into cells by endocytosis and therefore plays an important role in energy metabolism. Also binds to a wide range of other molecules including Reelin/RELN or apolipoprotein E/APOE-containing ligands as well as clusterin/CLU (PubMed:24381170, PubMed:30873003). In the off-state of the pathway, forms homooligomers or heterooligomers with LRP8 (PubMed:30873003). Upon binding to ligands, homooligomers are rearranged to higher order receptor clusters that transmit the extracellular RELN signal to intracellular signaling processes by binding to DAB1 (PubMed:30873003). This interaction results in phosphorylation of DAB1 leading to the ultimate cell responses required for the correct positioning of newly generated neurons. Later, mediates a stop signal for migrating neurons, preventing them from entering the marginal zone (By similarity)", "gene_name": "VLDLR", "glycan_count": 4, "glycosylation_sites": [ { "position": 151, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 765, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 781, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P98155", "name": "VLDLR", "organism": "Homo sapiens", "uniprot_id": "P98155" }, { "function": "Cell-surface receptor involved in the development of the cardiovascular system, in angiogenesis, in the formation of certain neuronal circuits and in organogenesis outside the nervous system. Mediates the chemorepulsant activity of semaphorins (PubMed:10688880, PubMed:9288753, PubMed:9529250). Recognizes a C-end rule (CendR) motif R/KXXR/K on its ligands which causes cellular internalization and vascular leakage (PubMed:19805273). It binds to semaphorin 3A, the PLGF-2 isoform of PGF, the VEGF165 isoform of VEGFA and VEGFB (PubMed:10688880, PubMed:19805273, PubMed:9288753, PubMed:9529250). Coexpression with KDR results in increased VEGF165 binding to KDR as well as increased chemotaxis. Regulates VEGF-induced angiogenesis. Binding to VEGFA initiates a signaling pathway needed for motor neuron axon guidance and cell body migration, including for the caudal migration of facial motor neurons from rhombomere 4 to rhombomere 6 during embryonic development (By similarity). Regulates mitochondrial iron transport via interaction with ABCB8/MITOSUR (PubMed:30623799)", "gene_name": "NRP1", "glycan_count": 59, "glycosylation_sites": [ { "position": 150, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 261, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 300, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 522, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 612, "type": "O-linked (Xyl...) (chondroitin sulfate) serine; alternate" }, { "position": 612, "type": "O-linked (Xyl...) (heparan sulfate) serine; alternate" }, { "position": 829, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 842, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O14786", "name": "Nrp1", "organism": "Homo sapiens", "uniprot_id": "O14786" }, { "function": "Tegument protein that can bind to various RNA transcripts. Plays a role in the attenuation of selective viral and cellular mRNA degradation by modulating the activity of host shutoff RNase ORF17/VHS. Also plays a role in the primary envelopment of virions in the perinuclear space, probably by interacting with two nuclear egress proteins ORF24 and ORF27", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P09263", "name": "Varicella glycoprotein E", "organism": "Varicella-zoster virus (strain Dumas)", "uniprot_id": "P09263" }, { "function": "Participates in the induction of key genes involved in the response to hypoxia and in the induction of angiogenesis such as HIF1A (PubMed:35455969). Involved in protecting cells from hypoxia-mediated cell death (By similarity)", "gene_name": "VEGFA", "glycan_count": 1, "glycosylation_sites": [ { "position": 281, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P15692", "name": "VEGF (VEGFA)", "organism": "Homo sapiens", "uniprot_id": "P15692" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8NUZ8", "name": "IL-27", "organism": "", "uniprot_id": "Q8NUZ8" }, { "function": "Part of the TCR-CD3 complex present on T-lymphocyte cell surface that plays an essential role in adaptive immune response. When antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transmitted across the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3 chains contain immunoreceptor tyrosine-based activation motifs (ITAMs) in their cytoplasmic domain. Upon TCR engagement, these motifs become phosphorylated by Src family protein tyrosine kinases LCK and FYN, resulting in the activation of downstream signaling pathways (PubMed:2470098). In addition of this role of signal transduction in T-cell activation, CD3D plays an essential role in thymocyte differentiation. Indeed, participates in correct intracellular TCR-CD3 complex assembly and surface expression. In absence of a functional TCR-CD3 complex, thymocytes are unable to differentiate properly. Interacts with CD4 and CD8 and thus serves to establish a functional link between the TCR and coreceptors CD4 and CD8, which is needed for activation and positive selection of CD4 or CD8 T-cells (PubMed:12215456)", "gene_name": "CD3D", "glycan_count": 10, "glycosylation_sites": [ { "position": 38, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 74, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P04234", "name": "CD3", "organism": "Homo sapiens", "uniprot_id": "P04234" }, { "function": "Functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination (PubMed:15350543). Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs (By similarity)", "gene_name": "NOTCH3", "glycan_count": 10, "glycosylation_sites": [ { "position": 1179, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1336, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1438, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UM47", "name": "NOTCH3", "organism": "Homo sapiens", "uniprot_id": "Q9UM47" }, { "function": "Binds low density lipoprotein /LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits. Forms a ternary complex with PGRMC1 and TMEM97 receptors which increases LDLR-mediated LDL internalization (PubMed:30443021)", "gene_name": "LDLR", "glycan_count": 28, "glycosylation_sites": [ { "position": 97, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 156, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 272, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 515, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 657, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01130", "name": "LDLR", "organism": "Homo sapiens", "uniprot_id": "P01130" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P05067 (APP precursor)", "name": "Amyloid-beta (A\u03b2)", "organism": "", "uniprot_id": "" }, { "function": "Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). Requires the other members of the gamma-secretase complex to have a protease activity. May play a role in intracellular signaling and gene expression or in linking chromatin to the nuclear membrane. May function in the cytoplasmic partitioning of proteins. The holoprotein functions as a calcium-leak channel that allows the passive movement of calcium from endoplasmic reticulum to cytosol and is involved in calcium homeostasis (PubMed:16959576). Is a regulator of mitochondrion-endoplasmic reticulum membrane tethering and modulates calcium ions shuttling between ER and mitochondria (PubMed:21285369)", "gene_name": "PSEN2", "glycan_count": 0, "glycosylation_sites": [], "id": "P49810", "name": "Presenilin-2 (PSN-2)", "organism": "Homo sapiens", "uniprot_id": "P49810" }, { "function": "Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells (PubMed:11907044, PubMed:12713657). Required for early embryonic development (By similarity). Involved in cellular lipid homeostasis. Involved in the plasma clearance of chylomicron remnants and activated LRPAP1 (alpha 2-macroglobulin), as well as the local metabolism of complexes between plasminogen activators and their endogenous inhibitors. Acts as an LRPAP1 alpha-2-macroglobulin receptor (PubMed:1702392, PubMed:26142438). Acts as TAU/MAPT receptor and controls the endocytosis of TAU/MAPT as well as its subsequent spread (PubMed:32296178). May modulate cellular events, such as APP metabolism, kinase-dependent intracellular signaling, neuronal calcium signaling as well as neurotransmission (PubMed:12888553). Also acts as a receptor for IGFBP3 to mediate cell growth inhibition (PubMed:9252371)", "gene_name": "LRP1", "glycan_count": 176, "glycosylation_sites": [ { "position": 114, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 136, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 185, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 239, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 274, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 357, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 446, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 729, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 928, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1050, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1154, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1155, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1195, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1218, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1511, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 1558, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1575, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1616, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1645, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1723, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1733, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1763, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1825, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1933, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1995, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2048, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2117, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2127, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2472, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2502, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2521, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2539, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2601, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2620, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2638, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2815, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2905, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3048, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3089, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3264, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3333, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3488, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3662, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3788, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3839, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3953, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4075, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4125, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4179, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4278, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4279, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4364, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q07954", "name": "Low-density lipoprotein receptor-related protein 1 (LPR-1)", "organism": "Homo sapiens", "uniprot_id": "Q07954" }, { "function": "Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids (PubMed:15283675, PubMed:6208535, PubMed:6349683, PubMed:8168535). Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond (PubMed:17101991, PubMed:6349683). Catalyzes cleavage of bradykinin, substance P and neurotensin peptides (PubMed:6208535). Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9 (PubMed:15283675, PubMed:6349683). Involved in the degradation of atrial natriuretic factor (ANF) and brain natriuretic factor (BNP(1-32)) (PubMed:16254193, PubMed:2531377, PubMed:2972276). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers (PubMed:20876573)", "gene_name": "MME", "glycan_count": 93, "glycosylation_sites": [ { "position": 145, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 285, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 325, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 628, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08473", "name": "Neprilysin (NEP)", "organism": "Homo sapiens", "uniprot_id": "P08473" }, { "function": "Plays a role in the cellular breakdown of insulin, APP peptides, IAPP peptides, natriuretic peptides, glucagon, bradykinin, kallidin, and other peptides, and thereby plays a role in intercellular peptide signaling (PubMed:10684867, PubMed:17051221, PubMed:17613531, PubMed:18986166, PubMed:19321446, PubMed:21098034, PubMed:2293021, PubMed:23922390, PubMed:24847884, PubMed:26394692, PubMed:26968463, PubMed:29596046). Substrate binding induces important conformation changes, making it possible to bind and degrade larger substrates, such as insulin (PubMed:23922390, PubMed:26394692, PubMed:29596046). Contributes to the regulation of peptide hormone signaling cascades and regulation of blood glucose homeostasis via its role in the degradation of insulin, glucagon and IAPP (By similarity). Plays a role in the degradation and clearance of APP-derived amyloidogenic peptides that are secreted by neurons and microglia (Probable) (PubMed:26394692, PubMed:9830016). Degrades the natriuretic peptides ANP, BNP and CNP, inactivating their ability to raise intracellular cGMP (PubMed:21098034). Also degrades an aberrant frameshifted 40-residue form of NPPA (fsNPPA) which is associated with familial atrial fibrillation in heterozygous patients (PubMed:21098034). Involved in antigen processing. Produces both the N terminus and the C terminus of MAGEA3-derived antigenic peptide (EVDPIGHLY) that is presented to cytotoxic T lymphocytes by MHC class I", "gene_name": "IDE", "glycan_count": 1, "glycosylation_sites": [], "id": "P14735", "name": "Insulin-degrading enzyme (IDE)", "organism": "Homo sapiens", "uniprot_id": "P14735" }, { "function": "Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain", "gene_name": "TTR", "glycan_count": 0, "glycosylation_sites": [ { "position": 118, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P02766", "name": "Transthyretin (TTR)", "organism": "Homo sapiens", "uniprot_id": "P02766" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P05067 (APP-derived)", "name": "Beta-amyloid (A\u03b2)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01857 (IgG1), P01859 (IgG2), P01860 (IgG3)", "name": "Immunoglobulin G (IgG)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "LRG1", "glycan_count": 92, "glycosylation_sites": [ { "position": 37, "type": "O-linked (GalNAc...) threonine" }, { "position": 79, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 186, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 269, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 325, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P02750", "name": "Leucine-rich alpha-2 glycoprotein", "organism": "Homo sapiens", "uniprot_id": "P02750" }, { "function": "Ligand for multiple Notch receptors and involved in the mediation of Notch signaling (PubMed:18660822, PubMed:20437614). May be involved in cell-fate decisions during hematopoiesis (PubMed:9462510). Seems to be involved in early and late stages of mammalian cardiovascular development. Inhibits myoblast differentiation (By similarity). Enhances fibroblast growth factor-induced angiogenesis (in vitro)", "gene_name": "JAG1", "glycan_count": 5, "glycosylation_sites": [ { "position": 143, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 217, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 382, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 559, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 745, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 960, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 991, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1045, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1064, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P78504", "name": "JAG1", "organism": "Homo sapiens", "uniprot_id": "P78504" }, { "function": "Functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus (PubMed:21378985, PubMed:21378989). Affects the implementation of differentiation, proliferation and apoptotic programs (By similarity). Involved in bone remodeling and homeostasis. In collaboration with RELA/p65 enhances NFATc1 promoter activity and positively regulates RANKL-induced osteoclast differentiation (PubMed:29149593). Positively regulates self-renewal of liver cancer cells (PubMed:25985737)", "gene_name": "NOTCH2", "glycan_count": 9, "glycosylation_sites": [ { "position": 46, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 155, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 613, "type": "O-linked (Glc...) serine; alternate" }, { "position": 613, "type": "O-linked (Xyl...) serine; alternate" }, { "position": 733, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1102, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1465, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q04721", "name": "NOTCH2", "organism": "Homo sapiens", "uniprot_id": "Q04721" }, { "function": "Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates (such as maresin conjugate (13R)-S-glutathionyl-(14S)-hydroxy-(4Z,7Z,9E,11E,16Z,19Z)-docosahexaenoate, MCTR1) and other gamma-glutamyl compounds (such as leukotriene C4, LTC4) (PubMed:17924658, PubMed:21447318, PubMed:27791009). The metabolism of glutathione by GGT1 releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases (PubMed:27791009). In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound (PubMed:17924658, PubMed:21447318, PubMed:7673200, PubMed:7759490, PubMed:8095045, PubMed:8827453). Contributes to cysteine homeostasis, glutathione homeostasis and in the conversion of the leukotriene LTC4 to LTD4", "gene_name": "GGT1", "glycan_count": 134, "glycosylation_sites": [ { "position": 95, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 120, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 230, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 266, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 297, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 344, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 511, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P19440", "name": "Gamma-glutamyl transferase (GGT)", "organism": "Homo sapiens", "uniprot_id": "P19440" }, { "function": "May form part of a complex of membrane proteins attached to acetylcholinesterase (AChE)", "gene_name": "CUTA", "glycan_count": 3, "glycosylation_sites": [], "id": "O60888", "name": "Stanniocalcin-1 (STC-1)", "organism": "Homo sapiens", "uniprot_id": "O60888" }, { "function": "Mitochondrial iron transporter that specifically mediates iron uptake in developing erythroid cells, thereby playing an essential role in heme biosynthesis", "gene_name": "SLC25A37", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NYZ2", "name": "Stanniocalcin-2 (STC-2)", "organism": "Homo sapiens", "uniprot_id": "Q9NYZ2" }, { "function": "Metalloproteinase which specifically cleaves IGFBP-4 and IGFBP-5, resulting in release of bound IGF. Cleavage of IGFBP-4 is dramatically enhanced by the presence of IGF, whereas cleavage of IGFBP-5 is slightly inhibited by the presence of IGF", "gene_name": "PAPPA", "glycan_count": 11, "glycosylation_sites": [ { "position": 390, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 402, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 429, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 480, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 601, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 619, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 725, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 825, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1026, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1222, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1226, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1323, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1465, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1519, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13219", "name": "Pregnancy-associated plasma protein-A (PAPP-A)", "organism": "Homo sapiens", "uniprot_id": "Q13219" }, { "function": "Important in the maintenance of hemostasis, it promotes adhesion of platelets to the sites of vascular injury by forming a molecular bridge between sub-endothelial collagen matrix and platelet-surface receptor complex GPIb-IX-V. Also acts as a chaperone for coagulation factor VIII, delivering it to the site of injury, stabilizing its heterodimeric structure and protecting it from premature clearance from plasma", "gene_name": "VWF", "glycan_count": 203, "glycosylation_sites": [ { "position": 99, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 156, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 211, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 666, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 857, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1147, "type": "N-linked (GlcNAc...) asparagine; atypical" }, { "position": 1231, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1248, "type": "O-linked (GalNAc...) threonine" }, { "position": 1255, "type": "O-linked (GalNAc...) threonine" }, { "position": 1256, "type": "O-linked (GalNAc...) threonine" }, { "position": 1263, "type": "O-linked (GalNAc...) serine" }, { "position": 1468, "type": "O-linked (GalNAc...) threonine" }, { "position": 1477, "type": "O-linked (GalNAc...) threonine" }, { "position": 1486, "type": "O-linked (GalNAc...) serine" }, { "position": 1487, "type": "O-linked (GalNAc...) threonine" }, { "position": 1515, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 1574, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1679, "type": "O-linked (GalNAc...) threonine" }, { "position": 2223, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2290, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2298, "type": "O-linked (GalNAc...) threonine" }, { "position": 2357, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2400, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2546, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2585, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2790, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P04275", "name": "von Willebrand factor (VWF)", "organism": "Homo sapiens", "uniprot_id": "P04275" }, { "function": "Factor VIII, along with calcium and phospholipid, acts as a cofactor for F9/factor IXa when it converts F10/factor X to the activated form, factor Xa", "gene_name": "F8", "glycan_count": 63, "glycosylation_sites": [ { "position": 60, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 258, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 601, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 776, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 803, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 847, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 919, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 962, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 982, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1020, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1024, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1074, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1085, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1204, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1274, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1278, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1301, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1319, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1431, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1461, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1829, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2137, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P00451", "name": "Factor VIII (FVIII)", "organism": "Homo sapiens", "uniprot_id": "P00451" }, { "function": "Mannosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. In the lumen of the endoplasmic reticulum, adds the eighth mannose residue in an alpha-1,6 linkage onto Man(7)GlcNAc(2)-PP-dolichol to produce Man(8)GlcNAc(2)-PP-dolichol", "gene_name": "ALG12", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9BV10", "name": "ALG12", "organism": "Homo sapiens", "uniprot_id": "Q9BV10" }, { "function": "Intramembrane glycolipid transporter that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. RFT1 could mediate the translocation of the cytosolically oriented intermediate DolPP-GlcNAc2Man5, produced by ALG11, into the ER lumen where dolichol-linked oligosaccharides assembly continues (PubMed:18313027, PubMed:19701946). However, the intramembrane lipid transporter activity could not be confirmed in vitro (By similarity)", "gene_name": "RFT1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q96AA3", "name": "RFT1", "organism": "Homo sapiens", "uniprot_id": "Q96AA3" }, { "function": "Glycoprotein that probably modulates membrane fusion events during secondary envelopment of cytoplasmic capsids that bud into specific trans-Golgi network (TGN)-derived membranes. Also plays a role, together with gB, in virus-induced cell-to-cell fusion (syncytia formation), which is extensive during VZV infection in cultured cells (By similarity)", "gene_name": "gK", "glycan_count": 0, "glycosylation_sites": [ { "position": 65, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P09261", "name": "Varicella Zoster Virus glycoprotein E (gE)", "organism": "Varicella-zoster virus (strain Dumas)", "uniprot_id": "P09261" }, { "function": "", "gene_name": "UL8", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6SWC2", "name": "UL148", "organism": "Human cytomegalovirus", "uniprot_id": "F5H984" }, { "function": "Blocks interferon-dependent interphase and stimulates DNA synthesis in cells. Involved in the translational regulation of the human papillomavirus type 16 E7 mRNA (HPV16 E7)", "gene_name": "KRT7", "glycan_count": 2, "glycosylation_sites": [ { "position": 12, "type": "O-linked (GlcNAc) serine" } ], "id": "P08729", "name": "Cytokeratin 7 (CK7)", "organism": "Homo sapiens", "uniprot_id": "P08729" }, { "function": "Plays a significant role in maintaining keratin filament organization in intestinal epithelia. When phosphorylated, plays a role in the secretion of mucin in the small intestine (By similarity)", "gene_name": "KRT20", "glycan_count": 0, "glycosylation_sites": [], "id": "P35900", "name": "CK20", "organism": "Homo sapiens", "uniprot_id": "P35900" }, { "function": "Transcription factor for the thyroid-specific expression of the genes exclusively expressed in the thyroid cell type, maintaining the functional differentiation of such cells", "gene_name": "PAX8", "glycan_count": 1, "glycosylation_sites": [], "id": "Q06710", "name": "PAX-8", "organism": "Homo sapiens", "uniprot_id": "Q06710" }, { "function": "Acts as a sequence specific DNA binding transcriptional activator or repressor. The isoforms contain a varying set of transactivation and auto-regulating transactivation inhibiting domains thus showing an isoform specific activity. Isoform 2 activates RIPK4 transcription. May be required in conjunction with TP73/p73 for initiation of p53/TP53 dependent apoptosis in response to genotoxic insults and the presence of activated oncogenes. Involved in Notch signaling by probably inducing JAG1 and JAG2. Plays a role in the regulation of epithelial morphogenesis. The ratio of DeltaN-type and TA*-type isoforms may govern the maintenance of epithelial stem cell compartments and regulate the initiation of epithelial stratification from the undifferentiated embryonal ectoderm. Required for limb formation from the apical ectodermal ridge. Activates transcription of the p21 promoter", "gene_name": "TP63", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H3D4", "name": "P40", "organism": "Homo sapiens", "uniprot_id": "Q9H3D4" }, { "function": "With NUS1, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery (PubMed:25066056, PubMed:28842490, PubMed:32817466, PubMed:33077723). Both subunits contribute to enzymatic activity, i.e. condensation of multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol phosphate which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER) (PubMed:25066056, PubMed:28842490, PubMed:32817466, PubMed:33077723). Synthesizes long-chain polyprenols, mostly of C95 and C100 chain length (PubMed:32817466). Regulates the glycosylation and stability of nascent NPC2, thereby promoting trafficking of LDL-derived cholesterol (PubMed:21572394)", "gene_name": "DHDDS", "glycan_count": 0, "glycosylation_sites": [], "id": "Q86SQ9", "name": "DHDDS", "organism": "Homo sapiens", "uniprot_id": "Q86SQ9" }, { "function": "Protein tyrosine-protein phosphatase required for T-cell activation through the antigen receptor (PubMed:35767951). Acts as a positive regulator of T-cell coactivation upon binding to DPP4. The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Upon T-cell activation, recruits and dephosphorylates SKAP1 and FYN. Dephosphorylates LYN, and thereby modulates LYN activity (By similarity). Interacts with CLEC10A at antigen presenting cell-T cell contact; CLEC10A on immature dendritic cells recognizes Tn antigen-carrying PTPRC/CD45 receptor on effector T cells and modulates T cell activation threshold to limit autoreactivity", "gene_name": "PTPRC", "glycan_count": 126, "glycosylation_sites": [ { "position": 80, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 92, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 97, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 186, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 192, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 199, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 234, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 262, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 272, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 278, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 286, "type": "N-linked (GlcNAc...) asparagine; atypical" }, { "position": 337, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 380, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 421, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 470, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 490, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 531, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08575", "name": "CD45", "organism": "Homo sapiens", "uniprot_id": "P08575" }, { "function": "Low-affinity receptor for immunoglobulin E (IgE) and CR2/CD21. Has essential roles in the regulation of IgE production and in the differentiation of B cells. On B cells, initiates IgE-dependent antigen uptake and presentation to T cells (PubMed:2167225). On macrophages, upon IgE binding and antigen cross-linking induces intracellular killing of parasites through activation of L-Arginine-nitric oxide pathway (PubMed:7544003)", "gene_name": "FCER2", "glycan_count": 1, "glycosylation_sites": [ { "position": 63, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 296, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" } ], "id": "P06734", "name": "CD11c", "organism": "Homo sapiens", "uniprot_id": "P06734" }, { "function": "Lectin that binds beta-galactoside and a wide array of complex carbohydrates. Plays a role in regulating apoptosis, cell proliferation and cell differentiation. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase. Strong inducer of T-cell apoptosis. Plays a negative role in Th17 cell differentiation via activation of the receptor CD69 (PubMed:24752896)", "gene_name": "LGALS1", "glycan_count": 2, "glycosylation_sites": [], "id": "P09382", "name": "Galectin 1", "organism": "Homo sapiens", "uniprot_id": "P09382" }, { "function": "Lineage-defining transcription factor which initiates Th1 lineage development from naive Th precursor cells both by activating Th1 genetic programs and by repressing the opposing Th2 and Th17 genetic programs (PubMed:10761931). Activates transcription of a set of genes important for Th1 cell function, including those encoding IFN-gamma and the chemokine receptor CXCR3. Induces permissive chromatin accessibilty and CpG methylation in IFNG (PubMed:33296702). Activates IFNG and CXCR3 genes in part by recruiting chromatin remodeling complexes including KDM6B, a SMARCA4-containing SWI/SNF-complex, and an H3K4me2-methyltransferase complex to their promoters and all of these complexes serve to establish a more permissive chromatin state conducive with transcriptional activation (By similarity). Can activate Th1 genes also via recruitment of Mediator complex and P-TEFb (composed of CDK9 and CCNT1/cyclin-T1) in the form of the super elongation complex (SEC) to super-enhancers and associated genes in activated Th1 cells (PubMed:27292648). Inhibits the Th17 cell lineage commitment by blocking RUNX1-mediated transactivation of Th17 cell-specific transcriptinal regulator RORC. Inhibits the Th2 cell lineage commitment by suppressing the production of Th2 cytokines, such as IL-4, IL-5, and IL- 13, via repression of transcriptional regulators GATA3 and NFATC2. Protects Th1 cells from amplifying aberrant type-I IFN response in an IFN-gamma abundant microenvironment by acting as a repressor of type-I IFN transcription factors and type-I IFN-stimulated genes. Acts as a regulator of antiviral B-cell responses; controls chronic viral infection by promoting the antiviral antibody IgG2a isotype switching and via regulation of a broad antiviral gene expression program (By similarity). Required for the correct development of natural killer (NK) and mucosal-associated invariant T (MAIT) cells (PubMed:33296702)", "gene_name": "TBX21", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UL17", "name": "T-bet", "organism": "Homo sapiens", "uniprot_id": "Q9UL17" }, { "function": "May function in a protective capacity by promoting the clearance of bacteria in the oral cavity and aiding in mastication, speech, and swallowing. Binds P.aeruginosa pili", "gene_name": "MUC7", "glycan_count": 22, "glycosylation_sites": [ { "position": 97, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 128, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 135, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 146, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 176, "type": "O-linked (GalNAc) threonine; by GALNT13" }, { "position": 182, "type": "O-linked (GalNAc) serine; by GALNT13" }, { "position": 183, "type": "O-linked (GalNAc) serine; by GALNT13" }, { "position": 188, "type": "O-linked (GalNAc) threonine; by GALNT13" }, { "position": 189, "type": "O-linked (GalNAc) threonine; by GALNT13" } ], "id": "Q8TAX7", "name": "MUC5AC", "organism": "Homo sapiens", "uniprot_id": "Q8TAX7" }, { "function": "May have a pivotal role in cell differentiation of different cell types. Signaling could be triggered by the binding of a lectin-like ligand to the CD24 carbohydrates, and transduced by the release of second messengers derived from the GPI-anchor. Modulates B-cell activation responses. Promotes AG-dependent proliferation of B-cells, and prevents their terminal differentiation into antibody-forming cells (PubMed:11313396). In association with SIGLEC10 may be involved in the selective suppression of the immune response to danger-associated molecular patterns (DAMPs) such as HMGB1, HSP70 and HSP90. Plays a role in the control of autoimmunity (By similarity)", "gene_name": "CD24", "glycan_count": 14, "glycosylation_sites": [ { "position": 36, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 52, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P25063", "name": "CD24", "organism": "Homo sapiens", "uniprot_id": "P25063" }, { "function": "Promotes endocytosis, possesses opsonic properties and influences the mineral phase of bone. Shows affinity for calcium and barium ions", "gene_name": "AHSG", "glycan_count": 182, "glycosylation_sites": [ { "position": 156, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 176, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 270, "type": "O-linked (GalNAc...) threonine" }, { "position": 280, "type": "O-linked (GalNAc...) serine" }, { "position": 293, "type": "O-linked (GalNAc...) serine" }, { "position": 339, "type": "O-linked (GalNAc...) threonine" }, { "position": 341, "type": "O-linked (GalNAc...) threonine" }, { "position": 346, "type": "O-linked (GalNAc...) serine" } ], "id": "P02765", "name": "Fetuin (Alpha-2-HS-glycoprotein)", "organism": "Homo sapiens", "uniprot_id": "P02765" }, { "function": "Incorporated into fibronectin-containing matrix fibers. May play a role in cell adhesion and migration along protein fibers within the extracellular matrix (ECM). Could be important for certain developmental processes and contribute to the supramolecular organization of ECM architecture, in particular to those of basement membranes. Has been implicated in a role in cellular transformation and tumor invasion, it appears to be a tumor suppressor. May play a role in haemostasis and thrombosis owing to its ability to bind fibrinogen and incorporate into clots. Could play a significant role in modulating the neurotrophic activities of APP, particularly soluble APP", "gene_name": "FBLN1", "glycan_count": 55, "glycosylation_sites": [ { "position": 98, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 535, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 539, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P23142", "name": "Fibulin 1", "organism": "Homo sapiens", "uniprot_id": "P23142" }, { "function": "Its binding to fibronectin and some other ligands is calcium dependent. May act as an adapter that mediates the interaction between FBN1 and ELN (PubMed:17255108)", "gene_name": "FBLN2", "glycan_count": 39, "glycosylation_sites": [ { "position": 180, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 507, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1035, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P98095", "name": "Fibulin 2", "organism": "Homo sapiens", "uniprot_id": "P98095" }, { "function": "Cardiac hormone that plays a key role in mediating cardio-renal homeostasis (PubMed:1672777, PubMed:17372040, PubMed:1914098, PubMed:9458824). May also function as a paracrine antifibrotic factor in the heart (By similarity). Acts by specifically binding and stimulating NPR1 to produce cGMP, which in turn activates effector proteins that drive various biological responses (PubMed:1672777, PubMed:17349887, PubMed:17372040, PubMed:21098034, PubMed:25339504, PubMed:9458824). Involved in regulating the extracellular fluid volume and maintaining the fluid-electrolyte balance through natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion (PubMed:1914098, PubMed:9458824). Binds the clearance receptor NPR3 (PubMed:16870210)", "gene_name": "NPPB", "glycan_count": 1, "glycosylation_sites": [ { "position": 41, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 62, "type": "O-linked (HexNAc...) threonine; Partial" }, { "position": 63, "type": "O-linked (HexNAc...) serine" }, { "position": 70, "type": "O-linked (HexNAc...) serine" }, { "position": 74, "type": "O-linked (HexNAc...) threonine" }, { "position": 79, "type": "O-linked (HexNAc...) serine" }, { "position": 84, "type": "O-linked (HexNAc...) threonine; Partial" }, { "position": 97, "type": "O-linked (HexNAc...) threonine" } ], "id": "P16860", "name": "NT-proBNP", "organism": "Homo sapiens", "uniprot_id": "P16860" }, { "function": "Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates nuclear import of STAT1 homodimers and STAT1/STAT2 heterodimers by recognizing non-classical NLSs of STAT1 and STAT2 through ARM repeats 8-9. Recognizes influenza A virus nucleoprotein through ARM repeat 7-9 In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS", "gene_name": "KPNA5", "glycan_count": 0, "glycosylation_sites": [], "id": "O15131", "name": "Sarcoglycan delta (SGCD)", "organism": "Homo sapiens", "uniprot_id": "O15131" }, { "function": "E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage (PubMed:10500182, PubMed:12887909, PubMed:12890688, PubMed:14976165, PubMed:16818604, PubMed:17525340, PubMed:19261748). It is unclear whether it also mediates the formation of other types of polyubiquitin chains (PubMed:12890688). The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability (PubMed:12890688, PubMed:14976165, PubMed:20351172). Regulates centrosomal microtubule nucleation (PubMed:18056443). Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle (PubMed:10724175, PubMed:11836499, PubMed:12183412, PubMed:19261748). Required for FANCD2 targeting to sites of DNA damage (PubMed:12887909). Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation (PubMed:16326698). Contributes to homologous recombination repair (HRR) via its direct interaction with PALB2, fine-tunes recombinational repair partly through its modulatory role in the PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks (PubMed:19369211). Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage via BRCA1-mediated ubiquitination of RBBP8 (PubMed:16818604). Acts as a transcriptional activator (PubMed:20160719)", "gene_name": "BRCA1", "glycan_count": 0, "glycosylation_sites": [], "id": "O15129", "name": "Sarcoglycan epsilon (SGCE)", "organism": "Homo sapiens", "uniprot_id": "P38398" }, { "function": "Functions in post-Golgi recycling pathways. Acts as a recycling carrier to the cell surface", "gene_name": "SCAMP2", "glycan_count": 1, "glycosylation_sites": [], "id": "O15127", "name": "Sarcospan (SSPN)", "organism": "Homo sapiens", "uniprot_id": "O15127" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "part of DAG1", "name": "Alpha-dystroglycan", "organism": "", "uniprot_id": "" }, { "function": "Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. May play a role in the repair of noise-induced stereocilia gaps thereby maintains hearing sensitivity following loud noise damage (By similarity)", "gene_name": "ACTG1", "glycan_count": 2, "glycosylation_sites": [], "id": "P63261", "name": "Actin gamma 1 (ACTG1)", "organism": "Homo sapiens", "uniprot_id": "P63261" }, { "function": "May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. May also regulate voltage-gated potassium channels. Plays a role in the sarcolemma repair mechanism of both skeletal muscle and cardiomyocytes that permits rapid resealing of membranes disrupted by mechanical stress (By similarity). Mediates the recruitment of CAVIN2 and CAVIN3 proteins to the caveolae (PubMed:19262564)", "gene_name": "CAV3", "glycan_count": 0, "glycosylation_sites": [], "id": "P56539", "name": "Caveolin-3", "organism": "Homo sapiens", "uniprot_id": "P56539" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q99NH8 (mouse), Q9NZC2 (human)", "name": "Trem2 (Triggering receptor expressed on myeloid cells 2)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Z1E5 (mouse), Q99519 (human)", "name": "NEU1 (Neuraminidase 1)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P12023 (mouse), P05067 (human)", "name": "APP (Amyloid precursor protein)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P11438 (mouse), P11279 (human)", "name": "LAMP1 (Lysosome-associated membrane glycoprotein 1)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q63994 (mouse), P20138 (human)", "name": "CD33", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O88500 (mouse), O43914 (human)", "name": "DAP12 (TYROBP)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "fragment of Trem2", "name": "sTrem2 (soluble Trem2)", "organism": "", "uniprot_id": "" }, { "function": "Effector cytokine of innate and adaptive immune system involved in antimicrobial host defense and maintenance of tissue integrity (PubMed:24120361). Signals via IL17RA-IL17RC heterodimeric receptor complex, triggering homotypic interaction of IL17RA and IL17RC chains with TRAF3IP2 adapter. This leads to downstream TRAF6-mediated activation of NF-kappa-B and MAPkinase pathways ultimately resulting in transcriptional activation of cytokines, chemokines, antimicrobial peptides and matrix metalloproteinases, with potential strong immune inflammation (PubMed:17911633, PubMed:18684971, PubMed:19825828, PubMed:21350122, PubMed:24120361, PubMed:8676080). Plays an important role in connecting T cell-mediated adaptive immunity and acute inflammatory response to destroy extracellular bacteria and fungi. As a signature effector cytokine of T-helper 17 cells (Th17), primarily induces neutrophil activation and recruitment at infection and inflammatory sites (By similarity). In airway epithelium, mediates neutrophil chemotaxis via induction of CXCL1 and CXCL5 chemokines (By similarity). In secondary lymphoid organs, contributes to germinal center formation by regulating the chemotactic response of B cells to CXCL12 and CXCL13, enhancing retention of B cells within the germinal centers, B cell somatic hypermutation rate and selection toward plasma cells (By similarity). Effector cytokine of a subset of gamma-delta T cells that functions as part of an inflammatory circuit downstream IL1B, TLR2 and IL23A-IL12B to promote neutrophil recruitment for efficient bacterial clearance (By similarity). Effector cytokine of innate immune cells including invariant natural killer cell (iNKT) and group 3 innate lymphoid cells that mediate initial neutrophilic inflammation (By similarity). Involved in the maintenance of the integrity of epithelial barriers during homeostasis and pathogen infection (PubMed:21350122). Upon acute injury, has a direct role in epithelial barrier formation by regulating OCLN localization and tight junction biogenesis (By similarity). As part of the mucosal immune response induced by commensal bacteria, enhances host's ability to resist pathogenic bacterial and fungal infections by promoting neutrophil recruitment and antimicrobial peptides release (By similarity). In synergy with IL17F, mediates the production of antimicrobial beta-defensins DEFB1, DEFB103A, and DEFB104A by mucosal epithelial cells, limiting the entry of microbes through the epithelial barriers (By similarity). Involved in antiviral host defense through various mechanisms (By similarity). Enhances immunity against West Nile virus by promoting T cell cytotoxicity (By similarity). May play a beneficial role in influenza A virus (H5N1) infection by enhancing B cell recruitment and immune response in the lung (By similarity). Contributes to influenza A virus (H1N1) clearance by driving the differentiation of B-1a B cells, providing for production of virus-specific IgM antibodies at first line of host defense (By similarity)", "gene_name": "IL17A", "glycan_count": 1, "glycosylation_sites": [ { "position": 68, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q16552", "name": "IL-17A", "organism": "Homo sapiens", "uniprot_id": "Q16552" }, { "function": "May play a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier. It is able to induce adhesion when expressed in cells lacking tight junctions", "gene_name": "OCLN", "glycan_count": 1, "glycosylation_sites": [], "id": "Q16625", "name": "Occludin", "organism": "Homo sapiens", "uniprot_id": "Q16625" }, { "function": "Claudins function as major constituents of the tight junction complexes that regulate the permeability of epithelia. While some claudin family members play essential roles in the formation of impermeable barriers, others mediate the permeability to ions and small molecules. Often, several claudin family members are coexpressed and interact with each other, and this determines the overall permeability. CLDN1 is required to prevent the paracellular diffusion of small molecules through tight junctions in the epidermis and is required for the normal barrier function of the skin. Required for normal water homeostasis and to prevent excessive water loss through the skin, probably via an indirect effect on the expression levels of other proteins, since CLDN1 itself seems to be dispensable for water barrier formation in keratinocyte tight junctions (PubMed:23407391)", "gene_name": "CLDN1", "glycan_count": 0, "glycosylation_sites": [], "id": "O95832", "name": "Claudin-1", "organism": "Homo sapiens", "uniprot_id": "O95832" }, { "function": "Potent mitogen for mature parenchymal hepatocyte cells, seems to be a hepatotrophic factor, and acts as a growth factor for a broad spectrum of tissues and cell types (PubMed:20624990). Activating ligand for the receptor tyrosine kinase MET by binding to it and promoting its dimerization (PubMed:15167892, PubMed:20977675). Activates MAPK signaling following TMPRSS13 cleavage and activation (PubMed:20977675)", "gene_name": "HGF", "glycan_count": 0, "glycosylation_sites": [ { "position": 294, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 402, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 476, "type": "O-linked (GalNAc...) threonine" }, { "position": 566, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 653, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "Q9BYL9", "name": "IFITM3", "organism": "Homo sapiens", "uniprot_id": "P14210" }, { "function": "Catalyzes both the synthesis of cyclic ADP-beta-D-ribose (cADPR) from NAD(+), and its hydrolysis to ADP-D-ribose (ADPR) (PubMed:7805847). Cyclic ADPR is known to serve as an endogenous second messenger that elicits calcium release from intracellular stores, and thus regulates the mobilization of intracellular calcium (Probable). May be involved in pre-B-cell growth (Probable)", "gene_name": "BST1", "glycan_count": 25, "glycosylation_sites": [ { "position": 66, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 95, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 148, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 192, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q10588", "name": "BST2 (Tetherin)", "organism": "Homo sapiens", "uniprot_id": "Q10588" }, { "function": "Interferon-induced dynamin-like GTPase with antiviral activity against a wide range of RNA viruses and some DNA viruses. Its target viruses include negative-stranded RNA viruses and HBV through binding and inactivation of their ribonucleocapsid. May also antagonize reoviridae and asfarviridae replication. Inhibits thogoto virus (THOV) replication by preventing the nuclear import of viral nucleocapsids. Inhibits La Crosse virus (LACV) replication by sequestering viral nucleoprotein in perinuclear complexes, preventing genome amplification, budding, and egress. Inhibits influenza A virus (IAV) replication by decreasing or delaying NP synthesis and by blocking endocytic traffic of incoming virus particles. Enhances ER stress-mediated cell death after influenza virus infection. May regulate the calcium channel activity of TRPCs", "gene_name": "MX1", "glycan_count": 0, "glycosylation_sites": [], "id": "P20591", "name": "MX1", "organism": "Homo sapiens", "uniprot_id": "P20591" }, { "function": "Together with IFNAR2, forms the heterodimeric receptor for type I interferons (including interferons alpha, beta, epsilon, omega and kappa) (PubMed:10049744, PubMed:14532120, PubMed:15337770, PubMed:2153461, PubMed:21854986, PubMed:24075985, PubMed:31270247, PubMed:33252644, PubMed:35442418, PubMed:7813427). Type I interferon binding activates the JAK-STAT signaling cascade, resulting in transcriptional activation or repression of interferon-regulated genes that encode the effectors of the interferon response (PubMed:10049744, PubMed:21854986, PubMed:7665574). Mechanistically, type I interferon-binding brings the IFNAR1 and IFNAR2 subunits into close proximity with one another, driving their associated Janus kinases (JAKs) (TYK2 bound to IFNAR1 and JAK1 bound to IFNAR2) to cross-phosphorylate one another (PubMed:21854986, PubMed:32972995, PubMed:7665574, PubMed:7813427). The activated kinases phosphorylate specific tyrosine residues on the intracellular domains of IFNAR1 and IFNAR2, forming docking sites for the STAT transcription factors (PubMed:21854986, PubMed:32972995, PubMed:7526154, PubMed:7665574, PubMed:7813427). STAT proteins are then phosphorylated by the JAKs, promoting their translocation into the nucleus to regulate expression of interferon-regulated genes (PubMed:19561067, PubMed:21854986, PubMed:32972995, PubMed:7665574, PubMed:7813427, PubMed:9121453). Can also act independently of IFNAR2: form an active IFNB1 receptor by itself and activate a signaling cascade that does not involve activation of the JAK-STAT pathway (By similarity)", "gene_name": "IFNAR1", "glycan_count": 13, "glycosylation_sites": [ { "position": 50, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 58, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 81, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 88, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 110, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 172, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 254, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 313, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 314, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 376, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 416, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 433, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P17181", "name": "IFNAR1", "organism": "Homo sapiens", "uniprot_id": "P17181" }, { "function": "Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response (PubMed:34581622). In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication (PubMed:34145065, PubMed:34581622). Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L. The secreted form displays antiviral effect against vesicular stomatitis virus (VSV), herpes simplex virus type 2 (HSV-2), and encephalomyocarditis virus (EMCV) and stimulates the alternative antiviral pathway independent of RNase L", "gene_name": "OAS1", "glycan_count": 0, "glycosylation_sites": [], "id": "P00973", "name": "OAS1", "organism": "Homo sapiens", "uniprot_id": "P00973" }, { "function": "Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response (PubMed:10464285, PubMed:9880569). Activated by detection of double stranded RNA (dsRNA): polymerizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNASEL) leading to its dimerization and subsequent activation (PubMed:10464285, PubMed:11682059, PubMed:9880569). Activation of RNASEL leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication (PubMed:10464285, PubMed:9880569). Can mediate the antiviral effect via the classical RNASEL-dependent pathway or an alternative antiviral pathway independent of RNASEL (PubMed:21142819). In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation (PubMed:21142819). May act as a negative regulator of lactation, stopping lactation in virally infected mammary gland lobules, thereby preventing transmission of viruses to neonates (By similarity). Non-infected lobules would not be affected, allowing efficient pup feeding during infection (By similarity)", "gene_name": "OAS2", "glycan_count": 0, "glycosylation_sites": [], "id": "P29728", "name": "OAS2", "organism": "Homo sapiens", "uniprot_id": "P29728" }, { "function": "Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes preferentially dimers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L. Displays antiviral activity against Chikungunya virus (CHIKV), Dengue virus, Sindbis virus (SINV) and Semliki forest virus (SFV)", "gene_name": "OAS3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y6K5", "name": "OAS3", "organism": "Homo sapiens", "uniprot_id": "Q9Y6K5" }, { "function": "Plays a key role in the innate immune response as part of an interferon-dependent multiprotein complex, recognizing and sequestering viral RNAs that lack host-specific 2'-O-methylation at their 5' cap. By distinguishing these RNAs from host mRNAs, inhibits their translation by competing with the translation initiation factor eIF4E (PubMed:21642987, PubMed:27240734, PubMed:39009378, PubMed:23334420, PubMed:28251928, PubMed:36285486). Could also prevent viral replication through its interaction with DNA replication origin-binding protein E1 of several viruses. Causes the translocation of E1 from the nucleus to the cytoplasm and can also inhibit its helicase activity in vitro (PubMed:19008854, PubMed:21976647). Exhibits antiviral activity against many viruses from the Flaviviridae (West Nile virus, Dengue virus, hepatitis C virus), Coronaviridae (human 229E coronavirus, SARS-CoV-2 and SARS-CoV), Poxviridae (vaccinia virus) and Togaviridae (Sindbis virus) families (PubMed:19008854, PubMed:21976647, PubMed:28251928, PubMed:36285486)", "gene_name": "IFIT1", "glycan_count": 0, "glycosylation_sites": [], "id": "P09914", "name": "IFIT1", "organism": "Homo sapiens", "uniprot_id": "P09914" }, { "function": "Receptor for angiotensin II, a vasoconstricting peptide, which acts as a key regulator of blood pressure and sodium retention by the kidney (PubMed:15611106, PubMed:1567413, PubMed:25913193, PubMed:26420482, PubMed:30639100, PubMed:32079768, PubMed:8987975). The activated receptor in turn couples to G-alpha proteins G(q) (GNAQ, GNA11, GNA14 or GNA15) and thus activates phospholipase C and increases the cytosolic Ca(2+) concentrations, which in turn triggers cellular responses such as stimulation of protein kinase C (PubMed:15611106)", "gene_name": "AGTR1", "glycan_count": 3, "glycosylation_sites": [ { "position": 4, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 176, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 188, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P30556", "name": "Angiotensin II receptor type 1 (AGTR1)", "organism": "Homo sapiens", "uniprot_id": "P30556" }, { "function": "Receptor for both mineralocorticoids (MC) such as aldosterone and glucocorticoids (GC) such as corticosterone or cortisol. Binds to mineralocorticoid response elements (MRE) and transactivates target genes. The effect of MC is to increase ion and water transport and thus raise extracellular fluid volume and blood pressure and lower potassium levels", "gene_name": "NR3C2", "glycan_count": 1, "glycosylation_sites": [], "id": "P08235", "name": "Mineralocorticoid receptor", "organism": "Homo sapiens", "uniprot_id": "P08235" }, { "function": "Electrogenic Na(+)-coupled sugar symporter that actively transports D-glucose at the plasma membrane, with a Na(+) to sugar coupling ratio of 1:1 (PubMed:20980548, PubMed:28592437, PubMed:34880493, PubMed:37217492, PubMed:38057552). Transporter activity is driven by a transmembrane Na(+) electrochemical gradient set by the Na(+)/K(+) pump (PubMed:20980548, PubMed:28592437, PubMed:34880493). Unlike SLC5A1/SGLT1, requires the auxiliary protein PDZK1IP1/MAP17 for full transporter activity (PubMed:37217492). Has a primary role in D-glucose reabsorption from glomerular filtrate across the brush border of the early proximal tubules of the kidney (By similarity)", "gene_name": "SLC5A2", "glycan_count": 1, "glycosylation_sites": [ { "position": 250, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P31639", "name": "Sodium-glucose cotransporter 2 (SGLT2)", "organism": "Homo sapiens", "uniprot_id": "P31639" }, { "function": "Required for normal male fertility via maintenance of epithelial cell morphology in the caput epididymis and subsequently correct epididymis lumen structure required for sperm development (By similarity). Plays a role in sperm motility, flagella morphology and tyrosine phosphorylation during sperm capacitance (By similarity). Plays a role in normal expression levels of HSPA5, ITM2B and ADAM2 in sperm both prior to and post-capacitation (By similarity). This is a non catalytic metalloprotease-like protein (By similarity)", "gene_name": "ADAM7", "glycan_count": 0, "glycosylation_sites": [ { "position": 84, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 167, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 174, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 184, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 584, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 668, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9H2U9", "name": "KCC2 (SLC12A5)", "organism": "Homo sapiens", "uniprot_id": "Q9H2U9" }, { "function": "Transcriptional coactivator which acts as a downstream regulatory target in the Hippo signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis (PubMed:11118213, PubMed:18227151, PubMed:23911299). The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ (PubMed:18227151). WWTR1 enhances PAX8 and NKX2-1/TTF1-dependent gene activation (PubMed:19010321). In conjunction with YAP1, involved in the regulation of TGFB1-dependent SMAD2 and SMAD3 nuclear accumulation (PubMed:18568018). Plays a key role in coupling SMADs to the transcriptional machinery such as the mediator complex (PubMed:18568018). Regulates embryonic stem-cell self-renewal, promotes cell proliferation and epithelial-mesenchymal transition (PubMed:18227151, PubMed:18568018)", "gene_name": "WWTR1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9GZV5", "name": "TAZ", "organism": "Homo sapiens", "uniprot_id": "Q9GZV5" }, { "function": "Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase (By similarity). Positively regulates postnatal regression of retinal hyaloid vessels via suppression of VEGFR2/KDR activity, downstream of OPN5 (PubMed:30936473)", "gene_name": "Drd2", "glycan_count": 0, "glycosylation_sites": [ { "position": 5, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 17, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 23, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P61168", "name": "ACTR2", "organism": "Mus musculus", "uniprot_id": "P61168" }, { "function": "Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon (IFN-alpha and IFN-beta) (PubMed:18724357, PubMed:18818105, PubMed:19433799, PubMed:19776740, PubMed:23027953, PubMed:23747010, PubMed:23910378, PubMed:27801882, PubMed:29973723, PubMed:30842659, PubMed:35045565, PubMed:35388221, PubMed:36808561, PubMed:37832545, PubMed:25704810, PubMed:39255680). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm (PubMed:26300263). Acts by binding cyclic dinucleotides: recognizes and binds cyclic di-GMP (c-di-GMP), a second messenger produced by bacteria, cyclic UMP-AMP (2',3'-cUAMP), and cyclic GMP-AMP (cGAMP), a messenger produced by CGAS in response to DNA virus in the cytosol (PubMed:21947006, PubMed:23258412, PubMed:23707065, PubMed:23722158, PubMed:23747010, PubMed:23910378, PubMed:26229117, PubMed:30842659, PubMed:35388221, PubMed:37379839). Upon binding to c-di-GMP, cUAMP or cGAMP, STING1 oligomerizes, translocates from the endoplasmic reticulum and is phosphorylated by TBK1 on the pLxIS motif, leading to recruitment and subsequent activation of the transcription factor IRF3 to induce expression of type I interferon and exert a potent anti-viral state (PubMed:22394562, PubMed:25636800, PubMed:29973723, PubMed:30842653, PubMed:35045565, PubMed:35388221). Exhibits 2',3' phosphodiester linkage-specific ligand recognition: can bind both 2'-3' linked cGAMP (2'-3'-cGAMP) and 3'-3' linked cGAMP but is preferentially activated by 2'-3' linked cGAMP (PubMed:23747010, PubMed:23910378, PubMed:26300263). The preference for 2'-3'-cGAMP, compared to other linkage isomers is probably due to the ligand itself, whichs adopts an organized free-ligand conformation that resembles the STING1-bound conformation and pays low energy costs in changing into the active conformation (PubMed:26150511). In addition to promote the production of type I interferons, plays a direct role in autophagy (PubMed:30568238, PubMed:30842662). Following cGAMP-binding, STING1 buds from the endoplasmic reticulum into COPII vesicles, which then form the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) (PubMed:30842662). The ERGIC serves as the membrane source for WIPI2 recruitment and LC3 lipidation, leading to formation of autophagosomes that target cytosolic DNA or DNA viruses for degradation by the lysosome (PubMed:30842662). Promotes autophagy by acting as a proton channel that directs proton efflux from the Golgi to facilitate MAP1LC3B/LC3B lipidation (PubMed:37535724). The autophagy- and interferon-inducing activities can be uncoupled and autophagy induction is independent of TBK1 phosphorylation (PubMed:30568238, PubMed:30842662). Autophagy is also triggered upon infection by bacteria: following c-di-GMP-binding, which is produced by live Gram-positive bacteria, promotes reticulophagy (By similarity). May be involved in translocon function, the translocon possibly being able to influence the induction of type I interferons (PubMed:18724357). May be involved in transduction of apoptotic signals via its association with the major histocompatibility complex class II (MHC-II) (By similarity)", "gene_name": "STING1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q86WV6", "name": "STING", "organism": "Homo sapiens", "uniprot_id": "Q86WV6" }, { "function": "Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity (PubMed:21478870, PubMed:23258413, PubMed:23707061, PubMed:23707065, PubMed:23722159, PubMed:24077100, PubMed:24116191, PubMed:24462292, PubMed:25131990, PubMed:26300263, PubMed:29976794, PubMed:30799039, PubMed:31142647, PubMed:32814054, PubMed:33273464, PubMed:33542149, PubMed:37217469, PubMed:37802025). Catalysis involves both the formation of a 2',5' phosphodiester linkage at the GpA step and the formation of a 3',5' phosphodiester linkage at the ApG step, producing c[G(2',5')pA(3',5')p] (PubMed:28214358, PubMed:28363908). Acts as a key DNA sensor: directly binds double-stranded DNA (dsDNA), inducing the formation of liquid-like droplets in which CGAS is activated, leading to synthesis of 2',3'-cGAMP, a second messenger that binds to and activates STING1, thereby triggering type-I interferon production (PubMed:28314590, PubMed:28363908, PubMed:29976794, PubMed:32817552, PubMed:33230297, PubMed:33606975, PubMed:35322803, PubMed:35438208, PubMed:35460603, PubMed:35503863). Preferentially recognizes and binds curved long dsDNAs of a minimal length of 40 bp (PubMed:30007416). Acts as a key foreign DNA sensor, the presence of double-stranded DNA (dsDNA) in the cytoplasm being a danger signal that triggers the immune responses (PubMed:28363908). Has antiviral activity by sensing the presence of dsDNA from DNA viruses in the cytoplasm (PubMed:28363908, PubMed:35613581). Also acts as an innate immune sensor of infection by retroviruses, such as HIV-2, by detecting the presence of reverse-transcribed DNA in the cytosol (PubMed:23929945, PubMed:24269171, PubMed:30270045, PubMed:32852081). In contrast, HIV-1 is poorly sensed by CGAS, due to its capsid that cloaks viral DNA from CGAS detection (PubMed:24269171, PubMed:30270045, PubMed:32852081). Detection of retroviral reverse-transcribed DNA in the cytosol may be indirect and be mediated via interaction with PQBP1, which directly binds reverse-transcribed retroviral DNA (PubMed:26046437). Also detects the presence of DNA from bacteria, such as M.tuberculosis (PubMed:26048138). 2',3'-cGAMP can be transferred from producing cells to neighboring cells through gap junctions, leading to promote STING1 activation and convey immune response to connecting cells (PubMed:24077100). 2',3'-cGAMP can also be transferred between cells by virtue of packaging within viral particles contributing to IFN-induction in newly infected cells in a cGAS-independent but STING1-dependent manner (PubMed:26229115). Also senses the presence of neutrophil extracellular traps (NETs) that are translocated to the cytosol following phagocytosis, leading to synthesis of 2',3'-cGAMP (PubMed:33688080). In addition to foreign DNA, can also be activated by endogenous nuclear or mitochondrial DNA (PubMed:28738408, PubMed:28759889, PubMed:31299200, PubMed:33031745, PubMed:33230297). When self-DNA leaks into the cytosol during cellular stress (such as mitochondrial stress, SARS-CoV-2 infection causing severe COVID-19 disease, DNA damage, mitotic arrest or senescence), or is present in form of cytosolic micronuclei, CGAS is activated leading to a state of sterile inflammation (PubMed:28738408, PubMed:28759889, PubMed:31299200, PubMed:33031745, PubMed:33230297, PubMed:35045565). Acts as a regulator of cellular senescence by binding to cytosolic chromatin fragments that are present in senescent cells, leading to trigger type-I interferon production via STING1 and promote cellular senescence (By similarity). Also involved in the inflammatory response to genome instability and double-stranded DNA breaks: acts by localizing to micronuclei arising from genome instability (PubMed:28738408, PubMed:28759889). Micronuclei, which are frequently found in cancer cells, consist of chromatin surrounded by their own nuclear membrane: following breakdown of the micronuclear envelope, a process associated with chromothripsis, CGAS binds self-DNA exposed to the cytosol, leading to 2',3'-cGAMP synthesis and subsequent activation of STING1 and type-I interferon production (PubMed:28738408, PubMed:28759889). Activated in response to prolonged mitotic arrest, promoting mitotic cell death (PubMed:31299200). In a healthy cell, CGAS is however kept inactive even in cellular events that directly expose it to self-DNA, such as mitosis, when cGAS associates with chromatin directly after nuclear envelope breakdown or remains in the form of postmitotic persistent nuclear cGAS pools bound to chromatin (PubMed:31299200, PubMed:33542149). Nuclear CGAS is inactivated by chromatin via direct interaction with nucleosomes, which block CGAS from DNA binding and thus prevent CGAS-induced autoimmunity (PubMed:31299200, PubMed:32911482, PubMed:32912999, PubMed:33051594, PubMed:33542149). Also acts as a suppressor of DNA repair in response to DNA damage: inhibits homologous recombination repair by interacting with PARP1, the CGAS-PARP1 interaction leading to impede the formation of the PARP1-TIMELESS complex (PubMed:30356214, PubMed:31544964). In addition to DNA, also sense translation stress: in response to translation stress, translocates to the cytosol and associates with collided ribosomes, promoting its activation and triggering type-I interferon production (PubMed:34111399). In contrast to other mammals, human CGAS displays species-specific mechanisms of DNA recognition and produces less 2',3'-cGAMP, allowing a more fine-tuned response to pathogens (PubMed:30007416)", "gene_name": "CGAS", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8N884", "name": "cGAS", "organism": "Homo sapiens", "uniprot_id": "Q8N884" }, { "function": "Required for normal hearing. It plays a role in cochlear amplification of auditory stimuli, likely through the positive regulation of prestin (SLC26A5) activity and outer hair cell (OHC) electromotility", "gene_name": "MYH1", "glycan_count": 1, "glycosylation_sites": [], "id": "P12882", "name": "MYHC", "organism": "Homo sapiens", "uniprot_id": "P12882" }, { "function": "Plays an important role in controlling cell cycle progression and DNA damage-induced G2 arrest (PubMed:9106657). Involved in p53/TP53 mediated inhibition of cellular proliferation in response to DNA damage. Also involved in p53-independent DNA damage-induced G2 arrest mediated by CREB3L1 in astrocytes and osteoblasts (By similarity). Binds to and inhibits cyclin-dependent kinase activity, preventing phosphorylation of critical cyclin-dependent kinase substrates and blocking cell cycle progression. Functions in the nuclear localization and assembly of cyclin D-CDK4 complex and promotes its kinase activity towards RB1. At higher stoichiometric ratios, inhibits the kinase activity of the cyclin D-CDK4 complex. Inhibits DNA synthesis by DNA polymerase delta by competing with POLD3 for PCNA binding (PubMed:11595739). Negatively regulates the CDK4- and CDK6-driven phosphorylation of RB1 in keratinocytes, thereby resulting in the release of E2F1 and subsequent transcription of E2F1-driven G1/S phase promoting genes (By similarity)", "gene_name": "CDKN1A", "glycan_count": 1, "glycosylation_sites": [], "id": "P38936", "name": "P21", "organism": "Homo sapiens", "uniprot_id": "P38936" }, { "function": "", "gene_name": "TMEM256", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8N2U0", "name": "Beta-1,4-glucuronyltransferase 1 (B4GAT1)", "organism": "Homo sapiens", "uniprot_id": "Q8N2U0" }, { "function": "Receptor for RTN4, OMG and MAG (PubMed:12037567, PubMed:12068310, PubMed:12089450, PubMed:12426574, PubMed:12839991, PubMed:16712417, PubMed:18411262, PubMed:19052207). Functions as a receptor for the sialylated gangliosides GT1b and GM1 (PubMed:18411262). Besides, functions as a receptor for chondroitin sulfate proteoglycans (By similarity). Can also bind heparin (By similarity). Intracellular signaling cascades are triggered via the coreceptor NGFR (PubMed:12426574). Signaling mediates activation of Rho and downstream reorganization of the actin cytoskeleton (PubMed:16712417, PubMed:22325200). Mediates axonal growth inhibition (PubMed:12839991, PubMed:19052207, PubMed:28892071). Plays a role in regulating axon regeneration and neuronal plasticity in the adult central nervous system. Plays a role in postnatal brain development. Required for normal axon migration across the brain midline and normal formation of the corpus callosum. Protects motoneurons against apoptosis; protection against apoptosis is probably mediated via interaction with MAG. Acts in conjunction with RTN4 and LINGO1 in regulating neuronal precursor cell motility during cortical development. Like other family members, plays a role in restricting the number dendritic spines and the number of synapses that are formed during brain development (PubMed:22325200)", "gene_name": "RTN4R", "glycan_count": 5, "glycosylation_sites": [ { "position": 82, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 179, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9BZR6", "name": "Reticulon-4 receptor (RTN4R)", "organism": "Homo sapiens", "uniprot_id": "Q9BZR6" }, { "function": "Component of the complement C1 complex, a multiprotein complex that initiates the classical pathway of the complement system, a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system (PubMed:11445589, PubMed:16169853, PubMed:417728, PubMed:467643, PubMed:6271784, PubMed:6282646, PubMed:6319179, PubMed:70787, PubMed:9422791). C1S is activated following association of the C1 complex with immunoglobulins (IgG or IgM) complexed with antigens to form antigen-antibody complexes on the surface of pathogens (PubMed:34155115). C1S is cleaved and activated by C1R to generate C1s subcomponent heavy and light chains (PubMed:11445589, PubMed:6271784). C1s subcomponent light chain then cleaves and activates C2 and C4, the next components of the classical complement pathway (PubMed:16169853, PubMed:467643, PubMed:6282646, PubMed:6319179, PubMed:6906228, PubMed:70787, PubMed:9422791)", "gene_name": "C1S", "glycan_count": 8, "glycosylation_sites": [ { "position": 174, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 406, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P09871", "name": "Complement C1s (C1S)", "organism": "Homo sapiens", "uniprot_id": "P09871" }, { "function": "Component of the membrane attack complex (MAC), a multiprotein complex activated by the complement cascade, which inserts into a target cell membrane and forms a pore, leading to target cell membrane rupture and cell lysis (PubMed:22832194, PubMed:26841837, PubMed:27052168, PubMed:30552328, PubMed:3335508). The MAC is initiated by proteolytic cleavage of C5 into complement C5b in response to the classical, alternative, lectin and GZMK complement pathways (PubMed:22832194, PubMed:30552328, PubMed:3335508). The complement pathways consist in a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system (PubMed:22832194, PubMed:30552328, PubMed:3335508). C7 serves as a membrane anchor (PubMed:30552328). During MAC assembly, associates with C5b and C6 to form the C5b-7 complex, a key lipophilic precursor of the MAC complex, which associates with the outer leaflet and reduces the energy for membrane bending (PubMed:30552328, PubMed:32569291)", "gene_name": "C7", "glycan_count": 37, "glycosylation_sites": [ { "position": 36, "type": "C-linked (Man) tryptophan" }, { "position": 202, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 503, "type": "C-linked (Man) tryptophan; partial" }, { "position": 506, "type": "C-linked (Man) tryptophan; partial" }, { "position": 509, "type": "C-linked (Man) tryptophan; partial" }, { "position": 696, "type": "O-linked (GalNAc...) threonine" }, { "position": 754, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P10643", "name": "Complement C7 (C7)", "organism": "Homo sapiens", "uniprot_id": "P10643" }, { "function": "Stabilizer subunit of the dolichol-phosphate mannose (DPM) synthase complex; tethers catalytic subunit DPM1 to the endoplasmic reticulum", "gene_name": "DPM3", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9P2X0", "name": "LARGE1 (Glycosyltransferase LARGE1)", "organism": "Homo sapiens", "uniprot_id": "Q9P2X0" }, { "function": "May be involved in the maintenance of the mucosal structure as a gel-like component of the mucosa", "gene_name": "FCGBP", "glycan_count": 47, "glycosylation_sites": [ { "position": 75, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 91, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1317, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 1743, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2138, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2518, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3719, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4145, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4540, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y6R7", "name": "FCGBP (IgG Fc-binding protein)", "organism": "Homo sapiens", "uniprot_id": "Q9Y6R7" }, { "function": "Kinase-defective receptor for members of the ephrin-B family. Binds to ephrin-B1 and ephrin-B2. Modulates cell adhesion and migration by exerting both positive and negative effects upon stimulation with ephrin-B2. Inhibits JNK activation, T-cell receptor-induced IL-2 secretion and CD25 expression upon stimulation with ephrin-B2", "gene_name": "EPHB6", "glycan_count": 0, "glycosylation_sites": [ { "position": 480, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O15197", "name": "Alpha-sarcoglycan (aSG)", "organism": "Homo sapiens", "uniprot_id": "O15197" }, { "function": "Probable serine lipid hydrolase associated with lipid droplets (By similarity). Has low cholesterol esterase activity (By similarity). Appears to lack triglyceride lipase activity (By similarity). Involved in cholesterol and triglyceride homeostasis; has opposing effects, stimulating cellular triglyceride accumulation and cellular cholesterol release (PubMed:24357060, PubMed:28578400). Acts antagonistically with PNPLA2/ATGL in regulation of cellular lipid stores (PubMed:28578400). May regulate triglyceride accumulation indirectly through stimulation of PNPLA2/ATGL ubiquitination and proteasomal degradation (PubMed:28578400). Promotes microtubule-dependent lipid droplet fusion (PubMed:28578400). Highly expressed in macrophage-rich areas in atherosclerotic lesions, suggesting that it could promote cholesterol ester turnover in macrophages (By similarity)", "gene_name": "LDAH", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H6V9", "name": "TMEM230", "organism": "Homo sapiens", "uniprot_id": "Q9H6V9" }, { "function": "Exhibits a potent RNase activity (PubMed:12244054, PubMed:12527768, PubMed:17150966). Has broad-spectrum antimicrobial activity against many pathogenic microorganisms including uropathogenic E.coli (UPEC), and remarkably potent activity (lethal dose of 90% < 30 nM) against a vancomycin resistant Enterococcus faecium (PubMed:12244054, PubMed:12527768, PubMed:17150966, PubMed:25075772, PubMed:33818125). Causes loss of bacterial membrane integrity (PubMed:17150966). Probably contributes to urinary tract sterility (PubMed:25075772). Bactericidal activity is independent of RNase activity (PubMed:17150966)", "gene_name": "RNASE7", "glycan_count": 0, "glycosylation_sites": [ { "position": 127, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9H1E1", "name": "RNASET2", "organism": "Homo sapiens", "uniprot_id": "Q9H1E1" }, { "function": "Induces cell attachment and spreading and plays a role in cell adhesion (PubMed:12235007). Enhances incorporation of BMP1 in the fibronectin matrix of connective tissues, and subsequent proteolytic activation of lysyl oxidase LOX (By similarity)", "gene_name": "POSTN", "glycan_count": 160, "glycosylation_sites": [ { "position": 599, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q15063", "name": "POSTN (periostin)", "organism": "Homo sapiens", "uniprot_id": "Q15063" }, { "function": "Chemoattractant active on T-lymphocytes and monocytes but not neutrophils. Activates the C-X-C chemokine receptor CXCR4 to induce a rapid and transient rise in the level of intracellular calcium ions and chemotaxis. SDF-1-beta(3-72) and SDF-1-alpha(3-67) show a reduced chemotactic activity. Binding to cell surface proteoglycans seems to inhibit formation of SDF-1-alpha(3-67) and thus to preserve activity on local sites. Also binds to atypical chemokine receptor ACKR3, which activates the beta-arrestin pathway and acts as a scavenger receptor for SDF-1. Binds to the allosteric site (site 2) of integrins and activates integrins ITGAV:ITGB3, ITGA4:ITGB1 and ITGA5:ITGB1 in a CXCR4-independent manner (PubMed:29301984). Acts as a positive regulator of monocyte migration and a negative regulator of monocyte adhesion via the LYN kinase. Stimulates migration of monocytes and T-lymphocytes through its receptors, CXCR4 and ACKR3, and decreases monocyte adherence to surfaces coated with ICAM-1, a ligand for beta-2 integrins. SDF1A/CXCR4 signaling axis inhibits beta-2 integrin LFA-1 mediated adhesion of monocytes to ICAM-1 through LYN kinase. Inhibits CXCR4-mediated infection by T-cell line-adapted HIV-1. Plays a protective role after myocardial infarction. Induces down-regulation and internalization of ACKR3 expressed in various cells. Has several critical functions during embryonic development; required for B-cell lymphopoiesis, myelopoiesis in bone marrow and heart ventricular septum formation. Stimulates the proliferation of bone marrow-derived B-cell progenitors in the presence of IL7 as well as growth of stromal cell-dependent pre-B-cells (By similarity)", "gene_name": "CXCL12", "glycan_count": 0, "glycosylation_sites": [], "id": "P48061", "name": "CXCL12", "organism": "Homo sapiens", "uniprot_id": "P48061" }, { "function": "This proteoglycan is a major component of extracellular matrix of cartilagenous tissues. A major function of this protein is to resist compression in cartilage. It binds avidly to hyaluronic acid via an N-terminal globular region", "gene_name": "ACAN", "glycan_count": 47, "glycosylation_sites": [ { "position": 126, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 239, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 333, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 371, "type": "O-linked (Xyl...) (keratan sulfate) threonine" }, { "position": 376, "type": "O-linked (Xyl...) (keratan sulfate) threonine" }, { "position": 387, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 434, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 602, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 658, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 738, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1530, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 1567, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 1581, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 1587, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 1591, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 1601, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 1703, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 2013, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P16112", "name": "Aggrecan", "organism": "Homo sapiens", "uniprot_id": "P16112" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q7L0J3 (SV2A)", "name": "SV2 (Synaptic Vesicle Glycoprotein 2)", "organism": "", "uniprot_id": "" }, { "function": "Involved in the regulation of both adhesion and cell morphology and cancer progression. Functions as an anti-adhesive molecule that maintains an open filtration pathway between neighboring foot processes in the podocyte by charge repulsion. Acts as a pro-adhesive molecule, enhancing the adherence of cells to immobilized ligands, increasing the rate of migration and cell-cell contacts in an integrin-dependent manner. Induces the formation of apical actin-dependent microvilli. Involved in the formation of a preapical plasma membrane subdomain to set up initial epithelial polarization and the apical lumen formation during renal tubulogenesis. Plays a role in cancer development and aggressiveness by inducing cell migration and invasion through its interaction with the actin-binding protein EZR. Affects EZR-dependent signaling events, leading to increased activities of the MAPK and PI3K pathways in cancer cells", "gene_name": "PODXL", "glycan_count": 64, "glycosylation_sites": [ { "position": 33, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 43, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 144, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 360, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O00592", "name": "Podocalyxcin", "organism": "Homo sapiens", "uniprot_id": "O00592" }, { "function": "", "gene_name": "LUM", "glycan_count": 297, "glycosylation_sites": [ { "position": 88, "type": "N-linked (GlcNAc...) (keratan sulfate) asparagine" }, { "position": 127, "type": "N-linked (GlcNAc...) (keratan sulfate) asparagine" }, { "position": 160, "type": "N-linked (GlcNAc...) (keratan sulfate) asparagine" }, { "position": 252, "type": "N-linked (GlcNAc...) (keratan sulfate) asparagine" } ], "id": "P51884", "name": "Lumican", "organism": "Homo sapiens", "uniprot_id": "P51884" }, { "function": "Affects the rate of fibrils formation. May have a primary role in collagen fibrillogenesis (By similarity)", "gene_name": "FMOD", "glycan_count": 105, "glycosylation_sites": [ { "position": 127, "type": "N-linked (GlcNAc...) (keratan sulfate) asparagine" }, { "position": 166, "type": "N-linked (GlcNAc...) (keratan sulfate) asparagine" }, { "position": 201, "type": "N-linked (GlcNAc...) (keratan sulfate) asparagine" }, { "position": 291, "type": "N-linked (GlcNAc...) (keratan sulfate) asparagine" }, { "position": 341, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q06828", "name": "Fibromodulin", "organism": "Homo sapiens", "uniprot_id": "Q06828" }, { "function": "Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components", "gene_name": "LAMA4", "glycan_count": 154, "glycosylation_sites": [ { "position": 39, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 215, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 315, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 465, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 531, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 557, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 578, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 581, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 638, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 646, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 742, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 758, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 761, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 787, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 810, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1093, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1288, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1366, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1418, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q16363", "name": "PRELP (Prolargin)", "organism": "Homo sapiens", "uniprot_id": "Q16363" }, { "function": "Protein tyrosine phosphatase that negatively regulates oligodendrocyte precursor proliferation in the embryonic spinal cord. Required for normal differentiation of the precursor cells into mature, fully myelinating oligodendrocytes. May play a role in protecting oligondendrocytes against apoptosis. May play a role in the establishment of contextual memory, probably via the dephosphorylation of proteins that are part of important signaling cascades (By similarity)", "gene_name": "PTPRZ1", "glycan_count": 7, "glycosylation_sites": [ { "position": 105, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 134, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 223, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 232, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 324, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 381, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 497, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 501, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 552, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 587, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 602, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 629, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 637, "type": "O-linked (Xyl...) (chondroitin sulfate) serine; alternate" }, { "position": 677, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 997, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 1017, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1050, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1082, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1122, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1457, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1549, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 1551, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 1562, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1618, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P23471", "name": "Phosphacan/RPTP-\u03b6", "organism": "Homo sapiens", "uniprot_id": "P23471" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9ULB1 (NRXN1)", "name": "Neurexins", "organism": "", "uniprot_id": "" }, { "function": "Beta-1,3-N-acetylglucosaminyltransferase involved in the synthesis of poly-N-acetyllactosamine. Catalyzes the initiation and elongation of poly-N-acetyllactosamine chains. Shows a marked preference for Gal(beta1-4)Glc(NAc)-based acceptors (PubMed:9892646). Probably constitutes the main polylactosamine synthase", "gene_name": "B3GNT2", "glycan_count": 25, "glycosylation_sites": [ { "position": 79, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 89, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 127, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 173, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 219, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NY97", "name": "B3GNT3", "organism": "Homo sapiens", "uniprot_id": "Q9NY97" }, { "function": "Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution. This endogenous envelope protein has lost its fusogenic properties. It can inhibit cell growth through decrease expression of cyclin B1 and increased expression of p21 in vitro", "gene_name": "ERV3-1", "glycan_count": 6, "glycosylation_sites": [ { "position": 64, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 105, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 201, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 316, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 369, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 382, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 399, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 527, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 569, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q14264", "name": "CD34", "organism": "Homo sapiens", "uniprot_id": "Q14264" }, { "function": "Sulfated glycoprotein widely distributed in basement membranes and tightly associated with laminin. Also binds to collagen IV and perlecan. It probably has a role in cell-extracellular matrix interactions", "gene_name": "NID1", "glycan_count": 7, "glycosylation_sites": [ { "position": 922, "type": "O-linked (GalNAc...) threonine" }, { "position": 935, "type": "O-linked (GalNAc...) threonine" } ], "id": "P14543", "name": "NID1", "organism": "Homo sapiens", "uniprot_id": "P14543" }, { "function": "Plays a major role in tight junction-specific obliteration of the intercellular space", "gene_name": "CLDN5", "glycan_count": 0, "glycosylation_sites": [], "id": "O00501", "name": "CLDN5", "organism": "Homo sapiens", "uniprot_id": "O00501" }, { "function": "Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate) (PubMed:8186255). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa (Probable). Acts as a key regulator of adaptive thermogenesis as part of the futile creatine cycle: localizes to the mitochondria of thermogenic fat cells and acts by mediating phosphorylation of creatine to initiate a futile cycle of creatine phosphorylation and dephosphorylation (By similarity). During the futile creatine cycle, creatine and N-phosphocreatine are in a futile cycle, which dissipates the high energy charge of N-phosphocreatine as heat without performing any mechanical or chemical work (By similarity)", "gene_name": "CKB", "glycan_count": 1, "glycosylation_sites": [], "id": "P12277", "name": "Creatine kinase (CK)", "organism": "Homo sapiens", "uniprot_id": "P12277" }, { "function": "Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa", "gene_name": "CKM", "glycan_count": 1, "glycosylation_sites": [], "id": "P06732", "name": "Creatine kinase-MB (CK-MB)", "organism": "Homo sapiens", "uniprot_id": "P06732" }, { "function": "Monomeric heme protein which primary function is to store oxygen and facilitate its diffusion within muscle tissues. Reversibly binds oxygen through a pentacoordinated heme iron and enables its timely and efficient release as needed during periods of heightened demand (PubMed:30918256, PubMed:34679218). Depending on the oxidative conditions of tissues and cells, and in addition to its ability to bind oxygen, it also has a nitrite reductase activity whereby it regulates the production of bioactive nitric oxide (PubMed:32891753). Under stress conditions, like hypoxia and anoxia, it also protects cells against reactive oxygen species thanks to its pseudoperoxidase activity (PubMed:34679218)", "gene_name": "MB", "glycan_count": 0, "glycosylation_sites": [], "id": "P02144", "name": "Myoglobin", "organism": "Homo sapiens", "uniprot_id": "P02144" }, { "function": "Catalyzes the production of glutathione from gamma-glutamylcysteine and glycine in an ATP-dependent manner (PubMed:7646467, PubMed:9215686). Glutathione (gamma-glutamylcysteinylglycine, GSH) is the most abundant intracellular thiol in living aerobic cells and is required for numerous processes including the protection of cells against oxidative damage, amino acid transport, the detoxification of foreign compounds, the maintenance of protein sulfhydryl groups in a reduced state and acts as a cofactor for a number of enzymes (PubMed:10369661). Participates in ophthalmate biosynthesis in hepatocytes (By similarity)", "gene_name": "GSS", "glycan_count": 0, "glycosylation_sites": [], "id": "P48637", "name": "Glutathione synthase", "organism": "Homo sapiens", "uniprot_id": "P48637" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "MUC16_HUMAN (Q8WXI7)", "name": "Carbohydrate Antigen 125 (CA125)", "organism": "", "uniprot_id": "" }, { "function": "Adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. Ligand for CD36 mediating antiangiogenic properties", "gene_name": "THBS2", "glycan_count": 76, "glycosylation_sites": [ { "position": 151, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 316, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 330, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 457, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 584, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 710, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1069, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P35442", "name": "Thrombospondin-2 (TSP2)", "organism": "Homo sapiens", "uniprot_id": "P35442" }, { "function": "Extracellular matrix protein implicated in guidance of migrating neurons as well as axons during development, synaptic plasticity as well as neuronal regeneration. Promotes neurite outgrowth from cortical neurons grown on a monolayer of astrocytes. Ligand for integrins alpha-8/beta-1, alpha-9/beta-1, alpha-V/beta-3 and alpha-V/beta-6. In tumors, stimulates angiogenesis by elongation, migration and sprouting of endothelial cells (PubMed:19884327)", "gene_name": "TNC", "glycan_count": 202, "glycosylation_sites": [ { "position": 38, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 72, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 166, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 184, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 327, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 788, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1018, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1034, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1079, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1093, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1119, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1184, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1210, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1261, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1275, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1301, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1366, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1392, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1445, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1455, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1485, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1534, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1809, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2162, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P24821", "name": "Tenascin C (TNC)", "organism": "Homo sapiens", "uniprot_id": "P24821" }, { "function": "Binds IGF1 and IGF2 with a relatively low affinity. Stimulates prostacyclin (PGI2) production. Stimulates cell adhesion. Acts as a ligand for CD93 to play a role in angiogenesis (PubMed:38218180)", "gene_name": "IGFBP7", "glycan_count": 3, "glycosylation_sites": [ { "position": 171, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q16270", "name": "IGFBP7", "organism": "Homo sapiens", "uniprot_id": "Q16270" }, { "function": "May play a role in hematopoiesis. In the cardiovascular system, could regulate growth factors or participate in cell signaling in maintaining large vessel integrity (By similarity). Component of the elastin-associated microfibrils (PubMed:8557636)", "gene_name": "MFAP5", "glycan_count": 36, "glycosylation_sites": [ { "position": 54, "type": "O-linked (GalNAc...) threonine" }, { "position": 79, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13361", "name": "MFAP4", "organism": "Homo sapiens", "uniprot_id": "Q13361" }, { "function": "Receptor that may have an important role in cell/cell signaling during nervous system formation", "gene_name": "CELSR2", "glycan_count": 28, "glycosylation_sites": [ { "position": 486, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 557, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 701, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1036, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1076, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1182, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1212, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1501, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1565, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1741, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1827, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1900, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2024, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2043, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2061, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2323, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2345, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9HCU4", "name": "SVEP1", "organism": "Homo sapiens", "uniprot_id": "Q9HCU4" }, { "function": "Cell adhesion protein that promotes the attachment of spinal cord and sensory neuron cells and the outgrowth of neurites in vitro. May contribute to the growth and guidance of axons in both the spinal cord and the PNS (By similarity). Major factor for vascular smooth muscle cell", "gene_name": "SPON1", "glycan_count": 26, "glycosylation_sites": [ { "position": 214, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 448, "type": "C-linked (Man) tryptophan" }, { "position": 451, "type": "C-linked (Man) tryptophan; partial" }, { "position": 507, "type": "C-linked (Man) tryptophan" }, { "position": 510, "type": "C-linked (Man) tryptophan; partial" }, { "position": 564, "type": "C-linked (Man) tryptophan" }, { "position": 620, "type": "C-linked (Man) tryptophan; partial" }, { "position": 623, "type": "C-linked (Man) tryptophan" }, { "position": 674, "type": "C-linked (Man) tryptophan" }, { "position": 681, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9HCB6", "name": "SPON1", "organism": "Homo sapiens", "uniprot_id": "Q9HCB6" }, { "function": "Isoform 1 or the secreted form is a binding and antagonizing protein for members of the TGF-beta family, such as activin, BMP2 and MSTN. Inhibits activin A-, activin B-, BMP2- and MSDT-induced cellular signaling; more effective on activin A than on activin B. Involved in bone formation; inhibits osteoclast differentiation. Involved in hematopoiesis; involved in differentiation of hemopoietic progenitor cells, increases hematopoietic cell adhesion to fibronectin and seems to contribute to the adhesion of hematopoietic precursor cells to the bone marrow stroma. Isoform 2 or the nuclear form is probably involved in transcriptional regulation via interaction with MLLT10", "gene_name": "FSTL3", "glycan_count": 2, "glycosylation_sites": [ { "position": 73, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 215, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O95633", "name": "FSTL3", "organism": "Homo sapiens", "uniprot_id": "O95633" }, { "function": "May be involved in cell adhesion and cell matrix association. May play a role in the regulation of anchorage versus migration or proliferation versus differentiation via its phosphorylation. May be a novel marker for leukemia diagnosis and for immature hematopoietic stem cell subsets. Belongs to the tetraspanin web involved in tumor progression and metastasis", "gene_name": "CDCP1", "glycan_count": 40, "glycosylation_sites": [ { "position": 39, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 122, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 180, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 205, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 270, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 310, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 386, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9H5V8", "name": "CDCP1", "organism": "Homo sapiens", "uniprot_id": "Q9H5V8" }, { "function": "Plays a role in cell adhesion (PubMed:8024701). May play a role in cell-collagen interactions (By similarity)", "gene_name": "TGFBI", "glycan_count": 2, "glycosylation_sites": [], "id": "Q15582", "name": "TGFBI", "organism": "Homo sapiens", "uniprot_id": "Q15582" }, { "function": "Receptor for ADP and ATP coupled to G-proteins that inhibit the adenylyl cyclase second messenger system. Not activated by UDP and UTP. Required for normal platelet aggregation and blood coagulation", "gene_name": "P2RY12", "glycan_count": 1, "glycosylation_sites": [ { "position": 6, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 13, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9H244", "name": "P2Y12 receptor", "organism": "Homo sapiens", "uniprot_id": "Q9H244" }, { "function": "Phosphatidylserine receptor that enhances the engulfment of apoptotic cells. Hyaluronan receptor that binds to and mediates endocytosis of hyaluronic acid (HA). Also acts, in different species, as a primary systemic scavenger receptor for heparin (Hep), chondroitin sulfate (CS), dermatan sulfate (DS), nonglycosaminoglycan (GAG), acetylated low-density lipoprotein (AcLDL), pro-collagen propeptides and advanced glycation end products (AGE). May serve to maintain tissue integrity by supporting extracellular matrix turnover or it may contribute to maintaining fluidity of bodily liquids by resorption of hyaluronan. Counter receptor which plays an important role in lymphocyte recruitment in the hepatic vasculature. Binds to both Gram-positive and Gram-negative bacteria and may play a role in defense against bacterial infection. The proteolytically processed 190 kDa form also functions as an endocytosis receptor for heparin internalization as well as HA and CS", "gene_name": "STAB2", "glycan_count": 6, "glycosylation_sites": [ { "position": 133, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 337, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 449, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 619, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 720, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 761, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 847, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 925, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1016, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1028, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1100, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1247, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1275, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1367, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1429, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1437, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1465, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1573, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1679, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1743, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1993, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2064, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2280, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2296, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2336, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2368, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2382, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2393, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8WWQ8", "name": "Mucin 5AC (MUC5AC)", "organism": "Homo sapiens", "uniprot_id": "Q8WWQ8" }, { "function": "May provide a mechanism for modulation of the composition of the protective mucus layer related to acid secretion or the presence of bacteria and noxious agents in the lumen. Plays an important role in the cytoprotection of epithelial surfaces and are used as tumor markers in a variety of cancers. May play a role in epithelial organogenesis", "gene_name": "MUC6", "glycan_count": 10, "glycosylation_sites": [ { "position": 268, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 486, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 659, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 975, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1179, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6W4X9", "name": "Mucin 6 (MUC6)", "organism": "Homo sapiens", "uniprot_id": "Q6W4X9" }, { "function": "Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways", "gene_name": "FGA", "glycan_count": 20, "glycosylation_sites": [ { "position": 320, "type": "O-linked (GalNAc...) threonine" }, { "position": 351, "type": "O-linked (GalNAc...) serine" }, { "position": 453, "type": "N-linked (GlcNAc...) asparagine; in variant Caracas-2" }, { "position": 686, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P02671", "name": "Fibrinogen", "organism": "Homo sapiens", "uniprot_id": "P02671" }, { "function": "E3 ubiquitin ligase that plays a role in various biological processes including neural stem cell differentiation, innate immunity, inflammatory resonse and autophagy (PubMed:19349376, PubMed:31123703). Plays a role in virus-triggered induction of IFN-beta and TNF-alpha by mediating the ubiquitination of STING1. Mechanistically, targets STING1 for 'Lys-63'-linked ubiquitination which promotes the interaction of STING1 with TBK1 (PubMed:22745133). Regulates bacterial clearance and promotes autophagy in Mycobacterium tuberculosis-infected macrophages (PubMed:37543647). Negatively regulates TLR3/4-mediated innate immune and inflammatory response by triggering the autophagic degradation of TICAM1 in an E3 activity-independent manner (PubMed:28898289). Plays an essential role in oxidative stress induced cell death by inducing loss of transmembrane potential and enhancing mitochondrial reactive oxygen species (ROS) production during oxidative stress conditions (PubMed:32918979). Ubiquitinates XIAP and targets it for proteasomal degradation (PubMed:21628460). Ubiquitinates DTNBP1 (dysbindin) and promotes its degradation (PubMed:19349376). May ubiquitinate BBS2 (PubMed:22500027). Ubiquitinates PIAS4/PIASY and promotes its degradation in keratinocytes treated with UVB and TNF-alpha (By similarity). Also acts as a regulator of autophagy by mediating formation of unanchored 'Lys-63'-linked polyubiquitin chains that activate ULK1: interaction with AMBRA1 is required for ULK1 activation (PubMed:31123703). Positively regulates dendritic branching by promoting ubiquitination and subsequent degradation of the epigenetic factor CDYL (PubMed:34888944). Under metabolic stress and phosphorylation by CHK2, mediates 'Lys-63'-linked ubiquitination of ATG7 at 'Lys-45' to initiate autophagy (PubMed:37943659)", "gene_name": "TRIM32", "glycan_count": 0, "glycosylation_sites": [], "id": "Q13049", "name": "TRIM32", "organism": "Homo sapiens", "uniprot_id": "Q13049" }, { "function": "Protein, which is both involved in DNA repair and protein ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box) complexes, respectively (PubMed:14739464, PubMed:15448697, PubMed:16260596, PubMed:16407242, PubMed:16407252, PubMed:16482215, PubMed:16940174, PubMed:17079684). Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair (PubMed:15448697, PubMed:16260596, PubMed:16407242, PubMed:16940174). The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches (PubMed:15448697, PubMed:16260596, PubMed:16407242, PubMed:16940174). Also functions as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:14739464, PubMed:16407252, PubMed:16482215, PubMed:17079684, PubMed:18332868, PubMed:18381890, PubMed:19966799, PubMed:22118460, PubMed:25043012, PubMed:25108355, PubMed:28886238). The functional specificity of the DCX E3 ubiquitin-protein ligase complex is determined by the variable substrate recognition component recruited by DDB1 (PubMed:14739464, PubMed:16407252, PubMed:16482215, PubMed:17079684, PubMed:18332868, PubMed:18381890, PubMed:19966799, PubMed:22118460, PubMed:25043012, PubMed:25108355). DCX(DDB2) (also known as DDB1-CUL4-ROC1, CUL4-DDB-ROC1 and CUL4-DDB-RBX1) may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage (PubMed:16473935, PubMed:16678110, PubMed:17041588, PubMed:18593899). The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair (PubMed:16473935, PubMed:16678110, PubMed:17041588, PubMed:18593899). DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER (PubMed:15882621). DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of TP53 in response to radiation-induced DNA damage and during DNA replication (PubMed:17041588). DCX(ERCC8) (the CSA complex) plays a role in transcription-coupled repair (TCR) (PubMed:12732143, PubMed:32355176, PubMed:38316879). The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1 (PubMed:26431207). DDB1-mediated CRY1 degradation promotes FOXO1 protein stability and FOXO1-mediated gluconeogenesis in the liver (By similarity). By acting on TET dioxygenses, essential for oocyte maintenance at the primordial follicle stage, hence essential for female fertility (By similarity). Maternal factor required for proper zygotic genome activation and genome reprogramming (By similarity)", "gene_name": "DDB1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q16531", "name": "Alpha-sarcoglycan", "organism": "Homo sapiens", "uniprot_id": "Q16531" }, { "function": "Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities. Transduces a signal by increasing the intracellular calcium ions and by stimulating adenylyl cyclase activity. The rank order of potency for agonists of this receptor is 1-oleoyl- > 1-stearoyl- > 1-palmitoyl- > 1-myristoyl- > 1-alkyl- > 1-alkenyl-LPA", "gene_name": "LPAR4", "glycan_count": 0, "glycosylation_sites": [ { "position": 15, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 24, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 28, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 183, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O15132", "name": "Gamma-sarcoglycan", "organism": "Homo sapiens", "uniprot_id": "Q99677" }, { "function": "Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix", "gene_name": "SGCE", "glycan_count": 5, "glycosylation_sites": [ { "position": 200, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O43556", "name": "Delta-sarcoglycan", "organism": "Homo sapiens", "uniprot_id": "O43556" }, { "function": "Regulator subunit of pancreatic ATP-sensitive potassium channel (KATP), playing a major role in the regulation of insulin release. In pancreatic cells, it forms KATP channels with KCNJ11; KCNJ11 forms the channel pore while ABCC8 is required for activation and regulation", "gene_name": "ABCC8", "glycan_count": 1, "glycosylation_sites": [ { "position": 10, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1049, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q09428", "name": "SUR1 (ABCC8)", "organism": "Homo sapiens", "uniprot_id": "Q09428" }, { "function": "Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X-X-S/T-C2 of thrombospondin type I repeats (TSRs) where C1 and C2 are the first and second cysteines of the repeat, respectively (PubMed:22588082). O-fucosylates members of several protein families including the ADAMTS, the thrombospondin (TSP) and spondin families (Probable) (PubMed:17395588). Required for the proper secretion of ADAMTS family members such as ADAMTSL1 and ADAMTS13 (PubMed:17395588, PubMed:17395589). The O-fucosylation of TSRs is also required for restricting epithelial to mesenchymal transition (EMT), maintaining the correct patterning of mesoderm and localization of the definite endoderm (By similarity)", "gene_name": "POFUT2", "glycan_count": 11, "glycosylation_sites": [ { "position": 189, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 209, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 259, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y2G5", "name": "POFUT2 (Protein O-fucosyltransferase 2)", "organism": "Homo sapiens", "uniprot_id": "Q9Y2G5" }, { "function": "Catalyzes the addition of fucose in alpha 1-6 linkage to the first GlcNAc residue, next to the peptide chains in N-glycans", "gene_name": "FUT8", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9BYC5", "name": "FUT8 (Alpha-1,6-fucosyltransferase)", "organism": "Homo sapiens", "uniprot_id": "Q9BYC5" }, { "function": "Antiporter specific for GDP-l-fucose and depending on the concomitant reverse transport of GMP. Involved in GDP-fucose import from the cytoplasm into the Golgi lumen", "gene_name": "SLC35C1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q96A29", "name": "SLC35C1 (GDP-fucose transporter)", "organism": "Homo sapiens", "uniprot_id": "Q96A29" }, { "function": "DNA/RNA-binding protein that plays a role in various cellular processes such as transcription regulation, RNA splicing, RNA transport, DNA repair and damage response (PubMed:27731383). Binds to ssRNA containing the consensus sequence 5'-AGGUAA-3' (PubMed:21256132). Binds to nascent pre-mRNAs and acts as a molecular mediator between RNA polymerase II and U1 small nuclear ribonucleoprotein thereby coupling transcription and splicing (PubMed:26124092). Also binds its own pre-mRNA and autoregulates its expression; this autoregulation mechanism is mediated by non-sense-mediated decay (PubMed:24204307). Plays a role in DNA repair mechanisms by promoting D-loop formation and homologous recombination during DNA double-strand break repair (PubMed:10567410). In neuronal cells, plays crucial roles in dendritic spine formation and stability, RNA transport, mRNA stability and synaptic homeostasis (By similarity)", "gene_name": "FUS", "glycan_count": 4, "glycosylation_sites": [], "id": "P35637", "name": "FUS", "organism": "Homo sapiens", "uniprot_id": "P35637" }, { "function": "May play a role in the integrity of hemidesmosome and the attachment of basal keratinocytes to the underlying basement membrane", "gene_name": "COL17A1", "glycan_count": 2, "glycosylation_sites": [ { "position": 1421, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UMD9", "name": "Laminin-211", "organism": "Homo sapiens", "uniprot_id": "Q9UMD9" }, { "function": "Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M (PubMed:33264373). Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication. Attenuates the stress granules formation by reducing host G3BP1 access to host mRNAs under stress conditions (PubMed:34901782, PubMed:36534661)", "gene_name": "N", "glycan_count": 0, "glycosylation_sites": [], "id": "P0DTC9", "name": "SARS-CoV-2 Nucleocapsid protein", "organism": "Severe acute respiratory syndrome coronavirus 2", "uniprot_id": "P0DTC9" }, { "function": "Precursor of the C5a anaphylatoxin and complement C5b components of the complement pathways, which consist in a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system (PubMed:12878586, PubMed:18204047, PubMed:30643019, PubMed:6554279). Activated downstream of classical, alternative, lectin and GZMK complement pathways (PubMed:12878586, PubMed:18204047, PubMed:30643019, PubMed:6554279)", "gene_name": "C5", "glycan_count": 29, "glycosylation_sites": [ { "position": 741, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 911, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1115, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1630, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01031", "name": "Complement component C5a", "organism": "Homo sapiens", "uniprot_id": "P01031" }, { "function": "May act as a scaffolding protein within caveolar membranes (PubMed:11751885). Forms a stable heterooligomeric complex with CAV2 that targets to lipid rafts and drives caveolae formation. Mediates the recruitment of CAVIN proteins (CAVIN1/2/3/4) to the caveolae (PubMed:19262564). Interacts directly with G-protein alpha subunits and can functionally regulate their activity (By similarity). Involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner (PubMed:17287217). Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway (By similarity). Negatively regulates TGFB1-mediated activation of SMAD2/3 by mediating the internalization of TGFBR1 from membrane rafts leading to its subsequent degradation (PubMed:25893292). Binds 20(S)-hydroxycholesterol (20(S)-OHC) (By similarity)", "gene_name": "CAV1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q03135", "name": "Caveolin 1 (CAV1)", "organism": "Homo sapiens", "uniprot_id": "Q03135" }, { "function": "Cell membrane receptor of natural killer/NK cells that is activated by binding of extracellular ligands including BAG6 and NCR3LG1. Stimulates NK cells cytotoxicity toward neighboring cells producing these ligands. It controls, for instance, NK cells cytotoxicity against tumor cells. Engagement of NCR3 by BAG6 also promotes myeloid dendritic cells (DC) maturation, both through killing DCs that did not acquire a mature phenotype, and inducing the release by NK cells of TNFA and IFNG which promote DC maturation", "gene_name": "NCR3", "glycan_count": 0, "glycosylation_sites": [ { "position": 42, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 121, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O14931", "name": "Interleukin-1 receptor-associated kinase 1 (IRAK1)", "organism": "Homo sapiens", "uniprot_id": "O14931" }, { "function": "E3 ubiquitin ligase that, together with UBE2N and UBE2V1, mediates the synthesis of 'Lys-63'-linked-polyubiquitin chains conjugated to proteins, such as ECSIT, IKBKG, IRAK1, AKT1 and AKT2 (PubMed:11057907, PubMed:18347055, PubMed:19465916, PubMed:19713527, PubMed:27746020, PubMed:31620128). Also mediates ubiquitination of free/unanchored polyubiquitin chain that leads to MAP3K7 activation (PubMed:19675569). Leads to the activation of NF-kappa-B and JUN (PubMed:16378096, PubMed:17135271, PubMed:17703191). Seems to also play a role in dendritic cells (DCs) maturation and/or activation (By similarity). Represses c-Myb-mediated transactivation, in B-lymphocytes (PubMed:18093978, PubMed:18758450). Adapter protein that seems to play a role in signal transduction initiated via TNF receptor, IL-1 receptor and IL-17 receptor (PubMed:12140561, PubMed:19825828, PubMed:8837778). Regulates osteoclast differentiation by mediating the activation of adapter protein complex 1 (AP-1) and NF-kappa-B, in response to RANK-L stimulation (By similarity). Together with MAP3K8, mediates CD40 signals that activate ERK in B-cells and macrophages, and thus may play a role in the regulation of immunoglobulin production (By similarity). Acts as a regulator of the JNK and NF-kappa-B signaling pathways by initiating assembly of heterotypic 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains that are then recognized by TAB2: TRAF6 catalyzes initial 'Lys-63'-linked-polyubiquitin chains that are then branched via 'Lys-48'-linked polyubiquitin by HUWE1 (PubMed:27746020). 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains protect 'Lys-63'-linkages from CYLD deubiquitination (PubMed:27746020). Participates also in the TCR signaling by ubiquitinating LAT (PubMed:23514740, PubMed:25907557)", "gene_name": "TRAF6", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y4K3", "name": "Tumor necrosis factor receptor-activated factor 6 (TRAF6)", "organism": "Homo sapiens", "uniprot_id": "Q9Y4K3" }, { "function": "Has activity against the synthetic substrates Boc-Phe-Ser-Arg-Mec, Boc-Leu-Thr-Arg-Mec, Boc-Gln-Ala-Arg-Mec and Boc-Val-Pro-Arg-Mec. The single-chain form is more active than the two-chain form against all of these substrates", "gene_name": "PRSS1", "glycan_count": 1, "glycosylation_sites": [], "id": "P07477", "name": "Immunoreactive Trypsinogen (IRT)", "organism": "Homo sapiens", "uniprot_id": "P07477" }, { "function": "Transcription regulator involved in inner cell mass and embryonic stem (ES) cells proliferation and self-renewal. Imposes pluripotency on ES cells and prevents their differentiation towards extraembryonic endoderm and trophectoderm lineages. Blocks bone morphogenetic protein-induced mesoderm differentiation of ES cells by physically interacting with SMAD1 and interfering with the recruitment of coactivators to the active SMAD transcriptional complexes. Acts as a transcriptional activator or repressor. Binds optimally to the DNA consensus sequence 5'-TAAT[GT][GT]-3' or 5'-[CG][GA][CG]C[GC]ATTAN[GC]-3'. Binds to the POU5F1/OCT4 promoter (PubMed:25825768). Able to autorepress its expression in differentiating (ES) cells: binds to its own promoter following interaction with ZNF281/ZFP281, leading to recruitment of the NuRD complex and subsequent repression of expression. When overexpressed, promotes cells to enter into S phase and proliferation", "gene_name": "NANOG", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H9S0", "name": "Nyctalopin", "organism": "Homo sapiens", "uniprot_id": "Q9H9S0" }, { "function": "Ligand for NRCAM and NFASC/neurofascin that plays a role in the formation and maintenance of the nodes of Ranvier on myelinated axons. Mediates interaction between Schwann cell microvilli and axons via its interactions with NRCAM and NFASC. Nodes of Ranvier contain clustered sodium channels that are crucial for the saltatory propagation of action potentials along myelinated axons. During development, nodes of Ranvier are formed by the fusion of two heminodes. Required for normal clustering of sodium channels at heminodes; not required for the formation of mature nodes with normal sodium channel clusters. Required, together with NRCAM, for maintaining NFASC and sodium channel clusters at mature nodes of Ranvier", "gene_name": "GLDN", "glycan_count": 5, "glycosylation_sites": [ { "position": 130, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 329, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 357, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 378, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 464, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6ZMI3", "name": "Pikachurin", "organism": "Homo sapiens", "uniprot_id": "Q6ZMI3" }, { "function": "", "gene_name": "UMODL1-AS1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8N2C9", "name": "ELFN1", "organism": "Homo sapiens", "uniprot_id": "Q8N2C9" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8N2C8", "name": "ELFN2", "organism": "", "uniprot_id": "Q8N2C8" }, { "function": "Auxiliary subunit of the NALCN sodium channel complex, a voltage-gated ion channel responsible for the resting Na(+) permeability that controls neuronal excitability (By similarity). Activated by neuropeptides substance P, neurotensin, and extracellular Ca(2+) that regulates neuronal excitability by controlling the sizes of NALCN-dependent sodium-leak current. UNC80 is essential for NALCN sensitivity to extracellular Ca(2+) (By similarity)", "gene_name": "UNC80", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8N2C7", "name": "LRIT3", "organism": "Homo sapiens", "uniprot_id": "Q8N2C7" }, { "function": "Ubiquitin-protein ligase that probably functions as an E3 ligase in conjunction with specific E1 and E2 ligases (By similarity). May also function as an E4 ligase mediating the assembly of polyubiquitin chains on substrates ubiquitinated by another E3 ubiquitin ligase (By similarity). May regulate myosin assembly in striated muscles together with STUB1 and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation (PubMed:17369820)", "gene_name": "UBE4B", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9BYI7", "name": "SynCAM1", "organism": "Homo sapiens", "uniprot_id": "O95155" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8N2C6", "name": "NGL2", "organism": "", "uniprot_id": "Q8N2C6" }, { "function": "", "gene_name": "KIR3DL1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8N6C9", "name": "AMIGO1", "organism": "Homo sapiens", "uniprot_id": "Q8N6C9" }, { "function": "May contribute to specialized endoplasmic reticulum functions in neurons", "gene_name": "SEZ6L2", "glycan_count": 22, "glycosylation_sites": [ { "position": 176, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 222, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 247, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 332, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 355, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 373, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 473, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 517, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 641, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6UXD5", "name": "LRRTM4", "organism": "Homo sapiens", "uniprot_id": "Q6UXD5" }, { "function": "Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement membrane and in the consequent activation of signaling transduction pathways. May play a role in cell fate determination and tissue morphogenesis. Acts as a PPP1R16B-dependent substrate of PPP1CA", "gene_name": "RPSA", "glycan_count": 1, "glycosylation_sites": [], "id": "P08865", "name": "67-kDa Laminin Receptor (67 kDa LR)", "organism": "Homo sapiens", "uniprot_id": "P08865" }, { "function": "Cell surface proteoglycan that contains both heparan sulfate and chondroitin sulfate and that links the cytoskeleton to the interstitial matrix (By similarity). Regulates exosome biogenesis in concert with SDCBP and PDCD6IP (PubMed:22660413). Able to induce its own expression in dental mesenchymal cells and also in the neighboring dental epithelial cells via an MSX1-mediated pathway (By similarity)", "gene_name": "SDC1", "glycan_count": 8, "glycosylation_sites": [ { "position": 37, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 43, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 45, "type": "O-linked (Xyl...) (heparan sulfate) serine" }, { "position": 47, "type": "O-linked (Xyl...) (heparan sulfate) serine" }, { "position": 206, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 216, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" } ], "id": "P18827", "name": "Syndecan-1", "organism": "Homo sapiens", "uniprot_id": "P18827" }, { "function": "Cell surface proteoglycan which regulates exosome biogenesis in concert with SDCBP and PDCD6IP (PubMed:22660413)", "gene_name": "SDC4", "glycan_count": 2, "glycosylation_sites": [ { "position": 39, "type": "O-linked (Xyl...) (glycosaminoglycan) serine" }, { "position": 61, "type": "O-linked (Xyl...) (glycosaminoglycan) serine" }, { "position": 63, "type": "O-linked (Xyl...) (glycosaminoglycan) serine" }, { "position": 95, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" } ], "id": "P31431", "name": "Syndecan-4", "organism": "Homo sapiens", "uniprot_id": "P31431" }, { "function": "Transmembrane glycoprotein that functions as both a receptor and an adhesion molecule playing a crucial role in cell adhesion, motility, migration and invasion (PubMed:9616226, PubMed:31413112). Extracellular domain enables binding to extracellular matrix proteins, such as laminin, integrin and other ligands while its intracellular domain interacts with cytoskeletal proteins like hemoglobin, facilitating cell signal transduction (PubMed:17158232). Serves as a receptor for laminin alpha-5/LAMA5 to promote cell adhesion (PubMed:15975931). Mechanistically, JAK2 induces BCAM phosphorylation and activates its adhesion to laminin by stimulating a Rap1/AKT signaling pathway in the absence of EPOR (PubMed:23160466)", "gene_name": "BCAM", "glycan_count": 66, "glycosylation_sites": [ { "position": 321, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 377, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 383, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 419, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 439, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P50895", "name": "Lu/BCAM (Lutheran/Basal Cell Adhesion Molecule)", "organism": "Homo sapiens", "uniprot_id": "P50895" }, { "function": "Binds fibroblast growth factor and E-selectin (cell-adhesion lectin on endothelial cells mediating the binding of neutrophils)", "gene_name": "GLG1", "glycan_count": 105, "glycosylation_sites": [ { "position": 165, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 210, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 581, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 677, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 786, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q92896", "name": "MCAM (Melanoma Cell Adhesion Molecule)", "organism": "Homo sapiens", "uniprot_id": "Q92896" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q14118-2", "name": "\u03b1-dystroglycan", "organism": "", "uniprot_id": "" }, { "function": "Membrane immune adherence receptor that plays a critical role in the capture and clearance of complement-opsonized pathogens by erythrocytes and monocytes/macrophages (PubMed:2963069). Mediates the binding by these cells of particles and immune complexes that have activated complement to eliminate them from the circulation (PubMed:2963069). Also acts in the inhibition of spontaneous complement activation by impairing the formation and function of the alternative and classical pathway C3/C5 convertases, and by serving as a cofactor for the cleavage by factor I of C3b to iC3b, C3c and C3d,g, and of C4b to C4c and C4d (PubMed:2972794, PubMed:8175757). Also plays a role in immune regulation by contributing, upon ligand binding, to the generation of regulatory T cells from activated helper T cells (PubMed:25742728)", "gene_name": "CR1", "glycan_count": 13, "glycosylation_sites": [ { "position": 56, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 252, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 410, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 447, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 509, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 578, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 702, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 860, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 897, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 959, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1028, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1152, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1310, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1481, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1504, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1534, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1540, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1605, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1763, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1908, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P17927", "name": "Complement receptor 1 (CR1)", "organism": "Homo sapiens", "uniprot_id": "P17927" }, { "function": "Acts as a decoy receptor for TNFSF11/RANKL and thereby neutralizes its function in osteoclastogenesis. Inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local ratio between TNFSF11 and TNFRSF11B. May also play a role in preventing arterial calcification. May act as decoy receptor for TNFSF10/TRAIL and protect against apoptosis. TNFSF10/TRAIL binding blocks the inhibition of osteoclastogenesis", "gene_name": "TNFRSF11B", "glycan_count": 30, "glycosylation_sites": [ { "position": 98, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 152, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 165, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 178, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 289, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O00300", "name": "Osteoprotegerin (OPG)", "organism": "Homo sapiens", "uniprot_id": "O00300" }, { "function": "Cytokine that plays an essential role in the regulation of survival, proliferation and differentiation of hematopoietic precursor cells, especially mononuclear phagocytes, such as macrophages and monocytes. Promotes the release of pro-inflammatory chemokines, and thereby plays an important role in innate immunity and in inflammatory processes. Plays an important role in the regulation of osteoclast proliferation and differentiation, the regulation of bone resorption, and is required for normal bone development. Required for normal male and female fertility. Promotes reorganization of the actin cytoskeleton, regulates formation of membrane ruffles, cell adhesion and cell migration. Plays a role in lipoprotein clearance", "gene_name": "CSF1", "glycan_count": 7, "glycosylation_sites": [ { "position": 154, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 172, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 309, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 363, "type": "O-linked (GalNAc...) threonine" }, { "position": 365, "type": "O-linked (GalNAc...) threonine" } ], "id": "P09603", "name": "Macrophage Colony-Stimulating Factor (M-CSF)", "organism": "Homo sapiens", "uniprot_id": "P09603" }, { "function": "Cytokine that binds to TNFRSF11B/OPG and to TNFRSF11A/RANK. Osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive T-cell proliferation. May be an important regulator of interactions between T-cells and dendritic cells and may play a role in the regulation of the T-cell-dependent immune response. May also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy (PubMed:22664871). Induces osteoclastogenesis by activating multiple signaling pathways in osteoclast precursor cells, chief among which is induction of long lasting oscillations in the intracellular concentration of Ca (2+) resulting in the activation of NFATC1, which translocates to the nucleus and induces osteoclast-specific gene transcription to allow differentiation of osteoclasts. During osteoclast differentiation, in a TMEM64 and ATP2A2-dependent manner induces activation of CREB1 and mitochondrial ROS generation necessary for proper osteoclast generation (By similarity)", "gene_name": "TNFSF11", "glycan_count": 0, "glycosylation_sites": [ { "position": 171, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 198, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O14788", "name": "Receptor Activator of Nuclear Factor \u03baB Ligand (RANKL)", "organism": "Homo sapiens", "uniprot_id": "O14788" }, { "function": "Cytokine that binds to TNFRSF13B/TACI and TNFRSF17/BCMA. TNFSF13/APRIL binds to the same 2 receptors. Together, they form a 2 ligands -2 receptors pathway involved in the stimulation of B- and T-cell function and the regulation of humoral immunity. A third B-cell specific BAFF-receptor (BAFFR/BR3) promotes the survival of mature B-cells and the B-cell response", "gene_name": "TNFSF13B", "glycan_count": 3, "glycosylation_sites": [ { "position": 124, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 242, "type": "N-linked (GlcNAc...) (high mannose) asparagine" } ], "id": "Q9Y275", "name": "BAFF (TNFSF13B)", "organism": "Homo sapiens", "uniprot_id": "Q9Y275" }, { "function": "B-cell receptor specific for TNFSF13B/TALL1/BAFF/BLyS. Promotes the survival of mature B-cells and the B-cell response", "gene_name": "TNFRSF13C", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96RJ3", "name": "BAFF-R (TNFRSF13C)", "organism": "Homo sapiens", "uniprot_id": "Q96RJ3" }, { "function": "Receptor for TNFSF5/CD40LG (PubMed:31331973). Transduces TRAF6- and MAP3K8-mediated signals that activate ERK in macrophages and B cells, leading to induction of immunoglobulin secretion (By similarity)", "gene_name": "CD40", "glycan_count": 27, "glycosylation_sites": [ { "position": 153, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 180, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P25942", "name": "CD40", "organism": "Homo sapiens", "uniprot_id": "P25942" }, { "function": "Cytokine that acts as a ligand to CD40/TNFRSF5 (PubMed:1280226, PubMed:31331973). Costimulates T-cell proliferation and cytokine production (PubMed:8617933). Its cross-linking on T-cells generates a costimulatory signal which enhances the production of IL4 and IL10 in conjunction with the TCR/CD3 ligation and CD28 costimulation (PubMed:8617933). Induces the activation of NF-kappa-B (PubMed:15067037, PubMed:31331973). Induces the activation of kinases MAPK8 and PAK2 in T-cells (PubMed:15067037). Induces tyrosine phosphorylation of isoform 3 of CD28 (PubMed:15067037). Mediates B-cell proliferation in the absence of co-stimulus as well as IgE production in the presence of IL4 (By similarity). Involved in immunoglobulin class switching (By similarity)", "gene_name": "CD40LG", "glycan_count": 33, "glycosylation_sites": [ { "position": 240, "type": "N-linked (GlcNAc...) (complex) asparagine; alternate" }, { "position": 240, "type": "N-linked (GlcNAc...) (high mannose) asparagine; alternate" } ], "id": "P29965", "name": "CD40L (CD154)", "organism": "Homo sapiens", "uniprot_id": "P29965" }, { "function": "Receptor for the Fc region of complexed or aggregated immunoglobulins gamma. Low affinity receptor. Involved in a variety of effector and regulatory functions such as phagocytosis of immune complexes and modulation of antibody production by B-cells. Binding to this receptor results in down-modulation of previous state of cell activation triggered via antigen receptors on B-cells (BCR), T-cells (TCR) or via another Fc receptor. Isoform IIB1 fails to mediate endocytosis or phagocytosis. Isoform IIB2 does not trigger phagocytosis", "gene_name": "FCGR2B", "glycan_count": 38, "glycosylation_sites": [ { "position": 106, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 180, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 187, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P31994", "name": "CD32B (Fc\u03b3RIIB)", "organism": "Homo sapiens", "uniprot_id": "P31994" }, { "function": "Required in cooperation with CD79A for initiation of the signal transduction cascade activated by the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Enhances phosphorylation of CD79A, possibly by recruiting kinases which phosphorylate CD79A or by recruiting proteins which bind to CD79A and protect it from dephosphorylation", "gene_name": "CD79B", "glycan_count": 0, "glycosylation_sites": [ { "position": 73, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 101, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 127, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 128, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P40259", "name": "CD79B", "organism": "Homo sapiens", "uniprot_id": "P40259" }, { "function": "Cytokine that binds to TNFRSF13B/TACI and to TNFRSF17/BCMA. Plays a role in the regulation of tumor cell growth. May be involved in monocyte/macrophage-mediated immunological processes", "gene_name": "TNFSF13", "glycan_count": 16, "glycosylation_sites": [ { "position": 124, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O75888", "name": "APRIL (TNFSF13)", "organism": "Homo sapiens", "uniprot_id": "O75888" }, { "function": "Cadherins are calcium-dependent cell adhesion proteins (PubMed:11976333). They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells (PubMed:11976333). Promotes organization of radial actin fiber structure and cellular response to contractile forces, via its interaction with AMOTL2 which facilitates anchoring of radial actin fibers to CDH1 junction complexes at the cell membrane (By similarity). Plays a role in the early stages of desmosome cell-cell junction formation via facilitating the recruitment of DSG2 and DSP to desmosome plaques (PubMed:29999492). Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7", "gene_name": "CDH1", "glycan_count": 2, "glycosylation_sites": [ { "position": 280, "type": "O-linked (Man...) serine" }, { "position": 285, "type": "O-linked (Man...) threonine" }, { "position": 358, "type": "O-linked (Man...) threonine" }, { "position": 470, "type": "O-linked (Man...) threonine" }, { "position": 472, "type": "O-linked (Man...) threonine" }, { "position": 509, "type": "O-linked (Man...) threonine" }, { "position": 558, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 570, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 576, "type": "O-linked (Man...) threonine" }, { "position": 578, "type": "O-linked (Man...) threonine" }, { "position": 580, "type": "O-linked (Man...) threonine" }, { "position": 622, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 637, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P12830", "name": "E-cadherin", "organism": "Homo sapiens", "uniprot_id": "P12830" }, { "function": "May play a role in neuropeptide signaling processes. Ligand for LGR7, RXFP3 and RXFP4", "gene_name": "RLN3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8WXF3", "name": "GALNT14", "organism": "Homo sapiens", "uniprot_id": "Q8WXF3" }, { "function": "ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits", "gene_name": "DDX51", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8N8A6", "name": "DTWD2", "organism": "Homo sapiens", "uniprot_id": "Q8N8A6" }, { "function": "Catalyzes the addition of N-acetylglucosamine (GlcNAc) in beta 1-6 linkage to the alpha-linked mannose of biantennary N-linked oligosaccharides (PubMed:10395745, PubMed:30140003). Catalyzes an important step in the biosynthesis of branched, complex-type N-glycans, such as those found on EGFR, TGFR (TGF-beta receptor) and CDH2 (PubMed:10395745, PubMed:22614033, PubMed:30140003). Via its role in the biosynthesis of complex N-glycans, plays an important role in the activation of cellular signaling pathways, reorganization of the actin cytoskeleton, cell-cell adhesion and cell migration. MGAT5-dependent EGFR N-glycosylation enhances the interaction between EGFR and LGALS3 and thereby prevents rapid EGFR endocytosis and prolongs EGFR signaling. Required for efficient interaction between TGFB1 and its receptor. Enhances activation of intracellular signaling pathways by several types of growth factors, including FGF2, PDGF, IGF, TGFB1 and EGF. MGAT5-dependent CDH2 N-glycosylation inhibits CDH2-mediated homotypic cell-cell adhesion and contributes to the regulation of downstream signaling pathways. Promotes cell migration. Contributes to the regulation of the inflammatory response. MGAT5-dependent TCR N-glycosylation enhances the interaction between TCR and LGALS3, limits agonist-induced TCR clustering, and thereby dampens TCR-mediated responses to antigens. Required for normal leukocyte evasation and accumulation at sites of inflammation (By similarity). Inhibits attachment of monocytes to the vascular endothelium and subsequent monocyte diapedesis (PubMed:22614033)", "gene_name": "MGAT5", "glycan_count": 6, "glycosylation_sites": [ { "position": 110, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 115, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 118, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 334, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 433, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 447, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q09328", "name": "N-acetylglucosaminyltransferase V", "organism": "Homo sapiens", "uniprot_id": "Q09328" }, { "function": "Integrin alpha-3/beta-1 is a receptor for fibronectin, laminin, collagen, epiligrin, thrombospondin and CSPG4. Integrin alpha-3/beta-1 provides a docking site for FAP (seprase) at invadopodia plasma membranes in a collagen-dependent manner and hence may participate in the adhesion, formation of invadopodia and matrix degradation processes, promoting cell invasion. Alpha-3/beta-1 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration", "gene_name": "ITGA3", "glycan_count": 98, "glycosylation_sites": [ { "position": 86, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 107, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 265, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 500, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 511, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 573, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 605, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 656, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 697, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 841, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 857, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 926, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 935, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 969, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P26006", "name": "ITGA3", "organism": "Homo sapiens", "uniprot_id": "P26006" }, { "function": "Integrin alpha-5/beta-1 (ITGA5:ITGB1) is a receptor for fibronectin and fibrinogen. It recognizes the sequence R-G-D in its ligands. ITGA5:ITGB1 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1 (PubMed:18635536, PubMed:25398877). ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1 (PubMed:12807887, PubMed:17158881). ITGA5:ITGB1 acts as a receptor for fibronectin (FN1) and mediates R-G-D-dependent cell adhesion to FN1 (PubMed:33962943). ITGA5:ITGB1 is a receptor for IL1B and binding is essential for IL1B signaling (PubMed:29030430). ITGA5:ITGB3 is a receptor for soluble CD40LG and is required for CD40/CD40LG signaling (PubMed:31331973)", "gene_name": "ITGA5", "glycan_count": 121, "glycosylation_sites": [ { "position": 84, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 182, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 297, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 307, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 316, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 524, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 530, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 593, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 609, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 675, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 712, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 724, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 773, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 868, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08648", "name": "ITGA5", "organism": "Homo sapiens", "uniprot_id": "P08648" }, { "function": "Integrin alpha-6/beta-1 (ITGA6:ITGB1) is a receptor for laminin on platelets (By similarity). Integrin alpha-6/beta-1 (ITGA6:ITGB1) is present in oocytes and is involved in sperm-egg fusion (By similarity). Integrin alpha-6/beta-4 (ITGA6:ITGB4) is a receptor for laminin in epithelial cells and it plays a critical structural role in the hemidesmosome (By similarity). ITGA6:ITGB4 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling (PubMed:20682778). ITGA6:ITGB4 binds to IGF1 and this binding is essential for IGF1 signaling (PubMed:22351760). ITGA6:ITGB4 binds to IGF2 and this binding is essential for IGF2 signaling (PubMed:28873464)", "gene_name": "ITGA6", "glycan_count": 84, "glycosylation_sites": [ { "position": 78, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 223, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 323, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 409, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 770, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 787, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 930, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 966, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 997, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P23229", "name": "ITGA6", "organism": "Homo sapiens", "uniprot_id": "P23229" }, { "function": "Involved in the maintenance of mitochondrial membrane potential in pancreatic ductal adenocarcinoma (PDAC) cells. Promotes pancreatic ductal adenocarcinoma (PDAC) cell growth. May play a role as a nucleotide-sugar transporter", "gene_name": "SLC35F6", "glycan_count": 1, "glycosylation_sites": [ { "position": 110, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8N357", "name": "SLC35A4", "organism": "Homo sapiens", "uniprot_id": "Q8N357" }, { "function": "Acts as a component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of the cycling of mannose 6-phosphate receptors between the TGN and endosomes, this cycling is necessary for proper lysosomal sorting of acid hydrolases such as CTSD (PubMed:15878329, PubMed:18367545). Acts as a component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4-positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane (PubMed:25799061)", "gene_name": "VPS52", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8N1B4", "name": "SLC35A5", "organism": "Homo sapiens", "uniprot_id": "Q8N1B4" }, { "function": "Hormone produced in response to various stresses to confer information about those stresses to the brain, and trigger an aversive response, characterized by nausea, vomiting, and/or loss of appetite (PubMed:23468844, PubMed:24971956, PubMed:28846097, PubMed:28846098, PubMed:28846099, PubMed:28953886, PubMed:29046435, PubMed:30639358, PubMed:31875646, PubMed:33589633, PubMed:38092039). The aversive response is both required to reduce continuing exposure to those stresses at the time of exposure and to promote avoidance behavior in the future (PubMed:30639358, PubMed:33589633, PubMed:38092039). Acts by binding to its receptor, GFRAL, activating GFRAL-expressing neurons localized in the area postrema and nucleus tractus solitarius of the brainstem (PubMed:28846097, PubMed:28846098, PubMed:28846099, PubMed:28953886, PubMed:31535977). It then triggers the activation of neurons localized within the parabrachial nucleus and central amygdala, which constitutes part of the 'emergency circuit' that shapes responses to stressful conditions (PubMed:28953886). The GDF15-GFRAL signal induces expression of genes involved in metabolism, such as lipid metabolism in adipose tissues (PubMed:31402172). Required for avoidance behavior in response to food allergens: induced downstream of mast cell activation to promote aversion and minimize harmful effects of exposure to noxious substances (By similarity). In addition to suppress appetite, also promotes weight loss by enhancing energy expenditure in muscle: acts by increasing calcium futile cycling in muscle (By similarity). Contributes to the effect of metformin, an anti-diabetic drug, on appetite reduction and weight loss: produced in the kidney in response to metformin treatment, thereby activating the GDF15-GFRAL response, leading to reduced appetite and weight (PubMed:31875646, PubMed:37060902). The contribution of GDF15 to weight loss following metformin treatment is however limited and subject to discussion (PubMed:36001956). Produced in response to anticancer drugs, such as camptothecin or cisplatin, promoting nausea, vomiting and contributing to malnutrition (By similarity). Overproduced in many cancers, promoting anorexia in cancer (cachexia) (PubMed:32661391). Responsible for the risk of nausea and vomiting during pregnancy: high levels of GDF15 during pregnancy, mostly originating from the fetus, are associated with increased nausea and vomiting (PubMed:38092039). Maternal sensitivity to nausea is probably determined by pre-pregnancy exposure to GDF15, women with naturally high level of GDF15 being less susceptible to nausea than women with low levels of GDF15 before pregnancy (PubMed:38092039). Promotes metabolic adaptation in response to systemic inflammation caused by bacterial and viral infections in order to promote tissue tolerance and prevent tissue damage (PubMed:31402172). Required for tissue tolerance in response to myocardial infarction by acting as an inhibitor of leukocyte integring activation, thereby protecting against cardiac rupture (By similarity). Inhibits growth hormone signaling on hepatocytes (By similarity)", "gene_name": "GDF15", "glycan_count": 4, "glycosylation_sites": [ { "position": 70, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q99988", "name": "GDF15", "organism": "Homo sapiens", "uniprot_id": "Q99988" }, { "function": "Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition", "gene_name": "INHBA", "glycan_count": 4, "glycosylation_sites": [ { "position": 165, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08476", "name": "Activin A", "organism": "Homo sapiens", "uniprot_id": "P08476" }, { "function": "Direct ligand for ERBB3 and ERBB4 tyrosine kinase receptors. Concomitantly recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. The multiple isoforms perform diverse functions such as inducing growth and differentiation of epithelial, glial, neuronal, and skeletal muscle cells; inducing expression of acetylcholine receptor in synaptic vesicles during the formation of the neuromuscular junction; stimulating lobuloalveolar budding and milk production in the mammary gland and inducing differentiation of mammary tumor cells; stimulating Schwann cell proliferation; implication in the development of the myocardium such as trabeculation of the developing heart. Isoform 10 may play a role in motor and sensory neuron development. Binds to ERBB4 (PubMed:10867024, PubMed:7902537). Binds to ERBB3 (PubMed:20682778). Acts as a ligand for integrins and binds (via EGF domain) to integrins ITGAV:ITGB3 or ITGA6:ITGB4. Its binding to integrins and subsequent ternary complex formation with integrins and ERRB3 are essential for NRG1-ERBB signaling. Induces the phosphorylation and activation of MAPK3/ERK1, MAPK1/ERK2 and AKT1 (PubMed:20682778). Ligand-dependent ERBB4 endocytosis is essential for the NRG1-mediated activation of these kinases in neurons (By similarity)", "gene_name": "NRG1", "glycan_count": 1, "glycosylation_sites": [ { "position": 120, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 126, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 164, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q02297", "name": "NRG1", "organism": "Homo sapiens", "uniprot_id": "Q02297" }, { "function": "Cell surface receptor that plays important roles in innate and adaptive immunity by amplifying inflammatory responses (PubMed:10799849, PubMed:21393102). Upon activation by various ligands such as PGLYRP1, HMGB1 or HSP70, multimerizes and forms a complex with transmembrane adapter TYROBP/DAP12 (PubMed:17568691, PubMed:25595774, PubMed:29568119). In turn, initiates a SYK-mediated cascade of tyrosine phosphorylation, activating multiple downstream mediators such as BTK, MAPK1, MAPK3 or phospholipase C-gamma (PubMed:14656437, PubMed:21659545). This cascade promotes the neutrophil- and macrophage-mediated release of pro-inflammatory cytokines and/or chemokines, as well as their migration and thereby amplifies inflammatory responses that are triggered by bacterial and fungal infections (PubMed:17098818, PubMed:17568691). By also promoting the amplification of inflammatory signals that are initially triggered by Toll-like receptor (TLR) and NOD-like receptor engagement, plays a major role in the pathophysiology of acute and chronic inflammatory diseases of different etiologies including septic shock and atherosclerosis (PubMed:11323674, PubMed:21393102)", "gene_name": "TREM1", "glycan_count": 0, "glycosylation_sites": [ { "position": 146, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 191, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 194, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NP99", "name": "TREM1", "organism": "Homo sapiens", "uniprot_id": "Q9NP99" }, { "function": "Binds to TEK/TIE2, competing for the ANGPT1 binding site, and modulating ANGPT1 signaling (PubMed:15284220, PubMed:19116766, PubMed:19223473, PubMed:9204896). Can induce tyrosine phosphorylation of TEK/TIE2 in the absence of ANGPT1 (PubMed:15284220, PubMed:19116766, PubMed:19223473, PubMed:9204896). In the absence of angiogenic inducers, such as VEGF, ANGPT2-mediated loosening of cell-matrix contacts may induce endothelial cell apoptosis with consequent vascular regression. In concert with VEGF, it may facilitate endothelial cell migration and proliferation, thus serving as a permissive angiogenic signal (PubMed:15284220, PubMed:19116766, PubMed:19223473, PubMed:9204896). Involved in the regulation of lymphangiogenesis (PubMed:32908006)", "gene_name": "ANGPT2", "glycan_count": 23, "glycosylation_sites": [ { "position": 89, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 119, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 133, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 151, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 240, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 304, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O15123", "name": "ANGPT2", "organism": "Homo sapiens", "uniprot_id": "O15123" }, { "function": "Transcription factor that binds and activates the promoter of thyroid specific genes such as thyroglobulin, thyroperoxidase, and thyrotropin receptor. Crucial in the maintenance of the thyroid differentiation phenotype. May play a role in lung development and surfactant homeostasis. Forms a regulatory loop with GRHL2 that coordinates lung epithelial cell morphogenesis and differentiation. Activates the transcription of GNRHR and plays a role in enhancing the circadian oscillation of its gene expression. Represses the transcription of the circadian transcriptional repressor NR1D1 (By similarity)", "gene_name": "NKX2-1", "glycan_count": 1, "glycosylation_sites": [], "id": "P43699", "name": "Thyroid transcription factor-1 (TTF-1)", "organism": "Homo sapiens", "uniprot_id": "P43699" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P25101/P24530", "name": "Endothelin receptor type A/B", "organism": "", "uniprot_id": "" }, { "function": "Heterodimerizes with IL12B to form the IL-12 cytokine or with EBI3/IL27B to form the IL-35 cytokine (PubMed:8605935, PubMed:8943050). IL-12 is primarily produced by professional antigen-presenting cells (APCs) such as B-cells and dendritic cells (DCs) as well as macrophages and granulocytes and regulates T-cell and natural killer-cell responses, induces the production of interferon-gamma (IFN-gamma), favors the differentiation of T-helper 1 (Th1) cells and is an important link between innate resistance and adaptive immunity (PubMed:1673147, PubMed:1674604, PubMed:8605935). Mechanistically, exerts its biological effects through a receptor composed of IL12R1 and IL12R2 subunits (PubMed:8943050). Binding to the receptor results in the rapid tyrosine phosphorylation of a number of cellular substrates including the JAK family kinases TYK2 and JAK2 (PubMed:7528775). In turn, recruited STAT4 gets phosphorylated and translocates to the nucleus where it regulates cytokine/growth factor responsive genes (PubMed:7638186). As part of IL-35, plays essential roles in maintaining the immune homeostasis of the liver microenvironment and also functions as an immune-suppressive cytokine (By similarity). Mediates biological events through unconventional receptors composed of IL12RB2 and gp130/IL6ST heterodimers or homodimers (PubMed:22306691). Signaling requires the transcription factors STAT1 and STAT4, which form a unique heterodimer that binds to distinct DNA sites (PubMed:22306691)", "gene_name": "IL12A", "glycan_count": 1, "glycosylation_sites": [ { "position": 93, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 107, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P29459", "name": "Interleukin-12 (IL-12)", "organism": "Homo sapiens", "uniprot_id": "P29459" }, { "function": "Associates with IL12B to form the pro-inflammatory cytokine IL-23 that plays different roles in innate and adaptive immunity (PubMed:11114383). Released by antigen-presenting cells such as dendritic cells or macrophages, binds to a heterodimeric receptor complex composed of IL12RB1 and IL23R to activate JAK2 and TYK2 which then phosphorylate the receptor to form a docking site leading to the phosphorylation of STAT3 and STAT4 (PubMed:29287995, PubMed:32474165, PubMed:33606986). This process leads to activation of several pathways including p38 MAPK or NF-kappa-B and promotes the production of pro-inflammatory cytokines such as interleukin-17A/IL17A (PubMed:12023369). In turn, participates in the early and effective intracellular bacterial clearance (PubMed:32474165). Promotes the expansion and survival of T-helper 17 cells, a CD4-positive helper T-cell subset that produces IL-17, as well as other IL-17-producing cells (PubMed:17676044)", "gene_name": "IL23A", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NPF7", "name": "Interleukin-23 (IL-23)", "organism": "Homo sapiens", "uniprot_id": "Q9NPF7" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P13612/P20701", "name": "Integrin alpha-4 beta-7 (\u03b14\u03b27)", "organism": "", "uniprot_id": "" }, { "function": "Tyrosine kinase of the non-receptor type, involved in the IFN-alpha/beta/gamma signal pathway (PubMed:16239216, PubMed:28111307, PubMed:32750333, PubMed:7615558, PubMed:8232552). Kinase partner for the interleukin (IL)-2 receptor (PubMed:11909529) as well as interleukin (IL)-10 receptor (PubMed:12133952). Kinase partner for the type I interferon receptor IFNAR2 (PubMed:16239216, PubMed:28111307, PubMed:32750333, PubMed:7615558, PubMed:8232552). In response to interferon-binding to IFNAR1-IFNAR2 heterodimer, phosphorylates and activates its binding partner IFNAR2, creating docking sites for STAT proteins (PubMed:7759950). Directly phosphorylates STAT proteins but also activates STAT signaling through the transactivation of other JAK kinases associated with signaling receptors (PubMed:16239216, PubMed:32750333, PubMed:8232552)", "gene_name": "JAK1", "glycan_count": 2, "glycosylation_sites": [], "id": "P23458", "name": "Janus kinase 1 (JAK1)", "organism": "Homo sapiens", "uniprot_id": "P23458" }, { "function": "Alkaline phosphatase that can hydrolyze various phosphate compounds", "gene_name": "ALPP", "glycan_count": 1, "glycosylation_sites": [ { "position": 144, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 271, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P05187", "name": "Alkaline phosphatase", "organism": "Homo sapiens", "uniprot_id": "P05187" }, { "function": "Attaches the virus to host cellular receptor, inducing endocytosis of the virion by using different host proteins including TFRC, GRM2 and ITGB1 (PubMed:30028877, PubMed:31666383, PubMed:36779762). In the endosome, the acidic pH induces conformational changes in the glycoprotein trimer, which trigger fusion between virus and cell membrane. There is convincing in vitro evidence that the muscular form of the nicotinic acetylcholine receptor (nAChR), the neuronal cell adhesion molecule (NCAM), and the p75 neurotrophin receptor (p75NTR) bind glycoprotein and thereby facilitate rabies virus entry into cells (By similarity)", "gene_name": "G", "glycan_count": 0, "glycosylation_sites": [ { "position": 56, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 266, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 338, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P08667", "name": "Rabies virus glycoprotein (G protein)", "organism": "Rabies virus (strain Pasteur vaccins / PV)", "uniprot_id": "P08667" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03437 (H1N1)", "name": "Influenza haemagglutinin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P06463 (HPV16)", "name": "HPV L1 protein", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6YMS4 (DENV2)", "name": "DENV envelope glycoprotein", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8KQF6", "name": "Human factor H binding protein (N. meningitidis)", "organism": "Staphylococcus epidermidis", "uniprot_id": "Q8KQF6" }, { "function": "Acts as a global negative controlling element, employing Fe(2+) as a cofactor to bind the operator of the repressed genes. Regulates the expression of the fbp protein", "gene_name": "fur", "glycan_count": 0, "glycosylation_sites": [], "id": "P0A0S9", "name": "Porin A (N. meningitidis)", "organism": "Neisseria meningitidis serogroup C", "uniprot_id": "P0A0S9" }, { "function": "G-protein coupled estrogen receptor that binds to 17-beta-estradiol (E2) with high affinity, leading to rapid and transient activation of numerous intracellular signaling pathways. Stimulates cAMP production, calcium mobilization and tyrosine kinase Src inducing the release of heparin-bound epidermal growth factor (HB-EGF) and subsequent transactivation of the epidermal growth factor receptor (EGFR), activating downstream signaling pathways such as PI3K/Akt and ERK/MAPK. Mediates pleiotropic functions among others in the cardiovascular, endocrine, reproductive, immune and central nervous systems. Has a role in cardioprotection by reducing cardiac hypertrophy and perivascular fibrosis in a RAMP3-dependent manner. Regulates arterial blood pressure by stimulating vasodilation and reducing vascular smooth muscle and microvascular endothelial cell proliferation. Plays a role in blood glucose homeostasis contributing to the insulin secretion response by pancreatic beta cells. Triggers mitochondrial apoptosis during pachytene spermatocyte differentiation. Stimulates uterine epithelial cell proliferation. Enhances uterine contractility in response to oxytocin. Contributes to thymic atrophy by inducing apoptosis. Attenuates TNF-mediated endothelial expression of leukocyte adhesion molecules. Promotes neuritogenesis in developing hippocampal neurons. Plays a role in acute neuroprotection against NMDA-induced excitotoxic neuronal death. Increases firing activity and intracellular calcium oscillations in luteinizing hormone-releasing hormone (LHRH) neurons. Inhibits early osteoblast proliferation at growth plate during skeletal development. Inhibits mature adipocyte differentiation and lipid accumulation. Involved in the recruitment of beta-arrestin 2 ARRB2 at the plasma membrane in epithelial cells. Also functions as a receptor for aldosterone mediating rapid regulation of vascular contractibility through the PI3K/ERK signaling pathway. Involved in cancer progression regulation. Stimulates cancer-associated fibroblast (CAF) proliferation by a rapid genomic response through the EGFR/ERK transduction pathway. Associated with EGFR, may act as a transcription factor activating growth regulatory genes (c-fos, cyclin D1). Promotes integrin alpha-5/beta-1 and fibronectin (FN) matrix assembly in breast cancer cells", "gene_name": "GPER1", "glycan_count": 0, "glycosylation_sites": [ { "position": 25, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 32, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 44, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q99527", "name": "Gper1 (G protein-coupled estrogen receptor 1)", "organism": "Homo sapiens", "uniprot_id": "Q99527" }, { "function": "Fatty acid synthetase is a multifunctional enzyme that catalyzes the de novo biosynthesis of long-chain saturated fatty acids starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This multifunctional protein contains 7 catalytic activities and a site for the binding of the prosthetic group 4'-phosphopantetheine of the acyl carrier protein ([ACP]) domain", "gene_name": "FASN", "glycan_count": 4, "glycosylation_sites": [], "id": "P49327", "name": "FASN (Fatty acid synthase)", "organism": "Homo sapiens", "uniprot_id": "P49327" }, { "function": "Calcium-dependent acyltransferase that catalyzes the formation of covalent bonds between peptide-bound glutamine and various primary amines, such as gamma-amino group of peptide-bound lysine, or mono- and polyamines, thereby producing cross-linked or aminated proteins, respectively (PubMed:23941696, PubMed:31991788, PubMed:9252372). Involved in many biological processes, such as bone development, angiogenesis, wound healing, cellular differentiation, chromatin modification and apoptosis (PubMed:1683874, PubMed:27270573, PubMed:28198360, PubMed:7935379, PubMed:9252372). Acts as a protein-glutamine gamma-glutamyltransferase by mediating the cross-linking of proteins, such as ACO2, HSPB6, FN1, HMGB1, RAP1GDS1, SLC25A4/ANT1, SPP1 and WDR54 (PubMed:23941696, PubMed:24349085, PubMed:29618516, PubMed:30458214). Under physiological conditions, the protein cross-linking activity is inhibited by GTP; inhibition is relieved by Ca(2+) in response to various stresses (PubMed:18092889, PubMed:7592956, PubMed:7649299). When secreted, catalyzes cross-linking of proteins of the extracellular matrix, such as FN1 and SPP1 resulting in the formation of scaffolds (PubMed:12506096). Plays a key role during apoptosis, both by (1) promoting the cross-linking of cytoskeletal proteins resulting in condensation of the cytoplasm, and by (2) mediating cross-linking proteins of the extracellular matrix, resulting in the irreversible formation of scaffolds that stabilize the integrity of the dying cells before their clearance by phagocytosis, thereby preventing the leakage of harmful intracellular components (PubMed:7935379, PubMed:9252372). In addition to protein cross-linking, can use different monoamine substrates to catalyze a vast array of protein post-translational modifications: mediates aminylation of serotonin, dopamine, noradrenaline or histamine into glutamine residues of target proteins to generate protein serotonylation, dopaminylation, noradrenalinylation or histaminylation, respectively (PubMed:23797785, PubMed:30867594). Mediates protein serotonylation of small GTPases during activation and aggregation of platelets, leading to constitutive activation of these GTPases (By similarity). Plays a key role in chromatin organization by mediating serotonylation and dopaminylation of histone H3 (PubMed:30867594, PubMed:32273471). Catalyzes serotonylation of 'Gln-5' of histone H3 (H3Q5ser) during serotonergic neuron differentiation, thereby facilitating transcription (PubMed:30867594). Acts as a mediator of neurotransmission-independent role of nuclear dopamine in ventral tegmental area (VTA) neurons: catalyzes dopaminylation of 'Gln-5' of histone H3 (H3Q5dop), thereby regulating relapse-related transcriptional plasticity in the reward system (PubMed:32273471). Regulates vein remodeling by mediating serotonylation and subsequent inactivation of ATP2A2/SERCA2 (By similarity). Also acts as a protein deamidase by mediating the side chain deamidation of specific glutamine residues of proteins to glutamate (PubMed:20547769, PubMed:9623982). Catalyzes specific deamidation of protein gliadin, a component of wheat gluten in the diet (PubMed:9623982). May also act as an isopeptidase cleaving the previously formed cross-links (PubMed:26250429, PubMed:27131890). Also able to participate in signaling pathways independently of its acyltransferase activity: acts as a signal transducer in alpha-1 adrenergic receptor-mediated stimulation of phospholipase C-delta (PLCD) activity and is required for coupling alpha-1 adrenergic agonists to the stimulation of phosphoinositide lipid metabolism (PubMed:8943303)", "gene_name": "TGM2", "glycan_count": 1, "glycosylation_sites": [], "id": "P21980", "name": "Tissue transglutaminase", "organism": "Homo sapiens", "uniprot_id": "P21980" }, { "function": "Acts as a negative regulator of the proliferation of normal cells by interacting strongly with CDK4 and CDK6. This inhibits their ability to interact with cyclins D and to phosphorylate the retinoblastoma protein", "gene_name": "CDKN2A", "glycan_count": 1, "glycosylation_sites": [], "id": "P42771", "name": "P16", "organism": "Homo sapiens", "uniprot_id": "P42771" }, { "function": "Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity (PubMed:9003196). Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation (PubMed:9003196). Also plays a role in delivery of iron to cells (By similarity). Mediates iron uptake in capsule cells of the developing kidney (By similarity). Delivery to lysosomes is mediated by the cargo receptor NCOA4 for autophagic degradation and release of iron (PubMed:24695223, PubMed:26436293)", "gene_name": "FTH1", "glycan_count": 3, "glycosylation_sites": [], "id": "P02794", "name": "Ferritin", "organism": "Homo sapiens", "uniprot_id": "P02794" }, { "function": "Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events. During oocyte activation, plays a role in cortical granule reaction in the zona reaction, which contributes to the block to polyspermy (By similarity)", "gene_name": "PLAT", "glycan_count": 111, "glycosylation_sites": [ { "position": 96, "type": "O-linked (Fuc) threonine" }, { "position": 152, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 219, "type": "N-linked (GlcNAc...) asparagine; partial" }, { "position": 483, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P00750", "name": "tissue plasminogen activator (tPA)", "organism": "Homo sapiens", "uniprot_id": "P00750" }, { "function": "Cell surface glycoprotein that plays a role in cell adhesion, intracellular signaling and tumor progression (PubMed:10864933, PubMed:10910050, PubMed:2803308). Mediates homophilic and heterophilic cell adhesion with other carcinoembryonic antigen-related cell adhesion molecules, such as CEACAM6 (PubMed:2803308). Plays a role as an oncogene by promoting tumor progression; induces resistance to anoikis of colorectal carcinoma cells (PubMed:10910050)", "gene_name": "CEACAM5", "glycan_count": 12, "glycosylation_sites": [ { "position": 104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 115, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 152, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 182, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 197, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 204, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 208, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 246, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 256, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 274, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 288, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 292, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 309, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 330, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 351, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 360, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 375, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 432, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 466, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 480, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 508, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 529, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 553, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 560, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 580, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 612, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 650, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 665, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P06731", "name": "carcinoembryonic antigen (CEA)", "organism": "Homo sapiens", "uniprot_id": "P06731" }, { "function": "Hydrolyzes semenogelin-1 thus leading to the liquefaction of the seminal coagulum", "gene_name": "KLK3", "glycan_count": 192, "glycosylation_sites": [ { "position": 69, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P07288", "name": "prostate-specific antigen (PSA)", "organism": "Homo sapiens", "uniprot_id": "P07288" }, { "function": "Apo(a) is the main constituent of lipoprotein(a) (Lp(a)). It has serine proteinase activity and is able of autoproteolysis. Inhibits tissue-type plasminogen activator 1. Lp(a) may be a ligand for megalin/Gp 330", "gene_name": "LPA", "glycan_count": 21, "glycosylation_sites": [ { "position": 61, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 101, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 215, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 329, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 443, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 557, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 671, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 785, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 899, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1013, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1127, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1241, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1347, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1381, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1461, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1575, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1689, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08519", "name": "Lipoprotein(a)", "organism": "Homo sapiens", "uniprot_id": "P08519" }, { "function": "Major non-collagenous bone protein that binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction", "gene_name": "SPP1", "glycan_count": 12, "glycosylation_sites": [ { "position": 134, "type": "O-linked (GalNAc...) threonine" }, { "position": 138, "type": "O-linked (GalNAc...) threonine" }, { "position": 143, "type": "O-linked (GalNAc...) threonine" }, { "position": 147, "type": "O-linked (GalNAc...) threonine" }, { "position": 152, "type": "O-linked (GalNAc...) threonine" }, { "position": 234, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 308, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" } ], "id": "P10451", "name": "Secreted phosphoprotein 1 (SPP1) / Osteopontin (OPN)", "organism": "Homo sapiens", "uniprot_id": "P10451" }, { "function": "Pore-forming protein that plays a key role in granzyme-mediated programmed cell death, and in defense against virus-infected or neoplastic cells (PubMed:20889983, PubMed:21037563, PubMed:24558045, PubMed:9058810, PubMed:9164947). Plays an important role in killing other cells that are recognized as non-self by the immune system, e.g. in transplant rejection or some forms of autoimmune disease (PubMed:9058810). Can insert into the membrane of target cells in its calcium-bound form, oligomerize and form large pores (PubMed:20889983, PubMed:21037563). Promotes cytolysis and apoptosis of target cells by mediating the passage and uptake of cytotoxic granzymes (PubMed:20038786, PubMed:20225066, PubMed:24558045, PubMed:32299851). Facilitates the delivery of cationic cargo protein, while anionic or neural proteins are not delivered efficiently (PubMed:24558045). Perforin pores allow the release of mature caspase-7 (CASP7) into the extracellular milieu (By similarity)", "gene_name": "PRF1", "glycan_count": 4, "glycosylation_sites": [ { "position": 205, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 549, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P14222", "name": "Perforin-1 (PRF1)", "organism": "Homo sapiens", "uniprot_id": "P14222" }, { "function": "Transcriptional coactivator for steroid receptors and nuclear receptors (PubMed:10713165, PubMed:20005308, PubMed:21376232, PubMed:28363985, PubMed:32433991). Greatly increases the transcriptional activity of PPARG and thyroid hormone receptor on the uncoupling protein promoter (PubMed:10713165, PubMed:20005308, PubMed:21376232). Can regulate key mitochondrial genes that contribute to the program of adaptive thermogenesis (PubMed:10713165, PubMed:20005308, PubMed:21376232). Plays an essential role in metabolic reprogramming in response to dietary availability through coordination of the expression of a wide array of genes involved in glucose and fatty acid metabolism (PubMed:10713165, PubMed:20005308, PubMed:21376232). Acts as a key regulator of gluconeogenesis: stimulates hepatic gluconeogenesis by increasing the expression of gluconeogenic enzymes, and acting together with FOXO1 to promote the fasting gluconeogenic program (PubMed:16753578, PubMed:23142079). Induces the expression of PERM1 in the skeletal muscle in an ESRRA-dependent manner (PubMed:23836911). Also involved in the integration of the circadian rhythms and energy metabolism (By similarity). Required for oscillatory expression of clock genes, such as BMAL1 and NR1D1, through the coactivation of RORA and RORC, and metabolic genes, such as PDK4 and PEPCK (By similarity)", "gene_name": "PPARGC1A", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9UBK2", "name": "PGC-1\u03b1", "organism": "Homo sapiens", "uniprot_id": "Q9UBK2" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "F1P6S5", "name": "Complement C1s", "organism": "", "uniprot_id": "F1P6S5" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "E2R0N6", "name": "Complement C7", "organism": "", "uniprot_id": "E2R0N6" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "E2R0G5", "name": "Fibrinogen alpha chain", "organism": "", "uniprot_id": "E2R0G5" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "E2R0G7", "name": "Fibrinogen gamma chain", "organism": "", "uniprot_id": "E2R0G7" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "E2R0G9", "name": "Coagulation factor III (Tissue Factor)", "organism": "", "uniprot_id": "E2R0G9" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "E2R0H0", "name": "Coagulation factor VII", "organism": "", "uniprot_id": "E2R0H0" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "E2R0H1", "name": "Coagulation factor XII", "organism": "", "uniprot_id": "E2R0H1" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "E2R0H2", "name": "Interleukin-2 receptor subunit beta", "organism": "", "uniprot_id": "E2R0H2" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "E2R0H3", "name": "Protein kinase C substrate 80K-H (PRKCSH)", "organism": "", "uniprot_id": "E2R0H3" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "E2R0H4", "name": "E3 ubiquitin-protein ligase Mdm2", "organism": "", "uniprot_id": "E2R0H4" }, { "function": "", "gene_name": "RNF148", "glycan_count": 0, "glycosylation_sites": [ { "position": 43, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8N7C7", "name": "GALNT9", "organism": "Homo sapiens", "uniprot_id": "Q8N7C7" }, { "function": "Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form (PubMed:11063746, PubMed:19478087). It is involved in the negative regulation of the angiotensin-activated signaling pathway (PubMed:28784619). Plays a role in the regulation of blood pressure in response to signaling via G protein-coupled receptors and GNAQ. Plays a role in regulating the constriction and relaxation of vascular smooth muscle (By similarity). Binds EIF2B5 and blocks its activity, thereby inhibiting the translation of mRNA into protein (PubMed:19736320)", "gene_name": "RGS2", "glycan_count": 0, "glycosylation_sites": [], "id": "P41220", "name": "RGS2", "organism": "Homo sapiens", "uniprot_id": "P41220" }, { "function": "May play a role in late hair differentiation", "gene_name": "KRT40", "glycan_count": 1, "glycosylation_sites": [], "id": "Q6A162", "name": "KRT80", "organism": "Homo sapiens", "uniprot_id": "Q6A162" }, { "function": "Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane", "gene_name": "SPRR2B", "glycan_count": 0, "glycosylation_sites": [], "id": "P35325", "name": "SPRR1A", "organism": "Homo sapiens", "uniprot_id": "P35325" }, { "function": "E3 ubiquitin-protein ligase (PubMed:22529100). May facilitate apoptosis by inhibiting APC/C-Cdh1-mediated poly-ubiquitination and subsequent proteasome-mediated degradation of the pro-apoptotic protein MOAP1 (PubMed:19100260, PubMed:22529100). Regulates the G1/S transition of the cell cycle and DNA damage-induced G2 arrest by stabilizing CDKN1A/p21 (PubMed:23213251). Positively regulates CDKN1A/p21 stability by competing with DTL for CDKN1A/p21 binding, therefore disrupting DCX(DTL) E3 ubiquitin ligase complex-mediated CDKN1A/p21 ubiquitination and degradation (PubMed:23213251)", "gene_name": "TRIM39", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9HCM9", "name": "TRIM39", "organism": "Homo sapiens", "uniprot_id": "Q9HCM9" }, { "function": "Involved in the biogenesis of the 60S ribosomal subunit (PubMed:32669547). Acts as a TP53 repressor, preventing TP53 stabilization and cell cycle arrest (PubMed:20308539)", "gene_name": "GTPBP4", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9BZE4", "name": "GTPBP10", "organism": "Homo sapiens", "uniprot_id": "Q9BZE4" }, { "function": "Involved in neural development, regulating the establishment of proper connectivity within the nervous system. Plays a role in the establishment of the anterior-posterior axis during gastrulation. Regulates the differentiation and cellular process formation of oligodendrocytes and myelination of small-diameter axons in the central nervous system (CNS) (PubMed:26188006). Promotes activation of focal adhesion kinase. May function as a cellular signal transducer (By similarity)", "gene_name": "TENM4", "glycan_count": 11, "glycosylation_sites": [ { "position": 467, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 940, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1259, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1609, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1705, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1741, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1799, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1884, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1985, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2188, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2328, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2646, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6N022", "name": "TENM4", "organism": "Homo sapiens", "uniprot_id": "Q6N022" }, { "function": "Transcription regulator of hematopoietic cell differentiation (PubMed:17934067). Binds gamma-satellite DNA (PubMed:17135265, PubMed:19141594). Plays a role in the development of lymphocytes, B- and T-cells. Binds and activates the enhancer (delta-A element) of the CD3-delta gene. Repressor of the TDT (fikzfterminal deoxynucleotidyltransferase) gene during thymocyte differentiation. Regulates transcription through association with both HDAC-dependent and HDAC-independent complexes. Targets the 2 chromatin-remodeling complexes, NuRD and BAF (SWI/SNF), in a single complex (PYR complex), to the beta-globin locus in adult erythrocytes. Increases normal apoptosis in adult erythroid cells. Confers early temporal competence to retinal progenitor cells (RPCs) (By similarity). Function is isoform-specific and is modulated by dominant-negative inactive isoforms (PubMed:17135265, PubMed:17934067)", "gene_name": "IKZF1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q13422", "name": "IK", "organism": "Homo sapiens", "uniprot_id": "Q13422" }, { "function": "Physiological suppressor of IKK-epsilon and TBK1 that plays an inhibitory role in virus- and TLR3-triggered IRF3. Inhibits TLR3-mediated activation of interferon-stimulated response elements (ISRE) and the IFN-beta promoter. May act by disrupting the interactions of IKBKE or TBK1 with TICAM1/TRIF, IRF3 and RIGI. Does not inhibit NF-kappa-B activation pathways (PubMed:16281057). Associates with the striatin-interacting phosphatase and kinase (STRIPAK) core complex, forming the extended (SIKE1:SLMAP)STRIPAK complex (PubMed:30622739). The (SIKE1:SLMAP)STRIPAK complex dephosphorylates STK3 leading to the inhibition of Hippo signaling and the control of cell growth (PubMed:30622739)", "gene_name": "SIKE1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9BRV8", "name": "SLC30A7", "organism": "Homo sapiens", "uniprot_id": "Q9BRV8" }, { "function": "Attaches the virus to host LDL receptors, inducing clathrin-dependent endocytosis of the virion (PubMed:20941355, PubMed:23589850). In the endosome, the acidic pH induces conformational changes in the glycoprotein trimer, which trigger fusion between virus and endosomal membrane (PubMed:20921141, PubMed:22383886)", "gene_name": "G", "glycan_count": 0, "glycosylation_sites": [ { "position": 179, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 336, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P03522", "name": "VSV-G", "organism": "Vesicular stomatitis Indiana virus (strain San Juan)", "uniprot_id": "P03522" }, { "function": "Functions as a master transcriptional regulator of the adaptive response to hypoxia (PubMed:11292861, PubMed:11566883, PubMed:15465032, PubMed:16973622, PubMed:17610843, PubMed:18658046, PubMed:20624928, PubMed:22009797, PubMed:30125331, PubMed:9887100). Under hypoxic conditions, activates the transcription of over 40 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia (PubMed:11292861, PubMed:11566883, PubMed:15465032, PubMed:16973622, PubMed:17610843, PubMed:20624928, PubMed:22009797, PubMed:30125331, PubMed:9887100). Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease (PubMed:22009797). Heterodimerizes with ARNT; heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters (By similarity). Activation requires recruitment of transcriptional coactivators such as CREBBP and EP300 (PubMed:16543236, PubMed:9887100). Activity is enhanced by interaction with NCOA1 and/or NCOA2 (PubMed:10594042). Interaction with redox regulatory protein APEX1 seems to activate CTAD and potentiates activation by NCOA1 and CREBBP (PubMed:10202154, PubMed:10594042). Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia (PubMed:19528298)", "gene_name": "HIF1A", "glycan_count": 2, "glycosylation_sites": [ { "position": 18, "type": "(Microbial infection) N-beta-linked (GlcNAc) arginine" } ], "id": "Q16665", "name": "HIF-1\u03b1", "organism": "Homo sapiens", "uniprot_id": "Q16665" }, { "function": "Potential calcium-dependent cell-adhesion protein", "gene_name": "PCDH9", "glycan_count": 22, "glycosylation_sites": [ { "position": 48, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 148, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 306, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 307, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 347, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 368, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 450, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 511, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 630, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 681, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 734, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 754, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 775, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 780, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9HC56", "name": "MUC7", "organism": "Homo sapiens", "uniprot_id": "Q9HC56" }, { "function": "This is the major myelin protein from the central nervous system. It plays an important role in the formation or maintenance of the multilamellar structure of myelin", "gene_name": "PLP1", "glycan_count": 1, "glycosylation_sites": [], "id": "P60201", "name": "Proteolipid Protein (PLP)", "organism": "Homo sapiens", "uniprot_id": "P60201" }, { "function": "Tyrosine-protein kinase that acts as a cell-surface receptor for PDGFA, PDGFB and PDGFC and plays an essential role in the regulation of embryonic development, cell proliferation, survival and chemotaxis. Depending on the context, promotes or inhibits cell proliferation and cell migration. Plays an important role in the differentiation of bone marrow-derived mesenchymal stem cells. Required for normal skeleton development and cephalic closure during embryonic development. Required for normal development of the mucosa lining the gastrointestinal tract, and for recruitment of mesenchymal cells and normal development of intestinal villi. Plays a role in cell migration and chemotaxis in wound healing. Plays a role in platelet activation, secretion of agonists from platelet granules, and in thrombin-induced platelet aggregation. Binding of its cognate ligands - homodimeric PDGFA, homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFC -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PIK3R1, PLCG1, and PTPN11. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the activation of protein kinase C. Phosphorylates PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and thereby mediates activation of the AKT1 signaling pathway. Mediates activation of HRAS and of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3 and STAT5A and/or STAT5B. Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor", "gene_name": "PDGFRA", "glycan_count": 4, "glycosylation_sites": [ { "position": 42, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 76, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 103, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 179, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 353, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 359, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 458, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 468, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P16234", "name": "Platelet-Derived Growth Factor Receptor Alpha (PDGFRA)", "organism": "Homo sapiens", "uniprot_id": "P16234" }, { "function": "Hydrolyzes the galactose ester bonds of glycolipids such as galactosylceramide and galactosylsphingosine (PubMed:8281145, PubMed:8399327). Enzyme with very low activity responsible for the lysosomal catabolism of galactosylceramide, a major lipid in myelin, kidney and epithelial cells of small intestine and colon (PubMed:8281145, PubMed:8399327)", "gene_name": "GALC", "glycan_count": 5, "glycosylation_sites": [ { "position": 143, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 379, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 403, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 556, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 559, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 602, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P54803", "name": "Galactocerebrosidase (GALC)", "organism": "Homo sapiens", "uniprot_id": "P54803" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P62988", "name": "Ubiquitin", "organism": "", "uniprot_id": "P62988" }, { "function": "Catalyzes the reversible isomerization of alpha-D-glucose 1-phosphate to alpha-D-glucose 6-phosphate (PubMed:15378030, PubMed:25288802). The mechanism proceeds via the intermediate compound alpha-D-glucose 1,6-bisphosphate (Probable) (PubMed:25288802). This enzyme participates in both the breakdown and synthesis of glucose (PubMed:17924679, PubMed:25288802)", "gene_name": "PGM1", "glycan_count": 1, "glycosylation_sites": [], "id": "P36871", "name": "PGM1 (Phosphoglucomutase-1)", "organism": "Homo sapiens", "uniprot_id": "P36871" }, { "function": "Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone", "gene_name": "NDUFA12", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UI09", "name": "NDUFA13", "organism": "Homo sapiens", "uniprot_id": "Q9UI09" }, { "function": "May function in the secretion of milk-fat droplets. May act as a specific membrane-associated receptor for the association of cytoplasmic droplets with the apical plasma membrane (By similarity). Inhibits the proliferation of CD4 and CD8 T-cells activated by anti-CD3 antibodies, T-cell metabolism and IL2 and IFNG secretion (By similarity)", "gene_name": "BTN1A1", "glycan_count": 44, "glycosylation_sites": [ { "position": 55, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 215, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13410", "name": "Butyrophilin subfamily 1 member A1 (BTN1A1)", "organism": "Homo sapiens", "uniprot_id": "Q13410" }, { "function": "Phosphorylates both NADH and NAD(+), with a twofold preference for NADH. Anti-oxidant factor and key source of the cellular reductant NADPH", "gene_name": "POS5", "glycan_count": 0, "glycosylation_sites": [], "id": "Q06892", "name": "Tyrosine-protein kinase receptor Tie-1 (TIE-1)", "organism": "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "uniprot_id": "Q06892" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O95080/O15455", "name": "MHC class I polypeptide-related sequence B_A (MICB_MICA)", "organism": "", "uniprot_id": "" }, { "function": "Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This CSF induces granulocytes", "gene_name": "CSF3", "glycan_count": 0, "glycosylation_sites": [ { "position": 166, "type": "O-linked (GalNAc...) threonine" } ], "id": "P09919", "name": "Granulocyte colony-stimulating factor (G-CSF)", "organism": "Homo sapiens", "uniprot_id": "P09919" }, { "function": "Filament-forming cytoskeletal GTPase. May play a role in cytokinesis (Potential). May play a role in the cytoarchitecture of neurons, including dendritic arborization and dendritic spines, and in GABAergic synaptic connectivity (By similarity). During Listeria monocytogenes infection, not required for the bacterial entry process, but restricts its efficacy", "gene_name": "SEPTIN11", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NVA2", "name": "Septin-8", "organism": "Homo sapiens", "uniprot_id": "Q9NVA2" }, { "function": "May be involved in several stages of intracellular trafficking", "gene_name": "SNX25", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H3E2", "name": "Tumor necrosis factor alpha-induced protein 8 (TNFAIP8)", "organism": "Homo sapiens", "uniprot_id": "Q9H3E2" }, { "function": "May inhibit cardiomyocyte growth", "gene_name": "PI16", "glycan_count": 6, "glycosylation_sites": [ { "position": 114, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 403, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 409, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6UXB8", "name": "C-X-C motif chemokine 17", "organism": "Homo sapiens", "uniprot_id": "Q6UXB8" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Z1S4", "name": "\u03b1-sarcoglycan", "organism": "", "uniprot_id": "Q9Z1S4" }, { "function": "Transcriptional regulator implicated in neuronal determination. Mediates calcium-dependent transcription activation by binding to E box-containing promoter. Critical factor essential for the repression of the genetic program for neuronal differentiation; prevents the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. Induces transcription of ZEB1, which in turn represses neuronal differentiation by down-regulating REST expression. Plays a role in the establishment and maturation of thalamocortical connections; involved in the segregation of thalamic afferents into distinct barrel domains within layer VI of the somatosensory cortex. Involved in the development of the cerebellar and hippocampal granular neurons, neurons in the basolateral nucleus of amygdala and the hypothalamic-pituitary axis. Associates with chromatin to the DPYSL3 E box-containing promoter", "gene_name": "Neurod2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q62414", "name": "utrophin", "organism": "Mus musculus", "uniprot_id": "Q62414" }, { "function": "Integrin alpha-6/beta-1 (ITGA6:ITGB1) is a receptor for laminin on platelets (PubMed:8081870). Integrin alpha-6/beta-1 (ITGA6:ITGB1) is present in oocytes and is involved in sperm-egg fusion (PubMed:10634791). Integrin alpha-6/beta-4 (ITGA6:ITGB4) is a receptor for laminin in epithelial cells and it plays a critical structural role in the hemidesmosome (PubMed:8673141). ITGA6:ITGB4 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling (By similarity). ITGA6:ITGB4 binds to IGF1 and this binding is essential for IGF1 signaling (By similarity). ITGA6:ITGB4 binds to IGF2 and this binding is essential for IGF2 signaling (By similarity)", "gene_name": "Itga6", "glycan_count": 11, "glycosylation_sites": [ { "position": 78, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 223, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 284, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 370, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 731, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 746, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 927, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 958, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q61739", "name": "integrin \u03b17B", "organism": "Mus musculus", "uniprot_id": "Q61739" }, { "function": "Integrin alpha-7/beta-1 is the primary laminin receptor on skeletal myoblasts and adult myofibers. During myogenic differentiation, it may induce changes in the shape and mobility of myoblasts, and facilitate their localization at laminin-rich sites of secondary fiber formation. Involved in the maintenance of the myofibers cytoarchitecture as well as for their anchorage, viability and functional integrity. Mice carrying a ITGA7 null allele are viable and fertile, but show progressive muscular dystrophy starting soon after birth, but with a distinct variability in different muscle types. Required to promote contractile phenotype acquisition in differentiated airway smooth muscle (ASM) cells. Acts as a Schwann cell receptor for laminin-2. Acts as a receptor of COMP and mediates its effect on vascular smooth muscle cells (VSMCs) maturation (By similarity)", "gene_name": "Itga7", "glycan_count": 13, "glycosylation_sites": [ { "position": 86, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 784, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 988, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1023, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1043, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q61738", "name": "integrin \u03b21D", "organism": "Mus musculus", "uniprot_id": "Q61738" }, { "function": "Cytosolic prostaglandin synthase that catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2). Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes. Facilitates HIF alpha proteins hydroxylation via interaction with EGLN1/PHD2, leading to recruit EGLN1/PHD2 to the HSP90 pathway", "gene_name": "Ptges3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9R0Q7", "name": "dysferlin", "organism": "Mus musculus", "uniprot_id": "Q9R0Q7" }, { "function": "Able to phosphorylate several exogenous substrates and to undergo autophosphorylation (PubMed:10421840). Negatively regulates cilium length in a cAMP and mTORC1 signaling-dependent manner (PubMed:25243405)", "gene_name": "Mok", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9WVS4", "name": "p38 MAPK", "organism": "Mus musculus", "uniprot_id": "Q9WVS4" }, { "function": "Key enzyme of the Krebs tricarboxylic acid cycle which catalyzes the synthesis of citrate from acetyl coenzyme A and oxaloacetate", "gene_name": "Cs", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9CZU6", "name": "Citrate Synthase", "organism": "Mus musculus", "uniprot_id": "Q9CZU6" }, { "function": "", "gene_name": "Farsb", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9CZU5", "name": "Mitochondrial Complex II (SDHB)", "organism": "Mus musculus", "uniprot_id": "Q9CZU5" }, { "function": "Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward non-glycosylated peptides such as Muc5AC, Muc1a and EA2, and no detectable activity with Muc2 and Muc7. Displays enzymatic activity toward the Gal-NAc-Muc5AC glycopeptide, but no detectable activity to mono-GalNAc-glycosylated Muc1a, Muc2, Muc7 and EA2. May play an important role in the initial step of mucin-type oligosaccharide biosynthesis in digestive organs", "gene_name": "GALNT12", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8IXK2", "name": "GalNAc-T14", "organism": "Homo sapiens", "uniprot_id": "Q8IXK2" }, { "function": "Serves to link two monomer units of either IgM or IgA. In the case of IgM, the J chain-joined dimer is a nucleating unit for the IgM pentamer, and in the case of IgA it induces dimers and/or larger polymers. It also helps to bind these immunoglobulins to secretory component", "gene_name": "JCHAIN", "glycan_count": 165, "glycosylation_sites": [ { "position": 71, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P01591", "name": "J-Chain", "organism": "Homo sapiens", "uniprot_id": "P01591" }, { "function": "Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity", "gene_name": "TNNI3", "glycan_count": 1, "glycosylation_sites": [], "id": "P19429", "name": "Cardiac Troponin I", "organism": "Homo sapiens", "uniprot_id": "P19429" }, { "function": "Plasmin dissolves the fibrin of blood clots and acts as a proteolytic factor in a variety of other processes including embryonic development, tissue remodeling, tumor invasion, and inflammation. In ovulation, weakens the walls of the Graafian follicle. It activates the urokinase-type plasminogen activator, collagenases and several complement zymogens, such as C1, C4 and C5 (PubMed:6447255). Cleavage of fibronectin and laminin leads to cell detachment and apoptosis. Also cleaves fibrin, thrombospondin and von Willebrand factor. Its role in tissue remodeling and tumor invasion may be modulated by CSPG4. Binds to cells", "gene_name": "PLG", "glycan_count": 67, "glycosylation_sites": [ { "position": 268, "type": "O-linked (GalNAc...) serine" }, { "position": 308, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 365, "type": "O-linked (GalNAc...) threonine" } ], "id": "P00747", "name": "Plasmin", "organism": "Homo sapiens", "uniprot_id": "P00747" }, { "function": "Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, chaperone-mediated autophagy, activation of proteolysis of misfolded proteins, formation and dissociation of protein complexes, and antigen presentation. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation (PubMed:21148293, PubMed:21150129, PubMed:23018488, PubMed:24732912, PubMed:27916661, PubMed:2799391, PubMed:36586411). This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones (PubMed:12526792, PubMed:21148293, PubMed:21150129, PubMed:23018488, PubMed:24732912, PubMed:27916661). The co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation (PubMed:12526792, PubMed:21148293, PubMed:21150129, PubMed:23018488, PubMed:24732912, PubMed:27916661). The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 (PubMed:24121476, PubMed:24318877, PubMed:26865365, PubMed:27474739). Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70 (PubMed:12526792). Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:10722728, PubMed:11276205). Substrate recognition component in chaperone-mediated autophagy (CMA), a selective protein degradation process that mediates degradation of proteins with a -KFERQ motif: HSPA8/HSC70 specifically recognizes and binds cytosolic proteins bearing a -KFERQ motif and promotes their recruitment to the surface of the lysosome where they bind to lysosomal protein LAMP2 (PubMed:11559757, PubMed:2799391, PubMed:36586411). KFERQ motif-containing proteins are eventually transported into the lysosomal lumen where they are degraded (PubMed:11559757, PubMed:2799391, PubMed:36586411). In conjunction with LAMP2, facilitates MHC class II presentation of cytoplasmic antigens by guiding antigens to the lysosomal membrane for interaction with LAMP2 which then elicits MHC class II presentation of peptides to the cell membrane (PubMed:15894275). Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1 (PubMed:23990462). It is recruited to clathrin-coated vesicles through its interaction with DNAJC6 leading to activation of HSPA8/HSC70 ATPase activity and therefore uncoating of clathrin-coated vesicles (By similarity)", "gene_name": "HSPA8", "glycan_count": 4, "glycosylation_sites": [], "id": "P11142", "name": "Heat shock cognate 71 kDa protein (Hsc70)", "organism": "Homo sapiens", "uniprot_id": "P11142" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01233", "name": "Human chorionic gonadotropin (hCG)", "organism": "", "uniprot_id": "P01233" }, { "function": "SRF is a transcription factor that binds to the serum response element (SRE), a short sequence of dyad symmetry located 300 bp to the 5' of the site of transcription initiation of some genes (such as FOS). Together with MRTFA transcription coactivator, controls expression of genes regulating the cytoskeleton during development, morphogenesis and cell migration. The SRF-MRTFA complex activity responds to Rho GTPase-induced changes in cellular globular actin (G-actin) concentration, thereby coupling cytoskeletal gene expression to cytoskeletal dynamics. Required for cardiac differentiation and maturation", "gene_name": "SRF", "glycan_count": 2, "glycosylation_sites": [ { "position": 277, "type": "O-linked (GlcNAc) serine" }, { "position": 307, "type": "O-linked (GlcNAc) serine" }, { "position": 309, "type": "O-linked (GlcNAc) serine" }, { "position": 316, "type": "O-linked (GlcNAc) serine" }, { "position": 383, "type": "O-linked (GlcNAc) serine" } ], "id": "P11831", "name": "Serum response factor", "organism": "Homo sapiens", "uniprot_id": "P11831" }, { "function": "Essential antioxidant peroxidase that directly reduces phospholipid hydroperoxide even if they are incorporated in membranes and lipoproteins (By similarity). Can also reduce cholesterol hydroperoxide and thymine hydroperoxide (By similarity). Plays a key role in protecting cells from oxidative damage by preventing membrane lipid peroxidation (By similarity). Required to prevent cells from ferroptosis, a non-apoptotic cell death resulting from an iron-dependent accumulation of lipid reactive oxygen species (PubMed:24439385). The presence of selenocysteine (Sec) versus Cys at the active site is essential for life: it provides resistance to overoxidation and prevents cells against ferroptosis (By similarity). The presence of Sec at the active site is also essential for the survival of a specific type of parvalbumin-positive interneurons, thereby preventing against fatal epileptic seizures (By similarity). May be required to protect cells from the toxicity of ingested lipid hydroperoxides (By similarity). Required for normal sperm development and male fertility (By similarity). Essential for maturation and survival of photoreceptor cells (By similarity). Plays a role in a primary T-cell response to viral and parasitic infection by protecting T-cells from ferroptosis and by supporting T-cell expansion (By similarity). Plays a role of glutathione peroxidase in platelets in the arachidonic acid metabolism (PubMed:11115402). Reduces hydroperoxy ester lipids formed by a 15-lipoxygenase that may play a role as down-regulator of the cellular 15-lipoxygenase pathway (By similarity). Can reduce fatty acid-derived hydroperoxides (PubMed:11115402, PubMed:36608588). Can also reduce small soluble hydroperoxides such as H2O2, cumene hydroperoxide and tert-butyl hydroperoxide (PubMed:17630701, PubMed:36608588)", "gene_name": "GPX4", "glycan_count": 1, "glycosylation_sites": [], "id": "P36969", "name": "Glutathione peroxidase 4 (GPX4)", "organism": "Homo sapiens", "uniprot_id": "P36969" }, { "function": "Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation", "gene_name": "UGGT1", "glycan_count": 30, "glycosylation_sites": [ { "position": 536, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1228, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NYU2", "name": "UGGT1", "organism": "Homo sapiens", "uniprot_id": "Q9NYU2" }, { "function": "In the context of N-glycan degradation, cleaves the distal alpha 1,2-linked glucose residue from the Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor in a highly specific manner", "gene_name": "MOGS", "glycan_count": 8, "glycosylation_sites": [ { "position": 657, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13724", "name": "MOGS", "organism": "Homo sapiens", "uniprot_id": "Q13724" }, { "function": "Catalytic subunit of glucosidase II that cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins (PubMed:10929008). Required for PKD1/Polycystin-1 and PKD2/Polycystin-2 maturation and localization to the cell surface and cilia (PubMed:27259053)", "gene_name": "GANAB", "glycan_count": 7, "glycosylation_sites": [ { "position": 97, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q14697", "name": "GANAB", "organism": "Homo sapiens", "uniprot_id": "Q14697" }, { "function": "Involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2), but at high enzyme concentrations, as found in the ER quality control compartment (ERQC), it further trims the carbohydrates to Man(5-6)GlcNAc(2)", "gene_name": "MAN1B1", "glycan_count": 4, "glycosylation_sites": [], "id": "Q9UKM7", "name": "MAN1B1", "organism": "Homo sapiens", "uniprot_id": "Q9UKM7" }, { "function": "", "gene_name": "STK3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8NBU1", "name": "EDEM3", "organism": "Homo sapiens", "uniprot_id": "Q8NBU1" }, { "function": "Calcium-binding protein that interacts with newly synthesized monoglucosylated glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor-mediated endocytosis at the synapse", "gene_name": "CANX", "glycan_count": 5, "glycosylation_sites": [], "id": "P27824", "name": "Calnexin (CNX)", "organism": "Homo sapiens", "uniprot_id": "P27824" }, { "function": "Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (PubMed:7876246). Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export (PubMed:11149926). Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity). Present in the cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation and might participate in the block to polyspermy (By similarity)", "gene_name": "CALR", "glycan_count": 39, "glycosylation_sites": [ { "position": 344, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P27797", "name": "Calreticulin (CRT)", "organism": "Homo sapiens", "uniprot_id": "P27797" }, { "function": "A SLe(x)-type proteoglycan, which through high affinity, calcium-dependent interactions with E-, P- and L-selectins, mediates rapid rolling of leukocytes over vascular surfaces during the initial steps in inflammation. Critical for the initial leukocyte capture", "gene_name": "SELPLG", "glycan_count": 11, "glycosylation_sites": [ { "position": 57, "type": "O-linked (GalNAc...) threonine" }, { "position": 65, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 111, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 302, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q14242", "name": "PSGL-1", "organism": "Homo sapiens", "uniprot_id": "Q14242" }, { "function": "Predominant cell surface sialoprotein of leukocytes which regulates multiple T-cell functions, including T-cell activation, proliferation, differentiation, trafficking and migration. Positively regulates T-cell trafficking to lymph-nodes via its association with ERM proteins (EZR, RDX and MSN) (By similarity). Negatively regulates Th2 cell differentiation and predisposes the differentiation of T-cells towards a Th1 lineage commitment. Promotes the expression of IFN-gamma by T-cells during T-cell receptor (TCR) activation of naive cells and induces the expression of IFN-gamma by CD4(+) T-cells and to a lesser extent by CD8(+) T-cells (PubMed:18036228). Plays a role in preparing T-cells for cytokine sensing and differentiation into effector cells by inducing the expression of cytokine receptors IFNGR and IL4R, promoting IFNGR and IL4R signaling and by mediating the clustering of IFNGR with TCR (PubMed:24328034). Acts as a major E-selectin ligand responsible for Th17 cell rolling on activated vasculature and recruitment during inflammation. Mediates Th17 cells, but not Th1 cells, adhesion to E-selectin. Acts as a T-cell counter-receptor for SIGLEC1 (By similarity)", "gene_name": "SPN", "glycan_count": 16, "glycosylation_sites": [ { "position": 21, "type": "O-linked (GalNAc...) threonine" }, { "position": 22, "type": "O-linked (GalNAc...) threonine" }, { "position": 26, "type": "O-linked (GalNAc...) threonine" }, { "position": 28, "type": "O-linked (GalNAc...) threonine" }, { "position": 29, "type": "O-linked (GalNAc...) serine" }, { "position": 35, "type": "O-linked (GalNAc...) serine" }, { "position": 36, "type": "O-linked (GalNAc...) threonine" }, { "position": 37, "type": "O-linked (GalNAc...) serine" }, { "position": 41, "type": "O-linked (GalNAc...) serine" }, { "position": 42, "type": "O-linked (GalNAc...) serine" }, { "position": 46, "type": "O-linked (GalNAc...) threonine" }, { "position": 47, "type": "O-linked (GalNAc...) threonine" }, { "position": 48, "type": "O-linked (GalNAc...) serine" }, { "position": 50, "type": "O-linked (GalNAc...) threonine" }, { "position": 58, "type": "O-linked (GalNAc...) threonine" }, { "position": 69, "type": "O-linked (GalNAc...) threonine" }, { "position": 99, "type": "O-linked (GalNAc...) serine" }, { "position": 103, "type": "O-linked (GalNAc...) serine" }, { "position": 109, "type": "O-linked (GalNAc...) threonine" }, { "position": 113, "type": "O-linked (GalNAc...) threonine" }, { "position": 114, "type": "O-linked (GalNAc...) serine" }, { "position": 136, "type": "O-linked (GalNAc...) threonine" }, { "position": 137, "type": "O-linked (GalNAc...) threonine" }, { "position": 173, "type": "O-linked (GalNAc...) threonine" }, { "position": 178, "type": "O-linked (GalNAc...) threonine" }, { "position": 239, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P16150", "name": "CD43 (Sialophorin)", "organism": "Homo sapiens", "uniprot_id": "P16150" }, { "function": "Coreceptor for SEMA3A, SEMA3C, SEMA3F and SEMA6D. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm. Acts as coreceptor of TREM2 for SEMA6D in dendritic cells and is involved in the generation of immune responses and skeletal homeostasis", "gene_name": "PLXNA1", "glycan_count": 9, "glycosylation_sites": [ { "position": 77, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 660, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 672, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 701, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1043, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1187, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1212, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UIW2", "name": "Heparanase (HPSE)", "organism": "Homo sapiens", "uniprot_id": "Q9UIW2" }, { "function": "Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates (PubMed:16214399, PubMed:18768481, PubMed:28420705, PubMed:32433610, PubMed:32433611, PubMed:9756920). Highly expressed in epithelial cells of the small intestine and its activity is essential for the absorption of dietary fats (PubMed:18768481). In liver, plays a role in esterifying exogenous fatty acids to glycerol, and is required to synthesize fat for storage (PubMed:16214399). Also present in female mammary glands, where it produces fat in the milk (By similarity). May be involved in VLDL (very low density lipoprotein) assembly (PubMed:18768481). In contrast to DGAT2 it is not essential for survival (By similarity). Functions as the major acyl-CoA retinol acyltransferase (ARAT) in the skin, where it acts to maintain retinoid homeostasis and prevent retinoid toxicity leading to skin and hair disorders (PubMed:16214399). Exhibits additional acyltransferase activities, includin acyl CoA:monoacylglycerol acyltransferase (MGAT), wax monoester and wax diester synthases (By similarity). Also able to use 1-monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG) (PubMed:28420705)", "gene_name": "DGAT1", "glycan_count": 0, "glycosylation_sites": [], "id": "O75907", "name": "UGCG (GlcCer synthase)", "organism": "Homo sapiens", "uniprot_id": "O75907" }, { "function": "Oxidoreductase that catalyzes the last step of the cholesterol synthesis pathway, which transforms cholesta-5,7-dien-3beta-ol (7-dehydrocholesterol,7-DHC) into cholesterol by reducing the C7-C8 double bond of its sterol core (PubMed:25637936, PubMed:38297129, PubMed:38297130, PubMed:9465114, PubMed:9634533). Can also metabolize cholesta-5,7,24-trien-3beta-ol (7-dehydrodemosterol, 7-DHD) to desmosterol, which is then metabolized by the Delta(24)-sterol reductase (DHCR24) to cholesterol (By similarity). Modulates ferroptosis (a form of regulated cell death driven by iron-dependent lipid peroxidation) through the metabolic breakdown of the anti-ferroptotic metabolites 7-DHC and 7-DHD which, when accumulated, divert the propagation of peroxyl radical-mediated damage from phospholipid components to its sterol core, protecting plasma and mitochondrial membranes from phospholipid autoxidation (PubMed:38297129, PubMed:38297130)", "gene_name": "DHCR7", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UBM7", "name": "UGT8 (GalCer synthase)", "organism": "Homo sapiens", "uniprot_id": "Q9UBM7" }, { "function": "Catalyzes the transfer of a sialic acid from a CMP-linked sialic acid donor onto a terminal alpha-2,3-, alpha-2,6-, or alpha-2,8-linked sialic acid of an N-linked glycan protein acceptor through alpha-2,8-linkages (PubMed:10766765, PubMed:11279095, PubMed:28810663, PubMed:9774483). Therefore, participates in polysialic acid synthesis on various sialylated N-acetyllactosaminyl oligosaccharides, including NCAM1 N-glycans, FETUB N-glycans and AHSG (PubMed:10766765, PubMed:11279095, PubMed:28810663, PubMed:9774483). It is noteworthy that alpha-2,3-linked sialic acid is apparently a better acceptor than alpha-2,6-linked sialic acid (PubMed:9774483)", "gene_name": "ST8SIA4", "glycan_count": 5, "glycosylation_sites": [ { "position": 50, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 74, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 119, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 204, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 219, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q92187", "name": "GD3S (ST8SIA1)", "organism": "Homo sapiens", "uniprot_id": "Q92187" }, { "function": "Cell adhesion molecule that mediates cell-cell contacts and regulates T-cell responses via its interaction with ALCAM/CD166 (PubMed:15048703, PubMed:15294938, PubMed:16352806, PubMed:16914752, PubMed:24584089, PubMed:24945728). Contributes to signaling cascades triggered by activation of the TCR/CD3 complex (PubMed:24584089). Functions as a costimulatory molecule; promotes T-cell activation and proliferation (PubMed:15294938, PubMed:16352806, PubMed:16914752). Contributes to the formation and maturation of the immunological synapse (PubMed:15294938, PubMed:16352806). Functions as a calcium-dependent pattern receptor that binds and aggregates both Gram-positive and Gram-negative bacteria. Binds both lipopolysaccharide (LPS) from Gram-negative bacteria and lipoteichoic acid from Gram-positive bacteria (PubMed:17601777). LPS binding leads to the activation of signaling cascades and down-stream MAP kinases (PubMed:17601777). Mediates activation of the inflammatory response and the secretion of pro-inflammatory cytokines in response to LPS (PubMed:17601777)", "gene_name": "CD6", "glycan_count": 2, "glycosylation_sites": [ { "position": 28, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 49, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 112, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 118, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 229, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 339, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 345, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 368, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P30203", "name": "T-cell surface glycoprotein CD6 isoform", "organism": "Homo sapiens", "uniprot_id": "P30203" }, { "function": "Within the IL18 receptor complex, responsible for the binding of the pro-inflammatory cytokine IL18, but not IL1A nor IL1B (PubMed:14528293, PubMed:25261253, PubMed:25500532, PubMed:37993714, PubMed:8626725). Involved in IL18-mediated IFNG synthesis from T-helper 1 (Th1) cells (PubMed:10653850). Contributes to IL18-induced cytokine production, either independently of SLC12A3, or as a complex with SLC12A3 (By similarity)", "gene_name": "IL18R1", "glycan_count": 6, "glycosylation_sites": [ { "position": 91, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 102, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 150, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 197, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 203, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 236, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 255, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 297, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13478", "name": "Interleukin-18 receptor 1", "organism": "Homo sapiens", "uniprot_id": "Q13478" }, { "function": "Cytokine that binds to and signals through the IL1RL1/ST2 receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells (PubMed:16286016, PubMed:19841166). Involved in the maturation of Th2 cells inducing the secretion of T-helper type 2-associated cytokines (PubMed:17853410, PubMed:18836528). Also involved in activation of mast cells, basophils, eosinophils and natural killer cells (PubMed:17853410, PubMed:18836528). Acts as an enhancer of polarization of alternatively activated macrophages (PubMed:19841166). Acts as a chemoattractant for Th2 cells, and may function as an 'alarmin', that amplifies immune responses during tissue injury (PubMed:17853410, PubMed:18836528). Induces rapid UCP2-dependent mitochondrial rewiring that attenuates the generation of reactive oxygen species and preserves the integrity of Krebs cycle required for persistent production of itaconate and subsequent GATA3-dependent differentiation of inflammation-resolving alternatively activated macrophages (By similarity)", "gene_name": "IL33", "glycan_count": 0, "glycosylation_sites": [], "id": "O95760", "name": "Interleukin-33", "organism": "Homo sapiens", "uniprot_id": "O95760" }, { "function": "Hematopoietic cytokine that plays an essential role in the development, expansion, and survival of naive and memory T-cells and B-cells thereby regulating the number of mature lymphocytes and maintaining lymphoid homeostasis (PubMed:25870237, PubMed:7527823). Mechanistically, exerts its biological effects through a receptor composed of IL7RA subunit and the cytokine receptor common subunit gamma/CSF2RG (PubMed:8128231). Binding to the receptor leads to activation of various kinases including JAK1 or JAK3 depending on the cell type and subsequently propagation of signals through activation of several downstream signaling pathways including the PI3K/Akt/mTOR or the JAK-STAT5 (PubMed:18523275, PubMed:20974963)", "gene_name": "IL7", "glycan_count": 0, "glycosylation_sites": [ { "position": 95, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 116, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 141, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P13232", "name": "Interleukin-7", "organism": "Homo sapiens", "uniprot_id": "P13232" }, { "function": "Binds to FN14 and possibly also to TNRFSF12/APO3. Weak inducer of apoptosis in some cell types. Mediates NF-kappa-B activation. Promotes angiogenesis and the proliferation of endothelial cells. Also involved in induction of inflammatory cytokines. Promotes IL8 secretion", "gene_name": "TNFSF12", "glycan_count": 1, "glycosylation_sites": [ { "position": 139, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O43508", "name": "Tumor necrosis factor ligand superfamily member 12 (TWEAK)", "organism": "Homo sapiens", "uniprot_id": "O43508" }, { "function": "Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling", "gene_name": "H3-3A", "glycan_count": 1, "glycosylation_sites": [], "id": "P84243", "name": "Cit-H3", "organism": "Homo sapiens", "uniprot_id": "P84243" }, { "function": "Acts as a substrate for the production of iodinated thyroid hormones thyroxine (T4) and triiodothyronine (T3) (PubMed:17532758, PubMed:32025030). The synthesis of T3 and T4 involves iodination of selected tyrosine residues of TG/thyroglobulin followed by their oxidative coupling in the thyroid follicle lumen (PubMed:32025030). Following TG re-internalization and lysosomal-mediated proteolysis, T3 and T4 are released from the polypeptide backbone leading to their secretion into the bloodstream (PubMed:32025030). One dimer produces 7 thyroid hormone molecules (PubMed:32025030)", "gene_name": "TG", "glycan_count": 21, "glycosylation_sites": [ { "position": 76, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 110, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 198, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 484, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 529, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 748, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 816, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 947, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1220, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1348, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1349, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1365, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1716, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1774, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1869, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2013, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2122, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2250, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2295, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2582, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2749, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" } ], "id": "P01266", "name": "Thyroglobulin", "organism": "Homo sapiens", "uniprot_id": "P01266" }, { "function": "Deacetylates a wide range of non-histone substrates (PubMed:12024216, PubMed:18606987, PubMed:20308065, PubMed:24882211, PubMed:26246421, PubMed:30538141, PubMed:31857589, PubMed:30770470, PubMed:38534334, PubMed:39567688). Plays a central role in microtubule-dependent cell motility by mediating deacetylation of tubulin (PubMed:12024216, PubMed:20308065, PubMed:26246421). Required for cilia disassembly via deacetylation of alpha-tubulin (PubMed:17604723, PubMed:26246421). Alpha-tubulin deacetylation results in destabilization of dynamic microtubules (By similarity). Promotes deacetylation of CTTN, leading to actin polymerization, promotion of autophagosome-lysosome fusion and completion of autophagy (PubMed:30538141). Deacetylates SQSTM1 (PubMed:31857589). Deacetylates peroxiredoxins PRDX1 and PRDX2, decreasing their reducing activity (PubMed:18606987). Deacetylates antiviral protein RIGI in the presence of viral mRNAs which is required for viral RNA detection by RIGI (By similarity). Sequentially deacetylates and polyubiquitinates DNA mismatch repair protein MSH2 which leads to MSH2 degradation, reducing cellular sensitivity to DNA-damaging agents and decreasing cellular DNA mismatch repair activities (PubMed:24882211). Deacetylates DNA mismatch repair protein MLH1 which prevents recruitment of the MutL alpha complex (formed by the MLH1-PMS2 heterodimer) to the MutS alpha complex (formed by the MSH2-MSH6 heterodimer), leading to tolerance of DNA damage (PubMed:30770470). Deacetylates RHOT1/MIRO1 which blocks mitochondrial transport and mediates axon growth inhibition (By similarity). Deacetylates transcription factor SP1 which leads to increased expression of ENG, positively regulating angiogenesis (PubMed:38534334). Deacetylates KHDRBS1/SAM68 which regulates alternative splicing by inhibiting the inclusion of CD44 alternate exons (PubMed:26080397). Acts as a valine sensor by binding to valine through the primate-specific SE14 repeat region (PubMed:39567688). In valine deprivation conditions, translocates from the cytoplasm to the nucleus where it deacetylates TET2 which promotes TET2-dependent DNA demethylation, leading to DNA damage (PubMed:39567688). Promotes odontoblast differentiation following IPO7-mediated nuclear import and subsequent repression of RUNX2 expression (By similarity). In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome (PubMed:17846173). Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and targets them to the aggresome, facilitating their clearance by autophagy (PubMed:17846173). Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer (PubMed:24413532)", "gene_name": "HDAC6", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9UBN7", "name": "HDAC4", "organism": "Homo sapiens", "uniprot_id": "Q9UBN7" }, { "function": "Seems to play a role in the development or function of the kidney glomerular filtration barrier. Regulates glomerular vascular permeability. May anchor the podocyte slit diaphragm to the actin cytoskeleton. Plays a role in skeletal muscle formation through regulation of myoblast fusion (By similarity)", "gene_name": "NPHS1", "glycan_count": 0, "glycosylation_sites": [ { "position": 40, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 356, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 401, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 547, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 553, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 564, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 577, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 680, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 708, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 908, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O60500", "name": "Nephrin", "organism": "Homo sapiens", "uniprot_id": "O60500" }, { "function": "Signal transducer and transcription activator that mediates cellular responses to interferons (IFNs), cytokine KITLG/SCF and other cytokines and other growth factors (PubMed:12764129, PubMed:12855578, PubMed:15322115, PubMed:23940278, PubMed:34508746, PubMed:35568036, PubMed:9724754). Following type I IFN (IFN-alpha and IFN-beta) binding to cell surface receptors, signaling via protein kinases leads to activation of Jak kinases (TYK2 and JAK1) and to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize and associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus (PubMed:28753426, PubMed:35568036). ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of IFN-stimulated genes (ISG), which drive the cell in an antiviral state (PubMed:28753426, PubMed:35568036). In response to type II IFN (IFN-gamma), STAT1 is tyrosine- and serine-phosphorylated (PubMed:26479788). It then forms a homodimer termed IFN-gamma-activated factor (GAF), migrates into the nucleus and binds to the IFN gamma activated sequence (GAS) to drive the expression of the target genes, inducing a cellular antiviral state (PubMed:8156998). Becomes activated in response to KITLG/SCF and KIT signaling (PubMed:15526160). May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4 (PubMed:19088846). Following bacterial lipopolysaccharide (LPS)-induced TLR4 endocytosis, phosphorylated at Thr-749 by IKBKB which promotes binding of STAT1 to the 5'-TTTGAGGC-3' sequence in the ARID5A promoter, resulting in transcriptional activation of ARID5A and subsequent ARID5A-mediated stabilization of IL6 (PubMed:32209697). Phosphorylation at Thr-749 also promotes binding of STAT1 to the 5'-TTTGAGTC-3' sequence in the IL12B promoter and activation of IL12B transcription (PubMed:32209697). Involved in food tolerance in small intestine: associates with the Gasdermin-D, p13 cleavage product (13 kDa GSDMD) and promotes transcription of CIITA, inducing type 1 regulatory T (Tr1) cells in upper small intestine (By similarity)", "gene_name": "STAT1", "glycan_count": 1, "glycosylation_sites": [], "id": "P42224", "name": "STAT1", "organism": "Homo sapiens", "uniprot_id": "P42224" }, { "function": "Transcription activator which binds specifically to the MEF2 element present in the regulatory regions of many muscle-specific genes. Controls cardiac morphogenesis and myogenesis, and is also involved in vascular development. Enhances transcriptional activation mediated by SOX18. Plays an essential role in hippocampal-dependent learning and memory by suppressing the number of excitatory synapses and thus regulating basal and evoked synaptic transmission. Crucial for normal neuronal development, distribution, and electrical activity in the neocortex. Necessary for proper development of megakaryocytes and platelets and for bone marrow B-lymphopoiesis. Required for B-cell survival and proliferation in response to BCR stimulation, efficient IgG1 antibody responses to T-cell-dependent antigens and for normal induction of germinal center B-cells. May also be involved in neurogenesis and in the development of cortical architecture (By similarity). Isoforms that lack the repressor domain are more active than isoform 1", "gene_name": "MEF2C", "glycan_count": 1, "glycosylation_sites": [], "id": "Q06413", "name": "MEF2C", "organism": "Homo sapiens", "uniprot_id": "Q06413" }, { "function": "Sensor component of the NLRP3 inflammasome, which mediates inflammasome activation in response to defects in membrane integrity, leading to secretion of inflammatory cytokines IL1B and IL18 and pyroptosis (PubMed:16407889, PubMed:18403674, PubMed:18604214, PubMed:23582325, PubMed:25686105, PubMed:27929086, PubMed:28656979, PubMed:28847925, PubMed:30487600, PubMed:30612879, PubMed:31086327, PubMed:31086329, PubMed:31189953, PubMed:33231615, PubMed:34133077, PubMed:34341353, PubMed:34512673, PubMed:36442502). In response to pathogens and other damage-associated signals that affect the integrity of membranes, initiates the formation of the inflammasome polymeric complex composed of NLRP3, CASP1 and PYCARD/ASC (PubMed:16407889, PubMed:18403674, PubMed:27432880, PubMed:28847925, PubMed:31189953, PubMed:33231615, PubMed:34133077, PubMed:34341353, PubMed:36142182, PubMed:36442502). Recruitment of pro-caspase-1 (proCASP1) to the NLRP3 inflammasome promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), promoting cytokine secretion and pyroptosis (PubMed:23582325, PubMed:28847925, PubMed:31189953, PubMed:33231615, PubMed:34133077, PubMed:34341353). Activation of NLRP3 inflammasome is also required for HMGB1 secretion; stimulating inflammatory responses (PubMed:22801494). Under resting conditions, ADP-bound NLRP3 is autoinhibited (PubMed:35114687). NLRP3 activation stimuli include extracellular ATP, nigericin, reactive oxygen species, crystals of monosodium urate or cholesterol, amyloid-beta fibers, environmental or industrial particles and nanoparticles, such as asbestos, silica, aluminum salts, cytosolic dsRNA, etc (PubMed:16407889, PubMed:18403674, PubMed:18604214, PubMed:19414800, PubMed:23871209). Almost all stimuli trigger intracellular K(+) efflux (By similarity). These stimuli lead to membrane perturbation and activation of NLRP3 (By similarity). Upon activation, NLRP3 is transported to microtubule organizing center (MTOC), where it is unlocked by NEK7, leading to its relocalization to dispersed trans-Golgi network (dTGN) vesicle membranes and formation of an active inflammasome complex (PubMed:36442502, PubMed:39173637). Associates with dTGN vesicle membranes by binding to phosphatidylinositol 4-phosphate (PtdIns4P) (PubMed:30487600, PubMed:34554188). Shows ATPase activity (PubMed:17483456)", "gene_name": "NLRP3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96P20", "name": "NLRP3", "organism": "Homo sapiens", "uniprot_id": "Q96P20" }, { "function": "Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in various processes, such as synaptic plasticity, neurotransmitter release and long-term potentiation (PubMed:14722083). Member of the NMDAR signaling complex in excitatory synapses, it regulates NMDAR-dependent potentiation of the AMPAR and therefore excitatory synaptic transmission (By similarity). Regulates dendritic spine development (PubMed:28130356). Also regulates the migration of developing neurons (PubMed:29100089). Phosphorylates the transcription factor FOXO3 to activate its transcriptional activity (PubMed:23805378). Phosphorylates the transcription factor ETS1 in response to calcium signaling, thereby decreasing ETS1 affinity for DNA (By similarity). In response to interferon-gamma (IFN-gamma) stimulation, catalyzes phosphorylation of STAT1, stimulating the JAK-STAT signaling pathway (PubMed:11972023). In response to interferon-beta (IFN-beta) stimulation, stimulates the JAK-STAT signaling pathway (PubMed:35568036). Acts as a negative regulator of 2-arachidonoylglycerol (2-AG)-mediated synaptic signaling via modulation of DAGLA activity (By similarity)", "gene_name": "CAMK2A", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UQM7", "name": "CaMKII", "organism": "Homo sapiens", "uniprot_id": "Q9UQM7" }, { "function": "Acts as a transcriptional activator and repressor required for cardiac development and may have key roles in the maintenance of functional and structural phenotypes in adult heart", "gene_name": "TBX20", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UMR3", "name": "MAN2A2", "organism": "Homo sapiens", "uniprot_id": "Q9UMR3" }, { "function": "Catalyzes the translocation of specific phospholipids from the cytoplasmic to the extracellular/lumenal leaflet of membrane coupled to the hydrolysis of ATP (PubMed:24097981, PubMed:35974019). Thereby, participates in phospholipid transfer to apolipoproteins to form nascent high density lipoproteins/HDLs (PubMed:14754908). Transports preferentially phosphatidylcholine over phosphatidylserine (PubMed:24097981). May play a similar role in the efflux of intracellular cholesterol to apolipoproteins and the formation of nascent high density lipoproteins/HDLs (PubMed:10533863, PubMed:14754908, PubMed:24097981, PubMed:35974019). Translocates phospholipids from the outer face of the plasma membrane and forces it through its gateway and annulus into an elongated hydrophobic tunnel in its extracellular domain (PubMed:35974019)", "gene_name": "ABCA1", "glycan_count": 12, "glycosylation_sites": [ { "position": 14, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 98, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 151, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 161, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 196, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 244, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 292, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 337, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 349, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 400, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 478, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 489, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 521, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 820, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1144, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1294, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1453, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1504, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1637, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2044, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2238, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O95477", "name": "ABCA1", "organism": "Homo sapiens", "uniprot_id": "O95477" }, { "function": "ABCG5 and ABCG8 form an obligate heterodimer that mediates Mg(2+)- and ATP-dependent sterol transport across the cell membrane (PubMed:27144356). Plays an essential role in the selective transport of dietary plant sterols and cholesterol in and out of the enterocytes and in the selective sterol excretion by the liver into bile (PubMed:11099417, PubMed:11138003, PubMed:15054092, PubMed:27144356). Required for normal sterol homeostasis (PubMed:11099417, PubMed:11138003, PubMed:15054092). The heterodimer with ABCG8 has ATPase activity (PubMed:16893193, PubMed:20210363, PubMed:27144356)", "gene_name": "ABCG5", "glycan_count": 1, "glycosylation_sites": [ { "position": 584, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 591, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9H222", "name": "ABCG1", "organism": "Homo sapiens", "uniprot_id": "Q9H222" }, { "function": "Catalytic component of the m-AAA protease, a protease that plays a key role in proteostasis of inner mitochondrial membrane proteins, and which is essential for axonal and neuron development (PubMed:19748354, PubMed:28396416, PubMed:29932645, PubMed:30683687, PubMed:31327635, PubMed:37917749, PubMed:38157846). AFG3L2 possesses both ATPase and protease activities: the ATPase activity is required to unfold substrates, threading them into the internal proteolytic cavity for hydrolysis into small peptide fragments (PubMed:19748354, PubMed:31327635). The m-AAA protease carries out quality control in the inner membrane of the mitochondria by mediating degradation of mistranslated or misfolded polypeptides (PubMed:26504172, PubMed:30683687, PubMed:34718584). The m-AAA protease complex also promotes the processing and maturation of mitochondrial proteins, such as MRPL32/bL32m, PINK1 and SP7 (PubMed:22354088, PubMed:29932645, PubMed:30252181). Mediates protein maturation of the mitochondrial ribosomal subunit MRPL32/bL32m by catalyzing the cleavage of the presequence of MRPL32/bL32m prior to assembly into the mitochondrial ribosome (PubMed:29932645). Required for SPG7 maturation into its active mature form after SPG7 cleavage by mitochondrial-processing peptidase (MPP) (PubMed:30252181). Required for the maturation of PINK1 into its 52kDa mature form after its cleavage by mitochondrial-processing peptidase (MPP) (PubMed:22354088). Acts as a regulator of calcium in neurons by mediating degradation of SMDT1/EMRE before its assembly with the uniporter complex, limiting the availability of SMDT1/EMRE for MCU assembly and promoting efficient assembly of gatekeeper subunits with MCU (PubMed:27642048, PubMed:28396416). Promotes the proteolytic degradation of GHITM upon hyperpolarization of mitochondria: progressive GHITM degradation leads to respiratory complex I degradation and broad reshaping of the mitochondrial proteome by AFG3L2 (PubMed:35912435). Also acts as a regulator of mitochondrial glutathione homeostasis by mediating cleavage and degradation of SLC25A39 (PubMed:37917749, PubMed:38157846). SLC25A39 cleavage is prevented when SLC25A39 binds iron-sulfur (PubMed:37917749, PubMed:38157846). Involved in the regulation of OMA1-dependent processing of OPA1 (PubMed:17615298, PubMed:29545505, PubMed:30252181, PubMed:30683687, PubMed:32600459). May act by mediating processing of OMA1 precursor, participating in OMA1 maturation (PubMed:29545505)", "gene_name": "AFG3L2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y4W6", "name": "LMF1", "organism": "Homo sapiens", "uniprot_id": "Q9Y4W6" }, { "function": "Precursor of the transcription factor form (Processed sterol regulatory element-binding protein 1), which is embedded in the endoplasmic reticulum membrane (PubMed:32322062). Low sterol concentrations promote processing of this form, releasing the transcription factor form that translocates into the nucleus and activates transcription of genes involved in cholesterol biosynthesis and lipid homeostasis (By similarity)", "gene_name": "SREBF1", "glycan_count": 2, "glycosylation_sites": [], "id": "P36956", "name": "SREBF1", "organism": "Homo sapiens", "uniprot_id": "P36956" }, { "function": "Phospholipase B that deacylates intracellular phosphatidylcholine (PtdCho), generating glycerophosphocholine (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of PtdCho. Catalyzes the hydrolysis of several naturally occurring membrane-associated lipids (PubMed:11927584). Hydrolyzes lysophospholipids and monoacylglycerols, preferring the 1-acyl to the 2-acyl isomer. Does not catalyze hydrolysis of di- or triacylglycerols or fatty acid amides (PubMed:11927584)", "gene_name": "PNPLA6", "glycan_count": 2, "glycosylation_sites": [ { "position": 20, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8IY17", "name": "PNPLA6", "organism": "Homo sapiens", "uniprot_id": "Q8IY17" }, { "function": "Receptor for Wnt proteins (PubMed:10097073, PubMed:20530549, PubMed:26908622, PubMed:9054360). Functions in the canonical Wnt/beta-catenin signaling pathway. In vitro activates WNT2, WNT10B, WNT5A, but not WNT2B or WNT4 signaling (By similarity). In neurons, activation by WNT7A promotes formation of synapses (PubMed:20530549). May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues (Probable). Plays a role in yolk sac angiogenesis and in placental vascularization (By similarity). Plays a role in ocular development (PubMed:26908622)", "gene_name": "FZD5", "glycan_count": 2, "glycosylation_sites": [ { "position": 47, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 151, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13467", "name": "FZD5", "organism": "Homo sapiens", "uniprot_id": "Q13467" }, { "function": "Seems to be a coreceptor in inhibin signaling, but seems not to be a high-affinity inhibin receptor. Antagonizes activin A signaling in the presence or absence of inhibin B (By similarity). Necessary to mediate a specific antagonistic effect of inhibin B on activin-stimulated transcription", "gene_name": "IGSF1", "glycan_count": 4, "glycosylation_sites": [ { "position": 53, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 338, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 374, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 381, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 607, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 747, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 798, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 846, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 939, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 986, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1027, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1082, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1147, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1223, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8N6C5", "name": "IGDCC4", "organism": "Homo sapiens", "uniprot_id": "Q8N6C5" }, { "function": "", "gene_name": "C11orf68", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H3H3", "name": "PRSS27", "organism": "Homo sapiens", "uniprot_id": "Q9H3H3" }, { "function": "May function as an inhibitor of the B-cell receptor signaling. May function in the B-cell-mediated immune response", "gene_name": "FCRL4", "glycan_count": 0, "glycosylation_sites": [ { "position": 374, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q96PJ5", "name": "FCMR", "organism": "Homo sapiens", "uniprot_id": "Q96PJ5" }, { "function": "Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain", "gene_name": "PCDHGA4", "glycan_count": 0, "glycosylation_sites": [ { "position": 450, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 576, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y5G9", "name": "PCDHGC3", "organism": "Homo sapiens", "uniprot_id": "Q9Y5G9" }, { "function": "Activator of the canonical Wnt signaling pathway by acting as a ligand for LGR4-6 receptors (PubMed:29769720). Upon binding to LGR4-6 (LGR4, LGR5 or LGR6), LGR4-6 associate with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. Also regulates the canonical Wnt/beta-catenin-dependent pathway and non-canonical Wnt signaling by acting as an inhibitor of ZNRF3, an important regulator of the Wnt signaling pathway. Acts as a ligand for frizzled FZD8 and LRP6. May negatively regulate the TGF-beta pathway. Has a essential roles in ovary determination. Regulates Wnt signaling by antagonizing DKK1/KREM1-mediated internalization of LRP6 through an interaction with KREM1 (PubMed:17804805)", "gene_name": "RSPO1", "glycan_count": 1, "glycosylation_sites": [ { "position": 137, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 153, "type": "C-linked (Man) tryptophan" }, { "position": 156, "type": "C-linked (Man) tryptophan" } ], "id": "Q2MKA7", "name": "RSPO4", "organism": "Homo sapiens", "uniprot_id": "Q2MKA7" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P07766 (CD3E)", "name": "CD3", "organism": "", "uniprot_id": "" }, { "function": "Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class I molecule:peptide complex. The antigens presented by class I peptides are derived from cytosolic proteins while class II derived from extracellular proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class I proteins presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of cytotoxic T-lymphocytes (CTLs). This mechanism enables CTLs to recognize and eliminate infected cells and tumor cells. In NK-cells, the presence of CD8A homodimers at the cell surface provides a survival mechanism allowing conjugation and lysis of multiple target cells. CD8A homodimer molecules also promote the survival and differentiation of activated lymphocytes into memory CD8 T-cells", "gene_name": "CD8A", "glycan_count": 2, "glycosylation_sites": [], "id": "P01732", "name": "CD8", "organism": "Homo sapiens", "uniprot_id": "P01732" }, { "function": "Non catalytic polymerase cofactor and regulatory protein that plays a role in viral transcription and replication. Stabilizes the RNA polymerase L to the N-RNA template and binds the soluble protein N, preventing it from encapsidating non-genomic RNA. Also inhibits host IFN-alpha and IFN-beta signaling by binding and retaining phosphorylated STAT1 in the cytoplasm or by inhibiting the DNA binding of STAT1 in the nucleus. Might be involved, through interaction with host dynein, in intracellular microtubule-dependent virus transport of incoming virus from the synapse toward the cell body (By similarity). Inhibits interferon induction pathways by interacting with host TBK1 and preventing the formation of dynamic cytoplasmic condensates that have liquid properties and that are essential for interferon production (By similarity)", "gene_name": "P", "glycan_count": 0, "glycosylation_sites": [], "id": "P06747", "name": "Rabies virus nucleoprotein (N)", "organism": "Rabies virus (strain Pasteur vaccins / PV)", "uniprot_id": "P06747" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "not specified", "name": "CCHFV glycoprotein precursor (GPC)", "organism": "", "uniprot_id": "" }, { "function": "Deubiquitinase that specifically cleaves 'Lys-63'- and linear 'Met-1'-linked polyubiquitin chains and is involved in NF-kappa-B activation and TNF-alpha-induced necroptosis (PubMed:18313383, PubMed:18636086, PubMed:26670046, PubMed:26997266, PubMed:27458237, PubMed:27591049, PubMed:27746020, PubMed:29291351, PubMed:32185393). Negatively regulates NF-kappa-B activation by deubiquitinating upstream signaling factors (PubMed:12917689, PubMed:12917691, PubMed:32185393). Contributes to the regulation of cell survival, proliferation and differentiation via its effects on NF-kappa-B activation (PubMed:12917690). Negative regulator of Wnt signaling (PubMed:20227366). Inhibits HDAC6 and thereby promotes acetylation of alpha-tubulin and stabilization of microtubules (PubMed:19893491). Plays a role in the regulation of microtubule dynamics, and thereby contributes to the regulation of cell proliferation, cell polarization, cell migration, and angiogenesis (PubMed:18222923, PubMed:20194890). Required for normal cell cycle progress and normal cytokinesis (PubMed:17495026, PubMed:19893491). Inhibits nuclear translocation of NF-kappa-B (PubMed:18636086). Plays a role in the regulation of inflammation and the innate immune response, via its effects on NF-kappa-B activation (PubMed:18636086). Dispensable for the maturation of intrathymic natural killer cells, but required for the continued survival of immature natural killer cells (By similarity). Negatively regulates TNFRSF11A signaling and osteoclastogenesis (By similarity). Involved in the regulation of ciliogenesis, allowing ciliary basal bodies to migrate and dock to the plasma membrane; this process does not depend on NF-kappa-B activation (By similarity). Ability to remove linear ('Met-1'-linked) polyubiquitin chains regulates innate immunity and TNF-alpha-induced necroptosis: recruited to the LUBAC complex via interaction with SPATA2 and restricts linear polyubiquitin formation on target proteins (PubMed:26670046, PubMed:26997266, PubMed:27458237, PubMed:27591049). Regulates innate immunity by restricting linear polyubiquitin formation on RIPK2 in response to NOD2 stimulation (PubMed:26997266). Involved in TNF-alpha-induced necroptosis by removing linear ('Met-1'-linked) polyubiquitin chains from RIPK1, thereby regulating the kinase activity of RIPK1 (By similarity). Negatively regulates intestinal inflammation by removing 'Lys-63' linked polyubiquitin chain of NLRP6, thereby reducing the interaction between NLRP6 and PYCARD/ASC and formation of the NLRP6 inflammasome (By similarity). Does not catalyze deubiquitination of heterotypic 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains (PubMed:27746020). Removes 'Lys-63' linked polyubiquitin chain of MAP3K7, which inhibits phosphorylation and blocks downstream activation of the JNK-p38 kinase cascades (PubMed:29291351). Also removes 'Lys-63'-linked polyubiquitin chains of MAP3K1 and MA3P3K3, which inhibit their interaction with MAP2K1 and MAP2K2 (PubMed:34497368)", "gene_name": "CYLD", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NQC7", "name": "TRIM21 (host cytoplasmic Fc receptor)", "organism": "Homo sapiens", "uniprot_id": "Q9NQC7" }, { "function": "This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade", "gene_name": "ANXA5", "glycan_count": 1, "glycosylation_sites": [], "id": "P08758", "name": "Annexin A5", "organism": "Homo sapiens", "uniprot_id": "P08758" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02671 (FGA), P02675 (FGB), P02679 (FGG)", "name": "Fibrinogen", "organism": "", "uniprot_id": "" }, { "function": "Glycoprotein that plays an essential role in maintaining a well-balanced immune response by modulating complement activation. Acts as a soluble inhibitor of complement, where its binding to self markers such as glycan structures prevents complement activation and amplification on cell surfaces (PubMed:21285368, PubMed:21317894, PubMed:25402769). Accelerates the decay of the complement alternative pathway (AP) C3 convertase C3bBb, thus preventing local formation of more C3b, the central player of the complement amplification loop (PubMed:19503104, PubMed:21317894, PubMed:26700768). As a cofactor of the serine protease factor I, CFH also regulates proteolytic degradation of already-deposited C3b (PubMed:18252712, PubMed:23332154, PubMed:28671664). In addition, mediates several cellular responses through interaction with specific receptors. For example, interacts with CR3/ITGAM receptor and thereby mediates the adhesion of human neutrophils to different pathogens. In turn, these pathogens are phagocytosed and destroyed (PubMed:20008295, PubMed:9558116)", "gene_name": "CFH", "glycan_count": 140, "glycosylation_sites": [ { "position": 217, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 529, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 718, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 802, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 822, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 882, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 911, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 1029, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 1095, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08603", "name": "Complement Factor H (CFH)", "organism": "Homo sapiens", "uniprot_id": "P08603" }, { "function": "Receptor for the invariable Fc fragment of immunoglobulin gamma (IgG). Optimally activated upon binding of clustered antigen-IgG complexes displayed on cell surfaces, triggers lysis of antibody-coated cells, a process known as antibody-dependent cellular cytotoxicity (ADCC). Does not bind free monomeric IgG, thus avoiding inappropriate effector cell activation in the absence of antigenic trigger (PubMed:11711607, PubMed:21768335, PubMed:22023369, PubMed:24412922, PubMed:25786175, PubMed:25816339, PubMed:28652325, PubMed:8609432, PubMed:9242542). Mediates IgG effector functions on natural killer (NK) cells. Binds antigen-IgG complexes generated upon infection and triggers NK cell-dependent cytokine production and degranulation to limit viral load and propagation. Involved in the generation of memory-like adaptive NK cells capable to produce high amounts of IFNG and to efficiently eliminate virus-infected cells via ADCC (PubMed:24412922, PubMed:25786175). Regulates NK cell survival and proliferation, in particular by preventing NK cell progenitor apoptosis (PubMed:29967280, PubMed:9916693). Fc-binding subunit that associates with CD247 and/or FCER1G adapters to form functional signaling complexes. Following the engagement of antigen-IgG complexes, triggers phosphorylation of immunoreceptor tyrosine-based activation motif (ITAM)-containing adapters with subsequent activation of phosphatidylinositol 3-kinase signaling and sustained elevation of intracellular calcium that ultimately drive NK cell activation. The ITAM-dependent signaling coupled to receptor phosphorylation by PKC mediates robust intracellular calcium flux that leads to production of pro-inflammatory cytokines, whereas in the absence of receptor phosphorylation it mainly activates phosphatidylinositol 3-kinase signaling leading to cell degranulation (PubMed:1825220, PubMed:23024279, PubMed:2532305). Costimulates NK cells and trigger lysis of target cells independently of IgG binding (PubMed:10318937, PubMed:23006327). Mediates the antitumor activities of therapeutic antibodies. Upon ligation on monocytes triggers TNFA-dependent ADCC of IgG-coated tumor cells (PubMed:27670158). Mediates enhanced ADCC in response to afucosylated IgGs (PubMed:34485821)", "gene_name": "FCGR3A", "glycan_count": 103, "glycosylation_sites": [ { "position": 56, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 63, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 92, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 180, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 187, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08637", "name": "CD16 (FCGR3A)", "organism": "Homo sapiens", "uniprot_id": "P08637" }, { "function": "Coreceptor for bacterial lipopolysaccharide (PubMed:1698311, PubMed:23264655). In concert with LBP, binds to monomeric lipopolysaccharide and delivers it to the LY96/TLR4 complex, thereby mediating the innate immune response to bacterial lipopolysaccharide (LPS) (PubMed:20133493, PubMed:22265692, PubMed:23264655). Acts via MyD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (PubMed:8612135). Acts as a coreceptor for TLR2:TLR6 heterodimer in response to diacylated lipopeptides and for TLR2:TLR1 heterodimer in response to triacylated lipopeptides, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway (PubMed:16880211). Binds electronegative LDL (LDL(-)) and mediates the cytokine release induced by LDL(-) (PubMed:23880187)", "gene_name": "CD14", "glycan_count": 51, "glycosylation_sites": [ { "position": 37, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 151, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 282, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 323, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 336, "type": "O-linked (GalNAc...) threonine" } ], "id": "P08571", "name": "CD14", "organism": "Homo sapiens", "uniprot_id": "P08571" }, { "function": "Plays a critical role in MHC class II antigen processing by stabilizing peptide-free class II alpha/beta heterodimers in a complex soon after their synthesis and directing transport of the complex from the endoplasmic reticulum to the endosomal/lysosomal system where the antigen processing and binding of antigenic peptides to MHC class II takes place. Serves as cell surface receptor for the cytokine MIF", "gene_name": "CD74", "glycan_count": 90, "glycosylation_sites": [ { "position": 130, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 136, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 203, "type": "O-linked (GalNAc...) threonine" }, { "position": 256, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 281, "type": "O-linked (GalNAc...) serine" }, { "position": 282, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" } ], "id": "P04233", "name": "CD74", "organism": "Homo sapiens", "uniprot_id": "P04233" }, { "function": "Inhibitory receptor that plays a role in the modulation of immune responses. Suppresses T-cell activation by promoting the generation of mature immunoregulatory dendritic cells (PubMed:19011627). Upon binding to its ligands PVR/CD155 or NECTIN2/CD112, which are expressed on antigen-presenting cells, sends inhibitory signals to the T-cell or NK cell. Mechanistically, interaction with ligand leads to phosphorylation of the cytoplasmic tail by Src family tyrosine kinases such as FYN or LCK, allowing subsequent binding to adapter GRB2 and SHIP1/INPP5D. In turn, inhibits PI3K and MAPK signaling cascades (PubMed:23154388). In addition, associates with beta-arrestin-2/ARRB2 to recruit SHIP1/INPP5D that suppresses autoubiquitination of TRAF6 and subsequently inhibits NF-kappa-B signaling pathway (PubMed:24817116). Also acts as a receptor for NECTIN4 to inhibit NK cell cytotoxicity (PubMed:32503945)", "gene_name": "TIGIT", "glycan_count": 0, "glycosylation_sites": [ { "position": 32, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 101, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q495A1", "name": "TIGIT", "organism": "Homo sapiens", "uniprot_id": "Q495A1" }, { "function": "Transcriptional regulator which is crucial for the development and inhibitory function of regulatory T-cells (Treg) (PubMed:17377532, PubMed:21458306, PubMed:23947341, PubMed:24354325, PubMed:24722479, PubMed:24835996, PubMed:30513302, PubMed:32644293). Plays an essential role in maintaining homeostasis of the immune system by allowing the acquisition of full suppressive function and stability of the Treg lineage, and by directly modulating the expansion and function of conventional T-cells (PubMed:23169781). Can act either as a transcriptional repressor or a transcriptional activator depending on its interactions with other transcription factors, histone acetylases and deacetylases (PubMed:17377532, PubMed:21458306, PubMed:23947341, PubMed:24354325, PubMed:24722479). The suppressive activity of Treg involves the coordinate activation of many genes, including CTLA4 and TNFRSF18 by FOXP3 along with repression of genes encoding cytokines such as interleukin-2 (IL2) and interferon-gamma (IFNG) (PubMed:17377532, PubMed:21458306, PubMed:23947341, PubMed:24354325, PubMed:24722479). Inhibits cytokine production and T-cell effector function by repressing the activity of two key transcription factors, RELA and NFATC2 (PubMed:15790681). Mediates transcriptional repression of IL2 via its association with histone acetylase KAT5 and histone deacetylase HDAC7 (PubMed:17360565). Can activate the expression of TNFRSF18, IL2RA and CTLA4 and repress the expression of IL2 and IFNG via its association with transcription factor RUNX1 (PubMed:17377532). Inhibits the differentiation of IL17 producing helper T-cells (Th17) by antagonizing RORC function, leading to down-regulation of IL17 expression, favoring Treg development (PubMed:18368049). Inhibits the transcriptional activator activity of RORA (PubMed:18354202). Can repress the expression of IL2 and IFNG via its association with transcription factor IKZF4 (By similarity)", "gene_name": "FOXP3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9BZS1", "name": "FOXP3", "organism": "Homo sapiens", "uniprot_id": "Q9BZS1" }, { "function": "Receptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. The TRAF1/TRAF2 complex recruits the apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2. This receptor mediates most of the metabolic effects of TNF-alpha. Isoform 2 blocks TNF-alpha-induced apoptosis, which suggests that it regulates TNF-alpha function by antagonizing its biological activity", "gene_name": "TNFRSF1B", "glycan_count": 7, "glycosylation_sites": [ { "position": 30, "type": "O-linked (GalNAc...) threonine" }, { "position": 171, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 193, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 206, "type": "O-linked (GalNAc...) threonine" }, { "position": 221, "type": "O-linked (GalNAc...) serine" }, { "position": 222, "type": "O-linked (GalNAc...) threonine" } ], "id": "P20333", "name": "TNFR2 (TNFRSF1B)", "organism": "Homo sapiens", "uniprot_id": "P20333" }, { "function": "Iron-trafficking protein involved in multiple processes such as apoptosis, innate immunity and renal development (PubMed:12453413, PubMed:20581821, PubMed:27780864). Binds iron through association with 2,3-dihydroxybenzoic acid (2,3-DHBA), a siderophore that shares structural similarities with bacterial enterobactin, and delivers or removes iron from the cell, depending on the context. Iron-bound form (holo-24p3) is internalized following binding to the SLC22A17 (24p3R) receptor, leading to release of iron and subsequent increase of intracellular iron concentration. In contrast, association of the iron-free form (apo-24p3) with the SLC22A17 (24p3R) receptor is followed by association with an intracellular siderophore, iron chelation and iron transfer to the extracellular medium, thereby reducing intracellular iron concentration. Involved in apoptosis due to interleukin-3 (IL3) deprivation: iron-loaded form increases intracellular iron concentration without promoting apoptosis, while iron-free form decreases intracellular iron levels, inducing expression of the proapoptotic protein BCL2L11/BIM, resulting in apoptosis (By similarity). Involved in innate immunity; limits bacterial proliferation by sequestering iron bound to microbial siderophores, such as enterobactin (PubMed:27780864). Can also bind siderophores from M.tuberculosis (PubMed:15642259, PubMed:21978368)", "gene_name": "LCN2", "glycan_count": 24, "glycosylation_sites": [ { "position": 85, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P80188", "name": "Lipocalin 2", "organism": "Homo sapiens", "uniprot_id": "P80188" }, { "function": "Involved in fertilization ability of sperm", "gene_name": "SPESP1", "glycan_count": 0, "glycosylation_sites": [ { "position": 128, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6UW49", "name": "SPESP1 (Sperm Equatorial Segment Protein 1)", "organism": "Homo sapiens", "uniprot_id": "Q6UW49" }, { "function": "Heparin-dependent serine protease inhibitor acting in body fluids and secretions. Inactivates serine proteases by binding irreversibly to their serine activation site. Involved in the regulation of intravascular and extravascular proteolytic activities. Plays hemostatic roles in the blood plasma. Acts as a procoagulant and pro-inflammatory factor by inhibiting the anticoagulant activated protein C factor as well as the generation of activated protein C factor by the thrombin/thrombomodulin complex. Acts as an anticoagulant factor by inhibiting blood coagulation factors like prothrombin, factor XI, factor Xa, plasma kallikrein and fibrinolytic enzymes such as tissue- and urinary-type plasminogen activators. In seminal plasma, inactivates several serine proteases implicated in the reproductive system. Inhibits the serpin acrosin; indirectly protects component of the male genital tract from being degraded by excessive released acrosin. Inhibits tissue- and urinary-type plasminogen activator, prostate-specific antigen and kallikrein activities; has a control on the sperm motility and fertilization. Inhibits the activated protein C-catalyzed degradation of SEMG1 and SEMG2; regulates the degradation of semenogelin during the process of transfer of spermatozoa from the male reproductive tract into the female tract. In urine, inhibits urinary-type plasminogen activator and kallikrein activities. Inactivates membrane-anchored serine proteases activities such as MPRSS7 and TMPRSS11E. Inhibits urinary-type plasminogen activator-dependent tumor cell invasion and metastasis. May also play a non-inhibitory role in seminal plasma and urine as a hydrophobic hormone carrier by its binding to retinoic acid", "gene_name": "SERPINA5", "glycan_count": 62, "glycosylation_sites": [ { "position": 39, "type": "O-linked (GalNAc...) threonine" }, { "position": 249, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 262, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 338, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P05154", "name": "SERPINA5 (Plasma Serine Protease Inhibitor)", "organism": "Homo sapiens", "uniprot_id": "P05154" }, { "function": "Glycoprotein that regulates critical steps during fertilization and also has immunomonomodulatory effects. Four glycoforms, namely glycodelin-S, -A, -F and -C have been identified in reproductive tissues that differ in glycosylation and biological activity. Glycodelin-A has contraceptive and immunosuppressive activities (PubMed:7531163, PubMed:9918684). Glycodelin-C stimulates binding of spermatozoa to the zona pellucida (PubMed:17192260). Glycodelin-F inhibits spermatozoa-zona pellucida binding and significantly suppresses progesterone-induced acrosome reaction of spermatozoa (PubMed:12672671). Glycodelin-S in seminal plasma maintains the uncapacitated state of human spermatozoa (PubMed:15883155)", "gene_name": "PAEP", "glycan_count": 42, "glycosylation_sites": [ { "position": 46, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 81, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P09466", "name": "Glycodelin", "organism": "Homo sapiens", "uniprot_id": "P09466" }, { "function": "Transfers 1,4-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of glucuronic acid (GlcUA). Required for addition of the first GalNAc to the core tetrasaccharide linker and for elongation of chondroitin chains", "gene_name": "CSGALNACT2", "glycan_count": 1, "glycosylation_sites": [ { "position": 41, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 333, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8N6G5", "name": "Leucine-rich repeat-containing protein 37A2", "organism": "Homo sapiens", "uniprot_id": "Q8N6G5" }, { "function": "E3 SUMO-protein ligase; has a preference for SUMO2 and SUMO3 and facilitates UBE2I/UBC9-mediated sumoylation of target proteins (PubMed:26524493, PubMed:26524494). Plays a role in protein SUMO2 modification in response to stress caused by DNA damage and by proteasome inhibitors (in vitro). Required for MCM4 sumoylation (By similarity). Has no activity with SUMO1 (PubMed:26524493). Preferentially transfers an additional SUMO2 chain onto the SUMO2 consensus site 'Lys-11' (PubMed:26524493). Negatively regulates transcriptional activation mediated by the SMAD4 complex in response to TGF-beta signaling. Inhibits EP300-mediated acetylation of histone H3 at 'Lys-9' (PubMed:24324267). Plays a role in regulating the transcription of AR targets (PubMed:18656483)", "gene_name": "ZNF451", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y4E5", "name": "Forkhead-associated domain-containing protein 1", "organism": "Homo sapiens", "uniprot_id": "Q9Y4E5" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03452 (A/Brisbane/02/2018)", "name": "Hemagglutinin (HA)", "organism": "", "uniprot_id": "" }, { "function": "Secreted glycoprotein regulating the activation of different signaling pathways in adjacent cells to control different processes including cell adhesion, cell-matrix adhesion, cytoskeleton organization and cell migration. Promotes substrate adhesion, spreading and formation of focal contacts. Negatively regulates cell-matrix adhesion and stress fiber assembly through Rho protein signal transduction. Modulates the organization of actin cytoskeleton by stimulating the formation of stress fibers through interactions with components of Wnt signaling pathways. Promotes cell migration through activation of PTK2 and the downstream phosphatidylinositol 3-kinase signaling. Plays a role in bone formation and promotes osteoblast differentiation in a dose-dependent manner through mitogen-activated protein kinase signaling. Mediates myelination in the peripheral nervous system through ERBB2/ERBB3 signaling. Plays a role as a regulator of muscle hypertrophy through the components of dystrophin-associated protein complex. Involved in positive regulation of mitochondrial depolarization. Plays a role in neurite outgrowth. May participate in the obstruction of fluid outflow in the trabecular meshwork", "gene_name": "MYOC", "glycan_count": 1, "glycosylation_sites": [ { "position": 57, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q99972", "name": "Myocilin", "organism": "Homo sapiens", "uniprot_id": "Q99972" }, { "function": "Serine protease inhibitor. Inhibits TMPRSS7 (PubMed:15853774). Is a primary inhibitor of tissue-type plasminogen activator (PLAT) and urokinase-type plasminogen activator (PLAU). As PLAT inhibitor, it is required for fibrinolysis down-regulation and is responsible for the controlled degradation of blood clots (PubMed:17912461, PubMed:8481516, PubMed:9207454, PubMed:21925150). As PLAU inhibitor, it is involved in the regulation of cell adhesion and spreading (PubMed:9175705). Acts as a regulator of cell migration, independently of its role as protease inhibitor (PubMed:15001579, PubMed:9168821). It is required for stimulation of keratinocyte migration during cutaneous injury repair (PubMed:18386027). It is involved in cellular and replicative senescence (PubMed:16862142). Plays a role in alveolar type 2 cells senescence in the lung (By similarity). Is involved in the regulation of cementogenic differentiation of periodontal ligament stem cells, and regulates odontoblast differentiation and dentin formation during odontogenesis (PubMed:25808697, PubMed:27046084)", "gene_name": "SERPINE1", "glycan_count": 16, "glycosylation_sites": [ { "position": 232, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 288, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 352, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P05121", "name": "Plasminogen Activator Inhibitor-1 (PAI-1)", "organism": "Homo sapiens", "uniprot_id": "P05121" }, { "function": "Acts as a receptor for urokinase plasminogen activator (PubMed:15677461). Plays a role in localizing and promoting plasmin formation. Mediates the proteolysis-independent signal transduction activation effects of U-PA. It is subject to negative-feedback regulation by U-PA which cleaves it into an inactive form", "gene_name": "PLAUR", "glycan_count": 4, "glycosylation_sites": [ { "position": 74, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 184, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 194, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 222, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 255, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q03405", "name": "Urokinase-type Plasminogen Activator Receptor (uPAR)", "organism": "Homo sapiens", "uniprot_id": "Q03405" }, { "function": "Dual-specificity kinase which possesses both serine/threonine and tyrosine kinase activities (PubMed:20981014, PubMed:21127067, PubMed:23665168, PubMed:30773093, PubMed:8769099). Exhibits a substrate preference for proline at position P+1 and arginine at position P-3 (PubMed:23665168). Plays an important role in double-strand breaks (DSBs) repair following DNA damage (PubMed:31024071). Mechanistically, phosphorylates RNF169 and increases its ability to block accumulation of TP53BP1 at the DSB sites thereby promoting homologous recombination repair (HRR) (PubMed:30773093). Also acts as a positive regulator of transcription by acting as a CTD kinase that mediates phosphorylation of the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II) POLR2A (PubMed:25620562, PubMed:29849146). May play a role in a signaling pathway regulating nuclear functions of cell proliferation (PubMed:14500717). Modulates alternative splicing by phosphorylating the splice factor SRSF6 (By similarity). Has pro-survival function and negatively regulates the apoptotic process (By similarity). Promotes cell survival upon genotoxic stress through phosphorylation of SIRT1 (By similarity). This in turn inhibits p53/TP53 activity and apoptosis (By similarity). Phosphorylates SEPTIN4, SEPTIN5 and SF3B1 at 'Thr-434' (By similarity)", "gene_name": "DYRK1A", "glycan_count": 0, "glycosylation_sites": [], "id": "O60769", "name": "SGLT2", "organism": "Homo sapiens", "uniprot_id": "Q13627" }, { "function": "Apolipoprotein B is a major protein constituent of chylomicrons (apo B-48), LDL (apo B-100) and VLDL (apo B-100). Apo B-100 functions as a recognition signal for the cellular binding and internalization of LDL particles by the apoB/E receptor", "gene_name": "APOB", "glycan_count": 140, "glycosylation_sites": [ { "position": 34, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 185, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 983, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1368, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1377, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1523, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2239, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2560, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2779, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2982, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3101, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3224, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3336, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3358, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3411, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3465, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3895, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4237, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4431, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P04114", "name": "ApoB100", "organism": "Homo sapiens", "uniprot_id": "P04114" }, { "function": "Cytokine that binds to TNFRSF6/FAS, a receptor that transduces the apoptotic signal into cells (PubMed:26334989, PubMed:9228058). Involved in cytotoxic T-cell-mediated apoptosis, natural killer cell-mediated apoptosis and in T-cell development (PubMed:7528780, PubMed:9228058, PubMed:9427603). Initiates fratricidal/suicidal activation-induced cell death (AICD) in antigen-activated T-cells contributing to the termination of immune responses (By similarity). TNFRSF6/FAS-mediated apoptosis also has a role in the induction of peripheral tolerance (By similarity). Binds to TNFRSF6B/DcR3, a decoy receptor that blocks apoptosis (PubMed:27806260)", "gene_name": "FASLG", "glycan_count": 1, "glycosylation_sites": [ { "position": 184, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 250, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 260, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P48023", "name": "Fas Ligand (FasL)", "organism": "Homo sapiens", "uniprot_id": "P48023" }, { "function": "Cytokine that binds to TNFRSF10A/TRAILR1, TNFRSF10B/TRAILR2, TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and possibly also to TNFRSF11B/OPG (PubMed:10549288, PubMed:26457518). Induces apoptosis. Its activity may be modulated by binding to the decoy receptors TNFRSF10C/TRAILR3, TNFRSF10D/TRAILR4 and TNFRSF11B/OPG that cannot induce apoptosis", "gene_name": "TNFSF10", "glycan_count": 0, "glycosylation_sites": [], "id": "P50591", "name": "TRAIL (TNFSF10)", "organism": "Homo sapiens", "uniprot_id": "P50591" }, { "function": "Receptor for the cytotoxic ligand TNFSF10/TRAIL (PubMed:10549288). The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis. Promotes the activation of NF-kappa-B. Essential for ER stress-induced apoptosis", "gene_name": "TNFRSF10B", "glycan_count": 2, "glycosylation_sites": [], "id": "O14763", "name": "DR5 (TRAIL-R2)", "organism": "Homo sapiens", "uniprot_id": "O14763" }, { "function": "Receptor for the cytotoxic ligand TNFSF10/TRAIL (PubMed:26457518, PubMed:38532423). The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis (PubMed:19090789). Promotes the activation of NF-kappa-B (PubMed:9430227)", "gene_name": "TNFRSF10A", "glycan_count": 4, "glycosylation_sites": [ { "position": 156, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O00220", "name": "DR4 (TRAIL-R1)", "organism": "Homo sapiens", "uniprot_id": "O00220" }, { "function": "Receptor for the C-X-C chemokine CXCL12/SDF-1 that transduces a signal by increasing intracellular calcium ion levels and enhancing MAPK1/MAPK3 activation (PubMed:10452968, PubMed:18799424, PubMed:24912431, PubMed:28978524). Involved in the AKT signaling cascade (PubMed:24912431). Plays a role in regulation of cell migration, e.g. during wound healing (PubMed:28978524). Acts as a receptor for extracellular ubiquitin; leading to enhanced intracellular calcium ions and reduced cellular cAMP levels (PubMed:20228059). Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11276205). Involved in hematopoiesis and in cardiac ventricular septum formation. Also plays an essential role in vascularization of the gastrointestinal tract, probably by regulating vascular branching and/or remodeling processes in endothelial cells. Involved in cerebellar development. In the CNS, could mediate hippocampal-neuron survival (By similarity)", "gene_name": "CXCR4", "glycan_count": 0, "glycosylation_sites": [ { "position": 11, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 18, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 176, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P61073", "name": "CXCR4", "organism": "Homo sapiens", "uniprot_id": "P61073" }, { "function": "Receptor for a number of inflammatory CC-chemokines including CCL3/MIP-1-alpha, CCL4/MIP-1-beta and RANTES and subsequently transduces a signal by increasing the intracellular calcium ion level. May play a role in the control of granulocytic lineage proliferation or differentiation. Participates in T-lymphocyte migration to the infection site by acting as a chemotactic receptor (PubMed:30713770)", "gene_name": "CCR5", "glycan_count": 0, "glycosylation_sites": [ { "position": 6, "type": "O-linked (GalNAc...) serine" }, { "position": 7, "type": "O-linked (GalNAc...) serine" } ], "id": "P51681", "name": "CCR5", "organism": "Homo sapiens", "uniprot_id": "P51681" }, { "function": "Costimulatory molecule that belongs to the immunoglobulin superfamily that plays an important role in T-lymphocyte activation (PubMed:38467718). Acts as the primary auxiliary signal augmenting the MHC/TCR signal in naive T-cells together with the CD28 receptor which is constitutively expressed on the cell surface of T-cells (PubMed:12196291). In turn, activates different signaling pathways such as NF-kappa-B or MAPK leading to the production of different cytokines (PubMed:10438913). In addition, CD28/CD80 costimulatory signal stimulates glucose metabolism and ATP synthesis of T-cells by activating the PI3K/Akt signaling pathway (PubMed:12121659). Also acts as a regulator of PDL1/PDCD1 interactions to limit excess engagement of PDL1 and its inhibitory role in immune responses (PubMed:36727298). Expressed on B-cells, plays a critical role in regulating interactions between B-cells and T-cells in both early and late germinal center responses, which are crucial for the generation of effective humoral immune responses (By similarity)", "gene_name": "CD80", "glycan_count": 2, "glycosylation_sites": [ { "position": 53, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 89, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 98, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 186, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 207, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 211, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 226, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 232, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P33681", "name": "CD80", "organism": "Homo sapiens", "uniprot_id": "P33681" }, { "function": "Receptor involved in the costimulatory signal essential for T-lymphocyte proliferation and interleukin-2 production, by binding CD28 or CTLA-4 (PubMed:12196291). May play a critical role in the early events of T-cell activation and costimulation of naive T-cells, such as deciding between immunity and anergy that is made by T-cells within 24 hours after activation (PubMed:7527824). Also involved in the regulation of B cells function, plays a role in regulating the level of IgG(1) produced. Upon CD40 engagement, activates NF-kappa-B signaling pathway via phospholipase C and protein kinase C activation (By similarity)", "gene_name": "CD86", "glycan_count": 0, "glycosylation_sites": [ { "position": 33, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 47, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 135, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 146, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 154, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 177, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 192, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 213, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P42081", "name": "CD86", "organism": "Homo sapiens", "uniprot_id": "P42081" }, { "function": "Most highly expressed siglec (sialic acid-binding immunoglobulin-like lectin) on B-cells that plays a role in various aspects of B-cell biology including differentiation, antigen presentation, and trafficking to bone marrow (PubMed:34330755, PubMed:8627166). Binds to alpha 2,6-linked sialic acid residues of surface molecules such as CD22 itself, CD45 and IgM in a cis configuration. Can also bind to ligands on other cells as an adhesion molecule in a trans configuration (PubMed:20172905). Acts as an inhibitory coreceptor on the surface of B-cells and inhibits B-cell receptor induced signaling, characterized by inhibition of the calcium mobilization and cellular activation. Mechanistically, the immunoreceptor tyrosine-based inhibitory motif domain is phosphorylated by the Src kinase LYN, which in turn leads to the recruitment of the protein tyrosine phosphatase 1/PTPN6, leading to the negative regulation of BCR signaling (PubMed:8627166). If this negative signaling from is of sufficient strength, apoptosis of the B-cell can be induced (PubMed:20516366)", "gene_name": "CD22", "glycan_count": 4, "glycosylation_sites": [ { "position": 67, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 101, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 112, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 135, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 164, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 231, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 363, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 445, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 479, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 574, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 634, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P20273", "name": "CD22", "organism": "Homo sapiens", "uniprot_id": "P20273" }, { "function": "May act as a modulatory subunit rather than a functional channel. Unlike other P2XRs members, P2RX6 does not seem to form functional homotrimers (PubMed:22378790). P2RX6 requires the presence of P2RX4 or P2RX2 to shuttle it to the plasma membrane where it may form functional heterotrimeric receptors at the plasma membrane (PubMed:22378790). P2RX6 can be translocated to the nucleus and functions as a nuclear regulator of post-transcriptional modifications in neurons (By similarity)", "gene_name": "P2RX6", "glycan_count": 2, "glycosylation_sites": [ { "position": 165, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 195, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 210, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O15547", "name": "CD138", "organism": "Homo sapiens", "uniprot_id": "O15547" }, { "function": "Costimulatory immune-checkpoint receptor expressed at the surface of T-cells, NK-cells and B-cells which binds to and is activated by its ligand CD70/CD27L expressed by B-cells (PubMed:28011863). The CD70-CD27 signaling pathway mediates antigen-specific T-cell activation and expansion which in turn provides immune surveillance of B-cells (PubMed:28011863). Mechanistically, CD70 ligation activates the TRAF2-PTPN6 axis that subsequently inhibits LCK phosphorylation to promote phenotypic and transcriptional adaptations of T-cell memory (PubMed:38354704). In addition, activation by CD70 on early progenitor cells provides a negative feedback signal to leukocyte differentiation during immune activation and thus modulates hematopoiesis (By similarity). Negatively regulates the function of Th2 lymphocytes in the adipose tissue (By similarity)", "gene_name": "CD27", "glycan_count": 5, "glycosylation_sites": [ { "position": 95, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 127, "type": "O-linked (GalNAc...) serine" } ], "id": "P26842", "name": "CD27", "organism": "Homo sapiens", "uniprot_id": "P26842" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04745", "name": "Alpha-amylase", "organism": "", "uniprot_id": "P04745" }, { "function": "Chemotactic activity for lymphocytes but not for monocytes or neutrophils", "gene_name": "XCL2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UBD3", "name": "Mucin-7 (MUC7)", "organism": "Homo sapiens", "uniprot_id": "Q9UBD3" }, { "function": "Strongly inhibits glucose induced insulin release from the pancreas", "gene_name": "CHGA", "glycan_count": 8, "glycosylation_sites": [ { "position": 181, "type": "O-linked (GalNAc...) threonine" }, { "position": 183, "type": "O-linked (GalNAc...) threonine" }, { "position": 251, "type": "O-linked (GalNAc...) threonine" }, { "position": 424, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" } ], "id": "P10645", "name": "Chromogranin A", "organism": "Homo sapiens", "uniprot_id": "P10645" }, { "function": "Possibly involved in structural functions as organizing other membrane components or in targeting the vesicles to the plasma membrane. Involved in the regulation of short-term and long-term synaptic plasticity (By similarity)", "gene_name": "SYP", "glycan_count": 0, "glycosylation_sites": [ { "position": 59, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08247", "name": "Synaptophysin", "organism": "Homo sapiens", "uniprot_id": "P08247" }, { "function": "Calcitonin is a peptide hormone that causes a rapid but short-lived drop in the level of calcium and phosphate in blood by promoting the incorporation of those ions in the bones. Calcitonin function is mediated by the calcitonin receptor/CALCR and the CALCR-RAMP2 (AMYR2) receptor complex (PubMed:35324283)", "gene_name": "CALCA", "glycan_count": 1, "glycosylation_sites": [], "id": "P01258", "name": "Calcitonin", "organism": "Homo sapiens", "uniprot_id": "P01258" }, { "function": "Lymphoid-specific receptor expressed by all T-cells and in a subset of B-cells known as B1a cells. Plays a role in the regulation of TCR and BCR signaling, thymocyte selection, T-cell effector differentiation and immune tolerance. Acts by interacting with several ligands expressed on B-cells such as CD5L or CD72 and thereby plays an important role in contact-mediated, T-dependent B-cell activation and in the maintenance of regulatory T and B-cell homeostasis. Functions as a negative regulator of TCR signaling during thymocyte development by associating with several signaling proteins including LCK, CD3Z chain, PI3K or CBL (PubMed:1384049, PubMed:1385158). Mechanistically, co-engagement of CD3 with CD5 enhances phosphorylated CBL recruitment leading to increased VAV1 phosphorylation and degradation (PubMed:23376399). Modulates B-cell biology through ERK1/2 activation in a Ca(2+)-dependent pathway via the non-selective Ca(2+) channel TRPC1, leading to IL-10 production (PubMed:27499044)", "gene_name": "CD5", "glycan_count": 9, "glycosylation_sites": [ { "position": 116, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 241, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P06127", "name": "T-cell surface glycoprotein CD5", "organism": "Homo sapiens", "uniprot_id": "P06127" }, { "function": "In response to the presence of allergens, this protein directly promotes the accumulation of eosinophils, a prominent feature of allergic inflammatory reactions (PubMed:8597956). Binds to CCR3 (PubMed:8631813)", "gene_name": "CCL11", "glycan_count": 1, "glycosylation_sites": [ { "position": 94, "type": "O-linked (GalNAc...) threonine" } ], "id": "P51671", "name": "Eotaxin (CCL11)", "organism": "Homo sapiens", "uniprot_id": "P51671" }, { "function": "Mediates apoptosis and actin stress fiber dissolution", "gene_name": "SLK", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H2G2", "name": "CUB domain-containing protein 1", "organism": "Homo sapiens", "uniprot_id": "Q9H2G2" }, { "function": "Neurotrophic factor that enhances survival and morphological differentiation of dopaminergic neurons and increases their high-affinity dopamine uptake (PubMed:8493557). Acts by binding to its coreceptor, GFRA1, leading to autophosphorylation and activation of the RET receptor (PubMed:10829012, PubMed:25242331, PubMed:31535977). Involved in the development of the neural crest (PubMed:15242795)", "gene_name": "GDNF", "glycan_count": 0, "glycosylation_sites": [ { "position": 126, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 162, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P39905", "name": "Glial cell line-derived neurotrophic factor (GDNF)", "organism": "Homo sapiens", "uniprot_id": "P39905" }, { "function": "Core component of the complement C1 complex, a multiprotein complex that initiates the classical pathway of the complement system, a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system (PubMed:12847249, PubMed:19006321, PubMed:24626930, PubMed:29449492, PubMed:3258649, PubMed:34155115, PubMed:6249812, PubMed:6776418). The classical complement pathway is initiated by the C1Q subcomplex of the C1 complex, which specifically binds IgG or IgM immunoglobulins complexed with antigens, forming antigen-antibody complexes on the surface of pathogens: C1QA, together with C1QB and C1QC, specifically recognizes and binds the Fc regions of IgG or IgM via its C1q domain (PubMed:12847249, PubMed:19006321, PubMed:24626930, PubMed:29449492, PubMed:3258649, PubMed:6776418). Immunoglobulin-binding activates the proenzyme C1R, which cleaves C1S, initiating the proteolytic cascade of the complement system (PubMed:29449492). The C1Q subcomplex is activated by a hexamer of IgG complexed with antigens, while it is activated by a pentameric IgM (PubMed:19706439, PubMed:24626930, PubMed:29449492). The C1Q subcomplex also recognizes and binds phosphatidylserine exposed on the surface of cells undergoing programmed cell death, possibly promoting activation of the complement system (PubMed:18250442)", "gene_name": "C1QA", "glycan_count": 47, "glycosylation_sites": [ { "position": 33, "type": "O-linked (Gal...) hydroxylysine" }, { "position": 48, "type": "O-linked (Gal...) hydroxylysine" }, { "position": 67, "type": "O-linked (Gal...) hydroxylysine" }, { "position": 100, "type": "O-linked (Gal...) hydroxylysine" }, { "position": 146, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P02745", "name": "C1q", "organism": "Homo sapiens", "uniprot_id": "P02745" }, { "function": "Component of the E3 ubiquitin ligase DCX DET1-COP1 complex, which is required for ubiquitination and subsequent degradation of target proteins. The complex is involved in JUN ubiquitination and degradation", "gene_name": "DET1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q7L5Y6", "name": "Neonatal Fc receptor (FcRn)", "organism": "Homo sapiens", "uniprot_id": "Q7L5Y6" }, { "function": "Part of the receptor for interleukin 6. Binds to IL6 with low affinity, but does not transduce a signal (PubMed:28265003). Signal activation necessitate an association with IL6ST. Activation leads to the regulation of the immune response, acute-phase reactions and hematopoiesis (PubMed:30995492, PubMed:31235509). The interaction with membrane-bound IL6R and IL6ST stimulates 'classic signaling', the restricted expression of the IL6R limits classic IL6 signaling to only a few tissues such as the liver and some cells of the immune system. Whereas the binding of IL6 and soluble IL6R to IL6ST stimulates 'trans-signaling'. Alternatively, 'cluster signaling' occurs when membrane-bound IL6:IL6R complexes on transmitter cells activate IL6ST receptors on neighboring receiver cells (Probable)", "gene_name": "IL6R", "glycan_count": 6, "glycosylation_sites": [ { "position": 55, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 93, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 221, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 245, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 350, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 352, "type": "O-linked (GlcNAc) threonine" } ], "id": "P08887", "name": "Interleukin-6 receptor (IL-6R)", "organism": "Homo sapiens", "uniprot_id": "P08887" }, { "function": "Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41", "gene_name": "env", "glycan_count": 0, "glycosylation_sites": [ { "position": 87, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 135, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 141, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 153, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 157, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 183, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 194, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 238, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 259, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 273, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 286, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 298, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 328, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 335, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 351, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 381, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 387, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 395, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 401, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 436, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 599, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 604, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 613, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 625, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 662, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "Q75008", "name": "Envelope glycoprotein (gp120)", "organism": "Human immunodeficiency virus type 1 group M subtype C (isolate ETH2220)", "uniprot_id": "Q75008" }, { "function": "Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). Gag-Pol polyprotein may regulate its own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, the polyprotein would promote translation, whereas at high concentration, the polyprotein would encapsidate genomic RNA and then shut off translation", "gene_name": "gag-pol", "glycan_count": 0, "glycosylation_sites": [], "id": "Q75002", "name": "Protease", "organism": "Human immunodeficiency virus type 1 group M subtype C (isolate ETH2220)", "uniprot_id": "Q75002" }, { "function": "Receptor for cholecystokinin. Mediates pancreatic growth and enzyme secretion, smooth muscle contraction of the gall bladder and stomach. Has a 1000-fold higher affinity for CCK rather than for gastrin. It modulates feeding and dopamine-induced behavior in the central and peripheral nervous system. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system", "gene_name": "CCKAR", "glycan_count": 0, "glycosylation_sites": [ { "position": 10, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 24, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 190, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P32238", "name": "Cholecystokinin receptor (CCK-1)", "organism": "Homo sapiens", "uniprot_id": "P32238" }, { "function": "Involved in the suppression of bile acid biosynthesis through down-regulation of CYP7A1 expression, following positive regulation of the JNK and ERK1/2 cascades. Stimulates glucose uptake in adipocytes. Activity requires the presence of KLB and FGFR4", "gene_name": "FGF19", "glycan_count": 0, "glycosylation_sites": [], "id": "O95750", "name": "Fibroblast growth factor 19 (FGF19)", "organism": "Homo sapiens", "uniprot_id": "O95750" }, { "function": "A cytochrome P450 monooxygenase involved in the metabolism of endogenous cholesterol and its oxygenated derivatives (oxysterols) (PubMed:11013305, PubMed:12077124, PubMed:19965590, PubMed:21813643, PubMed:2384150). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase) (PubMed:11013305, PubMed:12077124, PubMed:19965590, PubMed:21813643, PubMed:2384150). Functions as a critical regulatory enzyme of bile acid biosynthesis and cholesterol homeostasis. Catalyzes the hydroxylation of carbon hydrogen bond at 7-alpha position of cholesterol, a rate-limiting step in cholesterol catabolism and bile acid biosynthesis (PubMed:12077124, PubMed:19965590, PubMed:2384150). 7-alpha hydroxylates several oxysterols, including 4beta-hydroxycholesterol and 24-hydroxycholesterol (PubMed:11013305, PubMed:12077124). Catalyzes the oxidation of the 7,8 double bond of 7-dehydrocholesterol and lathosterol with direct and predominant formation of the 7-keto derivatives (PubMed:21813643)", "gene_name": "CYP7A1", "glycan_count": 0, "glycosylation_sites": [], "id": "P22680", "name": "Cholesterol 7-alpha hydroxylase (CYP7A1)", "organism": "Homo sapiens", "uniprot_id": "P22680" }, { "function": "Acts as a chaperone that facilitates biogenesis and trafficking of functional transporters heterodimers to the plasma membrane. Forms heterodimer with SLC7 family transporters (SLC7A5, SLC7A6, SLC7A7, SLC7A8, SLC7A10 and SLC7A11), a group of amino-acid antiporters (PubMed:10574970, PubMed:10903140, PubMed:11557028, PubMed:30867591, PubMed:33298890, PubMed:33758168, PubMed:34880232, PubMed:9751058, PubMed:9829974, PubMed:9878049). Heterodimers function as amino acids exchangers, the specificity of the substrate depending on the SLC7A subunit. Heterodimers SLC3A2/SLC7A6 or SLC3A2/SLC7A7 mediate the uptake of dibasic amino acids (PubMed:10903140, PubMed:9829974). Heterodimer SLC3A2/SLC7A11 functions as an antiporter by mediating the exchange of extracellular anionic L-cystine and intracellular L-glutamate across the cellular plasma membrane (PubMed:34880232). SLC3A2/SLC7A10 translocates small neutral L- and D-amino acids across the plasma membrane (By similarity). SLC3A2/SLC75 or SLC3A2/SLC7A8 translocates neutral amino acids with broad specificity, thyroid hormones and L-DOPA (PubMed:10574970, PubMed:11389679, PubMed:11557028, PubMed:11564694, PubMed:11742812, PubMed:12117417, PubMed:12225859, PubMed:12716892, PubMed:15980244, PubMed:30867591, PubMed:33298890, PubMed:33758168). SLC3A2 is essential for plasma membrane localization, stability, and the transport activity of SLC7A5 and SLC7A8 (PubMed:10391915, PubMed:10574970, PubMed:11311135, PubMed:15769744, PubMed:33066406). When associated with LAPTM4B, the heterodimer SLC7A5 is recruited to lysosomes to promote leucine uptake into these organelles, and thereby mediates mTORC1 activation (PubMed:25998567). Modulates integrin-related signaling and is essential for integrin-dependent cell spreading, migration and tumor progression (PubMed:11121428, PubMed:15625115)", "gene_name": "SLC3A2", "glycan_count": 148, "glycosylation_sites": [ { "position": 365, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 381, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 424, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 506, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08195", "name": "CD98hc (SLC3A2)", "organism": "Homo sapiens", "uniprot_id": "P08195" }, { "function": "Beta-galactoside-binding lectin that acts as a sensor of membrane damage caused by infection and restricts the proliferation of infecting pathogens by targeting them for autophagy (PubMed:22246324, PubMed:28077878). Detects membrane rupture by binding beta-galactoside ligands located on the lumenal side of the endosome membrane; these ligands becoming exposed to the cytoplasm following rupture (PubMed:22246324, PubMed:28077878). Restricts infection by initiating autophagy via interaction with CALCOCO2/NDP52 (PubMed:22246324, PubMed:28077878). Required to restrict infection of bacterial invasion such as S.typhimurium (PubMed:22246324). Also required to restrict infection of Picornaviridae viruses (PubMed:28077878). Has a marked preference for 3'-O-sialylated and 3'-O-sulfated glycans (PubMed:21288902)", "gene_name": "LGALS8", "glycan_count": 0, "glycosylation_sites": [], "id": "O00214", "name": "Galectin-8 (Gal-8)", "organism": "Homo sapiens", "uniprot_id": "O00214" }, { "function": "Cell adhesion molecule that mediates both heterotypic cell-cell contacts via its interaction with CD6, as well as homotypic cell-cell contacts (PubMed:15048703, PubMed:15496415, PubMed:16352806, PubMed:23169771, PubMed:24945728, PubMed:7760007). Promotes T-cell activation and proliferation via its interactions with CD6 (PubMed:15048703, PubMed:16352806, PubMed:24945728). Contributes to the formation and maturation of the immunological synapse via its interactions with CD6 (PubMed:15294938, PubMed:16352806). Mediates homotypic interactions with cells that express ALCAM (PubMed:15496415, PubMed:16352806). Acts as a ligand for the LILRB4 receptor, enhancing LILRB4-mediated inhibition of T cell proliferation (PubMed:29263213). Required for normal hematopoietic stem cell engraftment in the bone marrow (PubMed:24740813). Mediates attachment of dendritic cells onto endothelial cells via homotypic interaction (PubMed:23169771). Inhibits endothelial cell migration and promotes endothelial tube formation via homotypic interactions (PubMed:15496415, PubMed:23169771). Required for normal organization of the lymph vessel network. Required for normal hematopoietic stem cell engraftment in the bone marrow. Plays a role in hematopoiesis; required for normal numbers of hematopoietic stem cells in bone marrow. Promotes in vitro osteoblast proliferation and differentiation (By similarity). Promotes neurite extension, axon growth and axon guidance; axons grow preferentially on surfaces that contain ALCAM. Mediates outgrowth and pathfinding for retinal ganglion cell axons (By similarity)", "gene_name": "ALCAM", "glycan_count": 163, "glycosylation_sites": [ { "position": 91, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 95, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 167, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 265, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 306, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 361, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 457, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 480, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 499, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13740", "name": "CD166 (ALCAM)", "organism": "Homo sapiens", "uniprot_id": "Q13740" }, { "function": "Mediates effects on cell migration and adhesion through its different partners. During development plays a role in blood and lymphatic vessels separation by binding CLEC1B, triggering CLEC1B activation in platelets and leading to platelet activation and/or aggregation (PubMed:14522983, PubMed:15231832, PubMed:17222411, PubMed:17616532, PubMed:18215137). Interaction with CD9, on the contrary, attenuates platelet aggregation induced by PDPN (PubMed:18541721). Through MSN or EZR interaction promotes epithelial-mesenchymal transition (EMT) leading to ERZ phosphorylation and triggering RHOA activation leading to cell migration increase and invasiveness (PubMed:17046996, PubMed:21376833). Interaction with CD44 promotes directional cell migration in epithelial and tumor cells (PubMed:20962267). In lymph nodes (LNs), controls fibroblastic reticular cells (FRCs) adhesion to the extracellular matrix (ECM) and contraction of the actomyosin by maintaining ERM proteins (EZR; MSN and RDX) and MYL9 activation through association with unknown transmembrane proteins. Engagement of CLEC1B by PDPN promotes FRCs relaxation by blocking lateral membrane interactions leading to reduction of ERM proteins (EZR; MSN and RDX) and MYL9 activation (By similarity). Through binding with LGALS8 may participate in connection of the lymphatic endothelium to the surrounding extracellular matrix (PubMed:19268462). In keratinocytes, induces changes in cell morphology showing an elongated shape, numerous membrane protrusions, major reorganization of the actin cytoskeleton, increased motility and decreased cell adhesion (PubMed:15515019). Controls invadopodia stability and maturation leading to efficient degradation of the extracellular matrix (ECM) in tumor cells through modulation of RHOC activity in order to activate ROCK1/ROCK2 and LIMK1/LIMK2 and inactivation of CFL1 (PubMed:25486435). Required for normal lung cell proliferation and alveolus formation at birth (By similarity). Does not function as a water channel or as a regulator of aquaporin-type water channels (PubMed:9651190). Does not have any effect on folic acid or amino acid transport (By similarity)", "gene_name": "PDPN", "glycan_count": 6, "glycosylation_sites": [ { "position": 25, "type": "O-linked (GalNAc...) threonine" }, { "position": 32, "type": "O-linked (GalNAc...) threonine" }, { "position": 34, "type": "O-linked (GalNAc...) threonine" }, { "position": 35, "type": "O-linked (GalNAc...) threonine" }, { "position": 52, "type": "O-linked (GalNAc...) threonine" }, { "position": 55, "type": "O-linked (GalNAc...) threonine" }, { "position": 65, "type": "O-linked (GalNAc...) threonine" }, { "position": 66, "type": "O-linked (GalNAc...) threonine" }, { "position": 76, "type": "O-linked (GalNAc...) threonine" }, { "position": 85, "type": "O-linked (GalNAc...) threonine" }, { "position": 86, "type": "O-linked (GalNAc...) serine" }, { "position": 88, "type": "O-linked (GalNAc...) serine" }, { "position": 89, "type": "O-linked (GalNAc...) threonine" }, { "position": 96, "type": "O-linked (GalNAc...) serine" }, { "position": 98, "type": "O-linked (GalNAc...) serine" }, { "position": 100, "type": "O-linked (GalNAc...) threonine" }, { "position": 102, "type": "O-linked (GalNAc...) serine" }, { "position": 106, "type": "O-linked (GalNAc...) threonine" }, { "position": 107, "type": "O-linked (GalNAc...) serine" }, { "position": 109, "type": "O-linked (GalNAc...) serine" }, { "position": 110, "type": "O-linked (GalNAc...) threonine" }, { "position": 117, "type": "O-linked (GalNAc...) threonine" }, { "position": 119, "type": "O-linked (GalNAc...) threonine" }, { "position": 120, "type": "O-linked (GalNAc...) threonine" } ], "id": "Q86YL7", "name": "Podoplanin (PDPN)", "organism": "Homo sapiens", "uniprot_id": "Q86YL7" }, { "function": "Has neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons. Binds, in a calcium-dependent manner, to cultured neocortical neurons and promotes cell survival", "gene_name": "Eno2", "glycan_count": 1, "glycosylation_sites": [], "id": "P07323", "name": "Neuron-specific enolase (NSE)", "organism": "Rattus norvegicus", "uniprot_id": "P07323" }, { "function": "Involved in the organization of myofibers. Together with KRT8, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle", "gene_name": "KRT19", "glycan_count": 1, "glycosylation_sites": [], "id": "P08727", "name": "Cytokeratin-19-fragment (CYFRA21-1)", "organism": "Homo sapiens", "uniprot_id": "P08727" }, { "function": "Key downstream component of the canonical Wnt signaling pathway (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22155184, PubMed:22647378, PubMed:22699938). In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22155184, PubMed:22647378, PubMed:22699938). In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes (PubMed:17524503, PubMed:18077326, PubMed:18086858, PubMed:18957423, PubMed:21262353, PubMed:22155184, PubMed:22647378, PubMed:22699938). Also acts as a coactivator for other transcription factors, such as NR5A2 (PubMed:22187462). Promotes epithelial to mesenchymal transition/mesenchymal to epithelial transition (EMT/MET) via driving transcription of CTNNB1/TCF-target genes (PubMed:29910125). Involved in the regulation of cell adhesion, as component of an E-cadherin:catenin adhesion complex (By similarity). Acts as a negative regulator of centrosome cohesion (PubMed:18086858). Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization (PubMed:21262353). Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2 (PubMed:18957423). Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML (PubMed:22155184). Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle (By similarity). Involved in chondrocyte differentiation via interaction with SOX9: SOX9-binding competes with the binding sites of TCF/LEF within CTNNB1, thereby inhibiting the Wnt signaling (By similarity). Acts as a positive regulator of odontoblast differentiation during mesenchymal tooth germ formation, via promoting the transcription of differentiation factors such as LEF1, BMP2 and BMP4 (By similarity). Activity is repressed in a MSX1-mediated manner at the bell stage of mesenchymal tooth germ formation which prevents premature differentiation of odontoblasts (By similarity)", "gene_name": "CTNNB1", "glycan_count": 2, "glycosylation_sites": [ { "position": 23, "type": "O-linked (GlcNAc) serine; alternate" } ], "id": "P35222", "name": "\u03b2-catenin", "organism": "Homo sapiens", "uniprot_id": "P35222" }, { "function": "Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration. Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells. Associates with both microtubules and actin filaments, components of the cytoskeleton (PubMed:17293347). Plays a role in mediating the organization of F-actin into ordered bundles (PubMed:17293347). Functions downstream of Rho GTPases and DIAPH1 to selectively stabilize microtubules (By similarity). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization", "gene_name": "APC", "glycan_count": 4, "glycosylation_sites": [], "id": "P25054", "name": "APC", "organism": "Homo sapiens", "uniprot_id": "P25054" }, { "function": "Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD2/SMAD4 complex, activates transcription. Promotes TGFB1-mediated transcription of odontoblastic differentiation genes in dental papilla cells (By similarity). Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator. May act as a tumor suppressor in colorectal carcinoma (PubMed:8752209)", "gene_name": "SMAD2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q15796", "name": "SMAD2", "organism": "Homo sapiens", "uniprot_id": "Q15796" }, { "function": "In muscle physiology, plays a central role in the balance between atrophy and hypertrophy. When recruited by MSTN, promotes atrophy response via phosphorylated SMAD2/4. MSTN decrease causes SMAD4 release and subsequent recruitment by the BMP pathway to promote hypertrophy via phosphorylated SMAD1/5/8. Acts synergistically with SMAD1 and YY1 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression. Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions (By similarity). Common SMAD (co-SMAD) is the coactivator and mediator of signal transduction by TGF-beta (transforming growth factor). Component of the heterotrimeric SMAD2/SMAD3-SMAD4 complex that forms in the nucleus and is required for the TGF-mediated signaling (PubMed:25514493). Promotes binding of the SMAD2/SMAD4/FAST-1 complex to DNA and provides an activation function required for SMAD1 or SMAD2 to stimulate transcription. Component of the multimeric SMAD3/SMAD4/JUN/FOS complex which forms at the AP1 promoter site; required for synergistic transcriptional activity in response to TGF-beta. May act as a tumor suppressor. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator", "gene_name": "SMAD4", "glycan_count": 1, "glycosylation_sites": [], "id": "Q13485", "name": "SMAD4", "organism": "Homo sapiens", "uniprot_id": "Q13485" }, { "function": "Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility (PubMed:15386022, PubMed:16359901, PubMed:16714294, PubMed:21772249, PubMed:25355358, PubMed:26151332, PubMed:27827373). The complex composed of RNF2, UB2D3 and BMI1 binds nucleosomes, and has activity only with nucleosomal histone H2A (PubMed:21772249, PubMed:25355358). In the PRC1-like complex, regulates the E3 ubiquitin-protein ligase activity of RNF2/RING2 (PubMed:15386022, PubMed:21772249, PubMed:26151332)", "gene_name": "BMI1", "glycan_count": 1, "glycosylation_sites": [], "id": "P35226", "name": "BMI1", "organism": "Homo sapiens", "uniprot_id": "P35226" }, { "function": "Can hydrolyze NAD but cannot hydrolyze nucleotide di- and triphosphates (PubMed:28898552). Lacks lysopholipase D activity. May play a role in neuronal cell communication (By similarity)", "gene_name": "Enpp5", "glycan_count": 6, "glycosylation_sites": [ { "position": 101, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 158, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 292, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 329, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 362, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 369, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 382, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 389, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9EQG7", "name": "Patatin-like phospholipase domain-containing protein 3 (PNPLA3)", "organism": "Mus musculus", "uniprot_id": "Q9EQG7" }, { "function": "Adhesive protein that mediates cell-to-cell interactions (PubMed:11509594, PubMed:15383453). Acts as a receptor for thrombospondin THBS1 and as modulator of integrin signaling through the activation of heterotrimeric G proteins (PubMed:19004835, PubMed:7691831, PubMed:8550562). Involved in signal transduction, cardiovascular homeostasis, inflammation, apoptosis, angiogenesis, cellular self-renewal, and immunoregulation (PubMed:11509594, PubMed:15383453, PubMed:19004835, PubMed:27742621, PubMed:32679764, PubMed:7691831, PubMed:8550562). Plays a role in modulating pulmonary endothelin EDN1 signaling (PubMed:27742621). Modulates nitrous oxide (NO) signaling, in response to THBS1, hence playing a role as a pressor agent, supporting blood pressure (By similarity). Plays an important role in memory formation and synaptic plasticity in the hippocampus (By similarity). Receptor for SIRPA, binding to which prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells (PubMed:11509594). Interaction with SIRPG mediates cell-cell adhesion, enhances superantigen-dependent T-cell-mediated proliferation and costimulates T-cell activation (PubMed:15383453). Positively modulates FAS-dependent apoptosis in T-cells, perhaps by enhancing FAS clustering (By similarity). Plays a role in suppressing angiogenesis and may be involved in metabolic dysregulation during normal aging (PubMed:32679764). In response to THBS1, negatively modulates wound healing (By similarity). Inhibits stem cell self-renewal, in response to THBS1, probably by regulation of the stem cell transcription factors POU5F1/OCT4, SOX2, MYC/c-Myc and KLF4 (By similarity). May play a role in membrane transport and/or integrin dependent signal transduction (PubMed:7691831). May prevent premature elimination of red blood cells (By similarity)", "gene_name": "CD47", "glycan_count": 86, "glycosylation_sites": [ { "position": 23, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 34, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 50, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 73, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 111, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 206, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q08722", "name": "CD47", "organism": "Homo sapiens", "uniprot_id": "Q08722" }, { "function": "E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degradation by the proteasome (PubMed:29681526). Inhibits p53/TP53- and p73/TP73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Also acts as a ubiquitin ligase E3 toward itself and ARRB1. Permits the nuclear export of p53/TP53. Promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma RB1 protein. Inhibits DAXX-mediated apoptosis by inducing its ubiquitination and degradation. Component of the TRIM28/KAP1-MDM2-p53/TP53 complex involved in stabilizing p53/TP53. Also a component of the TRIM28/KAP1-ERBB4-MDM2 complex which links growth factor and DNA damage response pathways. Mediates ubiquitination and subsequent proteasome degradation of DYRK2 in nucleus. Ubiquitinates IGF1R and SNAI1 and promotes them to proteasomal degradation (PubMed:12821780, PubMed:15053880, PubMed:15195100, PubMed:15632057, PubMed:16337594, PubMed:17290220, PubMed:19098711, PubMed:19219073, PubMed:19837670, PubMed:19965871, PubMed:20173098, PubMed:20385133, PubMed:20858735, PubMed:22128911). Ubiquitinates DCX, leading to DCX degradation and reduction of the dendritic spine density of olfactory bulb granule cells (By similarity). Ubiquitinates DLG4, leading to proteasomal degradation of DLG4 which is required for AMPA receptor endocytosis (By similarity). Negatively regulates NDUFS1, leading to decreased mitochondrial respiration, marked oxidative stress, and commitment to the mitochondrial pathway of apoptosis (PubMed:30879903). Binds NDUFS1 leading to its cytosolic retention rather than mitochondrial localization resulting in decreased supercomplex assembly (interactions between complex I and complex III), decreased complex I activity, ROS production, and apoptosis (PubMed:30879903)", "gene_name": "MDM2", "glycan_count": 3, "glycosylation_sites": [], "id": "Q00987", "name": "MDM2", "organism": "Homo sapiens", "uniprot_id": "Q00987" }, { "function": "Cytokine that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes", "gene_name": "CSF2", "glycan_count": 1, "glycosylation_sites": [ { "position": 22, "type": "O-linked (GalNAc...) serine" }, { "position": 24, "type": "O-linked (GalNAc...) serine" }, { "position": 26, "type": "O-linked (GalNAc...) serine" }, { "position": 27, "type": "O-linked (GalNAc...) threonine; partial" }, { "position": 44, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 54, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P04141", "name": "Granulocyte-macrophage colony-stimulating factor (GM-CSF)", "organism": "Homo sapiens", "uniprot_id": "P04141" }, { "function": "Involved in cell-cell adhesion. Has both calcium-independent homophilic cell-cell adhesion activity and calcium-independent heterophilic cell-cell adhesion activity with IGSF4, NECTIN1 and NECTIN3. Interaction with EPB41L1 may regulate structure or function of cell-cell junctions (By similarity)", "gene_name": "CADM3", "glycan_count": 4, "glycosylation_sites": [ { "position": 290, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8N126", "name": "Krebs von den Lungen-6 (KL-6)", "organism": "Homo sapiens", "uniprot_id": "Q8N126" }, { "function": "", "gene_name": "MRPL57", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9BQC6", "name": "Threonyl-tRNA synthetase (PL-7)", "organism": "Homo sapiens", "uniprot_id": "Q9BQC6" }, { "function": "Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797). Positively regulates dimethylation of two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 18S rRNA (PubMed:25851604)", "gene_name": "PNO1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NRX1", "name": "SERINC5", "organism": "Homo sapiens", "uniprot_id": "Q9NRX1" }, { "function": "DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms (PubMed:12808465, PubMed:16527742, PubMed:17121840, PubMed:18288108, PubMed:18849968, PubMed:19153609, PubMed:21123384, PubMed:22791714, PubMed:25542899). Exhibits potent antiviral activity against Vif-deficient HIV-1 (PubMed:12167863, PubMed:12859895, PubMed:14557625, PubMed:20219927, PubMed:21835787, PubMed:22807680, PubMed:22915799, PubMed:23097438, PubMed:23152537, PubMed:31397674). After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA (PubMed:12808465, PubMed:12808466, PubMed:12809610, PubMed:12970355, PubMed:14528300, PubMed:22807680). The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells (PubMed:12808465, PubMed:12808466, PubMed:12809610, PubMed:12970355, PubMed:14528300). Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA (PubMed:12808465, PubMed:12809610, PubMed:12970355, PubMed:14528300). Exhibits antiviral activity also against simian immunodeficiency viruses (SIVs), hepatitis B virus (HBV), equine infectious anemia virus (EIAV), xenotropic MuLV-related virus (XMRV) and simian foamy virus (SFV) (PubMed:15031497, PubMed:16378963, PubMed:18448976, PubMed:19458006, PubMed:20335265). May inhibit the mobility of LTR and non-LTR retrotransposons (PubMed:16527742)", "gene_name": "APOBEC3G", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9HC16", "name": "APOBEC3G", "organism": "Homo sapiens", "uniprot_id": "Q9HC16" }, { "function": "CD2 interacts with lymphocyte function-associated antigen CD58 (LFA-3) and CD48/BCM1 to mediate adhesion between T-cells and other cell types. CD2 is implicated in the triggering of T-cells, the cytoplasmic domain is implicated in the signaling function", "gene_name": "CD2", "glycan_count": 20, "glycosylation_sites": [ { "position": 89, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 141, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 150, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P06729", "name": "CD2", "organism": "Homo sapiens", "uniprot_id": "P06729" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P27958 (E1), P27958 (E2)", "name": "E1E2 glycoprotein heterodimer", "organism": "", "uniprot_id": "" }, { "function": "Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (PubMed:18033802). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity) (PubMed:23799612). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (PubMed:11086025, PubMed:17881511). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (PubMed:14602201). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (PubMed:14602201)", "gene_name": "", "glycan_count": 14, "glycosylation_sites": [ { "position": 196, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 209, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 234, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 305, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 417, "type": "N-linked (GlcNAc...) (high mannose) asparagine; by host" }, { "position": 423, "type": "N-linked (GlcNAc...) (high mannose) asparagine; by host" }, { "position": 430, "type": "N-linked (GlcNAc...) (high mannose) asparagine; by host" }, { "position": 448, "type": "N-linked (GlcNAc...) (high mannose) asparagine; by host" }, { "position": 476, "type": "N-linked (GlcNAc...) (high mannose) asparagine; by host" }, { "position": 532, "type": "N-linked (GlcNAc...) (high mannose) asparagine; by host" }, { "position": 540, "type": "N-linked (GlcNAc...) (high mannose) asparagine; by host" }, { "position": 556, "type": "N-linked (GlcNAc...) (high mannose) asparagine; by host" }, { "position": 576, "type": "N-linked (GlcNAc...) (high mannose) asparagine; by host" }, { "position": 623, "type": "N-linked (GlcNAc...) (high mannose) asparagine; by host" }, { "position": 645, "type": "N-linked (GlcNAc...) (high mannose) asparagine; by host" } ], "id": "P27958", "name": "E2 glycoprotein", "organism": "Hepatitis C virus genotype 1a (isolate H77)", "uniprot_id": "P27958" }, { "function": "Involved in cell growth. Activates CDK2, a kinase involved in the control of the cell cycle, by phosphorylating residue 'Thr-160' (By similarity). Required for high-level Shh responses in the developing neural tube. Together with TBC1D32, controls the structure of the primary cilium by coordinating assembly of the ciliary membrane and axoneme, allowing GLI2 to be properly activated in response to SHH signaling", "gene_name": "Cdk20", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9JHU3", "name": "G glycoprotein (BRSV)", "organism": "Mus musculus", "uniprot_id": "Q9JHU3" }, { "function": "", "gene_name": "Palmd", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9JHU2", "name": "F protein (BRSV)", "organism": "Mus musculus", "uniprot_id": "Q9JHU2" }, { "function": "Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection", "gene_name": "S", "glycan_count": 0, "glycosylation_sites": [ { "position": 31, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 60, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 134, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 192, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 357, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 435, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 536, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 568, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 576, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 599, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 648, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 665, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 804, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1091, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1101, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1120, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1136, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1157, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P11225", "name": "HN glycoprotein (BPIV3)", "organism": "Murine coronavirus (strain JHM)", "uniprot_id": "P11225" }, { "function": "Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. Interacts with murine CEACAM1 to mediate viral entry", "gene_name": "S", "glycan_count": 0, "glycosylation_sites": [ { "position": 31, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 60, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 192, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 357, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 435, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 530, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 625, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 657, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 665, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 688, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 737, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 754, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 893, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1180, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1190, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1209, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1225, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1246, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P11224", "name": "F protein (BPIV3)", "organism": "Murine coronavirus (strain A59)", "uniprot_id": "P11224" }, { "function": "Serine/threonine kinase that plays an essential role in regulating inflammatory responses to foreign agents (PubMed:10581243, PubMed:11839743, PubMed:12692549, PubMed:12702806, PubMed:14703513, PubMed:15367631, PubMed:15485837, PubMed:18583960, PubMed:21138416, PubMed:23453971, PubMed:23453972, PubMed:23746807, PubMed:25636800, PubMed:26611359, PubMed:32404352, PubMed:34363755, PubMed:32298923). Following activation of toll-like receptors by viral or bacterial components, associates with TRAF3 and TANK and phosphorylates interferon regulatory factors (IRFs) IRF3 and IRF7 as well as DDX3X (PubMed:12692549, PubMed:12702806, PubMed:14703513, PubMed:15367631, PubMed:18583960, PubMed:25636800). This activity allows subsequent homodimerization and nuclear translocation of the IRFs leading to transcriptional activation of pro-inflammatory and antiviral genes including IFNA and IFNB (PubMed:12702806, PubMed:15367631, PubMed:25636800, PubMed:32972995). In order to establish such an antiviral state, TBK1 form several different complexes whose composition depends on the type of cell and cellular stimuli (PubMed:23453971, PubMed:23453972, PubMed:23746807). Plays a key role in IRF3 activation: acts by first phosphorylating innate adapter proteins MAVS, STING1 and TICAM1 on their pLxIS motif, leading to recruitment of IRF3, thereby licensing IRF3 for phosphorylation by TBK1 (PubMed:25636800, PubMed:30842653, PubMed:37926288). Phosphorylated IRF3 dissociates from the adapter proteins, dimerizes, and then enters the nucleus to induce expression of interferons (PubMed:25636800). Thus, several scaffolding molecules including FADD, TRADD, MAVS, AZI2, TANK or TBKBP1/SINTBAD can be recruited to the TBK1-containing-complexes (PubMed:21931631). Under particular conditions, functions as a NF-kappa-B effector by phosphorylating NF-kappa-B inhibitor alpha/NFKBIA, IKBKB or RELA to translocate NF-Kappa-B to the nucleus (PubMed:10783893, PubMed:15489227). Restricts bacterial proliferation by phosphorylating the autophagy receptor OPTN/Optineurin on 'Ser-177', thus enhancing LC3 binding affinity and antibacterial autophagy (PubMed:21617041). Phosphorylates SMCR8 component of the C9orf72-SMCR8 complex, promoting autophagosome maturation (PubMed:27103069). Phosphorylates ATG8 proteins MAP1LC3C and GABARAPL2, thereby preventing their delipidation and premature removal from nascent autophagosomes (PubMed:31709703). Seems to play a role in energy balance regulation by sustaining a state of chronic, low-grade inflammation in obesity, which leads to a negative impact on insulin sensitivity (By similarity). Attenuates retroviral budding by phosphorylating the endosomal sorting complex required for transport-I (ESCRT-I) subunit VPS37C (PubMed:21270402). Phosphorylates Borna disease virus (BDV) P protein (PubMed:16155125). Plays an essential role in the TLR3- and IFN-dependent control of herpes virus HSV-1 and HSV-2 infections in the central nervous system (PubMed:22851595). Acts both as a positive and negative regulator of the mTORC1 complex, depending on the context: activates mTORC1 in response to growth factors by catalyzing phosphorylation of MTOR, while it limits the mTORC1 complex by promoting phosphorylation of RPTOR (PubMed:29150432, PubMed:31530866). Acts as a positive regulator of the mTORC2 complex by mediating phosphorylation of MTOR, leading to increased phosphorylation and activation of AKT1 (By similarity). Phosphorylates and activates AKT1 (PubMed:21464307). Involved in the regulation of TNF-induced RIPK1-mediated cell death, probably acting via CYLD phosphorylation that in turn controls RIPK1 ubiquitination status (PubMed:34363755). Also participates in the differentiation of T follicular regulatory cells together with the receptor ICOS (PubMed:27135603)", "gene_name": "TBK1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UHD2", "name": "TBK1", "organism": "Homo sapiens", "uniprot_id": "Q9UHD2" }, { "function": "Functions as a ubiquitin E3 ligase and as an ISG15 E3 ligase (PubMed:16352599). Involved in innate immune defense against viruses by mediating ubiquitination of RIGI and IFIH1 (PubMed:17392790, PubMed:29357390, PubMed:30193849, PubMed:31710640, PubMed:33849980, PubMed:36045682). Mediates 'Lys-63'-linked polyubiquitination of the RIGI N-terminal CARD-like region and may play a role in signal transduction that leads to the production of interferons in response to viral infection (PubMed:17392790, PubMed:23950712). Mediates 'Lys-63'-linked polyubiquitination of IFIH1 (PubMed:30193849). Promotes ISGylation of 14-3-3 sigma (SFN), an adapter protein implicated in the regulation of a large spectrum signaling pathway (PubMed:16352599, PubMed:17069755). Mediates estrogen action in various target organs (PubMed:22452784). Mediates the ubiquitination and subsequent proteasomal degradation of ZFHX3 (PubMed:22452784). Plays a role in promoting the restart of stalled replication forks via interaction with the KHDC3L-OOEP scaffold and subsequent ubiquitination of BLM, resulting in the recruitment and retainment of BLM at DNA replication forks (By similarity). Plays an essential role in the antiviral activity of ZAP/ZC3HAV1; an antiviral protein which inhibits the replication of certain viruses. Mechanistically, mediates 'Lys-63'-linked polyubiquitination of ZAP/ZC3HAV1 that is required for its optimal binding to target mRNA (PubMed:28060952, PubMed:28202764). Also mediates the ubiquitination of various substrates implicated in stress granule formation, nonsense-mediated mRNA decay, nucleoside synthesis and mRNA translation and stability (PubMed:36067236)", "gene_name": "TRIM25", "glycan_count": 1, "glycosylation_sites": [], "id": "Q14258", "name": "TRIM25", "organism": "Homo sapiens", "uniprot_id": "Q14258" }, { "function": "Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation (PubMed:10900005, PubMed:10951221, PubMed:11772392, PubMed:17287217). Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC (PubMed:10900005, PubMed:10951221, PubMed:11772392, PubMed:14691230). Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner (PubMed:17287217). Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion (PubMed:11772392). In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM (PubMed:10593948, PubMed:16651416). May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation (PubMed:18708048). When overexpressed, enhanced cell proliferation, a process inhibited by GPC3 (PubMed:17549790). Also acts as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones such as brain natriuretic peptide 32 (PubMed:10570924, PubMed:16254193). Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline (PubMed:10593948)", "gene_name": "DPP4", "glycan_count": 92, "glycosylation_sites": [ { "position": 85, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 92, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 150, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 219, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 229, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 281, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 321, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 520, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 685, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P27487", "name": "CD26 (DPP4)", "organism": "Homo sapiens", "uniprot_id": "P27487" }, { "function": "Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine (PubMed:16670267, PubMed:23193172, PubMed:26166670, PubMed:8452534, PubMed:9361033). Plays an important role in purine metabolism and in adenosine homeostasis. Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events. Acts as a positive regulator of T-cell coactivation, by binding DPP4 (PubMed:20959412). Its interaction with DPP4 regulates lymphocyte-epithelial cell adhesion (PubMed:11772392). Enhances dendritic cell immunogenicity by affecting dendritic cell costimulatory molecule expression and cytokines and chemokines secretion (By similarity). Enhances CD4+ T-cell differentiation and proliferation (PubMed:20959412). Acts as a positive modulator of adenosine receptors ADORA1 and ADORA2A, by enhancing their ligand affinity via conformational change (PubMed:23193172). Stimulates plasminogen activation (PubMed:15016824). Plays a role in male fertility (PubMed:21919946, PubMed:26166670). Plays a protective role in early postimplantation embryonic development (By similarity). Also responsible for the deamination of cordycepin (3'-deoxyadenosine), a fungal natural product that shows antitumor, antibacterial, antifungal, antivirus, and immune regulation properties (PubMed:26038697)", "gene_name": "ADA", "glycan_count": 1, "glycosylation_sites": [], "id": "P00813", "name": "Adenosine deaminase 1 (ADA1)", "organism": "Homo sapiens", "uniprot_id": "P00813" }, { "function": "Adenosine deaminase that may contribute to the degradation of extracellular adenosine, a signaling molecule that controls a variety of cellular responses. Requires elevated adenosine levels for optimal enzyme activity. Binds to cell surfaces via proteoglycans and may play a role in the regulation of cell proliferation and differentiation, independently of its enzyme activity", "gene_name": "ADA2", "glycan_count": 23, "glycosylation_sites": [ { "position": 127, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 174, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 185, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 378, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NZK5", "name": "Adenosine deaminase 2 (ADA2)", "organism": "Homo sapiens", "uniprot_id": "Q9NZK5" }, { "function": "The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specificity and liver tropism. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis. The large envelope protein also assures fusion between virion membrane and endosomal membrane. In its internal conformation the protein plays a role in virion morphogenesis and mediates the contact with the nucleocapsid like a matrix protein", "gene_name": "S", "glycan_count": 0, "glycosylation_sites": [ { "position": 309, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 37, "type": "O-linked (GalNAc...) threonine" } ], "id": "P03138", "name": "Hepatitis B surface antigen", "organism": "Hepatitis B virus genotype D subtype ayw (isolate France/Tiollais/1979)", "uniprot_id": "P03138" }, { "function": "Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility", "gene_name": "APOA1", "glycan_count": 2, "glycosylation_sites": [ { "position": 263, "type": "N-linked (Glc) (glycation) lysine" } ], "id": "P02647", "name": "apolipoprotein A1", "organism": "Homo sapiens", "uniprot_id": "P02647" }, { "function": "Atypical E3 ubiquitin ligase that can catalyze ubiquitination of both proteins and lipids, and which is involved in various processes, such as lipid metabolism, angiogenesis and cell-autonomous immunity (PubMed:21799892, PubMed:26126547, PubMed:26278786, PubMed:26766444, PubMed:30705059, PubMed:32139119, PubMed:34012115). Acts as a key immune sensor by catalyzing ubiquitination of the lipid A moiety of bacterial lipopolysaccharide (LPS) via its RZ-type zinc-finger: restricts the proliferation of cytosolic bacteria, such as Salmonella, by generating the bacterial ubiquitin coat through the ubiquitination of LPS (PubMed:34012115). Also acts indirectly by mediating the recruitment of the LUBAC complex, which conjugates linear polyubiquitin chains (PubMed:34012115). Ubiquitination of LPS triggers cell-autonomous immunity, such as antibacterial autophagy, leading to degradation of the microbial invader (PubMed:34012115). Involved in lipid metabolism by regulating fat storage and lipid droplet formation; act by inhibiting the lipolytic process (PubMed:30705059). Also regulates lipotoxicity by inhibiting desaturation of fatty acids (PubMed:30846318). Also acts as an E3 ubiquitin-protein ligase via its RING-type zinc finger: mediates 'Lys-63'-linked ubiquitination of target proteins (PubMed:32139119, PubMed:33842849). Involved in the non-canonical Wnt signaling pathway in vascular development: acts by mediating ubiquitination and degradation of FLNA and NFATC2 downstream of RSPO3, leading to inhibit the non-canonical Wnt signaling pathway and promoting vessel regression (PubMed:26766444). Also has ATPase activity; ATPase activity is required for ubiquitination of LPS (PubMed:34012115)", "gene_name": "RNF213", "glycan_count": 3, "glycosylation_sites": [], "id": "Q63HN8", "name": "RNF213", "organism": "Homo sapiens", "uniprot_id": "Q63HN8" }, { "function": "Signal-transducing molecule. May have a common pathway with IL6ST. The soluble form inhibits the biological activity of LIF by blocking its binding to receptors on target cells", "gene_name": "LIFR", "glycan_count": 12, "glycosylation_sites": [ { "position": 64, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 85, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 131, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 143, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 191, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 243, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 303, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 390, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 407, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 426, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 445, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 481, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 489, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 572, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 652, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 663, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 680, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 729, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 787, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P42702", "name": "LIF receptor", "organism": "Homo sapiens", "uniprot_id": "P42702" }, { "function": "Stimulates the proliferation of early hematopoietic cells by activating FLT3. Synergizes well with a number of other colony stimulating factors and interleukins. Required for the development of B cells, and dendritic cells (DCs)", "gene_name": "FLT3LG", "glycan_count": 1, "glycosylation_sites": [ { "position": 126, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 149, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P49771", "name": "FLT-3L", "organism": "Homo sapiens", "uniprot_id": "P49771" }, { "function": "Receptor for TNFSF9/4-1BBL. Conveys a signal that enhances CD8(+) T-cell survival, cytotoxicity, and mitochondrial activity, thereby promoting immunity against viruses and tumors (Probable)", "gene_name": "TNFRSF9", "glycan_count": 2, "glycosylation_sites": [ { "position": 138, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 149, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q07011", "name": "TNFRSF9", "organism": "Homo sapiens", "uniprot_id": "Q07011" }, { "function": "Thiol protease that plays a key role in programmed cell death by acting as a molecular switch for apoptosis, necroptosis and pyroptosis, and is required to prevent tissue damage during embryonic development and adulthood (PubMed:23516580, PubMed:35338844, PubMed:35446120, PubMed:8681376, PubMed:8681377, PubMed:8962078, PubMed:9006941, PubMed:9184224). Initiator protease that induces extrinsic apoptosis by mediating cleavage and activation of effector caspases responsible for FAS/CD95-mediated and TNFRSF1A-induced cell death (PubMed:23516580, PubMed:35338844, PubMed:35446120, PubMed:8681376, PubMed:8681377, PubMed:8962078, PubMed:9006941, PubMed:9184224). Cleaves and activates effector caspases CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10 (PubMed:16916640, PubMed:8962078, PubMed:9006941). Binding to the adapter molecule FADD recruits it to either receptor FAS/TNFRSF6 or TNFRSF1A (PubMed:8681376, PubMed:8681377). The resulting aggregate called the death-inducing signaling complex (DISC) performs CASP8 proteolytic activation (PubMed:9184224). The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases (PubMed:9184224). Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC (PubMed:9184224). In addition to extrinsic apoptosis, also acts as a negative regulator of necroptosis: acts by cleaving RIPK1 at 'Asp-324', which is crucial to inhibit RIPK1 kinase activity, limiting TNF-induced apoptosis, necroptosis and inflammatory response (PubMed:31827280, PubMed:31827281). Also able to initiate pyroptosis by mediating cleavage and activation of gasdermin-C and -D (GSDMC and GSDMD, respectively): gasdermin cleavage promotes release of the N-terminal moiety that binds to membranes and forms pores, triggering pyroptosis (PubMed:32929201, PubMed:34012073). Initiates pyroptosis following inactivation of MAP3K7/TAK1 (By similarity). Also acts as a regulator of innate immunity by mediating cleavage and inactivation of N4BP1 downstream of TLR3 or TLR4, thereby promoting cytokine production (By similarity). May participate in the Granzyme B (GZMB) cell death pathways (PubMed:8755496). Cleaves PARP1 and PARP2 (PubMed:8681376). Independent of its protease activity, promotes cell migration following phosphorylation at Tyr-380 (PubMed:18216014, PubMed:27109099)", "gene_name": "CASP8", "glycan_count": 0, "glycosylation_sites": [], "id": "Q14790", "name": "Caspase-8", "organism": "Homo sapiens", "uniprot_id": "Q14790" }, { "function": "Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268)", "gene_name": "IGHG3", "glycan_count": 128, "glycosylation_sites": [ { "position": 122, "type": "O-linked (GalNAc...) threonine" }, { "position": 137, "type": "O-linked (GalNAc...) threonine" }, { "position": 152, "type": "O-linked (GalNAc...) threonine" }, { "position": 227, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 322, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01860", "name": "IgG4", "organism": "Homo sapiens", "uniprot_id": "P01860" }, { "function": "Integrin ITGAL/ITGB2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. Integrin ITGAL/ITGB2 is a receptor for F11R (PubMed:11812992, PubMed:15528364). Integrin ITGAL/ITGB2 is a receptor for the secreted form of ubiquitin-like protein ISG15; the interaction is mediated by ITGAL (PubMed:29100055). Involved in a variety of immune phenomena including leukocyte-endothelial cell interaction, cytotoxic T-cell mediated killing, and antibody dependent killing by granulocytes and monocytes. Contributes to natural killer cell cytotoxicity (PubMed:15356110). Involved in leukocyte adhesion and transmigration of leukocytes including T-cells and neutrophils (PubMed:11812992). Acts as a platform at the immunological synapse to translate TCR engagement and density of the ITGAL ligand ICAM1 into graded adhesion (PubMed:38195629). Required for generation of common lymphoid progenitor cells in bone marrow, indicating a role in lymphopoiesis (By similarity). Integrin ITGAL/ITGB2 in association with ICAM3, contributes to apoptotic neutrophil phagocytosis by macrophages (PubMed:23775590)", "gene_name": "ITGAL", "glycan_count": 63, "glycosylation_sites": [ { "position": 65, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 89, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 188, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 649, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 670, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 726, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 730, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 862, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 885, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 897, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1060, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1071, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P20701", "name": "Leukocyte function-associated antigen 1 (LFA-1)", "organism": "Homo sapiens", "uniprot_id": "P20701" }, { "function": "Receptor for IL17A and IL17F, major effector cytokines of innate and adaptive immune system involved in antimicrobial host defense and maintenance of tissue integrity. Receptor for IL17A (PubMed:17911633, PubMed:9367539). Receptor for IL17F (PubMed:17911633, PubMed:19838198). Binds to IL17A with higher affinity than to IL17F (PubMed:17911633). Binds IL17A and IL17F homodimers as part of a heterodimeric complex with IL17RC (PubMed:16785495). Also binds heterodimers formed by IL17A and IL17F as part of a heterodimeric complex with IL17RC (PubMed:18684971). Cytokine binding triggers homotypic interaction of IL17RA and IL17RC chains with TRAF3IP2 adapter, leading to TRAF6-mediated activation of NF-kappa-B and MAPkinase pathways, ultimately resulting in transcriptional activation of cytokines, chemokines, antimicrobial peptides and matrix metalloproteinases, with potential strong immune inflammation (PubMed:16785495, PubMed:17911633, PubMed:18684971, PubMed:21350122, PubMed:24120361). Involved in antimicrobial host defense primarily promoting neutrophil activation and recruitment at infection sites to destroy extracellular bacteria and fungi (By similarity). In secondary lymphoid organs, contributes to germinal center formation by regulating the chemotactic response of B cells to CXCL12 and CXCL13, enhancing retention of B cells within the germinal centers, B cell somatic hypermutation rate and selection toward plasma cells (By similarity). Plays a role in the maintenance of the integrity of epithelial barriers during homeostasis and pathogen infection. Stimulates the production of antimicrobial beta-defensins DEFB1, DEFB103A, and DEFB104A by mucosal epithelial cells, limiting the entry of microbes through the epithelial barriers (By similarity). Involved in antiviral host defense through various mechanisms. Enhances immunity against West Nile virus by promoting T cell cytotoxicity. Contributes to Influenza virus clearance by driving the differentiation of B-1a B cells, providing for production of virus-specific IgM antibodies at first line of host defense (By similarity). Receptor for IL17C as part of a heterodimeric complex with IL17RE (PubMed:21993848)", "gene_name": "IL17RA", "glycan_count": 11, "glycosylation_sites": [ { "position": 49, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 54, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 67, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 206, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 225, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 242, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 265, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q96F46", "name": "IL-17 receptor A (IL-17RA)", "organism": "Homo sapiens", "uniprot_id": "Q96F46" }, { "function": "Endosomal receptor that plays a key role in innate and adaptive immunity (PubMed:14976261, PubMed:32433612). Controls host immune response against pathogens through recognition of uridine-containing single strand RNAs (ssRNAs) of viral origin or guanosine analogs (PubMed:12738885, PubMed:27742543, PubMed:31608988, PubMed:32706371, PubMed:35477763). Upon binding to agonists, undergoes dimerization that brings TIR domains from the two molecules into direct contact, leading to the recruitment of TIR-containing downstream adapter MYD88 through homotypic interaction (PubMed:27742543). In turn, the Myddosome signaling complex is formed involving IRAK4, IRAK1, TRAF6, TRAF3 leading to activation of downstream transcription factors NF-kappa-B and IRF7 to induce pro-inflammatory cytokines and interferons, respectively (PubMed:27742543, PubMed:32706371). In plasmacytoid dendritic cells, RNASET2 endonuclease cooperates with PLD3 or PLD4 5'->3' exonucleases to process RNA and release 2',3'-cyclic guanosine monophosphate (2',3'-cGMP) and cytidine-rich RNA fragments that occupy TLR7 ligand-binding pockets and trigger a signaling-competent state", "gene_name": "TLR7", "glycan_count": 3, "glycosylation_sites": [ { "position": 66, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 69, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 167, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 202, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 215, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 361, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 413, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 488, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 523, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 534, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 590, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 679, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 720, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 799, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NYK1", "name": "Toll-like receptor 7 (TLR7)", "organism": "Homo sapiens", "uniprot_id": "Q9NYK1" }, { "function": "Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR9 is a nucleotide-sensing TLR which is activated by unmethylated cytidine-phosphate-guanosine (CpG) dinucleotides (PubMed:14716310). Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (PubMed:11564765, PubMed:17932028). Controls lymphocyte response to Helicobacter infection (By similarity). Upon CpG stimulation, induces B-cell proliferation, activation, survival and antibody production (PubMed:23857366)", "gene_name": "TLR9", "glycan_count": 5, "glycosylation_sites": [ { "position": 64, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 129, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 200, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 210, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 242, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 300, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 340, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 469, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 474, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 513, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 567, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 694, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 731, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NR96", "name": "Toll-like receptor 9 (TLR9)", "organism": "Homo sapiens", "uniprot_id": "Q9NR96" }, { "function": "5'->3' double-stranded DNA exonuclease which may also possess a cryptic 3'->5' double-stranded DNA exonuclease activity. Functions in DNA mismatch repair (MMR) to excise mismatch-containing DNA tracts directed by strand breaks located either 5' or 3' to the mismatch. Also exhibits endonuclease activity against 5'-overhanging flap structures similar to those generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Required for somatic hypermutation (SHM) and class switch recombination (CSR) of immunoglobulin genes. Essential for male and female meiosis", "gene_name": "EXO1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UQ84", "name": "LAMP3", "organism": "Homo sapiens", "uniprot_id": "Q9UQ84" }, { "function": "Plays an important role in several reproductive functions. Induces Muellerian duct regression during male fetal sexual differentiation (PubMed:34155118, PubMed:3754790, PubMed:8469238). Also plays a role in Leydig cell differentiation and function (By similarity). In female acts as a negative regulator of the primordial to primary follicle transition and decreases FSH sensitivity of growing follicles (PubMed:14742691). AMH signals by binding to a specific type-II receptor, AMHR2, that heterodimerizes with type-I receptors (ACVR1 and BMPR1A), and recruiting SMAD proteins that are translocated to the nucleus to regulate target gene expression (PubMed:20861221, PubMed:34155118)", "gene_name": "AMH", "glycan_count": 2, "glycosylation_sites": [ { "position": 64, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 329, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P03971", "name": "Anti-M\u00fcllerian Hormone (AMH)", "organism": "Homo sapiens", "uniprot_id": "P03971" }, { "function": "Together with the alpha chain CGA constitutes follitropin, the follicle-stimulating hormone, and provides its biological specificity to the hormone heterodimer. Binds FSHR, a G protein-coupled receptor, on target cells to activate downstream signaling pathways (PubMed:24692546, PubMed:2494176). Follitropin is involved in follicle development and spermatogenesis in reproductive organs (PubMed:407105, PubMed:8220432)", "gene_name": "FSHB", "glycan_count": 28, "glycosylation_sites": [ { "position": 25, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 42, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01225", "name": "Follicle-Stimulating Hormone (FSH)", "organism": "Homo sapiens", "uniprot_id": "P01225" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P05067-APP-derived", "name": "\u03b2-amyloid (A\u03b2)", "organism": "", "uniprot_id": "" }, { "function": "Involved in vitamin D transport and storage, scavenging of extracellular G-actin, enhancement of the chemotactic activity of C5 alpha for neutrophils in inflammation and macrophage activation", "gene_name": "GC", "glycan_count": 11, "glycosylation_sites": [], "id": "P02774", "name": "Vitamin D Binding Protein (DBP)", "organism": "Homo sapiens", "uniprot_id": "P02774" }, { "function": "Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed (PubMed:19666512). Plays a role in ciliogenesis (PubMed:20393563)", "gene_name": "GSN", "glycan_count": 5, "glycosylation_sites": [], "id": "P06396", "name": "Gelsolin (GSN)", "organism": "Homo sapiens", "uniprot_id": "P06396" }, { "function": "Small zinc- and- and calcium-binding protein that is highly expressed in astrocytes and constitutes one of the most abundant soluble proteins in brain (PubMed:20950652, PubMed:6487634). Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer (PubMed:20950652, PubMed:6487634). Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites (By similarity). Acts as a neurotrophic factor that promotes astrocytosis and axonal proliferation (By similarity). Involved in innervation of thermogenic adipose tissue by acting as an adipocyte-derived neurotrophic factor that promotes sympathetic innervation of adipose tissue (By similarity). Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase (By similarity). Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling (By similarity). Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization (PubMed:20351179). May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity (PubMed:22399290)", "gene_name": "S100B", "glycan_count": 0, "glycosylation_sites": [], "id": "P04271", "name": "S100B", "organism": "Homo sapiens", "uniprot_id": "P04271" }, { "function": "May have weak glycosidase activity towards glucuronylated steroids. However, it lacks essential active site Glu residues at positions 239 and 872, suggesting it may be inactive as a glycosidase in vivo. May be involved in the regulation of calcium and phosphorus homeostasis by inhibiting the synthesis of active vitamin D (By similarity). Essential factor for the specific interaction between FGF23 and FGFR1 (By similarity)", "gene_name": "KL", "glycan_count": 7, "glycosylation_sites": [ { "position": 106, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 159, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 283, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 344, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 607, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 612, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 694, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UEF7", "name": "Klotho", "organism": "Homo sapiens", "uniprot_id": "Q9UEF7" }, { "function": "The exact function of MAP2 is unknown but MAPs may stabilize the microtubules against depolymerization. They also seem to have a stiffening effect on microtubules", "gene_name": "Map2", "glycan_count": 3, "glycosylation_sites": [], "id": "P20357", "name": "MAP-2", "organism": "Mus musculus", "uniprot_id": "P20357" }, { "function": "Attaches the virion to the host cell membrane by interacting with heparan sulfate, initiating the infection (PubMed:10400758, PubMed:10864656, PubMed:3655746). Interacts with host CX3CR1, the receptor for the CX3C chemokine fractalkine, to modulate the immune response and facilitate infection (PubMed:11477410, PubMed:26107373, PubMed:26658574). Unlike the other paramyxovirus attachment proteins, lacks both neuraminidase and hemagglutinating activities (Probable)", "gene_name": "G", "glycan_count": 0, "glycosylation_sites": [ { "position": 70, "type": "O-linked (GalNAc...) threonine; by host" }, { "position": 72, "type": "O-linked (GalNAc...) threonine; by host" }, { "position": 80, "type": "O-linked (GalNAc...) threonine; by host" }, { "position": 86, "type": "O-linked (GalNAc...) threonine; by host" }, { "position": 87, "type": "O-linked (GalNAc...) threonine; by host" }, { "position": 92, "type": "O-linked (GalNAc...) threonine; by host" }, { "position": 100, "type": "O-linked (GalNAc...) serine; by host" }, { "position": 105, "type": "O-linked (GalNAc...) serine; by host" }, { "position": 113, "type": "O-linked (GalNAc...) threonine; by host" }, { "position": 117, "type": "O-linked (GalNAc...) serine; by host" }, { "position": 119, "type": "O-linked (GalNAc...) threonine; by host" }, { "position": 135, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 137, "type": "O-linked (GalNAc...) threonine; by host" }, { "position": 138, "type": "O-linked (GalNAc...) threonine; by host" }, { "position": 139, "type": "O-linked (GalNAc...) threonine; by host" }, { "position": 141, "type": "O-linked (GalNAc...) threonine; by host" }, { "position": 144, "type": "O-linked (GalNAc...) serine; by host" }, { "position": 147, "type": "O-linked (GalNAc...) threonine; by host" }, { "position": 199, "type": "O-linked (GalNAc...) threonine; by host" }, { "position": 203, "type": "O-linked (GalNAc...) threonine; by host" }, { "position": 219, "type": "O-linked (GalNAc...) threonine; by host" }, { "position": 231, "type": "O-linked (GalNAc...) threonine; by host" }, { "position": 235, "type": "O-linked (GalNAc...) threonine; by host" }, { "position": 237, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 251, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 253, "type": "O-linked (GalNAc...) threonine; by host" }, { "position": 269, "type": "O-linked (GalNAc...) serine; by host" }, { "position": 270, "type": "O-linked (GlcNAc...) serine; by host" }, { "position": 275, "type": "O-linked (GalNAc...) serine; by host" }, { "position": 282, "type": "O-linked (GalNAc...) threonine; by host" }, { "position": 283, "type": "O-linked (GalNAc...) serine; by host" }, { "position": 287, "type": "O-linked (GalNAc...) serine; by host" }, { "position": 290, "type": "O-linked (GalNAc...) serine; by host" } ], "id": "P03423", "name": "G glycoprotein", "organism": "Human respiratory syncytial virus A (strain A2)", "uniprot_id": "P03423" }, { "function": "Inactive precursor that is cleaved at two sites by a furin-like protease to give rise to the mature F1 and F2 fusion glycoproteins", "gene_name": "F", "glycan_count": 0, "glycosylation_sites": [ { "position": 27, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 70, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 116, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 120, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 126, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 500, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P03420", "name": "F glycoprotein", "organism": "Human respiratory syncytial virus A (strain A2)", "uniprot_id": "P03420" }, { "function": "Ribonucleocapsid-associated protein that interacts with the phosphoprotein (P), thereby increasing replication accuracy and processivity of the polymerase complex", "gene_name": "P/V/C", "glycan_count": 0, "glycosylation_sites": [], "id": "P03424", "name": "SH protein", "organism": "Measles virus (strain Edmonston)", "uniprot_id": "P03424" }, { "function": "Cell surface receptor that plays a functionally redundant role in the inhibition of neurite outgrowth mediated by MAG (By similarity). Plays a functionally redundant role in postnatal brain development. Contributes to normal axon migration across the brain midline and normal formation of the corpus callosum. Does not seem to play a significant role in regulating axon regeneration in the adult central nervous system. Protects motoneurons against apoptosis; protection against apoptosis is probably mediated by MAG (By similarity). Like other family members, plays a role in restricting the number dendritic spines and the number of synapses that are formed during brain development (PubMed:22325200). Signaling mediates activation of Rho and downstream reorganization of the actin cytoskeleton (PubMed:22325200)", "gene_name": "RTN4RL2", "glycan_count": 5, "glycosylation_sites": [ { "position": 50, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 93, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 236, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q86UN3", "name": "RTN4RL2", "organism": "Homo sapiens", "uniprot_id": "Q86UN3" }, { "function": "Acts as a transcriptional corepressor of orphan nuclear receptor NR2C2 (PubMed:15302918). Inhibits expression of the gluconeogenesis enzyme PCK2 through inhibition of NR2C2 activity (By similarity). Also involved in transcriptional activation of NAMPT by promoting expression of PPARA and PPARD (By similarity). Plays a role in lipid metabolism by suppressing lipogenesis, increasing lipolysis and decreasing lipid accumulation in adipose tissue (By similarity). Plays a role in glucose homeostasis by improving glucose metabolism and insulin sensitivity (By similarity)", "gene_name": "JAZF1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q86VZ6", "name": "NOMO2", "organism": "Homo sapiens", "uniprot_id": "Q86VZ6" }, { "function": "Tetranectin binds to plasminogen and to isolated kringle 4. May be involved in the packaging of molecules destined for exocytosis. Plays a role in retinal function (PubMed:35331648)", "gene_name": "CLEC3B", "glycan_count": 0, "glycosylation_sites": [ { "position": 25, "type": "O-linked (GalNAc...) threonine" } ], "id": "P05452", "name": "CLEC3B", "organism": "Homo sapiens", "uniprot_id": "P05452" }, { "function": "", "gene_name": "A1BG", "glycan_count": 29, "glycosylation_sites": [ { "position": 44, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 179, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 363, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 371, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P04217", "name": "A1BG", "organism": "Homo sapiens", "uniprot_id": "P04217" }, { "function": "Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor (PubMed:8690719, PubMed:9295285). Has a broad spectrum of substrates such as apomucin-, MUC5AC-, MUC1- and MUC2-derived peptides (PubMed:9295285)", "gene_name": "GALNT1", "glycan_count": 5, "glycosylation_sites": [ { "position": 95, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 552, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q10472", "name": "GALNT1", "organism": "Homo sapiens", "uniprot_id": "Q10472" }, { "function": "Inhibits human amidolytic and kininogenase activities of tissue kallikrein. Inhibition is achieved by formation of an equimolar, heat- and SDS-stable complex between the inhibitor and the enzyme, and generation of a small C-terminal fragment of the inhibitor due to cleavage at the reactive site by tissue kallikrein", "gene_name": "SERPINA4", "glycan_count": 39, "glycosylation_sites": [ { "position": 33, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 108, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 157, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 238, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P29622", "name": "SERPINA4", "organism": "Homo sapiens", "uniprot_id": "P29622" }, { "function": "Component of the membrane attack complex (MAC), a multiprotein complex activated by the complement cascade, which inserts into a target cell membrane and forms a pore, leading to target cell membrane rupture and cell lysis (PubMed:17872444, PubMed:22832194, PubMed:26841837, PubMed:27052168, PubMed:30552328, PubMed:7440581). The MAC is initiated by proteolytic cleavage of C5 into complement C5b in response to the classical, alternative, lectin and GZMK complement pathways (PubMed:17872444, PubMed:30552328, PubMed:7440581). The complement pathways consist in a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system (PubMed:17872444, PubMed:30552328, PubMed:7440581). C8A, together with C8B and C8G, inserts into the target membrane, but does not form pores by itself (PubMed:17872444, PubMed:30552328). During MAC assembly, associates with C5b, C6 and C7 to form the C5b8 intermediate complex that inserts into the target membrane and traverses the bilayer increasing membrane rigidity (PubMed:30552328, PubMed:6833260)", "gene_name": "C8A", "glycan_count": 18, "glycosylation_sites": [ { "position": 44, "type": "C-linked (Man) tryptophan" }, { "position": 437, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 542, "type": "C-linked (Man) tryptophan" }, { "position": 545, "type": "C-linked (Man) tryptophan" }, { "position": 548, "type": "C-linked (Man) tryptophan" } ], "id": "P07357", "name": "C8A", "organism": "Homo sapiens", "uniprot_id": "P07357" }, { "function": "Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268)", "gene_name": "IGHG4", "glycan_count": 151, "glycosylation_sites": [ { "position": 177, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P01861", "name": "Immunoglobulin G4", "organism": "Homo sapiens", "uniprot_id": "P01861" }, { "function": "Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins", "gene_name": "NGLY1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96IV0", "name": "N-glycanase 1 (NGLY1)", "organism": "Homo sapiens", "uniprot_id": "Q96IV0" }, { "function": "Forms a water channel that facilitates the transport of water across cell membranes, playing a crucial role in water homeostasis in various tissues (PubMed:1373524, PubMed:23219802). Could also be permeable to small solutes including hydrogen peroxide, glycerol and gases such as amonnia (NH3), nitric oxide (NO) and carbon dioxide (CO2) (PubMed:16682607, PubMed:17012249, PubMed:19273840, PubMed:33028705, PubMed:8584435). Recruited to the ankyrin-1 complex, a multiprotein complex of the erythrocyte membrane, it could be part of a CO2 metabolon, linking facilitated diffusion of CO2 across the membrane, anion exchange of Cl(-)/HCO3(-) and interconversion of dissolved CO2 and carbonic acid in the cytosol (PubMed:17012249, PubMed:35835865). In vitro, it shows non-selective gated cation channel activity and may be permeable to cations like K(+) and Na(+) in vivo (PubMed:36949749, PubMed:8703053)", "gene_name": "AQP1", "glycan_count": 1, "glycosylation_sites": [ { "position": 42, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 205, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P29972", "name": "Aquaporin 1 (AQP1)", "organism": "Homo sapiens", "uniprot_id": "P29972" }, { "function": "Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling", "gene_name": "UBB", "glycan_count": 1, "glycosylation_sites": [], "id": "P0CG47", "name": "Ubiquitin B (UBB)", "organism": "Homo sapiens", "uniprot_id": "P0CG47" }, { "function": "E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and transfers it to its substrates (PubMed:10373495, PubMed:16772533, PubMed:19204938, PubMed:19233847, PubMed:19325566, PubMed:19591933, PubMed:22645313, PubMed:24273172, PubMed:24728990, PubMed:30020076). Several substrates have been identified including the BMAL1, ARC, LAMTOR1, RAD23A and RAD23B, MCM7 (which is involved in DNA replication), annexin A1, the PML tumor suppressor, and the cell cycle regulator CDKN1B (PubMed:10373495, PubMed:19204938, PubMed:19325566, PubMed:19591933, PubMed:22645313, PubMed:24728990, PubMed:30020076). Additionally, may function as a cellular quality control ubiquitin ligase by helping the degradation of the cytoplasmic misfolded proteins (PubMed:19233847). Finally, UBE3A also promotes its own degradation in vivo. Plays an important role in the regulation of the circadian clock: involved in the ubiquitination of the core clock component BMAL1, leading to its proteasomal degradation (PubMed:24728990). Acts as transcriptional coactivator of progesterone receptor PGR upon progesterone hormone activation (PubMed:16772533). Acts as a regulator of synaptic development by mediating ubiquitination and degradation of ARC (By similarity). Required for synaptic remodeling in neurons by mediating ubiquitination and degradation of LAMTOR1, thereby limiting mTORC1 signaling and activity-dependent synaptic remodeling (By similarity). Synergizes with WBP2 in enhancing PGR activity (PubMed:16772533)", "gene_name": "UBE3A", "glycan_count": 2, "glycosylation_sites": [], "id": "Q05086", "name": "Ubiquitin-protein ligase E3A (UBE3A)", "organism": "Homo sapiens", "uniprot_id": "Q05086" }, { "function": "Signal-transducing molecule (PubMed:2261637). The receptor systems for IL6, LIF, OSM, CNTF, IL11, CTF1 and BSF3 can utilize IL6ST for initiating signal transmission. Binding of IL6 to IL6R induces IL6ST homodimerization and formation of a high-affinity receptor complex, which activates the intracellular JAK-MAPK and JAK-STAT3 signaling pathways (PubMed:19915009, PubMed:2261637, PubMed:23294003). That causes phosphorylation of IL6ST tyrosine residues which in turn activates STAT3 (PubMed:19915009, PubMed:23294003, PubMed:25731159). In parallel, the IL6 signaling pathway induces the expression of two cytokine receptor signaling inhibitors, SOCS1 and SOCS3, which inhibit JAK and terminate the activity of the IL6 signaling pathway as a negative feedback loop (By similarity). Also activates the yes-associated protein 1 (YAP) and NOTCH pathways to control inflammation-induced epithelial regeneration, independently of STAT3 (By similarity). Acts as a receptor for the neuroprotective peptide humanin as part of a complex with IL27RA/WSX1 and CNTFR (PubMed:19386761). Mediates signals which regulate immune response, hematopoiesis, pain control and bone metabolism (By similarity). Has a role in embryonic development (By similarity). Essential for survival of motor and sensory neurons and for differentiation of astrocytes (By similarity). Required for expression of TRPA1 in nociceptive neurons (By similarity). Required for the maintenance of PTH1R expression in the osteoblast lineage and for the stimulation of PTH-induced osteoblast differentiation (By similarity). Required for normal trabecular bone mass and cortical bone composition (By similarity)", "gene_name": "IL6ST", "glycan_count": 48, "glycosylation_sites": [ { "position": 43, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 83, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 131, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 157, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 227, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 379, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 383, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 390, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 553, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 564, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P40189", "name": "glycoprotein 130 (gp130)", "organism": "Homo sapiens", "uniprot_id": "P40189" }, { "function": "Type II interferon produced by immune cells such as T-cells and NK cells that plays crucial roles in antimicrobial, antiviral, and antitumor responses by activating effector immune cells and enhancing antigen presentation (PubMed:16914093, PubMed:8666937). Primarily signals through the JAK-STAT pathway after interaction with its receptor IFNGR1 to affect gene regulation (PubMed:8349687). Upon IFNG binding, IFNGR1 intracellular domain opens out to allow association of downstream signaling components JAK2, JAK1 and STAT1, leading to STAT1 activation, nuclear translocation and transcription of IFNG-regulated genes. Many of the induced genes are transcription factors such as IRF1 that are able to further drive regulation of a next wave of transcription (PubMed:16914093). Plays a role in class I antigen presentation pathway by inducing a replacement of catalytic proteasome subunits with immunoproteasome subunits (PubMed:8666937). In turn, increases the quantity, quality, and repertoire of peptides for class I MHC loading (PubMed:8163024). Increases the efficiency of peptide generation also by inducing the expression of activator PA28 that associates with the proteasome and alters its proteolytic cleavage preference (PubMed:11112687). Up-regulates as well MHC II complexes on the cell surface by promoting expression of several key molecules such as cathepsins B/CTSB, H/CTSH, and L/CTSL (PubMed:7729559). Participates in the regulation of hematopoietic stem cells during development and under homeostatic conditions by affecting their development, quiescence, and differentiation (By similarity)", "gene_name": "IFNG", "glycan_count": 41, "glycosylation_sites": [ { "position": 48, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 120, "type": "N-linked (GlcNAc...) asparagine; in dimeric form" } ], "id": "P01579", "name": "Interferon gamma (IFNG)", "organism": "Homo sapiens", "uniprot_id": "P01579" }, { "function": "Antagonist of signaling by TGF-beta (transforming growth factor) type 1 receptor superfamily members; has been shown to inhibit TGF-beta (Transforming growth factor) and activin signaling by associating with their receptors thus preventing SMAD2 access (PubMed:21791611). Functions as an adapter to recruit SMURF2 to the TGF-beta receptor complex. Also acts by recruiting the PPP1R15A-PP1 complex to TGFBR1, which promotes its dephosphorylation. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator", "gene_name": "SMAD7", "glycan_count": 0, "glycosylation_sites": [], "id": "O15105", "name": "SMAD7", "organism": "Homo sapiens", "uniprot_id": "O15105" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Not specified", "name": "GP63 (Leishmanolysin)", "organism": "", "uniprot_id": "" }, { "function": "Transcription factor that plays an essential role in commitment of lymphoid progenitors to the B-lymphocyte lineage (PubMed:10811620, PubMed:27181361). Fulfills a dual role by repressing B-lineage inappropriate genes and simultaneously activating B-lineage-specific genes (PubMed:10811620, PubMed:27181361). In turn, regulates cell adhesion and migration, induces V(H)-to-D(H)J(H) recombination, facilitates pre-B-cell receptor signaling and promotes development to the mature B-cell stage (PubMed:32612238). Repression of the cohesin-release factor WAPL causes global changes of the chromosomal architecture in pro-B cells to facilitate the generation of a diverse antibody repertoire (PubMed:32612238)", "gene_name": "PAX5", "glycan_count": 0, "glycosylation_sites": [], "id": "Q02548", "name": "PAX5", "organism": "Homo sapiens", "uniprot_id": "Q02548" }, { "function": "Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair (PubMed:10713044, PubMed:17575048, PubMed:20545769, PubMed:21659603, PubMed:31135337). The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex (PubMed:21659603). Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER) (PubMed:21659603). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates (PubMed:21659603). The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase (PubMed:21659603). RAD9A possesses 3'->5' double stranded DNA exonuclease activity (PubMed:10713044)", "gene_name": "RAD9A", "glycan_count": 1, "glycosylation_sites": [], "id": "Q99638", "name": "MUM1 (IRF4)", "organism": "Homo sapiens", "uniprot_id": "Q99638" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "not applicable", "name": "CA19-9", "organism": "", "uniprot_id": "" }, { "function": "The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Depending on the isoform, progesterone receptor functions as a transcriptional activator or repressor", "gene_name": "PGR", "glycan_count": 1, "glycosylation_sites": [], "id": "P06401", "name": "Progesterone Receptor", "organism": "Homo sapiens", "uniprot_id": "P06401" }, { "function": "Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization", "gene_name": "ERBB2", "glycan_count": 29, "glycosylation_sites": [ { "position": 68, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 124, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 187, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 259, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 530, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 571, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 629, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P04626", "name": "HER2/ErbB2", "organism": "Homo sapiens", "uniprot_id": "P04626" }, { "function": "Non-receptor tyrosine kinase involved in various processes such as cell growth, development, differentiation or histone modifications. Mediates essential signaling events in both innate and adaptive immunity. In the cytoplasm, plays a pivotal role in signal transduction via its association with type I receptors such as growth hormone (GHR), prolactin (PRLR), leptin (LEPR), erythropoietin (EPOR), thrombopoietin receptor (MPL/TPOR); or type II receptors including IFN-alpha, IFN-beta, IFN-gamma and multiple interleukins (PubMed:15690087, PubMed:7615558, PubMed:9657743, PubMed:15899890). Following ligand-binding to cell surface receptors, phosphorylates specific tyrosine residues on the cytoplasmic tails of the receptor, creating docking sites for STATs proteins (PubMed:15690087, PubMed:9618263). Subsequently, phosphorylates the STATs proteins once they are recruited to the receptor. Phosphorylated STATs then form homodimer or heterodimers and translocate to the nucleus to activate gene transcription. For example, cell stimulation with erythropoietin (EPO) during erythropoiesis leads to JAK2 autophosphorylation, activation, and its association with erythropoietin receptor (EPOR) that becomes phosphorylated in its cytoplasmic domain (PubMed:9657743). Then, STAT5 (STAT5A or STAT5B) is recruited, phosphorylated and activated by JAK2. Once activated, dimerized STAT5 translocates into the nucleus and promotes the transcription of several essential genes involved in the modulation of erythropoiesis. Part of a signaling cascade that is activated by increased cellular retinol and that leads to the activation of STAT5 (STAT5A or STAT5B) (PubMed:21368206). In addition, JAK2 mediates angiotensin-2-induced ARHGEF1 phosphorylation (PubMed:20098430). Plays a role in cell cycle by phosphorylating CDKN1B (PubMed:21423214). Cooperates with TEC through reciprocal phosphorylation to mediate cytokine-driven activation of FOS transcription. In the nucleus, plays a key role in chromatin by specifically mediating phosphorylation of 'Tyr-41' of histone H3 (H3Y41ph), a specific tag that promotes exclusion of CBX5 (HP1 alpha) from chromatin (PubMed:19783980). Up-regulates the potassium voltage-gated channel activity of KCNA3 (PubMed:25644777)", "gene_name": "JAK2", "glycan_count": 1, "glycosylation_sites": [], "id": "O60674", "name": "Janus Kinase 1 (JAK1)", "organism": "Homo sapiens", "uniprot_id": "O60674" }, { "function": "A cytochrome P450 monooxygenase that catalyzes the conversion of C19 androgens, androst-4-ene-3,17-dione (androstenedione) and testosterone to the C18 estrogens, estrone and estradiol, respectively (PubMed:27702664, PubMed:2848247). Catalyzes three successive oxidations of C19 androgens: two conventional oxidations at C19 yielding 19-hydroxy and 19-oxo/19-aldehyde derivatives, followed by a third oxidative aromatization step that involves C1-beta hydrogen abstraction combined with cleavage of the C10-C19 bond to yield a phenolic A ring and formic acid (PubMed:20385561). Alternatively, the third oxidative reaction yields a 19-norsteroid and formic acid. Converts dihydrotestosterone to delta1,10-dehydro 19-nordihydrotestosterone and may play a role in homeostasis of this potent androgen (PubMed:22773874). Also displays 2-hydroxylase activity toward estrone (PubMed:22773874). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase) (PubMed:20385561, PubMed:22773874)", "gene_name": "CYP19A1", "glycan_count": 0, "glycosylation_sites": [], "id": "P11511", "name": "Aromatase (CYP19A1)", "organism": "Homo sapiens", "uniprot_id": "P11511" }, { "function": "Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region, a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase", "gene_name": "A2M", "glycan_count": 172, "glycosylation_sites": [ { "position": 55, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 70, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 247, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 396, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 410, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 869, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 991, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1424, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P01023", "name": "Alpha-2-macroglobulin (\u03b12-MG)", "organism": "Homo sapiens", "uniprot_id": "P01023" }, { "function": "Stimulates lipid degradation in adipocytes and causes the extensive fat losses associated with some advanced cancers. May bind polyunsaturated fatty acids", "gene_name": "AZGP1", "glycan_count": 201, "glycosylation_sites": [ { "position": 109, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 112, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 128, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 259, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P25311", "name": "Zinc-\u03b12-glycoprotein (ZAG)", "organism": "Homo sapiens", "uniprot_id": "P25311" }, { "function": "May play a role in lipid exchange and transport throughout the body. May participate in reverse cholesterol transport from peripheral cells to the liver", "gene_name": "APOL1", "glycan_count": 3, "glycosylation_sites": [ { "position": 261, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O14791", "name": "Apolipoprotein L1", "organism": "Homo sapiens", "uniprot_id": "O14791" }, { "function": "Precursor of the catalytic component of the C3 and C5 convertase complexes of the alternative pathway of the complement system, a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system (PubMed:3638964, PubMed:624565, PubMed:6554279, PubMed:6919543, PubMed:9748277). The alternative complement pathway acts as an amplification loop that enhances other complement pathways (classical, lectin and GZMK) by promoting formation of additional C3 and C5 convertases (PubMed:3638964, PubMed:624565, PubMed:6554279, PubMed:6919543, PubMed:9748277). CFB is cleaved and activated by CFD to generate Ba and Bb chains; Bb chain constituting the catalytic component of the C3 and C5 convertases (PubMed:6769474, PubMed:9748277)", "gene_name": "CFB", "glycan_count": 84, "glycosylation_sites": [ { "position": 122, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 142, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 285, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 291, "type": "N-linked (Glc) (glycation) lysine" }, { "position": 378, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P00751", "name": "Complement factor B", "organism": "Homo sapiens", "uniprot_id": "P00751" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01019 (precursor: angiotensinogen)", "name": "Angiotensin II", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02452/P08123", "name": "Collagen type I (Col1a1/Col1a2)", "organism": "", "uniprot_id": "" }, { "function": "Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair (PubMed:17177976, PubMed:18055453, PubMed:18172500, PubMed:19344625, PubMed:19661379, PubMed:20388712, PubMed:21680843, PubMed:22582261, PubMed:23230272, PubMed:25043379, PubMed:26344098, PubMed:26626479, PubMed:26626480, PubMed:30104678, PubMed:31796734, PubMed:32028527, PubMed:32241924, PubMed:32358582, PubMed:33186521, PubMed:34465625, PubMed:34737271). Mediates glutamate, aspartate, serine, histidine or tyrosine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units (PubMed:19764761, PubMed:25043379, PubMed:28190768, PubMed:29954836, PubMed:35393539, PubMed:7852410, PubMed:9315851). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (PubMed:33186521, PubMed:34874266). Specificity for the different amino acids is conferred by interacting factors, such as HPF1 and NMNAT1 (PubMed:28190768, PubMed:29954836, PubMed:32028527, PubMed:33186521, PubMed:33589610, PubMed:34625544, PubMed:34874266). Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 confers serine specificity by completing the PARP1 active site (PubMed:28190768, PubMed:29954836, PubMed:32028527, PubMed:33186521, PubMed:33589610, PubMed:34625544, PubMed:34874266). Also catalyzes tyrosine ADP-ribosylation of target proteins following interaction with HPF1 (PubMed:29954836, PubMed:30257210). Following interaction with NMNAT1, catalyzes glutamate and aspartate ADP-ribosylation of target proteins; NMNAT1 confers glutamate and aspartate specificity (By similarity). PARP1 initiates the repair of DNA breaks: recognizes and binds DNA breaks within chromatin and recruits HPF1, licensing serine ADP-ribosylation of target proteins, such as histones (H2BS6ADPr and H3S10ADPr), thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks (PubMed:17177976, PubMed:18172500, PubMed:19344625, PubMed:19661379, PubMed:23230272, PubMed:27067600, PubMed:34465625, PubMed:34874266). HPF1 initiates serine ADP-ribosylation but restricts the polymerase activity of PARP1 in order to limit the length of poly-ADP-ribose chains (PubMed:33683197, PubMed:34732825, PubMed:34795260). In addition to base excision repair (BER) pathway, also involved in double-strand breaks (DSBs) repair: together with TIMELESS, accumulates at DNA damage sites and promotes homologous recombination repair by mediating poly-ADP-ribosylation (PubMed:26344098, PubMed:30356214). Mediates the poly-ADP-ribosylation of a number of proteins, including itself, APLF, CHFR, RPA1 and NFAT5 (PubMed:17396150, PubMed:19764761, PubMed:24906880, PubMed:34049076). In addition to proteins, also able to ADP-ribosylate DNA: catalyzes ADP-ribosylation of DNA strand break termini containing terminal phosphates and a 2'-OH group in single- and double-stranded DNA, respectively (PubMed:27471034). Required for PARP9 and DTX3L recruitment to DNA damage sites (PubMed:23230272). PARP1-dependent PARP9-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites (PubMed:23230272). PARP1-mediated DNA repair in neurons plays a role in sleep: senses DNA damage in neurons and promotes sleep, facilitating efficient DNA repair (By similarity). In addition to DNA repair, also involved in other processes, such as transcription regulation, programmed cell death, membrane repair, adipogenesis and innate immunity (PubMed:15607977, PubMed:17177976, PubMed:19344625, PubMed:27256882, PubMed:32315358, PubMed:32844745, PubMed:35124853, PubMed:35393539, PubMed:35460603). Acts as a repressor of transcription: binds to nucleosomes and modulates chromatin structure in a manner similar to histone H1, thereby altering RNA polymerase II (PubMed:15607977, PubMed:22464733). Acts both as a positive and negative regulator of transcription elongation, depending on the context (PubMed:27256882, PubMed:35393539). Acts as a positive regulator of transcription elongation by mediating poly-ADP-ribosylation of NELFE, preventing RNA-binding activity of NELFE and relieving transcription pausing (PubMed:27256882). Acts as a negative regulator of transcription elongation in response to DNA damage by catalyzing poly-ADP-ribosylation of CCNT1, disrupting the phase separation activity of CCNT1 and subsequent activation of CDK9 (PubMed:35393539). Involved in replication fork progression following interaction with CARM1: mediates poly-ADP-ribosylation at replication forks, slowing fork progression (PubMed:33412112). Poly-ADP-ribose chains generated by PARP1 also play a role in poly-ADP-ribose-dependent cell death, a process named parthanatos (By similarity). Also acts as a negative regulator of the cGAS-STING pathway (PubMed:32315358, PubMed:32844745, PubMed:35460603). Acts by mediating poly-ADP-ribosylation of CGAS: PARP1 translocates into the cytosol following phosphorylation by PRKDC and catalyzes poly-ADP-ribosylation and inactivation of CGAS (PubMed:35460603). Acts as a negative regulator of adipogenesis: catalyzes poly-ADP-ribosylation of histone H2B on 'Glu-35' (H2BE35ADPr) following interaction with NMNAT1, inhibiting phosphorylation of H2B at 'Ser-36' (H2BS36ph), thereby blocking expression of pro-adipogenetic genes (By similarity). Involved in the synthesis of ATP in the nucleus, together with NMNAT1, PARG and NUDT5 (PubMed:27257257). Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming (PubMed:27257257)", "gene_name": "PARP1", "glycan_count": 1, "glycosylation_sites": [], "id": "P09874", "name": "PARP1", "organism": "Homo sapiens", "uniprot_id": "P09874" }, { "function": "Non-catalytic component of a structure-specific DNA repair endonuclease responsible for the 5'-incision during DNA repair. Responsible, in conjunction with SLX4, for the first step in the repair of interstrand cross-links (ICL). Participates in the processing of anaphase bridge-generating DNA structures, which consist in incompletely processed DNA lesions arising during S or G2 phase, and can result in cytokinesis failure. Also required for homology-directed repair (HDR) of DNA double-strand breaks, in conjunction with SLX4", "gene_name": "ERCC1", "glycan_count": 0, "glycosylation_sites": [], "id": "P07992", "name": "Excision repair cross-complementation group 1 (ERCC1)", "organism": "Homo sapiens", "uniprot_id": "P07992" }, { "function": "Chemoattractant for blood monocytes, memory T-helper cells and eosinophils. Causes the release of histamine from basophils and activates eosinophils. May activate several chemokine receptors including CCR1, CCR3, CCR4 and CCR5. One of the major HIV-suppressive factors produced by CD8+ T-cells. Recombinant RANTES protein induces a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV). The processed form RANTES(3-68) acts as a natural chemotaxis inhibitor and is a more potent inhibitor of HIV-1-infection. The second processed form RANTES(4-68) exhibits reduced chemotactic and HIV-suppressive activity compared with RANTES(1-68) and RANTES(3-68) (PubMed:1380064, PubMed:15923218, PubMed:16791620, PubMed:8525373, PubMed:9516414). May also be an agonist of the G protein-coupled receptor GPR75, stimulating inositol trisphosphate production and calcium mobilization through its activation. Together with GPR75, may play a role in neuron survival through activation of a downstream signaling pathway involving the PI3, Akt and MAP kinases. By activating GPR75 may also play a role in insulin secretion by islet cells (PubMed:23979485)", "gene_name": "CCL5", "glycan_count": 0, "glycosylation_sites": [ { "position": 27, "type": "O-linked (GalNAc...) serine; partial" }, { "position": 28, "type": "O-linked (GalNAc...) serine; partial" } ], "id": "P13501", "name": "C-C motif chemokine ligand 5 (CCL5)", "organism": "Homo sapiens", "uniprot_id": "P13501" }, { "function": "Has a dual specificity toward Ser/Thr and Tyr-containing proteins", "gene_name": "DUSP19", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8WTR2", "name": "Tumor necrosis factor receptor-associated factor 3 interacting protein 2 (TRAF3IP2)", "organism": "Homo sapiens", "uniprot_id": "Q8WTR2" }, { "function": "Transcriptional regulator mainly expressed in hematopoietic cells that plays a critical role in cellular growth, differentiation and immune response (PubMed:10961885, PubMed:37256972, PubMed:8943379). Plays a key role in the differentiation of T-helper 1 cells and the production of interferon-gamma (PubMed:12213961, PubMed:35614130). Also participates in multiple neutrophil functions including chemotaxis and production of the neutrophil extracellular traps (By similarity). After IL12 binding to its receptor IL12RB2, STAT4 interacts with the intracellular domain of IL12RB2 and becomes tyrosine phosphorylated (PubMed:10415122, PubMed:7638186). Phosphorylated STAT4 then homodimerizes and migrates to the nucleus where it can recognize STAT target sequences present in IL12 responsive genes. Although IL12 appears to be the predominant activating signal, STAT4 can also be phosphorylated and activated in response to IFN-gamma stimulation via JAK1 and TYK2 and in response to different interleukins including IL23, IL2 and IL35 (PubMed:11114383, PubMed:34508746). Transcription activation of IFN-gamma gene is mediated by interaction with JUN that forms a complex that efficiently interacts with the AP-1-related sequence of the IFN-gamma promoter (By similarity). In response to IFN-alpha/beta signaling, acts as a transcriptional repressor and suppresses IL5 and IL13 mRNA expression during response to T-cell receptor (TCR) activation (PubMed:26990433)", "gene_name": "STAT4", "glycan_count": 1, "glycosylation_sites": [], "id": "Q14765", "name": "Signal transducer and activator of transcription 4 (STAT4)", "organism": "Homo sapiens", "uniprot_id": "Q14765" }, { "function": "Acts as a negative regulator of T-cell receptor (TCR) signaling by direct dephosphorylation of the Src family kinases LCK and FYN, ITAMs of the TCRz/CD3 complex, as well as ZAP70, VAV, VCP and other key signaling molecules (PubMed:16461343, PubMed:18056643). Associates with and probably dephosphorylates CBL. Dephosphorylates LCK at its activating 'Tyr-394' residue (PubMed:21719704). Dephosphorylates ZAP70 at its activating 'Tyr-493' residue (PubMed:16461343). Dephosphorylates the immune system activator SKAP2 (PubMed:21719704). Positively regulates toll-like receptor (TLR)-induced type 1 interferon production (PubMed:23871208). Promotes host antiviral responses mediated by type 1 interferon (By similarity). Regulates NOD2-induced pro-inflammatory cytokine secretion and autophagy (PubMed:23991106). Acts as an activator of NLRP3 inflammasome assembly by mediating dephosphorylation of 'Tyr-861' of NLRP3 (PubMed:27043286). Dephosphorylates phospho-anandamide (p-AEA), an endocannabinoid to anandamide (also called N-arachidonoylethanolamide) (By similarity)", "gene_name": "PTPN22", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y2R2", "name": "Protein tyrosine phosphatase non-receptor type 22 (PTPN22)", "organism": "Homo sapiens", "uniprot_id": "Q9Y2R2" }, { "function": "Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome (PubMed:19325628, PubMed:25555158). SNRNP70 binds to the loop I region of U1-snRNA (PubMed:19325628, PubMed:2467746, PubMed:25555158)", "gene_name": "SNRNP70", "glycan_count": 1, "glycosylation_sites": [], "id": "P08621", "name": "U1-ribonucleoprotein (U1-RNP)", "organism": "Homo sapiens", "uniprot_id": "P08621" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Ro52: Q9Y4W2, Ro60: P10155", "name": "Sj\u00f6gren\u2019s syndrome A (SSA/Ro52 and SSA/Ro60)", "organism": "", "uniprot_id": "" }, { "function": "Binds to the 3' poly(U) terminus of nascent RNA polymerase III transcripts, protecting them from exonuclease digestion and facilitating their folding and maturation (PubMed:2470590, PubMed:3192525). In case of Coxsackievirus B3 infection, binds to the viral internal ribosome entry site (IRES) and stimulates the IRES-mediated translation (PubMed:12384597)", "gene_name": "SSB", "glycan_count": 1, "glycosylation_sites": [], "id": "P05455", "name": "Sj\u00f6gren\u2019s syndrome B (SSB/La)", "organism": "Homo sapiens", "uniprot_id": "P05455" }, { "function": "Catalyzes the hydrolysis of glycosphingolipids and participates in their degradation in the lysosome", "gene_name": "GLA", "glycan_count": 51, "glycosylation_sites": [ { "position": 139, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 192, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 215, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P06280", "name": "\u03b1-galactosidase A (GLA)", "organism": "Homo sapiens", "uniprot_id": "P06280" }, { "function": "Involved in regulation of the actin cytoskeleton. May regulate WAS actin-bundling activity. Bridges the interaction between ABL1 and PTPN18 leading to ABL1 dephosphorylation. May play a role as a scaffold protein between PTPN12 and WAS and allow PTPN12 to dephosphorylate WAS. Has the potential to physically couple CD2 and CD2AP to WAS. Acts downstream of CD2 and CD2AP to recruit WAS to the T-cell:APC contact site so as to promote the actin polymerization required for synapse induction during T-cell activation (By similarity). Down-regulates CD2-stimulated adhesion through the coupling of PTPN12 to CD2. Also has a role in innate immunity and the inflammatory response. Recruited to inflammasomes by MEFV. Induces formation of pyroptosomes, large supramolecular structures composed of oligomerized PYCARD dimers which form prior to inflammatory apoptosis. Binding to MEFV allows MEFV to bind to PYCARD and facilitates pyroptosome formation. Regulates endocytosis and cell migration in neutrophils", "gene_name": "PSTPIP1", "glycan_count": 1, "glycosylation_sites": [], "id": "O43586", "name": "Rab escort protein 1 (REP1)", "organism": "Homo sapiens", "uniprot_id": "O43586" }, { "function": "Involved in hearing and vision as member of the USH2 complex. In the inner ear, required for the maintenance of the hair bundle ankle formation, which connects growing stereocilia in developing cochlear hair cells. In retina photoreceptors, the USH2 complex is required for the maintenance of periciliary membrane complex that seems to play a role in regulating intracellular protein transport", "gene_name": "USH2A", "glycan_count": 2, "glycosylation_sites": [ { "position": 361, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 451, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 587, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 611, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 650, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 697, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 839, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 856, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 862, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 888, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 944, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1011, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1071, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1151, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1174, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1379, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1388, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1479, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1635, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1779, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1903, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2011, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2014, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2048, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2130, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2182, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2195, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2258, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2285, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2322, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2377, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2382, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2407, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2413, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2581, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2584, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2656, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2710, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2770, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2788, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2930, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2937, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2970, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3032, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3099, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3217, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3330, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3419, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3433, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3653, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3694, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3733, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3780, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3849, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3984, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4202, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4226, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4317, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4418, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4564, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4583, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4691, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4754, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4800, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4943, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4950, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O75445", "name": "Usherin (USH2A)", "organism": "Homo sapiens", "uniprot_id": "O75445" }, { "function": "Is an adhesion molecule necessary for normal myelination in the peripheral nervous system. It mediates adhesion between adjacent myelin wraps and ultimately drives myelin compaction", "gene_name": "MPZ", "glycan_count": 15, "glycosylation_sites": [ { "position": 122, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P25189", "name": "Myelin protein zero (MPZ)", "organism": "Homo sapiens", "uniprot_id": "P25189" }, { "function": "Required for the assembly of mature ribosomes and ribosome biogenesis. Together with EFL1, triggers the GTP-dependent release of EIF6 from 60S pre-ribosomes in the cytoplasm, thereby activating ribosomes for translation competence by allowing 80S ribosome assembly and facilitating EIF6 recycling to the nucleus, where it is required for 60S rRNA processing and nuclear export. Required for normal levels of protein synthesis. May play a role in cellular stress resistance. May play a role in cellular response to DNA damage. May play a role in cell proliferation", "gene_name": "SBDS", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y3A5", "name": "SBDS", "organism": "Homo sapiens", "uniprot_id": "Q9Y3A5" }, { "function": "Thiol protease involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation. Involved in the release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen (PubMed:11082042)", "gene_name": "CTSK", "glycan_count": 0, "glycosylation_sites": [ { "position": 103, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P43235", "name": "Cathepsin K", "organism": "Homo sapiens", "uniprot_id": "P43235" }, { "function": "May function as a growth factor receptor", "gene_name": "TACSTD2", "glycan_count": 34, "glycosylation_sites": [ { "position": 33, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 120, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 168, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 208, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P09758", "name": "TROP-2", "organism": "Homo sapiens", "uniprot_id": "P09758" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P13688 (human ortholog)", "name": "CEACAM-1", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P14735 (human ortholog)", "name": "Insulin-Degrading Enzyme (IDE)", "organism": "", "uniprot_id": "" }, { "function": "Plays a role in the release of virion progenies by disrupting the host plasma membrane", "gene_name": "VP5", "glycan_count": 0, "glycosylation_sites": [], "id": "Q77DJ4", "name": "Marburg virus glycoprotein (GP)", "organism": "Avian infectious bursal disease virus", "uniprot_id": "Q77DJ4" }, { "function": "Pathogen-recognition receptor expressed on the surface of immature dendritic cells (DCs) and involved in initiation of primary immune response. Thought to mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. The receptor returns to the cell membrane surface and the pathogen-derived antigens are presented to resting T-cells via MHC class II proteins to initiate the adaptive immune response", "gene_name": "CD209", "glycan_count": 4, "glycosylation_sites": [ { "position": 80, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NNX6", "name": "DC-SIGN (CD209)", "organism": "Homo sapiens", "uniprot_id": "Q9NNX6" }, { "function": "Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). Ig alpha is the major immunoglobulin class in body secretions (PubMed:2241915)", "gene_name": "IGHA2", "glycan_count": 120, "glycosylation_sites": [ { "position": 47, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 92, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 131, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 205, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 327, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P01877", "name": "Immunoglobulin Y (IgY)", "organism": "Homo sapiens", "uniprot_id": "P01877" }, { "function": "Functions as transport protein in the blood stream", "gene_name": "ogchi", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8JIG5", "name": "Vitellogenin-1", "organism": "Gallus gallus", "uniprot_id": "Q8JIG5" }, { "function": "Together with the alpha chain CGA constitutes follitropin, the follicle-stimulating hormone, and provides its biological specificity to the hormone heterodimer. Binds FSHR, a G protein-coupled receptor, on target cells to activate downstream signaling pathways. Follitropin is involved in follicle development and spermatogenesis in reproductive organs", "gene_name": "FSHB", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8JIG4", "name": "Vitellogenin-2", "organism": "Coturnix japonica", "uniprot_id": "Q8JIG4" }, { "function": "High affinity receptor for melatonin. Likely to mediate the reproductive and circadian actions of melatonin. The activity of this receptor is mediated by pertussis toxin sensitive G proteins that inhibit adenylate cyclase activity", "gene_name": "MTNR1B", "glycan_count": 0, "glycosylation_sites": [ { "position": 4, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P49286", "name": "HCAR2", "organism": "Homo sapiens", "uniprot_id": "P49286" }, { "function": "Modulator of adipocyte lipid metabolism. Coats lipid storage droplets to protect them from breakdown by hormone-sensitive lipase (HSL). Its absence may result in leanness. Plays a role in unilocular lipid droplet formation by activating CIDEC. Their interaction promotes lipid droplet enlargement and directional net neutral lipid transfer. May modulate lipolysis and triglyceride levels", "gene_name": "PLIN1", "glycan_count": 1, "glycosylation_sites": [], "id": "O60240", "name": "Perilipin-1", "organism": "Homo sapiens", "uniprot_id": "O60240" }, { "function": "Innate immune receptor which acts as a cytoplasmic sensor of viral nucleic acids and plays a major role in sensing viral infection and in the activation of a cascade of antiviral responses including the induction of type I interferons and pro-inflammatory cytokines (PubMed:28594402, PubMed:32169843, PubMed:33727702). Its ligands include mRNA lacking 2'-O-methylation at their 5' cap and long-dsRNA (>1 kb in length) (PubMed:22160685). Upon ligand binding it associates with mitochondria antiviral signaling protein (MAVS/IPS1) which activates the IKK-related kinases: TBK1 and IKBKE which phosphorylate interferon regulatory factors: IRF3 and IRF7 which in turn activate transcription of antiviral immunological genes, including interferons (IFNs); IFN-alpha and IFN-beta. Responsible for detecting the Picornaviridae family members such as encephalomyocarditis virus (EMCV), mengo encephalomyocarditis virus (ENMG), and rhinovirus (PubMed:28606988). Detects coronavirus SARS-CoV-2 (PubMed:33440148, PubMed:33514628). Can also detect other viruses such as dengue virus (DENV), west Nile virus (WNV), and reovirus. Also involved in antiviral signaling in response to viruses containing a dsDNA genome, such as vaccinia virus. Plays an important role in amplifying innate immune signaling through recognition of RNA metabolites that are produced during virus infection by ribonuclease L (RNase L). May play an important role in enhancing natural killer cell function and may be involved in growth inhibition and apoptosis in several tumor cell lines", "gene_name": "IFIH1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9BYX4", "name": "MDA5 (Melanoma Differentiation-Associated Gene 5)", "organism": "Homo sapiens", "uniprot_id": "Q9BYX4" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P09261 (gE)", "name": "Varicella-Zoster Virus Glycoproteins (e.g., gE, gB)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "pol", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9QJY0", "name": "VZV DNA Polymerase (UL30)", "organism": "Human immunodeficiency virus type 1", "uniprot_id": "Q9QJY0" }, { "function": "May act as a papain-like cysteine protease inhibitor to modulate the host immune response against tumor cells. Also functions as an inhibitor of UV-induced apoptosis via suppression of the activity of c-Jun NH(2)-terminal kinase (JNK1)", "gene_name": "SERPINB3", "glycan_count": 1, "glycosylation_sites": [], "id": "P29508", "name": "Squamous cell carcinoma antigen (SCC antigen)", "organism": "Homo sapiens", "uniprot_id": "P29508" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P13647/P05787", "name": "Cytokeratin 5/6 (CK5/6)", "organism": "", "uniprot_id": "" }, { "function": "Transcription factor which regulates the transcription of multiple genes expressed in the intestinal epithelium (By similarity). Binds to the promoter of the intestinal sucrase-isomaltase SI and activates SI transcription (By similarity). Binds to the DNA sequence 5'-ATAAAAACTTAT-3' in the promoter region of VDR and activates VDR transcription (By similarity). Binds to and activates transcription of LPH (By similarity). Activates transcription of CLDN2 and intestinal mucin MUC2 (By similarity). Binds to the 5'-AATTTTTTACAACACCT-3' DNA sequence in the promoter region of CA1 and activates CA1 transcription (By similarity). Important in broad range of functions from early differentiation to maintenance of the intestinal epithelial lining of both the small and large intestine. Binds preferentially to methylated DNA (PubMed:28473536)", "gene_name": "CDX2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q99626", "name": "Caudal type homeobox 2 (CDX2)", "organism": "Homo sapiens", "uniprot_id": "Q99626" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P29990 (DENV2)", "name": "Envelope glycoprotein (E)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y8N3", "name": "Aquifex aeolicus Lumazine synthase (aaLS)", "organism": "", "uniprot_id": "Q9Y8N3" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O25710", "name": "Helicobacter pylori Ferritin (hpFer)", "organism": "Helicobacter pylori (strain ATCC 700392 / 26695)", "uniprot_id": "O25710" }, { "function": "Involved in the costimulatory signal, essential for T-cell proliferation and IFNG production in a PDCD1-independent manner. Interaction with PDCD1 inhibits T-cell proliferation by blocking cell cycle progression and cytokine production (By similarity)", "gene_name": "PDCD1LG2", "glycan_count": 0, "glycosylation_sites": [ { "position": 37, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 64, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 157, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 163, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 189, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9BQ51", "name": "PD-L2", "organism": "Homo sapiens", "uniprot_id": "Q9BQ51" }, { "function": "Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2 (PubMed:14751930, PubMed:16223769, PubMed:16410248, PubMed:16480718, PubMed:17381073, PubMed:18095711, PubMed:21288888, PubMed:24371721). Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vitronectin, tenascin, laminin, fibronectin, fibrin or casein (PubMed:10347120, PubMed:10455171, PubMed:12376466, PubMed:16223769, PubMed:16651416, PubMed:18095711, PubMed:2172980, PubMed:7923219, PubMed:9065413). Also has dipeptidyl peptidase activity, exhibiting the ability to hydrolyze the prolyl bond two residues from the N-terminus of synthetic dipeptide substrates provided that the penultimate residue is proline, with a preference for Ala-Pro, Ile-Pro, Gly-Pro, Arg-Pro and Pro-Pro (PubMed:10347120, PubMed:10593948, PubMed:16175601, PubMed:16223769, PubMed:16410248, PubMed:16651416, PubMed:17381073, PubMed:21314817, PubMed:24371721, PubMed:24717288). Natural neuropeptide hormones for dipeptidyl peptidase are the neuropeptide Y (NPY), peptide YY (PYY), substance P (TAC1) and brain natriuretic peptide 32 (NPPB) (PubMed:21314817). The plasma membrane form, in association with either DPP4, PLAUR or integrins, is involved in the pericellular proteolysis of the extracellular matrix (ECM), and hence promotes cell adhesion, migration and invasion through the ECM. Plays a role in tissue remodeling during development and wound healing. Participates in the cell invasiveness towards the ECM in malignant melanoma cancers. Enhances tumor growth progression by increasing angiogenesis, collagen fiber degradation and apoptosis and by reducing antitumor response of the immune system. Promotes glioma cell invasion through the brain parenchyma by degrading the proteoglycan brevican. Acts as a tumor suppressor in melanocytic cells through regulation of cell proliferation and survival in a serine protease activity-independent manner", "gene_name": "FAP", "glycan_count": 27, "glycosylation_sites": [ { "position": 49, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 92, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 99, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 227, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 314, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 679, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q12884", "name": "FAP (Fibroblast activation protein)", "organism": "Homo sapiens", "uniprot_id": "Q12884" }, { "function": "Binds galactosides (PubMed:18005988). Has high affinity for the Forssman pentasaccharide (PubMed:18005988). Ligand for HAVCR2/TIM3 (PubMed:16286920). Binding to HAVCR2 induces T-helper type 1 lymphocyte (Th1) death (PubMed:16286920). Also stimulates bactericidal activity in infected macrophages by causing macrophage activation and IL1B secretion which restricts intracellular bacterial growth (By similarity). Ligand for P4HB; the interaction retains P4HB at the cell surface of Th2 T-helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307). Ligand for CD44; the interaction enhances binding of SMAD3 to the FOXP3 promoter, leading to up-regulation of FOXP3 expression and increased induced regulatory T (iTreg) cell stability and suppressive function (By similarity). Promotes ability of mesenchymal stromal cells to suppress T-cell proliferation (PubMed:23817958). Expands regulatory T-cells and induces cytotoxic T-cell apoptosis following virus infection (PubMed:20209097). Activates ERK1/2 phosphorylation inducing cytokine (IL-6, IL-8, IL-12) and chemokine (CCL2) production in mast and dendritic cells (PubMed:16116184, PubMed:24465902). Inhibits degranulation and induces apoptosis of mast cells (PubMed:24465902). Induces maturation and migration of dendritic cells (PubMed:16116184, PubMed:25754930). Inhibits natural killer (NK) cell function (PubMed:23408620). Can transform NK cell phenotype from peripheral to decidual during pregnancy (PubMed:25578313). Astrocyte derived galectin-9 enhances microglial TNF production (By similarity). May play a role in thymocyte-epithelial interactions relevant to the biology of the thymus. May provide the molecular basis for urate flux across cell membranes, allowing urate that is formed during purine metabolism to efflux from cells and serving as an electrogenic transporter that plays an important role in renal and gastrointestinal urate excretion (By similarity). Highly selective to the anion urate (By similarity)", "gene_name": "LGALS9", "glycan_count": 0, "glycosylation_sites": [], "id": "O00182", "name": "Galectin-9", "organism": "Homo sapiens", "uniprot_id": "O00182" }, { "function": "May participate in the regulation of T-cell-mediated immune response. May play a protective role in tumor cells by inhibiting natural-killer mediated cell lysis as well as a role of marker for detection of neuroblastoma cells. May be involved in the development of acute and chronic transplant rejection and in the regulation of lymphocytic activity at mucosal surfaces. Could also play a key role in providing the placenta and fetus with a suitable immunological environment throughout pregnancy. Both isoform 1 and isoform 2 appear to be redundant in their ability to modulate CD4 T-cell responses. Isoform 2 is shown to enhance the induction of cytotoxic T-cells and selectively stimulates interferon gamma production in the presence of T-cell receptor signaling", "gene_name": "CD276", "glycan_count": 79, "glycosylation_sites": [ { "position": 104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 189, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 215, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 322, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 407, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 433, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q5ZPR3", "name": "CD276 (B7-H3)", "organism": "Homo sapiens", "uniprot_id": "Q5ZPR3" }, { "function": "Cell surface receptor for PLXNB1, PLXNB2, PLXNB3 and PLXND1 that plays an important role in cell-cell signaling (By similarity). Regulates glutamatergic and GABAergic synapse development (By similarity). Promotes the development of inhibitory synapses in a PLXNB1-dependent manner and promotes the development of excitatory synapses in a PLXNB2-dependent manner (By similarity). Plays a role in priming antigen-specific T-cells, promotes differentiation of Th1 T-helper cells, and thereby contributes to adaptive immunity (By similarity). Promotes phosphorylation of TIMD2 (By similarity). Inhibits angiogenesis (By similarity). Promotes axon growth cone collapse (By similarity). Inhibits axonal extension by providing local signals to specify territories inaccessible for growing axons (By similarity)", "gene_name": "SEMA4A", "glycan_count": 7, "glycosylation_sites": [ { "position": 120, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 135, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 496, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 607, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9H3S1", "name": "SEMA4A", "organism": "Homo sapiens", "uniprot_id": "Q9H3S1" }, { "function": "Calcium-dependent cell adhesion protein; preferentially mediates homotypic cell-cell adhesion by dimerization with a CDH2 chain from another cell. Cadherins may thus contribute to the sorting of heterogeneous cell types. Acts as a regulator of neural stem cells quiescence by mediating anchorage of neural stem cells to ependymocytes in the adult subependymal zone: upon cleavage by MMP24, CDH2-mediated anchorage is affected, leading to modulate neural stem cell quiescence. Plays a role in cell-to-cell junction formation between pancreatic beta cells and neural crest stem (NCS) cells, promoting the formation of processes by NCS cells (By similarity). Required for proper neurite branching. Required for pre- and postsynaptic organization (By similarity). CDH2 may be involved in neuronal recognition mechanism. In hippocampal neurons, may regulate dendritic spine density", "gene_name": "CDH2", "glycan_count": 37, "glycosylation_sites": [ { "position": 190, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 273, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 325, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 402, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 572, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 651, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 692, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P19022", "name": "N-cadherin", "organism": "Homo sapiens", "uniprot_id": "P19022" }, { "function": "Tubulin is the major constituent of microtubules, protein filaments consisting of alpha- and beta-tubulin heterodimers (PubMed:34996871, PubMed:38305685, PubMed:38609661). Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms (PubMed:34996871, PubMed:38305685, PubMed:38609661). Below the cap, alpha-beta tubulin heterodimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin (PubMed:34996871, PubMed:38609661). TUBB3 plays a critical role in proper axon guidance and maintenance (PubMed:20074521). Binding of NTN1/Netrin-1 to its receptor UNC5C might cause dissociation of UNC5C from polymerized TUBB3 in microtubules and thereby lead to increased microtubule dynamics and axon repulsion (PubMed:28483977). Plays a role in dorsal root ganglion axon projection towards the spinal cord (PubMed:28483977)", "gene_name": "TUBB3", "glycan_count": 2, "glycosylation_sites": [], "id": "Q13509", "name": "\u03b2-Tubulin III", "organism": "Homo sapiens", "uniprot_id": "Q13509" }, { "function": "Serine/threonine-protein kinase involved in various processes such as cell proliferation, differentiation, migration, transformation and programmed cell death. Extracellular stimuli such as pro-inflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway (PubMed:28943315). In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK8/JNK1. In turn, MAPK8/JNK1 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN, JDP2 and ATF2 and thus regulates AP-1 transcriptional activity (PubMed:18307971). Phosphorylates the replication licensing factor CDT1, inhibiting the interaction between CDT1 and the histone H4 acetylase HBO1 to replication origins (PubMed:21856198). Loss of this interaction abrogates the acetylation required for replication initiation (PubMed:21856198). Promotes stressed cell apoptosis by phosphorylating key regulatory factors including p53/TP53 and Yes-associates protein YAP1 (PubMed:21364637). In T-cells, MAPK8 and MAPK9 are required for polarized differentiation of T-helper cells into Th1 cells. Contributes to the survival of erythroid cells by phosphorylating the antagonist of cell death BAD upon EPO stimulation (PubMed:21095239). Mediates starvation-induced BCL2 phosphorylation, BCL2 dissociation from BECN1, and thus activation of autophagy (PubMed:18570871). Phosphorylates STMN2 and hence regulates microtubule dynamics, controlling neurite elongation in cortical neurons (By similarity). In the developing brain, through its cytoplasmic activity on STMN2, negatively regulates the rate of exit from multipolar stage and of radial migration from the ventricular zone (By similarity). Phosphorylates several other substrates including heat shock factor protein 4 (HSF4), the deacetylase SIRT1, ELK1, or the E3 ligase ITCH (PubMed:16581800, PubMed:17296730, PubMed:20027304). Phosphorylates the CLOCK-BMAL1 heterodimer and plays a role in the regulation of the circadian clock (PubMed:22441692). Phosphorylates the heat shock transcription factor HSF1, suppressing HSF1-induced transcriptional activity (PubMed:10747973). Phosphorylates POU5F1, which results in the inhibition of POU5F1's transcriptional activity and enhances its proteasomal degradation (By similarity). Phosphorylates JUND and this phosphorylation is inhibited in the presence of MEN1 (PubMed:22327296). In neurons, phosphorylates SYT4 which captures neuronal dense core vesicles at synapses (By similarity). Phosphorylates EIF4ENIF1/4-ET in response to oxidative stress, promoting P-body assembly (PubMed:22966201). Phosphorylates SIRT6 in response to oxidative stress, stimulating its mono-ADP-ribosyltransferase activity (PubMed:27568560). Phosphorylates NLRP3, promoting assembly of the NLRP3 inflammasome (PubMed:28943315). Phosphorylates ALKBH5 in response to reactive oxygen species (ROS), promoting ALKBH5 sumoylation and inactivation (PubMed:34048572)", "gene_name": "MAPK8", "glycan_count": 0, "glycosylation_sites": [], "id": "P45983", "name": "JNK", "organism": "Homo sapiens", "uniprot_id": "P45983" }, { "function": "Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway (PubMed:34497368). MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade also plays a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1) and a variety of other signaling-related molecules (like ARHGEF2, DEPTOR, FRS2 or GRB10) (PubMed:35216969). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade", "gene_name": "MAPK3", "glycan_count": 0, "glycosylation_sites": [], "id": "P27361", "name": "ERK", "organism": "Homo sapiens", "uniprot_id": "P27361" }, { "function": "Involved in the development of the olfactory system and in neuronal control of puberty. Induces the collapse and paralysis of neuronal growth cones. Could serve as a ligand that guides specific growth cones by a motility-inhibiting mechanism. Binds to the complex neuropilin-1/plexin-1", "gene_name": "SEMA3A", "glycan_count": 3, "glycosylation_sites": [ { "position": 53, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 125, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 590, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q14563", "name": "Semaphorin 3A (Sema3A)", "organism": "Homo sapiens", "uniprot_id": "Q14563" }, { "function": "Anti-inflammatory antagonist of interleukin-1 family of proinflammatory cytokines such as interleukin-1beta/IL1B and interleukin-1alpha/IL1A. Protects from immune dysregulation and uncontrolled systemic inflammation triggered by IL1 for a range of innate stimulatory agents such as pathogens", "gene_name": "IL1RN", "glycan_count": 2, "glycosylation_sites": [ { "position": 109, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P18510", "name": "Interleukin-1 receptor antagonist (IL-1Ra)", "organism": "Homo sapiens", "uniprot_id": "P18510" }, { "function": "Cytoskeletal linker protein. Acts as an integrator of intermediate filaments, actin and microtubule cytoskeleton networks. Required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. The proteins may self-aggregate to form filaments or a two-dimensional mesh. Regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport. Mediates docking of the dynein/dynactin motor complex to vesicle cargos for retrograde axonal transport through its interaction with TMEM108 and DCTN1 (By similarity)", "gene_name": "DST", "glycan_count": 2, "glycosylation_sites": [], "id": "Q03001", "name": "BP230", "organism": "Homo sapiens", "uniprot_id": "Q03001" }, { "function": "Forms physiological amyloids that play a central role in melanosome morphogenesis and pigmentation. The maturation of unpigmented premelanosomes from stage I to II is marked by assembly of processed amyloidogenic fragments into parallel fibrillar sheets, which elongate the vesicle into a striated ellipsoidal shape. In pigmented stage III and IV melanosomes, the amyloid matrix serves as a platform where eumelanin precursors accumulate at high local concentrations for pigment formation. May prevent pigmentation-associated toxicity by sequestering toxic reaction intermediates of eumelanin biosynthesis pathway", "gene_name": "PMEL", "glycan_count": 0, "glycosylation_sites": [ { "position": 81, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 106, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 111, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 321, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 568, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P40967", "name": "gp100 (melanocyte antigen)", "organism": "Homo sapiens", "uniprot_id": "P40967" }, { "function": "This endonuclease is specific to the thymidylate synthase (td) gene splice junction and is involved in intron homing", "gene_name": "ITEVIR", "glycan_count": 0, "glycosylation_sites": [], "id": "P13299", "name": "CMV envelope glycoprotein H", "organism": "Enterobacteria phage T4", "uniprot_id": "P13299" }, { "function": "Binds to the DNA consensus sequence 5'-GGGGAATCTCC-3'", "gene_name": "Nfrkb", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8K0X6", "name": "MYOM3 (Myomesin-3)", "organism": "Mus musculus", "uniprot_id": "Q6PIJ4" }, { "function": "Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity", "gene_name": "TNNT2", "glycan_count": 1, "glycosylation_sites": [], "id": "P45379", "name": "hs-cTnT (high-sensitivity cardiac troponin T)", "organism": "Homo sapiens", "uniprot_id": "P45379" }, { "function": "Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components", "gene_name": "Lamc1", "glycan_count": 44, "glycosylation_sites": [ { "position": 58, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 132, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 574, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 648, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1020, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1105, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1159, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1173, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1203, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1221, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1239, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1378, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1393, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1437, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P02468", "name": "Laminin", "organism": "Mus musculus", "uniprot_id": "P02468" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q02817 (human)", "name": "Mucin-2", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P15941 (human)", "name": "Mucin-1", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y2V2 (human)", "name": "FCGBP", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q07654 (human)", "name": "Intestinal Trefoil Factor (ITF/TFF3)", "organism": "", "uniprot_id": "" }, { "function": "Calcium sensor that participates in triggering neurotransmitter release at the synapse (By similarity). May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse (By similarity). It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2. Plays a role in dendrite formation by melanocytes (PubMed:23999003)", "gene_name": "SYT1", "glycan_count": 1, "glycosylation_sites": [ { "position": 25, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P21579", "name": "Synaptotagmin-1", "organism": "Homo sapiens", "uniprot_id": "P21579" }, { "function": "t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 in pancreatic beta cells", "gene_name": "SNAP25", "glycan_count": 1, "glycosylation_sites": [], "id": "P60880", "name": "Synaptosomal-associated protein 25 (SNAP25)", "organism": "Homo sapiens", "uniprot_id": "P60880" }, { "function": "Acts as a 'third messenger' substrate of protein kinase C-mediated molecular cascades during synaptic development and remodeling. Binds to calmodulin in the absence of calcium (By similarity)", "gene_name": "NRGN", "glycan_count": 0, "glycosylation_sites": [], "id": "Q92686", "name": "Neurogranin", "organism": "Homo sapiens", "uniprot_id": "Q92686" }, { "function": "This protein is associated with nerve growth. It is a major component of the motile 'growth cones' that form the tips of elongating axons. Plays a role in axonal and dendritic filopodia induction", "gene_name": "GAP43", "glycan_count": 1, "glycosylation_sites": [], "id": "P17677", "name": "Growth-associated protein 43 (GAP-43)", "organism": "Homo sapiens", "uniprot_id": "P17677" }, { "function": "Receptor for four distinct ligands: The TNF superfamily members TNFSF14/LIGHT and homotrimeric LTA/lymphotoxin-alpha and the immunoglobulin superfamily members BTLA and CD160, altogether defining a complex stimulatory and inhibitory signaling network (PubMed:10754304, PubMed:18193050, PubMed:23761635, PubMed:9462508). Signals via the TRAF2-TRAF3 E3 ligase pathway to promote immune cell survival and differentiation (PubMed:19915044, PubMed:9153189, PubMed:9162022). Participates in bidirectional cell-cell contact signaling between antigen presenting cells and lymphocytes. In response to ligation of TNFSF14/LIGHT, delivers costimulatory signals to T cells, promoting cell proliferation and effector functions (PubMed:10754304). Interacts with CD160 on NK cells, enhancing IFNG production and anti-tumor immune response (PubMed:23761635). In the context of bacterial infection, acts as a signaling receptor on epithelial cells for CD160 from intraepithelial lymphocytes, triggering the production of antimicrobial proteins and pro-inflammatory cytokines (By similarity). Upon binding to CD160 on activated CD4+ T cells, down-regulates CD28 costimulatory signaling, restricting memory and alloantigen-specific immune response (PubMed:18193050). May interact in cis (on the same cell) or in trans (on other cells) with BTLA (By similarity) (PubMed:19915044). In cis interactions, appears to play an immune regulatory role inhibiting in trans interactions in naive T cells to maintain a resting state. In trans interactions, can predominate during adaptive immune response to provide survival signals to effector T cells (By similarity) (PubMed:19915044)", "gene_name": "TNFRSF14", "glycan_count": 1, "glycosylation_sites": [ { "position": 110, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 173, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q92956", "name": "Syntaxin-1B", "organism": "Homo sapiens", "uniprot_id": "Q92956" }, { "function": "May be involved in protein trafficking from the plasma membrane to the early endosome (EE) as well as in homotypic fusion of endocytic organelles. Mediates the endocytic trafficking from early endosomes to late endosomes and lysosomes", "gene_name": "STX7", "glycan_count": 1, "glycosylation_sites": [], "id": "O15400", "name": "Syntaxin-7", "organism": "Homo sapiens", "uniprot_id": "O15400" }, { "function": "Binds ATP, opioids and phosphatidylethanolamine. Has lower affinity for phosphatidylinositol and phosphatidylcholine. Serine protease inhibitor which inhibits thrombin, neuropsin and chymotrypsin but not trypsin, tissue type plasminogen activator and elastase (By similarity). Inhibits the kinase activity of RAF1 by inhibiting its activation and by dissociating the RAF1/MEK complex and acting as a competitive inhibitor of MEK phosphorylation", "gene_name": "PEBP1", "glycan_count": 2, "glycosylation_sites": [], "id": "P30086", "name": "Phosphatidylethanolamine binding protein 1 (PEBP-1)", "organism": "Homo sapiens", "uniprot_id": "P30086" }, { "function": "Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments (PubMed:18039658). Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation (PubMed:17461796, PubMed:18197702, PubMed:18799458, PubMed:22074827). Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway (PubMed:18660751). Inhibits epithelial Na(+) channel (ENaC)-mediated Na(+) absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways", "gene_name": "PCSK9", "glycan_count": 1, "glycosylation_sites": [ { "position": 533, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8NBP7", "name": "Proprotein convertase subtilisin/kexin type 9 (PCSK9)", "organism": "Homo sapiens", "uniprot_id": "Q8NBP7" }, { "function": "S100A12 is a calcium-, zinc- and copper-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. Its pro-inflammatory activity involves recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to receptor for advanced glycation endproducts (AGER). Binding to AGER activates the MAP-kinase and NF-kappa-B signaling pathways leading to production of pro-inflammatory cytokines and up-regulation of cell adhesion molecules ICAM1 and VCAM1. Acts as a monocyte and mast cell chemoattractant. Can stimulate mast cell degranulation and activation which generates chemokines, histamine and cytokines inducing further leukocyte recruitment to the sites of inflammation. Can inhibit the activity of matrix metalloproteinases; MMP2, MMP3 and MMP9 by chelating Zn(2+) from their active sites. Possesses filariacidal and filariastatic activity. Calcitermin possesses antifungal activity against C.albicans and is also active against E.coli and P.aeruginosa but not L.monocytogenes and S.aureus", "gene_name": "S100A12", "glycan_count": 0, "glycosylation_sites": [], "id": "P80511", "name": "Protein S100-A12 (EN-RAGE/S100A12)", "organism": "Homo sapiens", "uniprot_id": "P80511" }, { "function": "Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage (PubMed:11342582, PubMed:27578112, PubMed:8675619). Although it has both phospholipase and triglyceride lipase activities it is primarily a triglyceride lipase with low but detectable phospholipase activity (PubMed:12032167, PubMed:7592706). Mediates margination of triglyceride-rich lipoprotein particles in capillaries (PubMed:24726386). Recruited to its site of action on the luminal surface of vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans (PubMed:11342582, PubMed:27811232)", "gene_name": "LPL", "glycan_count": 26, "glycosylation_sites": [ { "position": 70, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 386, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P06858", "name": "Lipoprotein lipase (LPL)", "organism": "Homo sapiens", "uniprot_id": "P06858" }, { "function": "Galactose-specific lectin which binds IgE. May mediate with the alpha-3, beta-1 integrin the stimulation by CSPG4 of endothelial cells migration. Together with DMBT1, required for terminal differentiation of columnar epithelial cells during early embryogenesis (By similarity). In the nucleus: acts as a pre-mRNA splicing factor. Involved in acute inflammatory responses including neutrophil activation and adhesion, chemoattraction of monocytes macrophages, opsonization of apoptotic neutrophils, and activation of mast cells. Together with TRIM16, coordinates the recognition of membrane damage with mobilization of the core autophagy regulators ATG16L1 and BECN1 in response to damaged endomembranes", "gene_name": "LGALS3", "glycan_count": 1, "glycosylation_sites": [], "id": "P17931", "name": "Galectin-3 (LGALS3)", "organism": "Homo sapiens", "uniprot_id": "P17931" }, { "function": "Plays important roles in the innate immune response as effector of glucocorticoid-mediated responses and regulator of the inflammatory process. Has anti-inflammatory activity (PubMed:8425544). Plays a role in glucocorticoid-mediated down-regulation of the early phase of the inflammatory response (By similarity). Contributes to the adaptive immune response by enhancing signaling cascades that are triggered by T-cell activation, regulates differentiation and proliferation of activated T-cells (PubMed:17008549). Promotes the differentiation of T-cells into Th1 cells and negatively regulates differentiation into Th2 cells (PubMed:17008549). Has no effect on unstimulated T cells (PubMed:17008549). Negatively regulates hormone exocytosis via activation of the formyl peptide receptors and reorganization of the actin cytoskeleton (PubMed:19625660). Has high affinity for Ca(2+) and can bind up to eight Ca(2+) ions (By similarity). Displays Ca(2+)-dependent binding to phospholipid membranes (PubMed:2532504, PubMed:8557678). Plays a role in the formation of phagocytic cups and phagosomes. Plays a role in phagocytosis by mediating the Ca(2+)-dependent interaction between phagosomes and the actin cytoskeleton (By similarity)", "gene_name": "ANXA1", "glycan_count": 2, "glycosylation_sites": [], "id": "P04083", "name": "Annexin A1", "organism": "Homo sapiens", "uniprot_id": "P04083" }, { "function": "Carrier protein for platelet (but not plasma) factor V/Va. Plays a role in the storage and stabilization of factor V in platelets. Upon release following platelet activation, may limit platelet and plasma factor Va-dependent thrombin generation. Ligand for integrin alpha-IIb/beta-3 and integrin alpha-V/beta-3 on activated platelets, and may function as an extracellular matrix or adhesive protein", "gene_name": "MMRN1", "glycan_count": 67, "glycosylation_sites": [ { "position": 21, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 97, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 114, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 120, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 136, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 216, "type": "O-linked (Fuc) threonine" }, { "position": 265, "type": "O-linked (Fuc) threonine" }, { "position": 344, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 431, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 507, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 541, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 576, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 618, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 680, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 729, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 783, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 816, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 828, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 840, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 921, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 933, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 942, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 981, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1020, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1055, "type": "O-linked (Fuc) threonine" }, { "position": 1075, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13201", "name": "Multimerin 1 (MMRN1)", "organism": "Homo sapiens", "uniprot_id": "Q13201" }, { "function": "Cadherins are calcium-dependent cell adhesion proteins (By similarity). They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types (PubMed:21269602). This cadherin may play a important role in endothelial cell biology through control of the cohesion and organization of the intercellular junctions (By similarity). It associates with alpha-catenin forming a link to the cytoskeleton (PubMed:10861224). Plays a role in coupling actin fibers to cell junctions in endothelial cells, via acting as a cell junctional complex anchor for AMOTL2 and MAGI1 (By similarity). Acts in concert with KRIT1 and PALS1 to establish and maintain correct endothelial cell polarity and vascular lumen (By similarity). These effects are mediated by recruitment and activation of the Par polarity complex and RAP1B (PubMed:20332120). Required for activation of PRKCZ and for the localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction (PubMed:20332120). Associates with CTNND1/p120-catenin to control CADH5 endocytosis (By similarity)", "gene_name": "CDH5", "glycan_count": 81, "glycosylation_sites": [ { "position": 61, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 112, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 157, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 362, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 442, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 523, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 535, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P33151", "name": "Cadherin-5 (CDH5/VE-cadherin)", "organism": "Homo sapiens", "uniprot_id": "P33151" }, { "function": "Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components", "gene_name": "LAMC1", "glycan_count": 201, "glycosylation_sites": [ { "position": 60, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 134, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 576, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 650, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1022, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1107, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1161, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1175, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1205, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1223, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1241, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1380, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1395, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1439, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P11047", "name": "Laminin subunit gamma 1 (LAMC1)", "organism": "Homo sapiens", "uniprot_id": "P11047" }, { "function": "Cell adhesion protein that promotes adhesion and outgrowth of hippocampal embryonic neurons. Binds directly to bacteria and their components and functions as an opsonin for macrophage phagocytosis of bacteria. Essential in the initiation of the innate immune response and represents a unique pattern-recognition molecule in the ECM for microbial pathogens (By similarity). Binds bacterial lipopolysaccharide (LPS)", "gene_name": "SPON2", "glycan_count": 0, "glycosylation_sites": [ { "position": 283, "type": "C-linked (Man) tryptophan" } ], "id": "Q9ULW1", "name": "Thrombospondin 4", "organism": "Homo sapiens", "uniprot_id": "Q9BUD6" }, { "function": "Type II collagen is specific for cartilaginous tissues. It is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces", "gene_name": "COL2A1", "glycan_count": 6, "glycosylation_sites": [ { "position": 190, "type": "O-linked (Gal...) hydroxylysine" }, { "position": 287, "type": "O-linked (Gal...) hydroxylysine" }, { "position": 299, "type": "O-linked (Gal...) hydroxylysine" }, { "position": 308, "type": "O-linked (Gal...) hydroxylysine" }, { "position": 374, "type": "O-linked (Gal...) hydroxylysine" }, { "position": 608, "type": "O-linked (Gal...) hydroxylysine" }, { "position": 620, "type": "O-linked (Gal...) hydroxylysine" }, { "position": 1130, "type": "O-linked (Gal...) hydroxylysine" }, { "position": 1388, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P02458", "name": "Collagen II (COL2A1)", "organism": "Homo sapiens", "uniprot_id": "P02458" }, { "function": "E3 ubiquitin ligase. Mediates the ubiquitination and subsequent proteasomal degradation of CKM, GMEB1 and HIBADH. Regulates the proteasomal degradation of muscle proteins under amino acid starvation, where muscle protein is catabolized to provide other organs with amino acids. Inhibits de novo skeletal muscle protein synthesis under amino acid starvation. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertrophy by regulating an anti-hypertrophic PKC-mediated signaling pathway. May regulate the organization of myofibrils through TTN in muscle cells", "gene_name": "TRIM63", "glycan_count": 1, "glycosylation_sites": [], "id": "Q969Q1", "name": "TRIM63 (MuRF1)", "organism": "Homo sapiens", "uniprot_id": "Q969Q1" }, { "function": "Serine/threonine-protein kinase that performs several important functions throughout M phase of the cell cycle, including the regulation of centrosome maturation and spindle assembly, the removal of cohesins from chromosome arms, the inactivation of anaphase-promoting complex/cyclosome (APC/C) inhibitors, and the regulation of mitotic exit and cytokinesis (PubMed:11202906, PubMed:12207013, PubMed:12447691, PubMed:12524548, PubMed:12738781, PubMed:12852856, PubMed:12939256, PubMed:14532005, PubMed:14734534, PubMed:15070733, PubMed:15148369, PubMed:15469984, PubMed:16198290, PubMed:16247472, PubMed:16980960, PubMed:17081991, PubMed:17351640, PubMed:17376779, PubMed:17617734, PubMed:18174154, PubMed:18331714, PubMed:18418051, PubMed:18477460, PubMed:18521620, PubMed:18615013, PubMed:19160488, PubMed:19351716, PubMed:19468300, PubMed:19468302, PubMed:19473992, PubMed:19509060, PubMed:19597481, PubMed:23455478, PubMed:23509069, PubMed:28512243, PubMed:8991084). Polo-like kinase proteins act by binding and phosphorylating proteins that are already phosphorylated on a specific motif recognized by the POLO box domains (PubMed:11202906, PubMed:12207013, PubMed:12447691, PubMed:12524548, PubMed:12738781, PubMed:12852856, PubMed:12939256, PubMed:14532005, PubMed:14734534, PubMed:15070733, PubMed:15148369, PubMed:15469984, PubMed:16198290, PubMed:16247472, PubMed:16980960, PubMed:17081991, PubMed:17351640, PubMed:17376779, PubMed:17617734, PubMed:18174154, PubMed:18331714, PubMed:18418051, PubMed:18477460, PubMed:18521620, PubMed:18615013, PubMed:19160488, PubMed:19351716, PubMed:19468300, PubMed:19468302, PubMed:19473992, PubMed:19509060, PubMed:19597481, PubMed:23455478, PubMed:23509069, PubMed:28512243, PubMed:8991084). Phosphorylates BORA, BUB1B/BUBR1, CCNB1, CDC25C, CEP55, ECT2, ERCC6L, FBXO5/EMI1, FOXM1, KIF20A/MKLP2, CENPU, NEDD1, NINL, NPM1, NUDC, PKMYT1/MYT1, KIZ, MRE11, PPP1R12A/MYPT1, POLQ, PRC1, RACGAP1/CYK4, RAD51, RHNO1, SGO1, STAG2/SA2, TEX14, TOPORS, p73/TP73, TPT1, WEE1 and HNRNPU (PubMed:11202906, PubMed:12207013, PubMed:12447691, PubMed:12524548, PubMed:12738781, PubMed:12852856, PubMed:12939256, PubMed:14532005, PubMed:14734534, PubMed:15070733, PubMed:15148369, PubMed:15469984, PubMed:16198290, PubMed:16247472, PubMed:16980960, PubMed:17081991, PubMed:17218258, PubMed:17351640, PubMed:17376779, PubMed:17617734, PubMed:18174154, PubMed:18331714, PubMed:18418051, PubMed:18477460, PubMed:18521620, PubMed:18615013, PubMed:19160488, PubMed:19351716, PubMed:19468300, PubMed:19468302, PubMed:19473992, PubMed:19509060, PubMed:19597481, PubMed:22325354, PubMed:23455478, PubMed:23509069, PubMed:25986610, PubMed:26811421, PubMed:28512243, PubMed:37440612, PubMed:37674080, PubMed:8991084). Plays a key role in centrosome functions and the assembly of bipolar spindles by phosphorylating KIZ, NEDD1 and NINL (PubMed:16980960, PubMed:19509060). NEDD1 phosphorylation promotes subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation (PubMed:19509060). Phosphorylation of NINL component of the centrosome leads to NINL dissociation from other centrosomal proteins (PubMed:12852856). Involved in mitosis exit and cytokinesis by phosphorylating CEP55, ECT2, KIF20A/MKLP2, CENPU, PRC1 and RACGAP1 (PubMed:12939256, PubMed:16247472, PubMed:17351640, PubMed:19468300, PubMed:19468302). Recruited at the central spindle by phosphorylating and docking PRC1 and KIF20A/MKLP2; creates its own docking sites on PRC1 and KIF20A/MKLP2 by mediating phosphorylation of sites subsequently recognized by the POLO box domains (PubMed:12939256, PubMed:17351640). Phosphorylates RACGAP1, thereby creating a docking site for the Rho GTP exchange factor ECT2 that is essential for the cleavage furrow formation (PubMed:19468300, PubMed:19468302). Promotes the central spindle recruitment of ECT2 (PubMed:16247472). Plays a central role in G2/M transition of mitotic cell cycle by phosphorylating CCNB1, CDC25C, FOXM1, CENPU, PKMYT1/MYT1, PPP1R12A/MYPT1 and WEE1 (PubMed:11202906, PubMed:12447691, PubMed:12524548, PubMed:19160488). Part of a regulatory circuit that promotes the activation of CDK1 by phosphorylating the positive regulator CDC25C and inhibiting the negative regulators WEE1 and PKMYT1/MYT1 (PubMed:11202906). Also acts by mediating phosphorylation of cyclin-B1 (CCNB1) on centrosomes in prophase (PubMed:12447691, PubMed:12524548). Phosphorylates FOXM1, a key mitotic transcription regulator, leading to enhance FOXM1 transcriptional activity (PubMed:19160488). Involved in kinetochore functions and sister chromatid cohesion by phosphorylating BUB1B/BUBR1, FBXO5/EMI1 and STAG2/SA2 (PubMed:15148369, PubMed:15469984, PubMed:17376779, PubMed:18331714). PLK1 is high on non-attached kinetochores suggesting a role of PLK1 in kinetochore attachment or in spindle assembly checkpoint (SAC) regulation (PubMed:17617734). Required for kinetochore localization of BUB1B (PubMed:17376779). Regulates the dissociation of cohesin from chromosomes by phosphorylating cohesin subunits such as STAG2/SA2 (By similarity). Phosphorylates SGO1: required for spindle pole localization of isoform 3 of SGO1 and plays a role in regulating its centriole cohesion function (PubMed:18331714). Mediates phosphorylation of FBXO5/EMI1, a negative regulator of the APC/C complex during prophase, leading to FBXO5/EMI1 ubiquitination and degradation by the proteasome (PubMed:15148369, PubMed:15469984). Acts as a negative regulator of p53 family members: phosphorylates TOPORS, leading to inhibit the sumoylation of p53/TP53 and simultaneously enhance the ubiquitination and subsequent degradation of p53/TP53 (PubMed:19473992). Phosphorylates the transactivation domain of the transcription factor p73/TP73, leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates BORA, and thereby promotes the degradation of BORA (PubMed:18521620). Contributes to the regulation of AURKA function (PubMed:18615013, PubMed:18662541). Also required for recovery after DNA damage checkpoint and entry into mitosis (PubMed:18615013, PubMed:18662541). Phosphorylates MISP, leading to stabilization of cortical and astral microtubule attachments required for proper spindle positioning (PubMed:23509069). Together with MEIKIN, acts as a regulator of kinetochore function during meiosis I: required both for mono-orientation of kinetochores on sister chromosomes and protection of centromeric cohesin from separase-mediated cleavage (By similarity). Phosphorylates CEP68 and is required for its degradation (PubMed:25503564). Regulates nuclear envelope breakdown during prophase by phosphorylating DCTN1 resulting in its localization in the nuclear envelope (PubMed:20679239). Phosphorylates the heat shock transcription factor HSF1, promoting HSF1 nuclear translocation upon heat shock (PubMed:15661742). Phosphorylates HSF1 also in the early mitotic period; this phosphorylation regulates HSF1 localization to the spindle pole, the recruitment of the SCF(BTRC) ubiquitin ligase complex induicing HSF1 degradation, and hence mitotic progression (PubMed:18794143). Regulates mitotic progression by phosphorylating RIOK2 (PubMed:21880710). Through the phosphorylation of DZIP1 regulates the localization during mitosis of the BBSome, a ciliary protein complex involved in cilium biogenesis (PubMed:27979967). Regulates DNA repair during mitosis by mediating phosphorylation of POLQ and RHNO1, thereby promoting POLQ recruitment to DNA damage sites (PubMed:37440612, PubMed:37674080). Phosphorylates ATXN10 which may play a role in the regulation of cytokinesis and may stimulate the proteasome-mediated degradation of ATXN10 (PubMed:21857149)", "gene_name": "PLK1", "glycan_count": 1, "glycosylation_sites": [], "id": "P53350", "name": "PLK1", "organism": "Homo sapiens", "uniprot_id": "P53350" }, { "function": "Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes) (PubMed:20418806, PubMed:23209295, PubMed:28017329). Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production (PubMed:23209295, PubMed:28017329). In response to cellular stress and upon mitochondria fission, binds C-18 ceramides and anchors autophagolysosomes to outer mitochondrial membranes to eliminate damaged mitochondria (PubMed:22922758). While LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation (PubMed:20418806, PubMed:23209295, PubMed:28017329). Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway (PubMed:24089205). Through its interaction with the reticulophagy receptor TEX264, participates in the remodeling of subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover (PubMed:31006537, PubMed:31006538). Upon nutrient stress, directly recruits cofactor JMY to the phagophore membrane surfaces and promotes JMY's actin nucleation activity and autophagosome biogenesis during autophagy (PubMed:30420355)", "gene_name": "MAP1LC3B", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9GZQ8", "name": "LC3B", "organism": "Homo sapiens", "uniprot_id": "Q9GZQ8" }, { "function": "Biosynthesis of L-glutamate from L-aspartate or L-cysteine. Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involved in hepatic glucose synthesis during development and in adipocyte glyceroneogenesis. Using L-cysteine as substrate, regulates levels of mercaptopyruvate, an important source of hydrogen sulfide. Mercaptopyruvate is converted into H(2)S via the action of 3-mercaptopyruvate sulfurtransferase (3MST). Hydrogen sulfide is an important synaptic modulator and neuroprotectant in the brain", "gene_name": "Got1", "glycan_count": 1, "glycosylation_sites": [], "id": "P05201", "name": "Alanine Aminotransferase (ALT/SGPT)", "organism": "Mus musculus", "uniprot_id": "P05201" }, { "function": "Catalyzes the formation of UDP-alpha-D-glucuronate, a constituent of complex glycosaminoglycans (PubMed:21502315, PubMed:21961565, PubMed:22123821, PubMed:23106432, PubMed:25478983, PubMed:27966912, PubMed:30420606, PubMed:30457329). Required for the biosynthesis of chondroitin sulfate and heparan sulfate. Required for embryonic development via its role in the biosynthesis of glycosaminoglycans (By similarity). Required for proper brain and neuronal development (PubMed:32001716)", "gene_name": "UGDH", "glycan_count": 1, "glycosylation_sites": [], "id": "O60701", "name": "UGDH (UDP-glucose dehydrogenase)", "organism": "Homo sapiens", "uniprot_id": "O60701" }, { "function": "Muscle-specific type III intermediate filament essential for proper muscular structure and function. Plays a crucial role in maintaining the structure of sarcomeres, inter-connecting the Z-disks and forming the myofibrils, linking them not only to the sarcolemmal cytoskeleton, but also to the nucleus and mitochondria, thus providing strength for the muscle fiber during activity (PubMed:25358400). In adult striated muscle they form a fibrous network connecting myofibrils to each other and to the plasma membrane from the periphery of the Z-line structures (PubMed:24200904, PubMed:25394388, PubMed:26724190). May act as a sarcomeric microtubule-anchoring protein: specifically associates with detyrosinated tubulin-alpha chains, leading to buckled microtubules and mechanical resistance to contraction. Required for nuclear membrane integrity, via anchoring at the cell tip and nuclear envelope, resulting in maintenance of microtubule-derived intracellular mechanical forces (By similarity). Contributes to the transcriptional regulation of the NKX2-5 gene in cardiac progenitor cells during a short period of cardiomyogenesis and in cardiac side population stem cells in the adult. Plays a role in maintaining an optimal conformation of nebulette (NEB) on heart muscle sarcomeres to bind and recruit cardiac alpha-actin (By similarity)", "gene_name": "DES", "glycan_count": 9, "glycosylation_sites": [], "id": "P17661", "name": "Desmin", "organism": "Homo sapiens", "uniprot_id": "P17661" }, { "function": "May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. In lens epithelial cells, stabilizes the ATP6V1A protein, preventing its degradation by the proteasome (By similarity)", "gene_name": "CRYAB", "glycan_count": 1, "glycosylation_sites": [ { "position": 41, "type": "O-linked (GlcNAc) serine" }, { "position": 170, "type": "O-linked (GlcNAc) threonine" } ], "id": "P02511", "name": "Alpha B-crystallin", "organism": "Homo sapiens", "uniprot_id": "P02511" }, { "function": "Involved in the regulation of innate immune response. Acts as negative regulator of Toll-like receptor and interferon-regulatory factor (IRF) signaling pathways. Contributes to the negative regulation of transcriptional activation of NF-kappa-B target genes in response to endogenous proinflammatory stimuli", "gene_name": "NFKBIL1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UBC1", "name": "Slow skeletal Myosin Binding Protein-C (sMyBP-C)", "organism": "Homo sapiens", "uniprot_id": "Q9UBC1" }, { "function": "Involved in the 3'-end formation of mRNA precursors (pre-mRNA) by the addition of a poly(A) tail of 200-250 nt to the upstream cleavage product (By similarity). Stimulates poly(A) polymerase (PAPOLA) conferring processivity on the poly(A) tail elongation reaction and also controls the poly(A) tail length (By similarity). Increases the affinity of poly(A) polymerase for RNA (By similarity). Is also present at various stages of mRNA metabolism including nucleocytoplasmic trafficking and nonsense-mediated decay (NMD) of mRNA. Cooperates with SKIP to synergistically activate E-box-mediated transcription through MYOD1 and may regulate the expression of muscle-specific genes (PubMed:11371506). Binds to poly(A) and to poly(G) with high affinity (By similarity). May protect the poly(A) tail from degradation (By similarity). Subunit of the trimeric poly(A) tail exosome targeting (PAXT) complex, a complex that directs a subset of long and polyadenylated poly(A) RNAs for exosomal degradation. The RNA exosome is fundamental for the degradation of RNA in eukaryotic nuclei. Substrate targeting is facilitated by its cofactor MTREX, which links to RNA-binding protein adapters (PubMed:27871484)", "gene_name": "PABPN1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q86U42", "name": "PABPN1", "organism": "Homo sapiens", "uniprot_id": "Q86U42" }, { "function": "Receptor for the netrin NTN4 that promotes neuronal cell survival (By similarity). Plays a role in cell-cell adhesion and cell guidance. Receptor for netrin involved in cell migration. Plays a role in axon guidance by mediating axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding (By similarity). May play a role in apoptosis in response to DNA damage (PubMed:24691657). It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand (PubMed:24519068). Mediates cell-cell adhesion via its interaction with FLRT3 on an adjacent cell (By similarity)", "gene_name": "UNC5D", "glycan_count": 0, "glycosylation_sites": [ { "position": 117, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 228, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 353, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 376, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6UXZ4", "name": "MEGF10", "organism": "Homo sapiens", "uniprot_id": "Q6UXZ4" }, { "function": "May have a role in maintaining the integrity of the blood vessels. Has growth promoting activity on endothelial cells, angiogenic activity in vivo and chemotactic activity on endothelial cells in vitro", "gene_name": "TYMP", "glycan_count": 1, "glycosylation_sites": [], "id": "P19971", "name": "Thymidine phosphorylase", "organism": "Homo sapiens", "uniprot_id": "P19971" }, { "function": "Collagen VI acts as a cell-binding protein", "gene_name": "COL6A1", "glycan_count": 82, "glycosylation_sites": [ { "position": 212, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 516, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 537, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 804, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 896, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P12109", "name": "Collagen VI", "organism": "Homo sapiens", "uniprot_id": "P12109" }, { "function": "Collagen VI acts as a cell-binding protein", "gene_name": "COL6A2", "glycan_count": 115, "glycosylation_sites": [ { "position": 140, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 327, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 630, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 785, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 897, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 954, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P12110", "name": "Collagen VI alpha-2 chain", "organism": "Homo sapiens", "uniprot_id": "P12110" }, { "function": "Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen", "gene_name": "COL4A6", "glycan_count": 1, "glycosylation_sites": [ { "position": 127, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q14031", "name": "Collagen VI alpha-3 chain", "organism": "Homo sapiens", "uniprot_id": "Q14031" }, { "function": "Plays a role in cell adhesion, and in cohesion of the endothelial monolayer at intercellular junctions in vascular tissue. Its expression may allow melanoma cells to interact with cellular elements of the vascular system, thereby enhancing hematogeneous tumor spread. Could be an adhesion molecule active in neural crest cells during embryonic development. Acts as a surface receptor that triggers tyrosine phosphorylation of FYN and PTK2/FAK1, and a transient increase in the intracellular calcium concentration", "gene_name": "MCAM", "glycan_count": 26, "glycosylation_sites": [ { "position": 56, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 418, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 449, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 467, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 508, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 518, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 527, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 544, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P43121", "name": "CD146 (MCAM)", "organism": "Homo sapiens", "uniprot_id": "P43121" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P43121 (soluble form)", "name": "sCD146", "organism": "", "uniprot_id": "" }, { "function": "Acts as a cofactor for XPO1/CRM1-mediated nuclear export, perhaps as export complex scaffolding protein. Bound to XPO1/CRM1, stabilizes the XPO1/CRM1-cargo interaction. In the absence of Ran-bound GTP prevents binding of XPO1/CRM1 to the nuclear pore complex. Binds to CHC1/RCC1 and increases the guanine nucleotide exchange activity of CHC1/RCC1. Recruits XPO1/CRM1 to CHC1/RCC1 in a Ran-dependent manner. Negative regulator of TGF-beta signaling through interaction with the R-SMAD proteins, SMAD2 and SMAD3, and mediating their nuclear export", "gene_name": "RANBP3", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9H6Z4", "name": "Endocan", "organism": "Homo sapiens", "uniprot_id": "Q9H6Z4" }, { "function": "Promotes degradation of target mRNA species. Plays a role in the regulation of circadian mRNA stability. Binds GTP and has GTPase activity (By similarity)", "gene_name": "Gtpbp1", "glycan_count": 1, "glycosylation_sites": [], "id": "O08582", "name": "SGLT2", "organism": "Mus musculus", "uniprot_id": "O08582" }, { "function": "Membrane-bound mucin, a family of highly glycosylated proteins that constitute the major component of the mucus, the slimy and viscous secretion covering epithelial surfaces (PubMed:10880978). These glycoproteins play important roles in the protection of the epithelium and are implicated in epithelial renewal and differentiation (PubMed:10880978). Regulates cellular behavior through both anti-adhesive effects on cell-cell and cell-extracellular matrix interactions and its ability to act as an intramembrane ligand for ERBB2. Plays an important role in proliferation and differentiation of epithelial cells by inducing specific phosphorylation of ERBB2. In polarized epithelial cells, segregates ERBB2 and other ERBB receptors and prevents ERBB2 from acting as a coreceptor. The interaction with ERBB2 leads to enhanced expression of CDKN1B. The formation of a MUC4-ERBB2-ERBB3-NRG1 complex leads to down-regulation of CDKN1B, resulting in repression of apoptosis and stimulation of proliferation. Its ability to promote tumor growth may be mainly due to repression of apoptosis as opposed to proliferation", "gene_name": "MUC4", "glycan_count": 17, "glycosylation_sites": [ { "position": 154, "type": "O-linked (GalNAc...) threonine" }, { "position": 156, "type": "O-linked (GalNAc...) threonine" }, { "position": 230, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 234, "type": "O-linked (GalNAc...) threonine" }, { "position": 255, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 364, "type": "O-linked (GalNAc...) threonine" }, { "position": 369, "type": "O-linked (GalNAc...) threonine" }, { "position": 376, "type": "O-linked (GalNAc...) threonine" }, { "position": 617, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 620, "type": "O-linked (GalNAc...) threonine" }, { "position": 666, "type": "O-linked (GalNAc...) threonine" }, { "position": 688, "type": "O-linked (GalNAc...) threonine" }, { "position": 747, "type": "O-linked (GalNAc...) threonine" }, { "position": 797, "type": "O-linked (GalNAc...) threonine" }, { "position": 798, "type": "O-linked (GalNAc...) threonine" }, { "position": 802, "type": "O-linked (GalNAc...) threonine" }, { "position": 804, "type": "O-linked (GalNAc...) threonine" }, { "position": 813, "type": "O-linked (GalNAc...) threonine" }, { "position": 814, "type": "O-linked (GalNAc...) threonine" }, { "position": 881, "type": "O-linked (GalNAc...) threonine" }, { "position": 886, "type": "O-linked (GalNAc...) threonine" }, { "position": 892, "type": "O-linked (GalNAc...) threonine" }, { "position": 931, "type": "O-linked (GalNAc...) threonine" }, { "position": 934, "type": "O-linked (GalNAc...) threonine" }, { "position": 938, "type": "O-linked (GalNAc...) threonine" }, { "position": 943, "type": "O-linked (GalNAc...) threonine" }, { "position": 945, "type": "O-linked (GalNAc...) threonine" }, { "position": 948, "type": "O-linked (GalNAc...) threonine" }, { "position": 952, "type": "O-linked (GalNAc...) threonine" }, { "position": 954, "type": "O-linked (GalNAc...) threonine" }, { "position": 1003, "type": "O-linked (GalNAc...) threonine" }, { "position": 1007, "type": "O-linked (GalNAc...) threonine" }, { "position": 1012, "type": "O-linked (GalNAc...) threonine" }, { "position": 1019, "type": "O-linked (GalNAc...) threonine" }, { "position": 1022, "type": "O-linked (GalNAc...) threonine" }, { "position": 1023, "type": "O-linked (GalNAc...) threonine" }, { "position": 1028, "type": "O-linked (GalNAc...) threonine" }, { "position": 1030, "type": "O-linked (GalNAc...) threonine" }, { "position": 1035, "type": "O-linked (GalNAc...) threonine" }, { "position": 1039, "type": "O-linked (GalNAc...) threonine" }, { "position": 1044, "type": "O-linked (GalNAc...) threonine" }, { "position": 1051, "type": "O-linked (GalNAc...) threonine" }, { "position": 1055, "type": "O-linked (GalNAc...) threonine" }, { "position": 1060, "type": "O-linked (GalNAc...) threonine" }, { "position": 1062, "type": "O-linked (GalNAc...) threonine" }, { "position": 1067, "type": "O-linked (GalNAc...) threonine" }, { "position": 1071, "type": "O-linked (GalNAc...) threonine" }, { "position": 1076, "type": "O-linked (GalNAc...) threonine" }, { "position": 1083, "type": "O-linked (GalNAc...) threonine" }, { "position": 1086, "type": "O-linked (GalNAc...) threonine" }, { "position": 1087, "type": "O-linked (GalNAc...) threonine" }, { "position": 1092, "type": "O-linked (GalNAc...) threonine" }, { "position": 1094, "type": "O-linked (GalNAc...) threonine" }, { "position": 1099, "type": "O-linked (GalNAc...) threonine" }, { "position": 1103, "type": "O-linked (GalNAc...) threonine" }, { "position": 1108, "type": "O-linked (GalNAc...) threonine" }, { "position": 1110, "type": "O-linked (GalNAc...) threonine" }, { "position": 1115, "type": "O-linked (GalNAc...) threonine" }, { "position": 1118, "type": "O-linked (GalNAc...) threonine" }, { "position": 1119, "type": "O-linked (GalNAc...) threonine" }, { "position": 1124, "type": "O-linked (GalNAc...) threonine" }, { "position": 1126, "type": "O-linked (GalNAc...) threonine" }, { "position": 1131, "type": "O-linked (GalNAc...) threonine" }, { "position": 1135, "type": "O-linked (GalNAc...) threonine" }, { "position": 1172, "type": "O-linked (GalNAc...) threonine" }, { "position": 1179, "type": "O-linked (GalNAc...) threonine" }, { "position": 1182, "type": "O-linked (GalNAc...) threonine" }, { "position": 1183, "type": "O-linked (GalNAc...) threonine" }, { "position": 1188, "type": "O-linked (GalNAc...) threonine" }, { "position": 1195, "type": "O-linked (GalNAc...) threonine" }, { "position": 1199, "type": "O-linked (GalNAc...) threonine" }, { "position": 1204, "type": "O-linked (GalNAc...) threonine" }, { "position": 1236, "type": "O-linked (GalNAc...) threonine" }, { "position": 1243, "type": "O-linked (GalNAc...) threonine" }, { "position": 1246, "type": "O-linked (GalNAc...) threonine" }, { "position": 1247, "type": "O-linked 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1343, "type": "O-linked (GalNAc...) threonine" }, { "position": 1348, "type": "O-linked (GalNAc...) threonine" }, { "position": 1380, "type": "O-linked (GalNAc...) threonine" }, { "position": 1387, "type": "O-linked (GalNAc...) threonine" }, { "position": 1390, "type": "O-linked (GalNAc...) threonine" }, { "position": 1391, "type": "O-linked (GalNAc...) threonine" }, { "position": 1396, "type": "O-linked (GalNAc...) threonine" }, { "position": 1403, "type": "O-linked (GalNAc...) threonine" }, { "position": 1407, "type": "O-linked (GalNAc...) threonine" }, { "position": 1412, "type": "O-linked (GalNAc...) threonine" }, { "position": 1444, "type": "O-linked (GalNAc...) threonine" }, { "position": 1451, "type": "O-linked (GalNAc...) threonine" }, { "position": 1454, "type": "O-linked (GalNAc...) threonine" }, { "position": 1455, "type": "O-linked (GalNAc...) threonine" }, { "position": 1486, "type": "O-linked (GalNAc...) threonine" }, { "position": 1487, "type": "O-linked (GalNAc...) 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"position": 1940, "type": "O-linked (GalNAc...) threonine" }, { "position": 1950, "type": "O-linked (GalNAc...) threonine" }, { "position": 1951, "type": "O-linked (GalNAc...) threonine" }, { "position": 1956, "type": "O-linked (GalNAc...) threonine" }, { "position": 1963, "type": "O-linked (GalNAc...) threonine" }, { "position": 1995, "type": "O-linked (GalNAc...) threonine" }, { "position": 1999, "type": "O-linked (GalNAc...) threonine" }, { "position": 2004, "type": "O-linked (GalNAc...) threonine" }, { "position": 2006, "type": "O-linked (GalNAc...) threonine" }, { "position": 2015, "type": "O-linked (GalNAc...) threonine" }, { "position": 2020, "type": "O-linked (GalNAc...) threonine" }, { "position": 2027, "type": "O-linked (GalNAc...) threonine" }, { "position": 2030, "type": "O-linked (GalNAc...) threonine" }, { "position": 2031, "type": "O-linked (GalNAc...) threonine" }, { "position": 2036, "type": "O-linked (GalNAc...) threonine" }, { "position": 2038, "type": "O-linked 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{ "position": 5119, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5185, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5192, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5292, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q99102", "name": "MUC4", "organism": "Homo sapiens", "uniprot_id": "Q99102" }, { "function": "Epithelial and hemopoietic transmembrane mucin that may play a role in cell signaling", "gene_name": "MUC13", "glycan_count": 1, "glycosylation_sites": [ { "position": 151, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 169, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 193, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 206, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 284, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 332, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9H3R2", "name": "MUC13", "organism": "Homo sapiens", "uniprot_id": "Q9H3R2" }, { "function": "Required for clearance of cellular formaldehyde, a cytotoxic and carcinogenic metabolite that induces DNA damage", "gene_name": "ALDH2", "glycan_count": 1, "glycosylation_sites": [], "id": "P05091", "name": "Aldehyde dehydrogenase 2 (ALDH2)", "organism": "Homo sapiens", "uniprot_id": "P05091" }, { "function": "Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. In addition, may be responsible for the degradation of glucose-1,6-bisphosphate in ischemic brain", "gene_name": "PMM1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q92871", "name": "Phosphomannomutase 1 (PMM1)", "organism": "Homo sapiens", "uniprot_id": "Q92871" }, { "function": "Involved in neutrophil activation. In vitro, ENA-78(8-78) and ENA-78(9-78) show a threefold higher chemotactic activity for neutrophil granulocytes", "gene_name": "CXCL5", "glycan_count": 0, "glycosylation_sites": [], "id": "P42830", "name": "CXCL5", "organism": "Homo sapiens", "uniprot_id": "P42830" }, { "function": "A beta-galactoside alpha2->3 sialyltransferase involved in terminal sialylation of glycoproteins and glycolipids (PubMed:31784620, PubMed:8027041). Catalyzes the transfer of sialic acid (N-acetyl-neuraminic acid; Neu5Ac) from the nucleotide sugar donor CMP-Neu5Ac onto acceptor Galbeta-(1->3)-GalNAc-terminated glycoconjugates through an alpha2-3 linkage (PubMed:31784620, PubMed:8027041, PubMed:31719620). Adds sialic acid to the core 1 O-glycan, Galbeta-(1->3)-GalNAc-O-Ser/Thr, which is a major structure of mucin-type O-glycans. As part of a homeostatic mechanism that regulates CD8-positive T cell numbers, sialylates core 1 O-glycans of T cell glycoproteins, SPN/CD43 and PTPRC/CD45. Prevents premature apoptosis of thymic CD8-positive T cells prior to peripheral emigration, whereas in the secondary lymphoid organs controls the survival of CD8-positive memory T cells generated following a successful immune response (By similarity). Transfers sialic acid to asialofetuin, presumably onto Galbeta-(1->3)-GalNAc-O-Ser (By similarity). Sialylates GM1a, GA1 and GD1b gangliosides to form GD1a, GM1b and GT1b, respectively (By similarity) (PubMed:8027041)", "gene_name": "ST3GAL1", "glycan_count": 34, "glycosylation_sites": [ { "position": 79, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 114, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 201, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 323, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q11201", "name": "ST3 beta-galactoside alpha-2,3-sialyltransferase 1 (ST3Gal1)", "organism": "Homo sapiens", "uniprot_id": "Q11201" }, { "function": "Protein sialyltransferase specifically expressed in goblet cells that plays a key role in intestinal host-commensal homeostasis (PubMed:35303419). Conjugates sialic acid with an alpha-2-6 linkage to N-acetylgalactosamine (GalNAc) glycan chains linked to serine or threonine in glycoproteins (PubMed:10536037, PubMed:15466199, PubMed:16319059, PubMed:31719620, PubMed:35303419). Catalyzes the formation of the sialyl-Tn (S-Tn) antigen, an antigen found in intestinal goblet cells, as well as ulcerative colitis (UC) and various cancers (PubMed:15466199, PubMed:16319059, PubMed:31719620, PubMed:35303419). Protein sialylation in globlet cells is essential for mucus integrity and is required to protect the intestinal mucus against excessive bacterial proteolytic degradation (PubMed:35303419)", "gene_name": "ST6GALNAC1", "glycan_count": 2, "glycosylation_sites": [ { "position": 300, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 311, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 331, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 375, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 460, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NSC7", "name": "ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 1 (ST6GalNAc1)", "organism": "Homo sapiens", "uniprot_id": "Q9NSC7" }, { "function": "Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,3- or alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface", "gene_name": "SIGLEC9", "glycan_count": 5, "glycosylation_sites": [ { "position": 101, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 138, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 161, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 225, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 231, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 238, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 256, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 334, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y336", "name": "Siglec-9", "organism": "Homo sapiens", "uniprot_id": "Q9Y336" }, { "function": "", "gene_name": "APP", "glycan_count": 0, "glycosylation_sites": [], "id": "P05067-4", "name": "Amyloid-beta 42 (A\u03b242)", "organism": "Homo sapiens", "uniprot_id": "P05067-4" }, { "function": "", "gene_name": "APP", "glycan_count": 0, "glycosylation_sites": [], "id": "P05067-3", "name": "Amyloid-beta 40 (A\u03b240)", "organism": "Homo sapiens", "uniprot_id": "P05067-3" }, { "function": "K(+) channel subunit that may homo- and heterodimerize to form functional channels with distinct regulatory and gating properties. Can heterodimerize with KCNK13 subunit to conduct K(+) outward rectifying currents at the plasma membrane. The homodimers are mainly retained in the endoplasmic reticulum compartment and may be targeted to the cell surface upon phosphorylation or other activation signals yet to be elucidated", "gene_name": "KCNK12", "glycan_count": 0, "glycosylation_sites": [ { "position": 78, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9HB15", "name": "Kir4.2 (KCNJ15)", "organism": "Homo sapiens", "uniprot_id": "Q9HB15" }, { "function": "Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This potassium channel is controlled by G proteins (By similarity). Forms a functional channel in association with KCNJ3/GIRK1 (PubMed:10341034)", "gene_name": "Kcnj6", "glycan_count": 0, "glycosylation_sites": [], "id": "P48542", "name": "Kir3.2 (GIRK2)", "organism": "Mus musculus", "uniprot_id": "P48542" }, { "function": "This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients (PubMed:29499166, PubMed:30388404). Could also be part of an osmosensory signaling pathway that senses body-fluid sodium levels and controls salt intake behavior as well as voluntary water intake to regulate sodium homeostasis (By similarity)", "gene_name": "ATP1A1", "glycan_count": 2, "glycosylation_sites": [], "id": "P05023", "name": "Na+/K+ ATPase", "organism": "Homo sapiens", "uniprot_id": "P05023" }, { "function": "E1-like activating enzyme involved in the 2 ubiquitin-like systems required for cytoplasm to vacuole transport (Cvt) and autophagy. Activates ATG12 for its conjugation with ATG5 as well as the ATG8 family proteins for their conjugation with phosphatidylethanolamine. Both systems are needed for the ATG8 association to Cvt vesicles and autophagosomes membranes. Required for autophagic death induced by caspase-8 inhibition. Facilitates LC3-I lipidation with phosphatidylethanolamine to form LC3-II which is found on autophagosomal membranes (PubMed:34161705). Required for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Modulates p53/TP53 activity to regulate cell cycle and survival during metabolic stress. Also plays a key role in the maintenance of axonal homeostasis, the prevention of axonal degeneration, the maintenance of hematopoietic stem cells, the formation of Paneth cell granules, as well as in adipose differentiation. Plays a role in regulating the liver clock and glucose metabolism by mediating the autophagic degradation of CRY1 (clock repressor) in a time-dependent manner (By similarity)", "gene_name": "ATG7", "glycan_count": 0, "glycosylation_sites": [], "id": "O95352", "name": "Phosphomannomutase 2 (PMM2)", "organism": "Homo sapiens", "uniprot_id": "O95352" }, { "function": "Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters", "gene_name": "BCHE", "glycan_count": 40, "glycosylation_sites": [ { "position": 45, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 85, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 134, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 269, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 284, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 369, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 483, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 509, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 513, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 514, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P06276", "name": "Cholinesterase", "organism": "Homo sapiens", "uniprot_id": "P06276" }, { "function": "Elastase that enhances insulin signaling and might have a physiologic role in cellular glucose metabolism. Circulates in plasma and reduces platelet hyperactivation, triggers both insulin secretion and degradation, and increases insulin sensitivity", "gene_name": "CELA2A", "glycan_count": 1, "glycosylation_sites": [], "id": "P08217", "name": "Elastase-1", "organism": "Homo sapiens", "uniprot_id": "P08217" }, { "function": "Promotes integrin-mediated cell adhesion. May stimulate host defense against viruses and tumor cells", "gene_name": "LGALS3BP", "glycan_count": 222, "glycosylation_sites": [ { "position": 69, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 125, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 192, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 362, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 398, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 551, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 580, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "Q08380", "name": "Mac-2 binding protein (M2BP)", "organism": "Homo sapiens", "uniprot_id": "Q08380" }, { "function": "Plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis. A counterregulatory hormone of insulin, raises plasma glucose levels in response to insulin-induced hypoglycemia. Plays an important role in initiating and maintaining hyperglycemic conditions in diabetes", "gene_name": "GCG", "glycan_count": 0, "glycosylation_sites": [], "id": "P01275", "name": "Glucagon (GCG)", "organism": "Homo sapiens", "uniprot_id": "P01275" }, { "function": "Stabilizer of the mucous gel overlying the gastrointestinal mucosa that provides a physical barrier against various noxious agents. May inhibit the growth of calcium oxalate crystals in urine", "gene_name": "TFF1", "glycan_count": 1, "glycosylation_sites": [], "id": "P04155", "name": "Testosterone (T)", "organism": "Homo sapiens", "uniprot_id": "P04155" }, { "function": "Functions as an androgen transport protein, but may also be involved in receptor mediated processes. Each dimer binds one molecule of steroid. Specific for 5-alpha-dihydrotestosterone, testosterone, and 17-beta-estradiol. Regulates the plasma metabolic clearance rate of steroid hormones by controlling their plasma concentration", "gene_name": "SHBG", "glycan_count": 23, "glycosylation_sites": [ { "position": 36, "type": "O-linked (GalNAc...) threonine" }, { "position": 380, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 396, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P04278", "name": "Sex Hormone-Binding Globulin (SHBG)", "organism": "Homo sapiens", "uniprot_id": "P04278" }, { "function": "Steroid hormone receptors are ligand-activated transcription factors that regulate eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues (PubMed:19022849). Transcription factor activity is modulated by bound coactivator and corepressor proteins like ZBTB7A that recruits NCOR1 and NCOR2 to the androgen response elements/ARE on target genes, negatively regulating androgen receptor signaling and androgen-induced cell proliferation (PubMed:20812024). Transcription activation is also down-regulated by NR0B2. Activated, but not phosphorylated, by HIPK3 and ZIPK/DAPK3", "gene_name": "AR", "glycan_count": 1, "glycosylation_sites": [], "id": "P10275", "name": "Androgen Receptor (AR)", "organism": "Homo sapiens", "uniprot_id": "P10275" }, { "function": "Key player in the regulation of energy balance and body weight control. Once released into the circulation, has central and peripheral effects by binding LEPR, found in many tissues, which results in the activation of several major signaling pathways (PubMed:15899045, PubMed:17344214, PubMed:19688109). In the hypothalamus, acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption by inducing anorexinogenic factors and suppressing orexigenic neuropeptides, also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, influences reproductive function, regulates pancreatic beta-cell function and insulin secretion, is pro-angiogenic for endothelial cell and affects innate and adaptive immunity (By similarity) (PubMed:11460888, PubMed:19688109, PubMed:24340098, PubMed:25060689, PubMed:8589726). In the arcuate nucleus of the hypothalamus, activates by depolarization POMC neurons inducing FOS and SOCS3 expression to release anorexigenic peptides and inhibits by hyperpolarization NPY neurons inducing SOCS3 with a consequent reduction on release of orexigenic peptides (By similarity). In addition to its known satiety inducing effect, has a modulatory role in nutrient absorption. In the intestine, reduces glucose absorption by enterocytes by activating PKC and leading to a sequential activation of p38, PI3K and ERK signaling pathways which exerts an inhibitory effect on glucose absorption (PubMed:24340098). Acts as a growth factor on certain tissues, through the activation of different signaling pathways increases expression of genes involved in cell cycle regulation such as CCND1, via JAK2-STAT3 pathway, or VEGFA, via MAPK1/3 and PI3K-AKT1 pathways (By similarity) (PubMed:17344214). May also play an apoptotic role via JAK2-STAT3 pathway and up-regulation of BIRC5 expression (PubMed:18242580). Pro-angiogenic, has mitogenic activity on vascular endothelial cells and plays a role in matrix remodeling by regulating the expression of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) (PubMed:11460888). In innate immunity, modulates the activity and function of neutrophils by increasing chemotaxis and the secretion of oxygen radicals. Increases phagocytosis by macrophages and enhances secretion of pro-inflammatory mediators. Increases cytotoxic ability of NK cells (PubMed:12504075). Plays a pro-inflammatory role, in synergy with IL1B, by inducing NOS2 which promotes the production of IL6, IL8 and Prostaglandin E2, through a signaling pathway that involves JAK2, PI3K, MAP2K1/MEK1 and MAPK14/p38 (PubMed:15899045, PubMed:19688109). In adaptive immunity, promotes the switch of memory T-cells towards T helper-1 cell immune responses (By similarity). Increases CD4(+)CD25(-) T-cell proliferation and reduces autophagy during TCR (T-cell receptor) stimulation, through MTOR signaling pathway activation and BCL2 up-regulation (PubMed:25060689)", "gene_name": "LEP", "glycan_count": 0, "glycosylation_sites": [], "id": "P41159", "name": "Leptin", "organism": "Homo sapiens", "uniprot_id": "P41159" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P08183 (human)", "name": "P-glycoprotein (ABCB1/MDR1)", "organism": "", "uniprot_id": "" }, { "function": "Stabilizer of the mucous gel overlying the gastrointestinal mucosa that provides a physical barrier against various noxious agents", "gene_name": "Tff1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q08423", "name": "MFGE8 (Lactadherin)", "organism": "Mus musculus", "uniprot_id": "Q08423" }, { "function": "Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion with a high affinity", "gene_name": "SPARC", "glycan_count": 72, "glycosylation_sites": [ { "position": 116, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P09486", "name": "Complement proteins (e.g., C1S)", "organism": "Homo sapiens", "uniprot_id": "P09486" }, { "function": "Involved in L-serine biosynthesis via the phosphorylated pathway, a three-step pathway converting the glycolytic intermediate 3-phospho-D-glycerate into L-serine. Catalyzes the second step, that is the pyridoxal 5'-phosphate-dependent transamination of 3-phosphohydroxypyruvate and L-glutamate to O-phosphoserine (OPS) and alpha-ketoglutarate", "gene_name": "PSAT1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9Y617", "name": "NPTX2 (Neuronal pentraxin-2)", "organism": "Homo sapiens", "uniprot_id": "Q9Y617" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01857 (IgG1)", "name": "Immunoglobulin G (IgG)", "organism": "", "uniprot_id": "" }, { "function": "Minor component of the myelin sheath. May be involved in completion and/or maintenance of the myelin sheath and in cell-cell communication. Mediates homophilic cell-cell adhesion", "gene_name": "Mog", "glycan_count": 16, "glycosylation_sites": [ { "position": 59, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q61885", "name": "Myelin oligodendrocyte glycoprotein (MOG)", "organism": "Mus musculus", "uniprot_id": "Q61885" }, { "function": "Transcriptional corepressor that mediates the transcriptional repression activity of some nuclear receptors by promoting chromatin condensation, thus preventing access of the basal transcription (PubMed:19144721). Acts by recruiting chromatin modifiers, such as histone deacetylases HDAC1, HDAC2 and HDAC3 (By similarity). Required to activate the histone deacetylase activity of HDAC3 (By similarity). Involved in the regulation BCL6-dependent of the germinal center (GC) reactions, mainly through the control of the GC B-cells proliferation and survival (By similarity). Recruited by ZBTB7A to the androgen response elements/ARE on target genes, negatively regulates androgen receptor signaling and androgen-induced cell proliferation (By similarity)", "gene_name": "Ncor2", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9WU42", "name": "CD4 (T cell marker)", "organism": "Mus musculus", "uniprot_id": "Q9WU42" }, { "function": "Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body (PubMed:7503239). In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such PTGS2/COX2 (PubMed:16373578). As component of the iNOS-S100A8/9 transnitrosylase complex involved in the selective inflammatory stimulus-dependent S-nitrosylation of GAPDH implicated in regulation of the GAIT complex activity and probably multiple targets including ANXA5, EZR, MSN and VIM (By similarity). Involved in inflammation, enhances the synthesis of pro-inflammatory mediators such as IL6 and IL8 (By similarity)", "gene_name": "Nos2", "glycan_count": 1, "glycosylation_sites": [], "id": "P29477", "name": "Inducible nitric oxide synthase (iNOS)", "organism": "Mus musculus", "uniprot_id": "P29477" }, { "function": "Component of the large ribosomal subunit (PubMed:36517592). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:36517592)", "gene_name": "Rpl13", "glycan_count": 1, "glycosylation_sites": [], "id": "P47963", "name": "Arginase 1 (Arg1)", "organism": "Mus musculus", "uniprot_id": "P47963" }, { "function": "Transcriptional regulator which is crucial for the development and inhibitory function of regulatory T-cells (Treg) (PubMed:22813742). Plays an essential role in maintaining homeostasis of the immune system by allowing the acquisition of full suppressive function and stability of the Treg lineage, and by directly modulating the expansion and function of conventional T-cells. Can act either as a transcriptional repressor or a transcriptional activator depending on its interactions with other transcription factors, histone acetylases and deacetylases. The suppressive activity of Treg involves the coordinate activation of many genes, including CTLA4 and TNFRSF18 by FOXP3 along with repression of genes encoding cytokines such as interleukin-2 (IL2) and interferon-gamma (IFNG). Inhibits cytokine production and T-cell effector function by repressing the activity of two key transcription factors, RELA and NFATC2 (PubMed:15790681). Mediates transcriptional repression of IL2 via its association with histone acetylase KAT5 and histone deacetylase HDAC7 (By similarity). Can activate the expression of TNFRSF18, IL2RA and CTLA4 and repress the expression of IL2 and IFNG via its association with transcription factor RUNX1 (PubMed:17377532). Inhibits the differentiation of IL17 producing helper T-cells (Th17) by antagonizing RORC function, leading to down-regulation of IL17 expression, favoring Treg development (PubMed:18368049). Inhibits the transcriptional activator activity of RORA (By similarity). Can repress the expression of IL2 and IFNG via its association with transcription factor IKZF4 (PubMed:19696312)", "gene_name": "Foxp3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q99JB6", "name": "FoxP3", "organism": "Mus musculus", "uniprot_id": "Q99JB6" }, { "function": "Major immune regulatory cytokine that acts on many cells of the immune system where it has profound anti-inflammatory functions, limiting excessive tissue disruption caused by inflammation. Mechanistically, IL10 binds to its heterotetrameric receptor comprising IL10RA and IL10RB leading to JAK1 and STAT2-mediated phosphorylation of STAT3. In turn, STAT3 translocates to the nucleus where it drives expression of anti-inflammatory mediators. Targets antigen-presenting cells (APCs) such as macrophages and monocytes and inhibits their release of pro-inflammatory cytokines including granulocyte-macrophage colony-stimulating factor /GM-CSF, granulocyte colony-stimulating factor/G-CSF, IL-1 alpha, IL-1 beta, IL-6, IL-8 and TNF-alpha. Also interferes with antigen presentation by reducing the expression of MHC-class II and co-stimulatory molecules, thereby inhibiting their ability to induce T cell activation (By similarity). In addition, controls the inflammatory response of macrophages by reprogramming essential metabolic pathways including mTOR signaling (By similarity) (PubMed:28473584)", "gene_name": "Il10", "glycan_count": 0, "glycosylation_sites": [ { "position": 29, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 134, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P18893", "name": "Interleukin-10 (IL-10)", "organism": "Mus musculus", "uniprot_id": "P18893" }, { "function": "Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation (By similarity). Induces insulin resistance in adipocytes via inhibition of insulin-induced IRS1 tyrosine phosphorylation and insulin-induced glucose uptake. Induces GKAP42 protein degradation in adipocytes which is partially responsible for TNF-induced insulin resistance (PubMed:25586176). Plays a role in angiogenesis by inducing VEGF production synergistically with IL1B and IL6 (By similarity). Promotes osteoclastogenesis and therefore mediates bone resorption (PubMed:32741026)", "gene_name": "Tnf", "glycan_count": 0, "glycosylation_sites": [ { "position": 83, "type": "O-linked (GalNAc...) serine; in soluble form" }, { "position": 86, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P06804", "name": "Tumor necrosis factor (TNF)", "organism": "Mus musculus", "uniprot_id": "P06804" }, { "function": "Type II interferon produced by immune cells such as T-cells and NK cells that plays crucial roles in antimicrobial, antiviral, and antitumor responses by activating effector immune cells and enhancing antigen presentation (PubMed:11585387, PubMed:8456301). Primarily signals through the JAK-STAT pathway after interaction with its receptor IFNGR1 to affect gene regulation. Upon IFNG binding, IFNGR1 intracellular domain opens out to allow association of downstream signaling components JAK2, JAK1 and STAT1, leading to STAT1 activation, nuclear translocation and transcription of IFNG-regulated genes. Many of the induced genes are transcription factors such as IRF1 that are able to further drive regulation of a next wave of transcription. Plays a role in class I antigen presentation pathway by inducing a replacement of catalytic proteasome subunits with immunoproteasome subunits. In turn, increases the quantity, quality, and repertoire of peptides for class I MHC loading. Increases the efficiency of peptide generation also by inducing the expression of activator PA28 that associates with the proteasome and alters its proteolytic cleavage preference. Up-regulates as well MHC II complexes on the cell surface by promoting expression of several key molecules such as cathepsins B/CTSB, H/CTSH, and L/CTSL (By similarity). Participates in the regulation of hematopoietic stem cells during development and under homeostatic conditions by affecting their development, quiescence, and differentiation (PubMed:20535209, PubMed:25078851)", "gene_name": "Ifng", "glycan_count": 0, "glycosylation_sites": [ { "position": 38, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 90, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01580", "name": "Interferon gamma (IFN-\u03b3)", "organism": "Mus musculus", "uniprot_id": "P01580" }, { "function": "Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription (By similarity). Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template (By similarity). Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability (By similarity). DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling (By similarity). Involved in stable X chromosome inactivation (By similarity). Inhibits the binding of transcription factors, including NF-kappa-B, and interferes with the activity of remodeling SWI/SNF complexes (By similarity). Inhibits histone acetylation by EP300 and recruits class I HDACs, which induces a hypoacetylated state of chromatin (PubMed:16107708)", "gene_name": "Macroh2a1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9QZQ8", "name": "NPTX1", "organism": "Mus musculus", "uniprot_id": "Q9QZQ8" }, { "function": "Multifunctional cell surface receptor that binds VLDL and transports it into cells by endocytosis and therefore plays an important role in energy metabolism (PubMed:11108739, PubMed:24293365). Also binds to a wide range of other molecules including Reelin/RELN or apolipoprotein E/APOE-containing ligands as well as clusterin/CLU. In the off-state of the pathway LRP8 and VLDLR form homo or heterooligomers (By similarity). Upon binding to ligands, homooligomers are rearranged to higher order receptor clusters that transmit the extracellular RELN signal to intracellular signaling processes by binding to DAB1 on its cytoplasmic tail (By similarity). This interaction results in phosphorylation of DAB1 leading to the ultimate cell responses required for the correct positioning of newly generated neurons (PubMed:23506116). Later, mediates a stop signal for migrating neurons, preventing them from entering the marginal zone (PubMed:17913789)", "gene_name": "Vldlr", "glycan_count": 2, "glycosylation_sites": [ { "position": 151, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 765, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 781, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P98156", "name": "MPRD (Mannose-6-phosphate receptor, Cation dependent)", "organism": "Mus musculus", "uniprot_id": "P98156" }, { "function": "Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions (PubMed:21796099). Contributes to the native pacemaker currents in heart (If) and in neurons (Ih). Can also transport ammonium in the distal nephron (PubMed:21796099). Involved in the initiation of neuropathic pain in sensory neurons. Produces a large instantaneous current (PubMed:21796099)", "gene_name": "Hcn2", "glycan_count": 1, "glycosylation_sites": [ { "position": 380, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9JKA9", "name": "CA2D1 (Voltage-dependent calcium channel subunit alpha-2/delta-1)", "organism": "Rattus norvegicus", "uniprot_id": "Q9JKA9" }, { "function": "May play a role in cell-cell or cell-ligand interactions during synaptogenesis and other events in the brain", "gene_name": "Thy1", "glycan_count": 43, "glycosylation_sites": [ { "position": 42, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 94, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 118, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01831", "name": "THY1", "organism": "Mus musculus", "uniprot_id": "P01831" }, { "function": "Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression", "gene_name": "Eif3i", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9QZD9", "name": "NRCAM", "organism": "Mus musculus", "uniprot_id": "Q9QZD9" }, { "function": "Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription (By similarity). Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template (By similarity). Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability (By similarity). DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling (By similarity). Involved in stable X chromosome inactivation (By similarity). Inhibits the binding of transcription factors, including NF-kappa-B, and interferes with the activity of remodeling SWI/SNF complexes (By similarity). Inhibits histone acetylation by EP300 and recruits class I HDACs, which induces a hypoacetylated state of chromatin (PubMed:16107708)", "gene_name": "Macroh2a1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9QZQ7", "name": "NPTN", "organism": "Mus musculus", "uniprot_id": "Q9QZQ8" }, { "function": "Hydrolyzes the non-reducing end N-acetyl-D-hexosamine and/or sulfated N-acetyl-D-hexosamine of glycoconjugates, such as the oligosaccharide moieties from proteins and neutral glycolipids, or from certain mucopolysaccharides. The isozyme S is as active as the isozyme A on the anionic bis-sulfated glycans, the chondroitin-6-sulfate trisaccharide (C6S-3), and the dermatan sulfate pentasaccharide, and the sulfated glycosphingolipid SM2. The isozyme B does not hydrolyze each of these substrates, however hydrolyzes efficiently neutral oligosaccharide. Only the isozyme A is responsible for the degradation of GM2 gangliosides in the presence of GM2A", "gene_name": "Hexa", "glycan_count": 3, "glycosylation_sites": [ { "position": 115, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 157, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 295, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 487, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P29416", "name": "Hexa (Beta-hexosaminidase subunit alpha)", "organism": "Mus musculus", "uniprot_id": "P29416" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q05403", "name": "CD36", "organism": "", "uniprot_id": "Q05403" }, { "function": "This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of the beta-2 subunit is not known", "gene_name": "ATP1B2", "glycan_count": 8, "glycosylation_sites": [ { "position": 96, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 118, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 153, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 159, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 193, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 197, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 238, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P14415", "name": "AT1B2 (Sodium/potassium-transporting ATPase subunit beta-2)", "organism": "Homo sapiens", "uniprot_id": "P14415" }, { "function": "Binds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation", "gene_name": "HPX", "glycan_count": 236, "glycosylation_sites": [ { "position": 24, "type": "O-linked (GalNAc...) threonine" }, { "position": 29, "type": "O-linked (GalNAc...) threonine" }, { "position": 64, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 187, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 240, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 246, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 453, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P02790", "name": "Hemopexin", "organism": "Homo sapiens", "uniprot_id": "P02790" }, { "function": "Primate-specific plasma protein associated with apolipoprotein L-I (apoL-I)-containing high-density lipoprotein (HDL). This HDL particle, termed trypanosome lytic factor-1 (TLF-1), mediates human innate immune protection against many species of African trypanosomes. Binds hemoglobin with high affinity and may contribute to the clearance of cell-free hemoglobin to allow hepatic recycling of heme iron", "gene_name": "HPR", "glycan_count": 0, "glycosylation_sites": [], "id": "P00739", "name": "Haptoglobin-related protein", "organism": "Homo sapiens", "uniprot_id": "P00739" }, { "function": "Type II acute-phase protein (APP) involved in inflammatory responses to trauma. May also play a role in liver development or regeneration", "gene_name": "ITIH4", "glycan_count": 191, "glycosylation_sites": [ { "position": 81, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 207, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 274, "type": "N-linked (GlcNAc...) asparagine; atypical" }, { "position": 517, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 577, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 719, "type": "O-linked (GalNAc...) threonine" }, { "position": 720, "type": "O-linked (GalNAc...) threonine" }, { "position": 722, "type": "O-linked (GalNAc...) threonine" } ], "id": "Q14624", "name": "Inter-alpha-trypsin inhibitor heavy chain H4", "organism": "Homo sapiens", "uniprot_id": "Q14624" }, { "function": "Receptor for ecdysone. May be an important modulator of insect metamorphosis. Plays an important part in embryonic and post-embryonic development. Binds to ecdysone response elements (ECRES) such as in the promoter region of s15 chorion gene", "gene_name": "usp", "glycan_count": 0, "glycosylation_sites": [], "id": "P20153", "name": "Human Kallikrein-2 (hK2)", "organism": "Drosophila melanogaster", "uniprot_id": "P20153" }, { "function": "Polycomb group (PcG) protein. Catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Displays a preference for substrates with less methylation, loses activity when progressively more methyl groups are incorporated into H3K27, H3K27me0 > H3K27me1 > H3K27me2 (PubMed:22323599, PubMed:30923826). Compared to EZH1-containing complexes, it is more abundant in embryonic stem cells and plays a major role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1, CDKN2A and retinoic acid target genes. EZH2 can also methylate non-histone proteins such as the transcription factor GATA4 and the nuclear receptor RORA. Regulates the circadian clock via histone methylation at the promoter of the circadian genes. Essential for the CRY1/2-mediated repression of the transcriptional activation of PER1/2 by the CLOCK-BMAL1 heterodimer; involved in the di and trimethylation of 'Lys-27' of histone H3 on PER1/2 promoters which is necessary for the CRY1/2 proteins to inhibit transcription", "gene_name": "EZH2", "glycan_count": 1, "glycosylation_sites": [ { "position": 75, "type": "O-linked (GlcNAc) serine" } ], "id": "Q15910", "name": "EZH2", "organism": "Homo sapiens", "uniprot_id": "Q15910" }, { "function": "RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:11169732, PubMed:17581632). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773, PubMed:27462815)", "gene_name": "EIF3A", "glycan_count": 2, "glycosylation_sites": [], "id": "Q14152", "name": "EIF3S (EIF3A)", "organism": "Homo sapiens", "uniprot_id": "Q14152" }, { "function": "", "gene_name": "TPD52L1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q16890", "name": "TPD52", "organism": "Homo sapiens", "uniprot_id": "Q16890" }, { "function": "Signal transducer and transcription activator that mediates cellular responses to interleukins, KITLG/SCF, LEP and other growth factors (PubMed:10688651, PubMed:12359225, PubMed:12873986, PubMed:15194700, PubMed:15653507, PubMed:16285960, PubMed:17344214, PubMed:18242580, PubMed:18782771, PubMed:22306293, PubMed:23084476, PubMed:28262505, PubMed:32929201, PubMed:38404237). Once activated, recruits coactivators, such as NCOA1 or MED1, to the promoter region of the target gene (PubMed:15653507, PubMed:16285960, PubMed:17344214, PubMed:18782771, PubMed:28262505, PubMed:32929201). May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4 (PubMed:12873986). Upon activation of IL6ST/gp130 signaling by interleukin-6 (IL6), binds to the IL6-responsive elements identified in the promoters of various acute-phase protein genes (PubMed:12359225). Activated by IL31 through IL31RA (PubMed:15194700). Acts as a regulator of inflammatory response by regulating differentiation of naive CD4(+) T-cells into T-helper Th17 or regulatory T-cells (Treg): acetylation promotes its transcription activity and cell differentiation while deacetylation and oxidation of lysine residues by LOXL3 inhibits differentiation (PubMed:28065600, PubMed:28262505). Involved in cell cycle regulation by inducing the expression of key genes for the progression from G1 to S phase, such as CCND1 (PubMed:17344214). Mediates the effects of LEP on melanocortin production, body energy homeostasis and lactation (By similarity). May play an apoptotic role by transctivating BIRC5 expression under LEP activation (PubMed:18242580). Cytoplasmic STAT3 represses macroautophagy by inhibiting EIF2AK2/PKR activity (PubMed:23084476). Plays a crucial role in basal beta cell functions, such as regulation of insulin secretion (By similarity). Following JAK/STAT signaling activation and as part of a complex with NFATC3 and NFATC4, binds to the alpha-beta E4 promoter region of CRYAB and activates transcription in cardiomyocytes (By similarity)", "gene_name": "STAT3", "glycan_count": 2, "glycosylation_sites": [], "id": "P40763", "name": "STAT3 (Signal transducer and activator of transcription 3)", "organism": "Homo sapiens", "uniprot_id": "P40763" }, { "function": "Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TEFb complex) that will in turn hyperphosphorylate the RNA polymerase II to allow efficient elongation. The CDK9 component of P-TEFb and other Tat-activated kinases hyperphosphorylate the C-terminus of RNA Pol II that becomes stabilized and much more processive. Other factors such as HTATSF1/Tat-SF1, SUPT5H/SPT5, and HTATIP2 are also important for Tat's function. Besides its effect on RNA Pol II processivity, Tat induces chromatin remodeling of proviral genes by recruiting the histone acetyltransferases (HATs) CREBBP, EP300 and PCAF to the chromatin. This also contributes to the increase in proviral transcription rate, especially when the provirus integrates in transcriptionally silent region of the host genome. To ensure maximal activation of the LTR, Tat mediates nuclear translocation of NF-kappa-B by interacting with host RELA. Through its interaction with host TBP, Tat may also modulate transcription initiation. Tat can reactivate a latently infected cell by penetrating in it and transactivating its LTR promoter. In the cytoplasm, Tat is thought to act as a translational activator of HIV-1 mRNAs", "gene_name": "tat", "glycan_count": 0, "glycosylation_sites": [], "id": "P04608", "name": "tat (HIV transactivator of transcription)", "organism": "Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)", "uniprot_id": "P04608" }, { "function": "Escorts unspliced or incompletely spliced viral pre-mRNAs (late transcripts) out of the nucleus of infected cells. These pre-mRNAs carry a recognition sequence called Rev responsive element (RRE) located in the env gene, that is not present in fully spliced viral mRNAs (early transcripts). This function is essential since most viral proteins are translated from unspliced or partially spliced pre-mRNAs which cannot exit the nucleus by the pathway used by fully processed cellular mRNAs. Rev itself is translated from a fully spliced mRNA that readily exits the nucleus. Rev's nuclear localization signal (NLS) binds directly to KPNB1/Importin beta-1 without previous binding to KPNA1/Importin alpha-1. KPNB1 binds to the GDP bound form of RAN (Ran-GDP) and targets Rev to the nucleus. In the nucleus, the conversion from Ran-GDP to Ran-GTP dissociates Rev from KPNB1 and allows Rev's binding to the RRE in viral pre-mRNAs. Rev multimerization on the RRE via cooperative assembly exposes its nuclear export signal (NES) to the surface. Rev can then form a complex with XPO1/CRM1 and Ran-GTP, leading to nuclear export of the complex. Conversion from Ran-GTP to Ran-GDP mediates dissociation of the Rev/RRE/XPO1/RAN complex, so that Rev can return to the nucleus for a subsequent round of export. Beside KPNB1, also seems to interact with TNPO1/Transportin-1, RANBP5/IPO5 and IPO7/RANBP7 for nuclear import. The nucleoporin-like HRB/RIP is an essential cofactor that probably indirectly interacts with Rev to release HIV RNAs from the perinuclear region to the cytoplasm", "gene_name": "rev", "glycan_count": 0, "glycosylation_sites": [], "id": "P69718", "name": "rev (HIV regulator of virion expression)", "organism": "Human immunodeficiency virus type 1 group M subtype B (isolate HXB3)", "uniprot_id": "P69718" }, { "function": "Core component of the complement C1 complex, a multiprotein complex that initiates the classical pathway of the complement system, a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system (PubMed:12847249, PubMed:19006321, PubMed:24626930, PubMed:29449492, PubMed:3258649, PubMed:34155115, PubMed:6249812, PubMed:6776418). The classical complement pathway is initiated by the C1Q subcomplex of the C1 complex, which specifically binds IgG or IgM immunoglobulins complexed with antigens, forming antigen-antibody complexes on the surface of pathogens: C1QA, together with C1QB and C1QC, specifically recognizes and binds the Fc regions of IgG or IgM via its C1q domain (PubMed:12847249, PubMed:19006321, PubMed:24626930, PubMed:29449492, PubMed:3258649, PubMed:6776418). Immunoglobulin-binding activates the proenzyme C1R, which cleaves C1S, initiating the proteolytic cascade of the complement system (PubMed:29449492). The C1Q subcomplex is activated by a hexamer of IgG complexed with antigens, while it is activated by a pentameric IgM (PubMed:19706439, PubMed:24626930, PubMed:29449492). The C1Q subcomplex also recognizes and binds phosphatidylserine exposed on the surface of cells undergoing programmed cell death, possibly promoting activation of the complement system (PubMed:18250442)", "gene_name": "C1QC", "glycan_count": 0, "glycosylation_sites": [ { "position": 75, "type": "O-linked (Gal...) hydroxylysine" } ], "id": "P02747", "name": "C1q", "organism": "Homo sapiens", "uniprot_id": "P02747" }, { "function": "Tautomerization of D-dopachrome with decarboxylation to give 5,6-dihydroxyindole (DHI)", "gene_name": "DDT", "glycan_count": 0, "glycosylation_sites": [], "id": "P30046", "name": "CD55", "organism": "Homo sapiens", "uniprot_id": "P30046" }, { "function": "Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement-mediated injury by cleaving C3b and C4b deposited on host tissue. May be involved in the fusion of the spermatozoa with the oocyte during fertilization. Also acts as a costimulatory factor for T-cells which induces the differentiation of CD4+ into T-regulatory 1 cells. T-regulatory 1 cells suppress immune responses by secreting interleukin-10, and therefore are thought to prevent autoimmunity", "gene_name": "CD46", "glycan_count": 60, "glycosylation_sites": [ { "position": 83, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 114, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 163, "type": "O-linked (GalNAc...) threonine" }, { "position": 273, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 290, "type": "O-linked (GalNAc...) serine" }, { "position": 291, "type": "O-linked (GalNAc...) serine" }, { "position": 292, "type": "O-linked (GalNAc...) threonine" }, { "position": 298, "type": "O-linked (GalNAc...) serine" }, { "position": 300, "type": "O-linked (GalNAc...) serine" }, { "position": 302, "type": "O-linked (GalNAc...) serine" }, { "position": 303, "type": "O-linked (GalNAc...) threonine" }, { "position": 304, "type": "O-linked (GalNAc...) serine" }, { "position": 305, "type": "O-linked (GalNAc...) serine" }, { "position": 306, "type": "O-linked (GalNAc...) threonine" }, { "position": 307, "type": "O-linked (GalNAc...) threonine" }, { "position": 309, "type": "O-linked (GalNAc...) serine" }, { "position": 312, "type": "O-linked (GalNAc...) serine" }, { "position": 313, "type": "O-linked (GalNAc...) serine" }, { "position": 315, "type": "O-linked (GalNAc...) serine" }, { "position": 320, "type": "O-linked (GalNAc...) threonine" }, { "position": 326, "type": "O-linked (GalNAc...) serine" } ], "id": "P15529", "name": "CD46", "organism": "Homo sapiens", "uniprot_id": "P15529" }, { "function": "Calcium-dependent lectin involved in innate immune defense (PubMed:35102342). Binds mannose, fucose and N-acetylglucosamine on different microorganisms and activates the lectin complement pathway. Binds to late apoptotic cells, as well as to apoptotic blebs and to necrotic cells, but not to early apoptotic cells, facilitating their uptake by macrophages. May bind DNA. Upon SARS coronavirus-2/SARS-CoV-2 infection, activates the complement lectin pathway which leads to the inhibition SARS-CoV-2 infection and a reduction of the induced inflammatory response (PubMed:35102342)", "gene_name": "MBL2", "glycan_count": 0, "glycosylation_sites": [], "id": "P11226", "name": "Mannose-binding lectin (MBL)", "organism": "Homo sapiens", "uniprot_id": "P11226" }, { "function": "Electroneutral antiporter that translocates urate across the apical membrane of proximal tubular cells in exchange for monovalent organic or inorganic anions (PubMed:12024214, PubMed:22194875, PubMed:35144162, PubMed:35462902). Involved in renal reabsorption of urate and helps maintaining blood levels of uric acid (PubMed:12024214, PubMed:22194875). Mediates urate uptake by an exchange with organic anions such as (S)-lactate and nicotinate, and inorganic anion Cl(-) (PubMed:12024214). Other inorganic anions such as Br(-), I(-) and NO3(-) may also act as counteranions that exchange for urate (PubMed:12024214). Also mediates orotate tubular uptake coupled with nicotinate efflux and to a lesser extent with lactate efflux, therefore displaying a potential role in orotate renal reabsorption (PubMed:21350910). Orotate transport is Cl(-)-dependent (PubMed:21350910)", "gene_name": "SLC22A12", "glycan_count": 1, "glycosylation_sites": [ { "position": 56, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 102, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q96S37", "name": "Serum uric acid transporter (URAT1/SLC22A12)", "organism": "Homo sapiens", "uniprot_id": "Q96S37" }, { "function": "Major acute phase protein", "gene_name": "SAA1", "glycan_count": 0, "glycosylation_sites": [], "id": "P0DJI8", "name": "Serum amyloid A (SAA)", "organism": "Homo sapiens", "uniprot_id": "P0DJI8" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6P1M8 (mouse)", "name": "CD36", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P22777 (mouse)", "name": "Plasminogen activator inhibitor-1 (PAI-1)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O00767 (human ortholog)", "name": "SREBP-1c", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y478 (human ortholog)", "name": "AMPK", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P19096 (mouse)", "name": "FAS", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8R1J8 (mouse)", "name": "ACC1", "organism": "", "uniprot_id": "" }, { "function": "Involved in the targeting and/or fusion of transport vesicles to their target membrane (By similarity). Major SNARE protein of synaptic vesicles which mediates fusion of synaptic vesicles to release neurotransmitters. Essential for fast vesicular exocytosis and activity-dependent neurotransmitter release as well as fast endocytosis that mediates rapid reuse of synaptic vesicles (By similarity) (PubMed:30929742). Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1", "gene_name": "VAMP2", "glycan_count": 1, "glycosylation_sites": [], "id": "P63027", "name": "Vesicle-associated membrane protein 2 (VAMP2)", "organism": "Homo sapiens", "uniprot_id": "P63027" }, { "function": "Regulator of phosphate homeostasis (PubMed:11062477). Inhibits renal tubular phosphate transport by reducing SLC34A1 levels (PubMed:11409890). Up-regulates EGR1 expression in the presence of KL (By similarity). Acts directly on the parathyroid to decrease PTH secretion (By similarity). Regulator of vitamin-D metabolism (PubMed:15040831). Negatively regulates osteoblast differentiation and matrix mineralization (PubMed:18282132)", "gene_name": "FGF23", "glycan_count": 0, "glycosylation_sites": [ { "position": 171, "type": "O-linked (GalNAc) threonine" }, { "position": 178, "type": "O-linked (GalNAc) threonine" } ], "id": "Q9GZV9", "name": "Fibroblast Growth Factor 23", "organism": "Homo sapiens", "uniprot_id": "Q9GZV9" }, { "function": "Parathyroid hormone elevates calcium level by dissolving the salts in bone and preventing their renal excretion (PubMed:11604398, PubMed:35932760). Acts by binding to its receptor, PTH1R, activating G protein-coupled receptor signaling (PubMed:18375760, PubMed:35932760). Stimulates [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblastic cells (PubMed:21076856)", "gene_name": "PTH", "glycan_count": 0, "glycosylation_sites": [], "id": "P01270", "name": "Intact Parathyroid Hormone", "organism": "Homo sapiens", "uniprot_id": "P01270" }, { "function": "Functions in biogenesis and organization of the apical membrane of epithelial cells of the thick ascending limb of Henle's loop (TALH), where it promotes formation of complex filamentous gel-like structure that may play a role in the water barrier permeability (Probable). May serve as a receptor for binding and endocytosis of cytokines (IL-1, IL-2) and TNF (PubMed:3498215). Facilitates neutrophil migration across renal epithelia (PubMed:20798515)", "gene_name": "UMOD", "glycan_count": 403, "glycosylation_sites": [ { "position": 38, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 76, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 80, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 232, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 275, "type": "N-linked (GlcNAc...) (high mannose) asparagine" }, { "position": 322, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 396, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 513, "type": "N-linked (GlcNAc...) (complex) asparagine; alternate" }, { "position": 513, "type": "N-linked (GlcNAc...) (high mannose) asparagine; alternate" } ], "id": "P07911", "name": "Uromodulin (Tamm-Horsfall protein)", "organism": "Homo sapiens", "uniprot_id": "P07911" }, { "function": "Antioxidant and tissue repair protein with reductase, heme-binding and radical-scavenging activities. Removes and protects against harmful oxidants and repairs macromolecules in intravascular and extravascular spaces and in intracellular compartments (PubMed:11877257, PubMed:15683711, PubMed:22096585, PubMed:23157686, PubMed:23642167, PubMed:25698971, PubMed:32092412, PubMed:32823731). Intravascularly, plays a regulatory role in red cell homeostasis by preventing heme- and reactive oxygen species-induced cell damage. Binds and degrades free heme to protect fetal and adult red blood cells from hemolysis (PubMed:11877257, PubMed:32092412). Reduces extracellular methemoglobin, a Fe3+ (ferric) form of hemoglobin that cannot bind oxygen, back to the Fe2+ (ferrous) form deoxyhemoglobin, which has oxygen-carrying potential (PubMed:15683711). Upon acute inflammation, inhibits oxidation of low-density lipoprotein particles by MPO and limits vascular damage (PubMed:25698971). Extravascularly, protects from oxidation products formed on extracellular matrix structures and cell membranes. Catalyzes the reduction of carbonyl groups on oxidized collagen fibers and preserves cellular and extracellular matrix ultrastructures (PubMed:22096585, PubMed:23642167). Importantly, counteracts the oxidative damage at blood-placenta interface, preventing leakage of free fetal hemoglobin into the maternal circulation (PubMed:21356557). Intracellularly, has a role in maintaining mitochondrial redox homeostasis. Bound to complex I of the respiratory chain of mitochondria, may scavenge free radicals and preserve mitochondrial ATP synthesis. Protects renal tubule epithelial cells from heme-induced oxidative damage to mitochondria (PubMed:23157686, PubMed:32823731). Reduces cytochrome c from Fe3+ (ferric) to the Fe2+ (ferrous) state through formation of superoxide anion radicals in the presence of ascorbate or NADH/NADPH electron donor cofactors, ascorbate being the preferred cofactor (PubMed:15683711). Has a chaperone role in facilitating the correct folding of bikunin in the endoplasmic reticulum compartment (By similarity)", "gene_name": "AMBP", "glycan_count": 104, "glycosylation_sites": [ { "position": 24, "type": "O-linked (GalNAc...) threonine" }, { "position": 36, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 115, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 215, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 250, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P02760", "name": "Protein AMBP", "organism": "Homo sapiens", "uniprot_id": "P02760" }, { "function": "APOD occurs in the macromolecular complex with lecithin-cholesterol acyltransferase. It is probably involved in the transport and binding of bilin. Appears to be able to transport a variety of ligands in a number of different contexts", "gene_name": "APOD", "glycan_count": 216, "glycosylation_sites": [ { "position": 65, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 98, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P05090", "name": "Apolipoprotein D", "organism": "Homo sapiens", "uniprot_id": "P05090" }, { "function": "Kininogens are inhibitors of thiol proteases. HMW-kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII; HMW-kininogen inhibits the thrombin- and plasmin-induced aggregation of thrombocytes. LMW-kininogen inhibits the aggregation of thrombocytes. LMW-kininogen is in contrast to HMW-kininogen not involved in blood clotting", "gene_name": "KNG1", "glycan_count": 190, "glycosylation_sites": [ { "position": 48, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 169, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 205, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 294, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 401, "type": "O-linked (GalNAc...) threonine" }, { "position": 533, "type": "O-linked (GalNAc...) threonine" }, { "position": 542, "type": "O-linked (GalNAc...) threonine" }, { "position": 546, "type": "O-linked (GalNAc...) threonine" }, { "position": 557, "type": "O-linked (GalNAc...) threonine" }, { "position": 571, "type": "O-linked (GalNAc...) threonine" }, { "position": 577, "type": "O-linked (GalNAc...) serine" }, { "position": 628, "type": "O-linked (GalNAc...) threonine" } ], "id": "P01042", "name": "Kininogen-1", "organism": "Homo sapiens", "uniprot_id": "P01042" }, { "function": "EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. Magnesiotropic hormone that stimulates magnesium reabsorption in the renal distal convoluted tubule via engagement of EGFR and activation of the magnesium channel TRPM6. Can induce neurite outgrowth in motoneurons of the pond snail Lymnaea stagnalis in vitro (PubMed:10964941)", "gene_name": "EGF", "glycan_count": 12, "glycosylation_sites": [ { "position": 38, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 117, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 148, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 324, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 404, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 596, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 815, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 926, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01133", "name": "Pro-epidermal growth factor", "organism": "Homo sapiens", "uniprot_id": "P01133" }, { "function": "Catalyzes the conversion of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate, a cosubstrate for homocysteine remethylation to methionine (PubMed:29891918). Represents a key regulatory connection between the folate and methionine cycles (Probable)", "gene_name": "MTHFR", "glycan_count": 0, "glycosylation_sites": [], "id": "P42898", "name": "Methylenetetrahydrofolate reductase (MTHFR)", "organism": "Homo sapiens", "uniprot_id": "P42898" }, { "function": "Regulatory subunit which plays a role in the allosteric regulation of the enzyme catalyzing the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers", "gene_name": "IDH3G", "glycan_count": 1, "glycosylation_sites": [], "id": "P51553", "name": "Methionine synthase", "organism": "Homo sapiens", "uniprot_id": "P51553" }, { "function": "Plays a role in boundary lubrication within articulating joints. Prevents protein deposition onto cartilage from synovial fluid by controlling adhesion-dependent synovial growth and inhibiting the adhesion of synovial cells to the cartilage surface", "gene_name": "Prg4", "glycan_count": 2, "glycosylation_sites": [ { "position": 109, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 135, "type": "O-linked (GalNAc...) serine" }, { "position": 237, "type": "O-linked (GalNAc...) threonine" }, { "position": 250, "type": "O-linked (GalNAc...) threonine" }, { "position": 301, "type": "O-linked (GalNAc...) threonine" }, { "position": 302, "type": "O-linked (GalNAc...) serine" }, { "position": 306, "type": "O-linked (GalNAc...) threonine" }, { "position": 313, "type": "O-linked (GalNAc...) serine" }, { "position": 327, "type": "O-linked (GalNAc...) serine" }, { "position": 330, "type": "O-linked (GalNAc...) threonine" }, { "position": 338, "type": "O-linked (GalNAc...) threonine" }, { "position": 354, "type": "O-linked (GalNAc...) threonine" }, { "position": 362, "type": "O-linked (GalNAc...) threonine" }, { "position": 369, "type": "O-linked (GalNAc...) threonine" }, { "position": 377, "type": "O-linked (GalNAc...) threonine" }, { "position": 378, "type": "O-linked (GalNAc...) threonine" }, { "position": 385, "type": "O-linked (GalNAc...) threonine" }, { "position": 386, "type": "O-linked (GalNAc...) threonine" }, { "position": 393, "type": "O-linked (GalNAc...) threonine" }, { "position": 394, "type": "O-linked (GalNAc...) threonine" }, { "position": 416, "type": "O-linked (GalNAc...) threonine" }, { "position": 417, "type": "O-linked (GalNAc...) threonine" }, { "position": 424, "type": "O-linked (GalNAc...) threonine" }, { "position": 432, "type": "O-linked (GalNAc...) threonine" }, { "position": 433, "type": "O-linked (GalNAc...) threonine" }, { "position": 440, "type": "O-linked (GalNAc...) threonine" }, { "position": 441, "type": "O-linked (GalNAc...) threonine" }, { "position": 448, "type": "O-linked (GalNAc...) threonine" }, { "position": 472, "type": "O-linked (GalNAc...) threonine" }, { "position": 480, "type": "O-linked (GalNAc...) threonine" }, { "position": 481, "type": "O-linked (GalNAc...) threonine" }, { "position": 488, "type": "O-linked (GalNAc...) threonine" }, { "position": 489, "type": "O-linked (GalNAc...) threonine" }, { "position": 496, "type": "O-linked (GalNAc...) threonine" }, { "position": 497, "type": "O-linked (GalNAc...) threonine" }, { "position": 504, "type": "O-linked (GalNAc...) threonine" }, { "position": 505, "type": "O-linked (GalNAc...) threonine" }, { "position": 512, "type": "O-linked (GalNAc...) threonine" }, { "position": 520, "type": "O-linked (GalNAc...) threonine" }, { "position": 521, "type": "O-linked (GalNAc...) threonine" }, { "position": 528, "type": "O-linked (GalNAc...) threonine" }, { "position": 529, "type": "O-linked (GalNAc...) threonine" }, { "position": 553, "type": "O-linked (GalNAc...) threonine" }, { "position": 560, "type": "O-linked (GalNAc...) threonine" }, { "position": 561, "type": "O-linked (GalNAc...) threonine" }, { "position": 568, "type": "O-linked (GalNAc...) threonine" }, { "position": 569, "type": "O-linked (GalNAc...) threonine" }, { "position": 576, "type": "O-linked (GalNAc...) threonine" }, { "position": 577, "type": "O-linked (GalNAc...) threonine" }, { "position": 592, "type": "O-linked (GalNAc...) threonine" }, { "position": 600, "type": "O-linked (GalNAc...) threonine" }, { "position": 601, "type": "O-linked (GalNAc...) threonine" }, { "position": 622, "type": "O-linked (GalNAc...) threonine" }, { "position": 624, "type": "O-linked (GalNAc...) threonine" }, { "position": 628, "type": "O-linked (GalNAc...) threonine" }, { "position": 629, "type": "O-linked (GalNAc...) threonine" }, { "position": 692, "type": "O-linked (GalNAc...) threonine" }, { "position": 808, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 810, "type": "O-linked (GalNAc...) threonine" }, { "position": 938, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9JM99", "name": "SiglecF", "organism": "Mus musculus", "uniprot_id": "Q9JM99" }, { "function": "Tyrosine-protein kinase that acts as a cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation and apoptosis. Plays an essential role in the regulation of chondrocyte differentiation, proliferation and apoptosis, and is required for normal skeleton development. Regulates both osteogenesis and postnatal bone mineralization by osteoblasts. Promotes apoptosis in chondrocytes, but can also promote cancer cell proliferation. Required for normal development of the inner ear. Phosphorylates PLCG1, CBL and FRS2. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Plays a role in the regulation of vitamin D metabolism. Mutations that lead to constitutive kinase activation or impair normal FGFR3 maturation, internalization and degradation lead to aberrant signaling. Over-expressed or constitutively activated FGFR3 promotes activation of STAT1, STAT5A and STAT5B. Plays a role in postnatal lung development", "gene_name": "Fgfr3", "glycan_count": 8, "glycosylation_sites": [ { "position": 96, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 219, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 256, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 288, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 309, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 322, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q61851", "name": "Myelin oligodendrocyte glycoprotein (MOG)", "organism": "Mus musculus", "uniprot_id": "Q61851" }, { "function": "Part of the receptor for interleukin 6. Binds to IL6 with low affinity, but does not transduce a signal. Signal activation necessitate an association with IL6ST. Activation leads to the regulation of the immune response, acute-phase reactions and hematopoiesis. The interaction with membrane-bound IL6R and IL6ST stimulates 'classic signaling', the restricted expression of the IL6R limits classic IL6 signaling to only a few tissues such as the liver and some cells of the immune system. Whereas the binding of IL6 and soluble IL6R to IL6ST stimulates 'trans-signaling'. Alternatively, 'cluster signaling' occurs when membrane-bound IL6:IL6R complexes on transmitter cells activate IL6ST receptors on neighboring receiver cells", "gene_name": "Il6ra", "glycan_count": 1, "glycosylation_sites": [ { "position": 32, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 55, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 150, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 218, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P22272", "name": "IL-6 receptor alpha (IL-6R\u03b1)", "organism": "Mus musculus", "uniprot_id": "P22272" }, { "function": "Peptidyl-tRNA hydrolase which releases tRNAs from the ribosome during protein synthesis. Promotes caspase-independent apoptosis by regulating the function of two transcriptional regulators, AES and TLE1", "gene_name": "Ptrh2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8R2Y8", "name": "IL-23 receptor", "organism": "Mus musculus", "uniprot_id": "Q8R2Y8" }, { "function": "Growth regulator. Inhibits the proliferation of a number of tumor cell lines. Stimulates proliferation of AIDS-KS cells. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells. Uses both type I OSM receptor (heterodimers composed of LIFR and IL6ST) and type II OSM receptor (heterodimers composed of OSMR and IL6ST). Involved in the maturation of fetal hepatocytes, thereby promoting liver development and regeneration (By similarity)", "gene_name": "OSM", "glycan_count": 1, "glycosylation_sites": [ { "position": 100, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 217, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P13725", "name": "Oncostatin M (OSM)", "organism": "Homo sapiens", "uniprot_id": "P13725" }, { "function": "Cytokine that stimulates the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells and induces megakaryocyte maturation resulting in increased platelet production (PubMed:2145578). Also promotes the proliferation of hepatocytes in response to liver damage. Binding to its receptor formed by IL6ST and IL11RA activates a signaling cascade that promotes cell proliferation (PubMed:12919066). Signaling leads to the activation of intracellular protein kinases and the phosphorylation of STAT3. The interaction with the membrane-bound IL11RA and IL6ST stimulates 'classic signaling', whereas the binding of IL11 and soluble IL11RA to IL6ST stimulates 'trans-signaling' (PubMed:30279168)", "gene_name": "IL11", "glycan_count": 0, "glycosylation_sites": [], "id": "P20809", "name": "IL-11", "organism": "Homo sapiens", "uniprot_id": "P20809" }, { "function": "Cytidine deaminase catalyzing the cytidine to uridine postranscriptional editing of a variety of mRNAs (PubMed:30844405). Form complexes with cofactors that confer differential editing activity and selectivity. Responsible for the postranscriptional editing of a CAA codon for Gln to a UAA codon for stop in the apolipoprotein B mRNA (PubMed:24916387). Also involved in CGA (Arg) to UGA (Stop) editing in the NF1 mRNA (PubMed:11727199). May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation (By similarity)", "gene_name": "APOBEC1", "glycan_count": 0, "glycosylation_sites": [], "id": "P41238", "name": "APOBEC", "organism": "Homo sapiens", "uniprot_id": "P41238" }, { "function": "Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing (PubMed:12618436, PubMed:7565688, PubMed:7972084). This may affect gene expression and function in a number of ways that include mRNA translation by changing codons and hence the amino acid sequence of proteins since the translational machinery read the inosine as a guanosine; pre-mRNA splicing by altering splice site recognition sequences; RNA stability by changing sequences involved in nuclease recognition; genetic stability in the case of RNA virus genomes by changing sequences during viral RNA replication; and RNA structure-dependent activities such as microRNA production or targeting or protein-RNA interactions. Can edit both viral and cellular RNAs and can edit RNAs at multiple sites (hyper-editing) or at specific sites (site-specific editing). Its cellular RNA substrates include: bladder cancer-associated protein (BLCAP), neurotransmitter receptors for glutamate (GRIA2) and serotonin (HTR2C) and GABA receptor (GABRA3). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alters their functional activities. Exhibits low-level editing at the GRIA2 Q/R site, but edits efficiently at the R/G site and HOTSPOT1. Its viral RNA substrates include: hepatitis C virus (HCV), vesicular stomatitis virus (VSV), measles virus (MV), hepatitis delta virus (HDV), and human immunodeficiency virus type 1 (HIV-1). Exhibits either a proviral (HDV, MV, VSV and HIV-1) or an antiviral effect (HCV) and this can be editing-dependent (HDV and HCV), editing-independent (VSV and MV) or both (HIV-1). Impairs HCV replication via RNA editing at multiple sites. Enhances the replication of MV, VSV and HIV-1 through an editing-independent mechanism via suppression of EIF2AK2/PKR activation and function. Stimulates both the release and infectivity of HIV-1 viral particles by an editing-dependent mechanism where it associates with viral RNAs and edits adenosines in the 5'UTR and the Rev and Tat coding sequence. Can enhance viral replication of HDV via A-to-I editing at a site designated as amber/W, thereby changing an UAG amber stop codon to an UIG tryptophan (W) codon that permits synthesis of the large delta antigen (L-HDAg) which has a key role in the assembly of viral particles. However, high levels of ADAR1 inhibit HDV replication", "gene_name": "ADAR", "glycan_count": 2, "glycosylation_sites": [], "id": "P55265", "name": "ADAR", "organism": "Homo sapiens", "uniprot_id": "P55265" }, { "function": "Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes) (PubMed:20713600, PubMed:24290141). While LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation (PubMed:20713600). Through its interaction with the reticulophagy receptor TEX264, participates in the remodeling of subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover (PubMed:31006537, PubMed:31006538)", "gene_name": "MAP1LC3A", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H492", "name": "LC3 (Microtubule-associated proteins 1A/1B light chain 3)", "organism": "Homo sapiens", "uniprot_id": "Q9H492" }, { "function": "Involved in autophagic vesicle formation. Conjugation with ATG12, through a ubiquitin-like conjugating system involving ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. Involved in mitochondrial quality control after oxidative damage, and in subsequent cellular longevity. Plays a critical role in multiple aspects of lymphocyte development and is essential for both B and T lymphocyte survival and proliferation. Required for optimal processing and presentation of antigens for MHC II. Involved in the maintenance of axon morphology and membrane structures, as well as in normal adipocyte differentiation. Promotes primary ciliogenesis through removal of OFD1 from centriolar satellites and degradation of IFT20 via the autophagic pathway. As part of the ATG8 conjugation system with ATG12 and ATG16L1, required for recruitment of LRRK2 to stressed lysosomes and induction of LRRK2 kinase activity in response to lysosomal stress (By similarity)", "gene_name": "ATG5", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H1Y0", "name": "Atg5", "organism": "Homo sapiens", "uniprot_id": "Q9H1Y0" }, { "function": "Inhibits the activity of dimeric NF-kappa-B/REL complexes by trapping REL (RELA/p65 and NFKB1/p50) dimers in the cytoplasm by masking their nuclear localization signals (PubMed:1493333, PubMed:36651806, PubMed:7479976). On cellular stimulation by immune and pro-inflammatory responses, becomes phosphorylated promoting ubiquitination and degradation, enabling the dimeric RELA to translocate to the nucleus and activate transcription (PubMed:7479976, PubMed:7628694, PubMed:7796813, PubMed:7878466)", "gene_name": "NFKBIA", "glycan_count": 0, "glycosylation_sites": [], "id": "P25963", "name": "I\u03baB\u03b1", "organism": "Homo sapiens", "uniprot_id": "P25963" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P23219/P35354", "name": "Cyclooxygenase-1/2 (COX-1/2)", "organism": "", "uniprot_id": "" }, { "function": "Collagen receptor involved in collagen-induced platelet adhesion and activation. Plays a key role in platelet procoagulant activity and subsequent thrombin and fibrin formation. This procoagulant function may contribute to arterial and venous thrombus formation. The signaling pathway involves the FcR gamma-chain, the Src kinases (likely FYN or LYN) and SYK, the adapter protein LAT and leads to the activation of PLCG2", "gene_name": "GP6", "glycan_count": 0, "glycosylation_sites": [ { "position": 92, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9HCN6", "name": "glycoprotein VI", "organism": "Homo sapiens", "uniprot_id": "Q9HCN6" }, { "function": "Exhibits a high coumarin 7-hydroxylase activity. Can act in the hydroxylation of the anti-cancer drugs cyclophosphamide and ifosphamide. Competent in the metabolic activation of aflatoxin B1. Constitutes the major nicotine C-oxidase. Acts as a 1,4-cineole 2-exo-monooxygenase. Possesses low phenacetin O-deethylation activity", "gene_name": "CYP2A6", "glycan_count": 0, "glycosylation_sites": [], "id": "P11509", "name": "Cytochrome P450 2C8", "organism": "Homo sapiens", "uniprot_id": "P11509" }, { "function": "A cytochrome P450 monooxygenase involved in the metabolism of fatty acids, steroids and retinoids (PubMed:18698000, PubMed:19965576, PubMed:20972997, PubMed:21289075, PubMed:21576599). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase) (PubMed:18698000, PubMed:19965576, PubMed:20972997, PubMed:21289075, PubMed:21576599). Catalyzes the epoxidation of double bonds of polyunsaturated fatty acids (PUFA) (PubMed:19965576, PubMed:20972997). Metabolizes endocannabinoid arachidonoylethanolamide (anandamide) to 20-hydroxyeicosatetraenoic acid ethanolamide (20-HETE-EA) and 8,9-, 11,12-, and 14,15-epoxyeicosatrienoic acid ethanolamides (EpETrE-EAs), potentially modulating endocannabinoid system signaling (PubMed:18698000, PubMed:21289075). Catalyzes the hydroxylation of carbon-hydrogen bonds. Metabolizes cholesterol toward 25-hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis (PubMed:21576599). Catalyzes the oxidative transformations of all-trans retinol to all-trans retinal, a precursor for the active form all-trans-retinoic acid (PubMed:10681376). Also involved in the oxidative metabolism of drugs such as antiarrhythmics, adrenoceptor antagonists, and tricyclic antidepressants", "gene_name": "CYP2D6", "glycan_count": 0, "glycosylation_sites": [], "id": "P10635", "name": "Cytochrome P450 2D6", "organism": "Homo sapiens", "uniprot_id": "P10635" }, { "function": "UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile (PubMed:15472229, PubMed:16595710, PubMed:18004212, PubMed:18052087, PubMed:18674515, PubMed:18719240, PubMed:19545173, PubMed:23288867, PubMed:21422672). Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds (PubMed:15472229, PubMed:16595710, PubMed:23288867). Catalyzes the glucuronidation of endogenous steroid hormones such as androgens and estrogens (PubMed:15472229, PubMed:16595710, PubMed:18719240, PubMed:23288867). Produces dihydrotestosterone (DHT) diglucuronide from the DHT after two subsequent glucoronidation steps (PubMed:16595710). Involved in the glucuronidation of the phytochemical ferulic acid at the phenolic or the carboxylic acid group (PubMed:21422672). Also catalyzes the glucuronidation of the isoflavones genistein, daidzein, glycitein, formononetin, biochanin A and prunetin, which are phytoestrogens with anticancer and cardiovascular properties (PubMed:18052087, PubMed:19545173). Involved in the glucuronidation of the AGTR1 angiotensin receptor antagonist caderastan, a drug which can inhibit the effect of angiotensin II (PubMed:18674515). Also metabolizes mycophenolate, an immunosuppressive agent (PubMed:15470161, PubMed:18004212)", "gene_name": "UGT1A8", "glycan_count": 2, "glycosylation_sites": [ { "position": 71, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 292, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 344, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9HAW9", "name": "UDP-glucuronosyltransferase 1A9", "organism": "Homo sapiens", "uniprot_id": "Q9HAW9" }, { "function": "Plays a role in mitochondrial and peroxisomal fission (PubMed:18353969, PubMed:23530241, PubMed:24196833). Promotes the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface (PubMed:23530241). May be involved in regulation of synaptic vesicle membrane dynamics by recruitment of DNM1L to clathrin-containing vesicles (By similarity)", "gene_name": "MFF", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9GZY8", "name": "Optic atrophy 1 (Opa1)", "organism": "Homo sapiens", "uniprot_id": "Q9GZY8" }, { "function": "Functions in mitochondrial and peroxisomal division (PubMed:11514614, PubMed:12499366, PubMed:17301055, PubMed:17460227, PubMed:17553808, PubMed:18695047, PubMed:18838687, PubMed:19342591, PubMed:19411255, PubMed:19638400, PubMed:23283981, PubMed:23530241, PubMed:23921378, PubMed:26992161, PubMed:27145208, PubMed:27145933, PubMed:27301544, PubMed:27328748, PubMed:29478834, PubMed:32439975, PubMed:32484300, PubMed:9570752, PubMed:9786947). Mediates membrane fission through oligomerization into membrane-associated tubular structures that wrap around the scission site to constrict and sever the mitochondrial membrane through a GTP hydrolysis-dependent mechanism (PubMed:23530241, PubMed:23584531, PubMed:33850055). The specific recruitment at scission sites is mediated by membrane receptors like MFF, MIEF1 and MIEF2 for mitochondrial membranes (PubMed:23283981, PubMed:23921378, PubMed:29899447). While the recruitment by the membrane receptors is GTP-dependent, the following hydrolysis of GTP induces the dissociation from the receptors and allows DNM1L filaments to curl into closed rings that are probably sufficient to sever a double membrane (PubMed:29899447). Acts downstream of PINK1 to promote mitochondrial fission in a PRKN-dependent manner (PubMed:32484300). Plays an important role in mitochondrial fission during mitosis (PubMed:19411255, PubMed:26992161, PubMed:27301544, PubMed:27328748). Through its function in mitochondrial division, ensures the survival of at least some types of postmitotic neurons, including Purkinje cells, by suppressing oxidative damage (By similarity). Required for normal brain development, including that of cerebellum (PubMed:17460227, PubMed:26992161, PubMed:27145208, PubMed:27301544, PubMed:27328748). Facilitates developmentally regulated apoptosis during neural tube formation (By similarity). Required for a normal rate of cytochrome c release and caspase activation during apoptosis; this requirement may depend upon the cell type and the physiological apoptotic cues (By similarity). Required for formation of endocytic vesicles (PubMed:20688057, PubMed:23792689, PubMed:9570752). Proposed to regulate synaptic vesicle membrane dynamics through association with BCL2L1 isoform Bcl-X(L) which stimulates its GTPase activity in synaptic vesicles; the function may require its recruitment by MFF to clathrin-containing vesicles (PubMed:17015472, PubMed:23792689). Required for programmed necrosis execution (PubMed:22265414). Rhythmic control of its activity following phosphorylation at Ser-637 is essential for the circadian control of mitochondrial ATP production (PubMed:29478834)", "gene_name": "DNM1L", "glycan_count": 1, "glycosylation_sites": [ { "position": 585, "type": "O-linked (GlcNAc) threonine" }, { "position": 586, "type": "O-linked (GlcNAc) threonine" } ], "id": "O00429", "name": "Dynamin-related protein 1 (Drp1)", "organism": "Homo sapiens", "uniprot_id": "O00429" }, { "function": "Involved in the regulation of apoptosis versus cell survival, and in the maintenance of viability but not of proliferation. Mediates its effects by interactions with a number of other regulators of apoptosis. Isoform 1 inhibits apoptosis. Isoform 2 promotes apoptosis", "gene_name": "MCL1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q07820", "name": "Myeloid cell leukemia factor-1 (MCL-1)", "organism": "Homo sapiens", "uniprot_id": "Q07820" }, { "function": "Serine/threonine-protein kinase which acts as a sensor of mitochondrial damage and protects against mitochondrial dysfunction during cellular stress. It phosphorylates mitochondrial proteins to coordinate mitochondrial quality control mechanisms that remove and replace dysfunctional mitochondrial components (PubMed:14607334, PubMed:15087508, PubMed:18443288, PubMed:18957282, PubMed:19229105, PubMed:19966284, PubMed:20404107, PubMed:20547144, PubMed:20798600, PubMed:22396657, PubMed:23620051, PubMed:23754282, PubMed:23933751, PubMed:24660806, PubMed:24751536, PubMed:24784582, PubMed:24896179, PubMed:24898855, PubMed:25527291, PubMed:32484300). Depending on the severity of mitochondrial damage, activity ranges from preventing apoptosis and stimulating mitochondrial biogenesis to eliminating severely damaged mitochondria via PINK1-PRKN-dependent mitophagy (PubMed:14607334, PubMed:15087508, PubMed:18443288, PubMed:19966284, PubMed:20404107, PubMed:20798600, PubMed:22396657, PubMed:23620051, PubMed:23933751, PubMed:24898855, PubMed:32047033, PubMed:32484300). When cellular stress results in irreversible mitochondrial damage, PINK1 accumulates at the outer mitochondrial membrane (OMM) where it phosphorylates pre-existing polyubiquitin chains at 'Ser-65', recruits PRKN from the cytosol to the OMM and activates PRKN by phosphorylation at 'Ser-65'; activated PRKN then ubiquinates VDAC1 and other OMM proteins to initiate mitophagy (PubMed:14607334, PubMed:15087508, PubMed:19966284, PubMed:20404107, PubMed:20798600, PubMed:23754282, PubMed:23933751, PubMed:24660806, PubMed:24751536, PubMed:24784582, PubMed:25474007, PubMed:25527291, PubMed:32047033). The PINK1-PRKN pathway also promotes fission of damaged mitochondria through phosphorylation and PRKN-dependent degradation of mitochondrial proteins involved in fission such as MFN2 (PubMed:18443288, PubMed:23620051, PubMed:24898855). This prevents the refusion of unhealthy mitochondria with the mitochondrial network or initiates mitochondrial fragmentation facilitating their later engulfment by autophagosomes (PubMed:18443288, PubMed:23620051). Also promotes mitochondrial fission independently of PRKN and ATG7-mediated mitophagy, via the phosphorylation and activation of DNM1L (PubMed:18443288, PubMed:32484300). Regulates motility of damaged mitochondria by promoting the ubiquitination and subsequent degradation of MIRO1 and MIRO2; in motor neurons, this likely inhibits mitochondrial intracellular anterograde transport along the axons which probably increases the chance of the mitochondria undergoing mitophagy in the soma (PubMed:22396657). Required for ubiquinone reduction by mitochondrial complex I by mediating phosphorylation of complex I subunit NDUFA10 (By similarity). Phosphorylates LETM1, positively regulating its mitochondrial calcium transport activity (PubMed:29123128)", "gene_name": "PINK1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9BXM7", "name": "PTEN-induced kinase 1 (PINK1)", "organism": "Homo sapiens", "uniprot_id": "Q9BXM7" }, { "function": "Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins (PubMed:10888878, PubMed:10973942, PubMed:11431533, PubMed:12150907, PubMed:12628165, PubMed:15105460, PubMed:16135753, PubMed:21376232, PubMed:21532592, PubMed:22396657, PubMed:23620051, PubMed:23754282, PubMed:24660806, PubMed:24751536, PubMed:29311685, PubMed:32047033). Substrates include SYT11 and VDAC1 (PubMed:29311685, PubMed:32047033). Other substrates are BCL2, CCNE1, GPR37, RHOT1/MIRO1, MFN1, MFN2, STUB1, SNCAIP, SEPTIN5, TOMM20, USP30, ZNF746, MIRO1 and AIMP2 (PubMed:10888878, PubMed:10973942, PubMed:11431533, PubMed:12150907, PubMed:12628165, PubMed:15105460, PubMed:16135753, PubMed:21376232, PubMed:21532592, PubMed:22396657, PubMed:23620051, PubMed:23754282, PubMed:24660806, PubMed:24751536). Mediates monoubiquitination as well as 'Lys-6', 'Lys-11', 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination of substrates depending on the context (PubMed:19229105, PubMed:20889974, PubMed:25474007, PubMed:25621951, PubMed:32047033). Participates in the removal and/or detoxification of abnormally folded or damaged protein by mediating 'Lys-63'-linked polyubiquitination of misfolded proteins such as PARK7: 'Lys-63'-linked polyubiquitinated misfolded proteins are then recognized by HDAC6, leading to their recruitment to aggresomes, followed by degradation (PubMed:17846173, PubMed:19229105). Mediates 'Lys-63'-linked polyubiquitination of a 22 kDa O-linked glycosylated isoform of SNCAIP, possibly playing a role in Lewy-body formation (PubMed:11431533, PubMed:11590439, PubMed:15105460, PubMed:15728840, PubMed:19229105). Mediates monoubiquitination of BCL2, thereby acting as a positive regulator of autophagy (PubMed:20889974). Protects against mitochondrial dysfunction during cellular stress, by acting downstream of PINK1 to coordinate mitochondrial quality control mechanisms that remove and replace dysfunctional mitochondrial components (PubMed:11439185, PubMed:18957282, PubMed:19029340, PubMed:19966284, PubMed:21376232, PubMed:22082830, PubMed:22396657, PubMed:23620051, PubMed:23933751, PubMed:24660806, PubMed:24784582, PubMed:24896179, PubMed:25474007, PubMed:25527291, PubMed:32047033). Depending on the severity of mitochondrial damage and/or dysfunction, activity ranges from preventing apoptosis and stimulating mitochondrial biogenesis to regulating mitochondrial dynamics and eliminating severely damaged mitochondria via mitophagy (PubMed:11439185, PubMed:19029340, PubMed:19801972, PubMed:19966284, PubMed:21376232, PubMed:22082830, PubMed:22396657, PubMed:23620051, PubMed:23685073, PubMed:23933751, PubMed:24896179, PubMed:25527291, PubMed:32047033, PubMed:33499712). Activation and recruitment onto the outer membrane of damaged/dysfunctional mitochondria (OMM) requires PINK1-mediated phosphorylation of both PRKN and ubiquitin (PubMed:24660806, PubMed:24784582, PubMed:25474007, PubMed:25527291). After mitochondrial damage, functions with PINK1 to mediate the decision between mitophagy or preventing apoptosis by inducing either the poly- or monoubiquitination of VDAC1, respectively; polyubiquitination of VDAC1 promotes mitophagy, while monoubiquitination of VDAC1 decreases mitochondrial calcium influx which ultimately inhibits apoptosis (PubMed:27534820, PubMed:32047033). When cellular stress results in irreversible mitochondrial damage, promotes the autophagic degradation of dysfunctional depolarized mitochondria (mitophagy) by promoting the ubiquitination of mitochondrial proteins such as TOMM20, RHOT1/MIRO1, MFN1 and USP30 (PubMed:19029340, PubMed:19966284, PubMed:21753002, PubMed:22396657, PubMed:23620051, PubMed:23685073, PubMed:23933751, PubMed:24896179, PubMed:25527291). Preferentially assembles 'Lys-6'-, 'Lys-11'- and 'Lys-63'-linked polyubiquitin chains, leading to mitophagy (PubMed:25621951, PubMed:32047033). The PINK1-PRKN pathway also promotes fission of damaged mitochondria by PINK1-mediated phosphorylation which promotes the PRKN-dependent degradation of mitochondrial proteins involved in fission such as MFN2 (PubMed:23620051). This prevents the refusion of unhealthy mitochondria with the mitochondrial network or initiates mitochondrial fragmentation facilitating their later engulfment by autophagosomes (PubMed:23620051). Regulates motility of damaged mitochondria via the ubiquitination and subsequent degradation of MIRO1 and MIRO2; in motor neurons, this likely inhibits mitochondrial intracellular anterograde transport along the axons which probably increases the chance of the mitochondria undergoing mitophagy in the soma (PubMed:22396657). Involved in mitochondrial biogenesis via the 'Lys-48'-linked polyubiquitination of transcriptional repressor ZNF746/PARIS which leads to its subsequent proteasomal degradation and allows activation of the transcription factor PPARGC1A (PubMed:21376232). Limits the production of reactive oxygen species (ROS) (PubMed:18541373). Regulates cyclin-E during neuronal apoptosis (PubMed:12628165). In collaboration with CHPF isoform 2, may enhance cell viability and protect cells from oxidative stress (PubMed:22082830). Independently of its ubiquitin ligase activity, protects from apoptosis by the transcriptional repression of p53/TP53 (PubMed:19801972). May protect neurons against alpha synuclein toxicity, proteasomal dysfunction, GPR37 accumulation, and kainate-induced excitotoxicity (PubMed:11439185). May play a role in controlling neurotransmitter trafficking at the presynaptic terminal and in calcium-dependent exocytosis. May represent a tumor suppressor gene (PubMed:12719539)", "gene_name": "PRKN", "glycan_count": 1, "glycosylation_sites": [], "id": "O60260", "name": "Parkin", "organism": "Homo sapiens", "uniprot_id": "O60260" }, { "function": "Plays a central role in autophagy (PubMed:18570871, PubMed:21358617, PubMed:23184933, PubMed:23974797, PubMed:25484083, PubMed:28445460, PubMed:37776275). Acts as a core subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. Involved in regulation of degradative endocytic trafficking and required for the abscission step in cytokinesis, probably in the context of PI3KC3-C2 (PubMed:20208530, PubMed:20643123, PubMed:23974797, PubMed:26783301). Essential for the formation of PI3KC3-C2 but not PI3KC3-C1 PI3K complex forms. Involved in endocytosis (PubMed:25275521). May play a role in antiviral host defense", "gene_name": "BECN1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q14457", "name": "Beclin 1", "organism": "Homo sapiens", "uniprot_id": "Q14457" }, { "function": "UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. Catalyzes the initial step of dolichol-linked oligosaccharide biosynthesis, transfering GlcNAc-1-P from cytosolic UDP-GlcNAc onto the carrier lipid dolichyl phosphate (P-dolichol), yielding GlcNAc-P-P-dolichol embedded in the cytoplasmic leaflet of the endoplasmic reticulum membrane", "gene_name": "DPAGT1", "glycan_count": 2, "glycosylation_sites": [ { "position": 146, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9H3H5", "name": "Cardiolipin synthase 1 (CRLS1)", "organism": "Homo sapiens", "uniprot_id": "Q9H3H5" }, { "function": "Extracellular matrix protein implicated in guidance of migrating neurons as well as axons during development, synaptic plasticity as well as neuronal regeneration. Promotes neurite outgrowth when provided to neurons in culture. May play a role in supporting the growth of epithelial tumors. Ligand for integrins ITGA8:ITGB1, ITGA9:ITGB1, ITGAV:ITGB3 and ITGAV:ITGB6. In tumors, stimulates angiogenesis by elongation, migration and sprouting of endothelial cells (By similarity)", "gene_name": "Tnc", "glycan_count": 13, "glycosylation_sites": [ { "position": 38, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 72, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 166, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 184, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 327, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 788, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1018, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1079, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1093, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1119, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1184, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1210, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1275, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1301, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1354, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1364, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1394, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1443, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1718, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1969, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2071, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q80YX1", "name": "Mucin-2 (Muc2)", "organism": "Mus musculus", "uniprot_id": "Q80YX1" }, { "function": "Serine protease that modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (PubMed:15140022). Promotes cleavage of GSDMB, thereby inhibiting pyroptosis (PubMed:36899106). Promotes blood coagulation (PubMed:20676107). Through the activation of the platelet fibrinogen receptor integrin alpha-IIb/beta-3, potentiates platelet aggregation induced by a threshold concentration of cathepsin G (CTSG) (PubMed:25211214, PubMed:9111081). Cleaves and thus inactivates tissue factor pathway inhibitor (TFPI) (PubMed:20676107, PubMed:25211214). Capable of killing E.coli but not S.aureus in vitro; digests outer membrane protein A (ompA) in E.coli and K.pneumoniae (PubMed:10947984)", "gene_name": "ELANE", "glycan_count": 18, "glycosylation_sites": [ { "position": 88, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 124, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 173, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08246", "name": "Neutrophil elastase", "organism": "Homo sapiens", "uniprot_id": "P08246" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P48594 (SERPINB3), P48595 (SERPINB4)", "name": "Squamous cell carcinoma antigen (SCCA)", "organism": "", "uniprot_id": "" }, { "function": "Receptor for TNFSF8/CD30L (PubMed:8391931). May play a role in the regulation of cellular growth and transformation of activated lymphoblasts. Regulates gene expression through activation of NF-kappa-B (PubMed:8999898)", "gene_name": "TNFRSF8", "glycan_count": 1, "glycosylation_sites": [ { "position": 32, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 101, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 276, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 336, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P28908", "name": "CD30 (TNFRSF8)", "organism": "Homo sapiens", "uniprot_id": "P28908" }, { "function": "Receptor for different ligands such as phospholipids, cholesterol ester, lipoproteins, phosphatidylserine and apoptotic cells (PubMed:12016218, PubMed:12519372, PubMed:21226579). Receptor for HDL, mediating selective uptake of cholesteryl ether and HDL-dependent cholesterol efflux (PubMed:26965621). Also facilitates the flux of free and esterified cholesterol between the cell surface and apoB-containing lipoproteins and modified lipoproteins, although less efficiently than HDL. May be involved in the phagocytosis of apoptotic cells, via its phosphatidylserine binding activity (PubMed:12016218)", "gene_name": "SCARB1", "glycan_count": 12, "glycosylation_sites": [ { "position": 102, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 108, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 173, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 212, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 227, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 255, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 310, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 330, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 383, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8WTV0", "name": "SR-BI (Scavenger receptor class B type I)", "organism": "Homo sapiens", "uniprot_id": "Q8WTV0" }, { "function": "Escort protein required for cholesterol as well as lipid homeostasis (By similarity). Regulates export of the SCAP-SREBP complex from the endoplasmic reticulum to the Golgi upon low cholesterol, thereby regulating the processing of sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2 (PubMed:26311497). At high sterol concentrations, formation of a ternary complex with INSIG (INSIG1 or INSIG2) leads to mask the ER export signal in SCAP, promoting retention of the complex in the endoplasmic reticulum (By similarity). Low sterol concentrations trigger release of INSIG, a conformational change in the SSD domain of SCAP, unmasking of the ER export signal, promoting recruitment into COPII-coated vesicles and transport of the SCAP-SREBP to the Golgi: in the Golgi, SREBPs are then processed, releasing the transcription factor fragment of SREBPs from the membrane, its import into the nucleus and up-regulation of LDLR, INSIG1 and the mevalonate pathway (PubMed:26311497). Binds cholesterol via its SSD domain (By similarity)", "gene_name": "SCAP", "glycan_count": 7, "glycosylation_sites": [ { "position": 263, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 590, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 641, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q12770", "name": "SREBP cleavage-activating protein (SCAP)", "organism": "Homo sapiens", "uniprot_id": "Q12770" }, { "function": "Essential regulatory subunit of the mitochondrial calcium uniporter complex (uniplex), a complex that mediates calcium uptake into mitochondria (PubMed:24231807, PubMed:26774479, PubMed:27099988, PubMed:30454562, PubMed:31080062, PubMed:32315830, PubMed:32494073, PubMed:32762847, PubMed:32790952, PubMed:33296646). Required to bridge the calcium-sensing proteins MICU1 with the calcium-conducting subunit MCU (PubMed:24231807, PubMed:30454562, PubMed:32494073, PubMed:32762847, PubMed:32790952). Acts by mediating activation of MCU and retention of MICU1 to the MCU pore, in order to ensure tight regulation of the uniplex complex and appropriate responses to intracellular calcium signaling (PubMed:27099988, PubMed:31080062, PubMed:32315830, PubMed:33296646)", "gene_name": "SMDT1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H4I9", "name": "DWORF (Dwarf Open Reading Frame)", "organism": "Homo sapiens", "uniprot_id": "Q9H4I9" }, { "function": "Cell surface receptor that transfers passive humoral immunity from the mother to the newborn. Binds to the Fc region of monomeric immunoglobulin gamma and mediates its selective uptake from milk (PubMed:10933786, PubMed:7964511). IgG in the milk is bound at the apical surface of the intestinal epithelium. The resultant FcRn-IgG complexes are transcytosed across the intestinal epithelium and IgG is released from FcRn into blood or tissue fluids. Throughout life, contributes to effective humoral immunity by recycling IgG and extending its half-life in the circulation. Mechanistically, monomeric IgG binding to FcRn in acidic endosomes of endothelial and hematopoietic cells recycles IgG to the cell surface where it is released into the circulation (PubMed:10998088). In addition of IgG, regulates homeostasis of the other most abundant circulating protein albumin/ALB (PubMed:24469444, PubMed:28330995)", "gene_name": "FCGRT", "glycan_count": 49, "glycosylation_sites": [ { "position": 125, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P55899", "name": "Neonatal Fc receptor (FcRn)", "organism": "Homo sapiens", "uniprot_id": "P55899" }, { "function": "Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system. Exogenously applied M.tuberculosis EsxA or EsxA-EsxB (or EsxA expressed in host) binds B2M and decreases its export to the cell surface (total protein levels do not change), probably leading to defects in class I antigen presentation (PubMed:25356553)", "gene_name": "B2M", "glycan_count": 2, "glycosylation_sites": [ { "position": 21, "type": "N-linked (Glc) (glycation) isoleucine; in hemodialysis-associated amyloidosis" }, { "position": 39, "type": "N-linked (Glc) (glycation) lysine; in vitro" }, { "position": 61, "type": "N-linked (Glc) (glycation) lysine; in vitro" }, { "position": 68, "type": "N-linked (Glc) (glycation) lysine; in vitro" }, { "position": 78, "type": "N-linked (Glc) (glycation) lysine; in vitro" }, { "position": 111, "type": "N-linked (Glc) (glycation) lysine; in vitro" }, { "position": 114, "type": "N-linked (Glc) (glycation) lysine; in vitro" } ], "id": "P61769", "name": "\u03b22-microglobulin (\u03b22m)", "organism": "Homo sapiens", "uniprot_id": "P61769" }, { "function": "Negatively regulates T-cell-mediated immune response by inhibiting T-cell activation, proliferation, cytokine production and development of cytotoxicity. When expressed on the cell surface of tumor macrophages, plays an important role, together with regulatory T-cells (Treg), in the suppression of tumor-associated antigen-specific T-cell immunity. Involved in promoting epithelial cell transformation", "gene_name": "VTCN1", "glycan_count": 7, "glycosylation_sites": [ { "position": 216, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q7Z7D3", "name": "B7-H4", "organism": "Homo sapiens", "uniprot_id": "Q7Z7D3" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6ZMI9", "name": "B7-H6", "organism": "Homo sapiens", "uniprot_id": "Q6ZMI9" }, { "function": "Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway", "gene_name": "MAN2A1", "glycan_count": 15, "glycosylation_sites": [ { "position": 78, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 93, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1125, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q16706", "name": "MAN2A2", "organism": "Homo sapiens", "uniprot_id": "Q16706" }, { "function": "Tyrosine phosphatase which dephosphorylates or contributes to the dephosphorylation of CTNND1, FLT3, PDGFRB, MET, KDR, LYN, SRC, MAPK1, MAPK3, EGFR, TJP1, OCLN, PIK3R1 and PIK3R2 (PubMed:10821867, PubMed:12062403, PubMed:12370829, PubMed:12475979, PubMed:18348712, PubMed:19494114, PubMed:19922411, PubMed:21262971). Plays a role in cell adhesion, migration, proliferation and differentiation (PubMed:12370829, PubMed:14709717, PubMed:16682945, PubMed:19836242). Has a role in megakaryocytes and platelet formation (PubMed:30591527). Involved in vascular development (By similarity). Regulator of macrophage adhesion and spreading (By similarity). Positively affects cell-matrix adhesion (By similarity). Positive regulator of platelet activation and thrombosis. Negative regulator of cell proliferation (PubMed:16682945). Negative regulator of PDGF-stimulated cell migration; through dephosphorylation of PDGFR (PubMed:21091576). Positive regulator of endothelial cell survival, as well as of VEGF-induced SRC and AKT activation; through KDR dephosphorylation (PubMed:18936167). Negative regulator of EGFR signaling pathway; through EGFR dephosphorylation (PubMed:19836242). Enhances the barrier function of epithelial junctions during reassembly (PubMed:19332538). Negatively regulates T-cell receptor (TCR) signaling (PubMed:11259588, PubMed:9531590, PubMed:9780142). Upon T-cell TCR activation, it is up-regulated and excluded from the immunological synapses, while upon T-cell-antigen presenting cells (APC) disengagement, it is no longer excluded and can dephosphorylate PLCG1 and LAT to down-regulate prolongation of signaling (PubMed:11259588, PubMed:12913111)", "gene_name": "PTPRJ", "glycan_count": 44, "glycosylation_sites": [ { "position": 72, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 82, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 93, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 142, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 172, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 192, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 231, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 258, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 278, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 342, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 351, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 376, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 391, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 396, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 413, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 431, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 501, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 525, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 536, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 582, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 603, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 618, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 628, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 637, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 666, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 669, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 761, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 772, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 784, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 790, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 824, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 910, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 937, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q12913", "name": "PTPRJ", "organism": "Homo sapiens", "uniprot_id": "Q12913" }, { "function": "Sulfur dioxygenase that plays an essential role in hydrogen sulfide catabolism in the mitochondrial matrix. Hydrogen sulfide (H(2)S) is first oxidized by SQRDL, giving rise to cysteine persulfide residues. ETHE1 consumes molecular oxygen to catalyze the oxidation of the persulfide, once it has been transferred to a thiophilic acceptor, such as glutathione (R-SSH). Plays an important role in metabolic homeostasis in mitochondria by metabolizing hydrogen sulfide and preventing the accumulation of supraphysiological H(2)S levels that have toxic effects, due to the inhibition of cytochrome c oxidase. First described as a protein that can shuttle between the nucleus and the cytoplasm and suppress p53-induced apoptosis by sequestering the transcription factor RELA/NFKB3 in the cytoplasm and preventing its accumulation in the nucleus (PubMed:12398897)", "gene_name": "ETHE1", "glycan_count": 1, "glycosylation_sites": [], "id": "O95571", "name": "Neuronal Pentraxin 1 (NPTX1)", "organism": "Homo sapiens", "uniprot_id": "O95571" }, { "function": "Likely to play role in the modification of cellular properties that underlie long-term plasticity. Binds to agar matrix in a calcium-dependent manner (By similarity)", "gene_name": "NPTX2", "glycan_count": 4, "glycosylation_sites": [ { "position": 148, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 189, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 393, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P47972", "name": "Neuronal Pentraxin 2 (NPTX2)", "organism": "Homo sapiens", "uniprot_id": "P47972" }, { "function": "Mitochondrial outer membrane GTPase that mediates mitochondrial clustering and fusion (PubMed:11181170, PubMed:11950885, PubMed:19889647, PubMed:26214738, PubMed:28114303). Mitochondria are highly dynamic organelles, and their morphology is determined by the equilibrium between mitochondrial fusion and fission events (PubMed:28114303). Overexpression induces the formation of mitochondrial networks (PubMed:28114303). Membrane clustering requires GTPase activity and may involve a major rearrangement of the coiled coil domains (Probable). Plays a central role in mitochondrial metabolism and may be associated with obesity and/or apoptosis processes (By similarity). Plays an important role in the regulation of vascular smooth muscle cell proliferation (By similarity). Involved in the clearance of damaged mitochondria via selective autophagy (mitophagy) (PubMed:23620051). Is required for PRKN recruitment to dysfunctional mitochondria (PubMed:23620051). Involved in the control of unfolded protein response (UPR) upon ER stress including activation of apoptosis and autophagy during ER stress (By similarity). Acts as an upstream regulator of EIF2AK3 and suppresses EIF2AK3 activation under basal conditions (By similarity)", "gene_name": "MFN2", "glycan_count": 0, "glycosylation_sites": [], "id": "O95572", "name": "Neuronal Pentraxin Receptor (NPTXR)", "organism": "Homo sapiens", "uniprot_id": "O95140" }, { "function": "May play a role in regulated exocytosis. Modulates the localization of synaptophysin/SYP into synaptic-like microvesicles and may therefore play a role in synaptic-like microvesicle formation and/or maturation (By similarity). Involved in the regulation of short-term and long-term synaptic plasticity (By similarity)", "gene_name": "SYNGR1", "glycan_count": 1, "glycosylation_sites": [], "id": "O43759", "name": "Syntaxin-7", "organism": "Homo sapiens", "uniprot_id": "O43759" }, { "function": "Functions as a guanine nucleotide exchange factor (GEF) that promotes the exchange of GDP to GTP, converting inactive GDP-bound small GTPases into their active GTP-bound form (PubMed:12628187, PubMed:16464467). Involved in regulation of adherens junction between cells (PubMed:12628187). Plays a role in cell migration (PubMed:20679435)", "gene_name": "DOCK4", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8N1I0", "name": "AP2B1 (Activating Protein 2 subunit beta)", "organism": "Homo sapiens", "uniprot_id": "Q8N1I0" }, { "function": "Regulates the GDP/GTP exchange reaction of most Rab proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Promotes the dissociation of GDP-bound Rab proteins from the membrane and inhibits their activation. Promotes the dissociation of RAB1A, RAB3A, RAB5A and RAB10 from membranes", "gene_name": "GDI1", "glycan_count": 1, "glycosylation_sites": [], "id": "P31150", "name": "GDI-1 (Rab GDP Dissociation Inhibitor Alpha)", "organism": "Homo sapiens", "uniprot_id": "P31150" }, { "function": "Plays a role in neurofilament network integrity. May be involved in modulating axonal architecture during development and in the adult. In vitro, increases the susceptibility of neurofilament-H to calcium-dependent proteases (By similarity). May also function in modulating the keratin network in skin. Activates the MAPK and Elk-1 signal transduction pathway (By similarity)", "gene_name": "SNCG", "glycan_count": 1, "glycosylation_sites": [], "id": "O76070", "name": "\u03b3-Synuclein", "organism": "Homo sapiens", "uniprot_id": "O76070" }, { "function": "Involved in skeletal muscle regeneration, specifically at the onset of cell fusion. Also involved in macrophage-derived giant cells (MGC) and osteoclast formation from mononuclear precursors (By similarity)", "gene_name": "ADAM12", "glycan_count": 1, "glycosylation_sites": [ { "position": 111, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 149, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 381, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 452, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 651, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O43184", "name": "ADAM12", "organism": "Homo sapiens", "uniprot_id": "O43184" }, { "function": "Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types (By similarity). SFRP4 plays a role in bone morphogenesis. May also act as a regulator of adult uterine morphology and function. May also increase apoptosis during ovulation possibly through modulation of FZ1/FZ4/WNT4 signaling (By similarity). Has phosphaturic effects by specifically inhibiting sodium-dependent phosphate uptake (PubMed:12952927)", "gene_name": "SFRP4", "glycan_count": 31, "glycosylation_sites": [ { "position": 38, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 68, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 116, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 194, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 240, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6FHJ7", "name": "SFRP4", "organism": "Homo sapiens", "uniprot_id": "Q6FHJ7" }, { "function": "Does not exhibit calcium-activated chloride channel (CaCC) activity", "gene_name": "ANO8", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9HCE9", "name": "SMAD8 (SMAD9)", "organism": "Homo sapiens", "uniprot_id": "Q9HCE9" }, { "function": "Acts as a high affinity receptor for both nicotinic acid (also known as niacin) and (D)-beta-hydroxybutyrate and mediates increased adiponectin secretion and decreased lipolysis through G(i)-protein-mediated inhibition of adenylyl cyclase. This pharmacological effect requires nicotinic acid doses that are much higher than those provided by a normal diet. Mediates nicotinic acid-induced apoptosis in mature neutrophils. Receptor activation by nicotinic acid results in reduced cAMP levels which may affect activity of cAMP-dependent protein kinase A and phosphorylation of target proteins, leading to neutrophil apoptosis. The rank order of potency for the displacement of nicotinic acid binding is 5-methyl pyrazole-3-carboxylic acid = pyridine-3-acetic acid > acifran > 5-methyl nicotinic acid = acipimox >> nicotinuric acid = nicotinamide", "gene_name": "HCAR2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8TDS4", "name": "HCAR2", "organism": "Homo sapiens", "uniprot_id": "Q8TDS4" }, { "function": "Neuroendocrine protein of the granin family that regulates the biogenesis of secretory granules", "gene_name": "SCG2", "glycan_count": 0, "glycosylation_sites": [], "id": "P13521", "name": "SCG2", "organism": "Homo sapiens", "uniprot_id": "P13521" }, { "function": "May play a role in the proliferation or differentiation of keratinocytes", "gene_name": "SERPINB13", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UIV8", "name": "SERPINB12", "organism": "Homo sapiens", "uniprot_id": "Q9UIV8" }, { "function": "Cleaves 'Lys-63'-linked poly-ubiquitin chains, and with lesser efficiency 'Lys-48'-linked poly-ubiquitin chains (in vitro). May act as a deubiquitinating enzyme", "gene_name": "JOSD2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8TAC2", "name": "UNC13C", "organism": "Homo sapiens", "uniprot_id": "Q8TAC2" }, { "function": "Antigen-presenting major histocompatibility complex class I (MHCI) molecule. In complex with B2M/beta 2 microglobulin displays primarily viral and tumor-derived peptides on antigen-presenting cells for recognition by alpha-beta T cell receptor (TCR) on HLA-A-restricted CD8-positive T cells, guiding antigen-specific T cell immune response to eliminate infected or transformed cells (PubMed:10449296, PubMed:12138174, PubMed:12393434, PubMed:1402688, PubMed:15893615, PubMed:17189421, PubMed:19543285, PubMed:21498667, PubMed:24192765, PubMed:24395804, PubMed:2456340, PubMed:2784196, PubMed:28250417, PubMed:7504010, PubMed:7694806, PubMed:9862734). May also present self-peptides derived from the signal sequence of secreted or membrane proteins, although T cells specific for these peptides are usually inactivated to prevent autoreactivity (PubMed:25880248, PubMed:7506728, PubMed:7679507). Both the peptide and the MHC molecule are recognized by TCR, the peptide is responsible for the fine specificity of antigen recognition and MHC residues account for the MHC restriction of T cells (PubMed:12796775, PubMed:18275829, PubMed:19542454, PubMed:28250417). Typically presents intracellular peptide antigens of 8 to 13 amino acids that arise from cytosolic proteolysis via IFNG-induced immunoproteasome or via endopeptidase IDE/insulin-degrading enzyme (PubMed:17079320, PubMed:17189421, PubMed:20364150, PubMed:26929325, PubMed:27049119). Can bind different peptides containing allele-specific binding motifs, which are mainly defined by anchor residues at position 2 and 9 (PubMed:7504010, PubMed:9862734)", "gene_name": "HLA-A", "glycan_count": 0, "glycosylation_sites": [ { "position": 110, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01892", "name": "HLA-A", "organism": "Homo sapiens", "uniprot_id": "P04439" }, { "function": "Potential tumor suppressor. Required for death receptor-dependent apoptosis. Mediates activation of STK3/MST2 and STK4/MST1 during Fas-induced apoptosis by preventing their dephosphorylation. When associated with MOAP1, promotes BAX conformational change and translocation to mitochondrial membranes in response to TNF and TNFSF10 stimulation. Isoform A interacts with CDC20, an activator of the anaphase-promoting complex, APC, resulting in the inhibition of APC activity and mitotic progression. Inhibits proliferation by negatively regulating cell cycle progression at the level of G1/S-phase transition by regulating accumulation of cyclin D1 protein. Isoform C has been shown not to perform these roles, no function has been identified for this isoform. Isoform A disrupts interactions among MDM2, DAXX and USP7, thus contributing to the efficient activation of TP53 by promoting MDM2 self-ubiquitination in cell-cycle checkpoint control in response to DNA damage", "gene_name": "RASSF1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NS23", "name": "RASSF1A", "organism": "Homo sapiens", "uniprot_id": "Q9NS23" }, { "function": "Essential counter-regulatory carboxypeptidase of the renin-angiotensin hormone system that is a critical regulator of blood volume, systemic vascular resistance, and thus cardiovascular homeostasis (PubMed:27217402). Converts angiotensin I to angiotensin 1-9, a nine-amino acid peptide with anti-hypertrophic effects in cardiomyocytes, and angiotensin II to angiotensin 1-7, which then acts as a beneficial vasodilator and anti-proliferation agent, counterbalancing the actions of the vasoconstrictor angiotensin II (PubMed:10924499, PubMed:10969042, PubMed:11815627, PubMed:14504186, PubMed:19021774). Also removes the C-terminal residue from three other vasoactive peptides, neurotensin, kinetensin, and des-Arg bradykinin, but is not active on bradykinin (PubMed:10969042, PubMed:11815627). Also cleaves other biological peptides, such as apelins (apelin-13, [Pyr1]apelin-13, apelin-17, apelin-36), casomorphins (beta-casomorphin-7, neocasomorphin) and dynorphin A with high efficiency (PubMed:11815627, PubMed:27217402, PubMed:28293165). In addition, ACE2 C-terminus is homologous to collectrin and is responsible for the trafficking of the neutral amino acid transporter SL6A19 to the plasma membrane of gut epithelial cells via direct interaction, regulating its expression on the cell surface and its catalytic activity (PubMed:18424768, PubMed:19185582)", "gene_name": "ACE2", "glycan_count": 349, "glycosylation_sites": [ { "position": 53, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 90, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 103, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 322, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 432, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 546, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 690, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9BYF1", "name": "Angiotensin-Converting Enzyme 2 (ACE2)", "organism": "Homo sapiens", "uniprot_id": "Q9BYF1" }, { "function": "May play a role as endocytotic lectin receptor displaying calcium-dependent lectin activity. Internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. May be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. May contribute to cellular uptake, remodeling and degradation of extracellular collagen matrices. May play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. May participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs)", "gene_name": "MRC2", "glycan_count": 50, "glycosylation_sites": [ { "position": 69, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 140, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 364, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 588, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 954, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1029, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1350, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UBG0", "name": "CD206 (Mannose Receptor)", "organism": "Homo sapiens", "uniprot_id": "Q9UBG0" }, { "function": "Cytokine secreted primarily by mast cells, T-cells, eosinophils, and basophils that plays a role in regulating antibody production, hematopoiesis and inflammation, and the development of effector T-cell responses (PubMed:1993171, PubMed:3016727). Induces the expression of class II MHC molecules on resting B-cells. Enhances both secretion and cell surface expression of IgE and IgG1 (PubMed:1993171). Also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes (PubMed:2521231). Positively regulates IL31RA expression in macrophages. Stimulates autophagy in dendritic cells by interfering with mTORC1 signaling and through the induction of RUFY4. In addition, plays a critical role in higher functions of the normal brain, such as memory and learning (By similarity). Upon binding to IL4, IL4R receptor dimerizes either with the common IL2R gamma chain/IL2RG to produce the type 1 signaling complex, located mainly on hematopoietic cells, or with the IL13RA1 to produce the type 2 complex, which is also expressed on nonhematopoietic cells (PubMed:10219247, PubMed:11526337, PubMed:18243101). Engagement of both types of receptors initiates JAK3 and to a lower extend JAK1 phosphorylation leading to activation of the signal transducer and activator of transcription 6/STAT6 (PubMed:7721895)", "gene_name": "IL4", "glycan_count": 0, "glycosylation_sites": [ { "position": 62, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P05112", "name": "IL4", "organism": "Homo sapiens", "uniprot_id": "P05112" }, { "function": "Cytokine that plays important roles in allergic inflammation and immune response to parasite infection (PubMed:8096327, PubMed:8097324). Synergizes with IL2 in regulating interferon-gamma synthesis (PubMed:8096327). Stimulates B-cell proliferation, and activation of eosinophils, basophils, and mast cells (PubMed:7903680, PubMed:8759755). Plays an important role in controlling IL33 activity by modulating the production of transmembrane and soluble forms of interleukin-1 receptor-like 1/IL1RL1 (By similarity). Displays the capacity to antagonize Th1-driven proinflammatory immune response and downregulates synthesis of many proinflammatory cytokines including IL1, IL6, IL10, IL12 and TNF-alpha through a mechanism that partially involves suppression of NF-kappa-B (By similarity). Also functions on nonhematopoietic cells, including endothelial cells where it induces vascular cell adhesion protein 1/VCAM1, which is important in the recruitment of eosinophils (PubMed:8639787). Exerts its biological effects through its receptors which comprises the IL4R chain and the IL13RA1 chain, to activate JAK1 and TYK2, leading to the activation of STAT6 (PubMed:9013879). Aside from IL13RA1, another receptor IL13RA2 acts as a high affinity decoy for IL13 and mediates internalization and depletion of extracellular IL13 (PubMed:21622864)", "gene_name": "IL13", "glycan_count": 0, "glycosylation_sites": [ { "position": 52, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 63, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 71, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 86, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P35225", "name": "IL13", "organism": "Homo sapiens", "uniprot_id": "P35225" }, { "function": "Ezrin-radixin-moesin (ERM) family protein that connects the actin cytoskeleton to the plasma membrane and thereby regulates the structure and function of specific domains of the cell cortex. Tethers actin filaments by oscillating between a resting and an activated state providing transient interactions between moesin and the actin cytoskeleton (PubMed:10212266). Once phosphorylated on its C-terminal threonine, moesin is activated leading to interaction with F-actin and cytoskeletal rearrangement (PubMed:10212266). These rearrangements regulate many cellular processes, including cell shape determination, membrane transport, and signal transduction (PubMed:12387735, PubMed:15039356). The role of moesin is particularly important in immunity acting on both T and B-cells homeostasis and self-tolerance, regulating lymphocyte egress from lymphoid organs (PubMed:9298994, PubMed:9616160). Modulates phagolysosomal biogenesis in macrophages (By similarity). Also participates in immunologic synapse formation (PubMed:27405666)", "gene_name": "MSN", "glycan_count": 2, "glycosylation_sites": [], "id": "P26038", "name": "Moesin", "organism": "Homo sapiens", "uniprot_id": "P26038" }, { "function": "May be involved in transcriptional regulation", "gene_name": "ZSCAN5A", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9BUG6", "name": "O-GlcNAcase (OGA)", "organism": "Homo sapiens", "uniprot_id": "Q9BUG6" }, { "function": "ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). ICAM2 may play a role in lymphocyte recirculation by blocking LFA-1-dependent cell adhesion. It mediates adhesive interactions important for antigen-specific immune response, NK-cell mediated clearance, lymphocyte recirculation, and other cellular interactions important for immune response and surveillance", "gene_name": "ICAM2", "glycan_count": 26, "glycosylation_sites": [ { "position": 47, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 82, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 105, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 153, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 176, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 187, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P13598", "name": "ICAM2", "organism": "Homo sapiens", "uniprot_id": "P13598" }, { "function": "Glycolytic enzyme the catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate (PubMed:1369209, PubMed:29775581). In addition to glycolysis, involved in various processes such as growth control, hypoxia tolerance and allergic responses (PubMed:10802057, PubMed:12666133, PubMed:2005901, PubMed:29775581). May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons (PubMed:12666133). Stimulates immunoglobulin production (PubMed:1369209)", "gene_name": "ENO1", "glycan_count": 6, "glycosylation_sites": [], "id": "P06733", "name": "ENOLASE 1 (ENO1)", "organism": "Homo sapiens", "uniprot_id": "P06733" }, { "function": "Integral membrane protein that functions as a NADPH-dependent ferric-chelate reductase, using NADPH from one side of the membrane to reduce a Fe(3+) chelate that is bound on the other side of the membrane (By similarity). Mediates sequential transmembrane electron transfer from NADPH to FAD and onto heme, and finally to the Fe(3+) chelate (By similarity). Can also reduce Cu(2+) to Cu(1+) (By similarity)", "gene_name": "STEAP2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8NFT2", "name": "STEAP3", "organism": "Homo sapiens", "uniprot_id": "Q8NFT2" }, { "function": "Enzyme which catalyzes the acetylation of polyamines (PubMed:15283699, PubMed:16455797, PubMed:17516632). Substrate specificity: norspermidine = spermidine >> spermine > N(1)-acetylspermine (PubMed:17516632). This highly regulated enzyme allows a fine attenuation of the intracellular concentration of polyamines (PubMed:16455797). Also involved in the regulation of polyamine transport out of cells (PubMed:16455797). Also acts on 1,3-diaminopropane and 1,5-diaminopentane (PubMed:16455797, PubMed:17516632)", "gene_name": "SAT1", "glycan_count": 0, "glycosylation_sites": [], "id": "P21673", "name": "SAT1", "organism": "Homo sapiens", "uniprot_id": "P21673" }, { "function": "Associates with SLC3A1/rBAT to form a functional heterodimeric complex that transports anionic and neutral amino acids across the apical plasma membrane of renal epithelium. Preferentially mediates exchange transport, but can also operate via facilitated diffusion. May act as a major transporter for L-cystine in late proximal tubules, ensuring its reabsorption from the luminal fluid in exchange for cytosolic L-glutamate or L-aspartate", "gene_name": "SLC7A13", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8TCU3", "name": "LPCAT3", "organism": "Homo sapiens", "uniprot_id": "Q8TCU3" }, { "function": "Cytosolic aldo-keto reductase that catalyzes the NADH and NADPH-dependent reduction of ketosteroids to hydroxysteroids (PubMed:19218247). Most probably acts as a reductase in vivo since the oxidase activity measured in vitro is inhibited by physiological concentrations of NADPH (PubMed:14672942). Displays a broad positional specificity acting on positions 3, 17 and 20 of steroids and regulates the metabolism of hormones like estrogens and androgens (PubMed:10998348). May also reduce conjugated steroids such as 5alpha-dihydrotestosterone sulfate (PubMed:19218247). Displays affinity for bile acids (PubMed:8486699)", "gene_name": "AKR1C1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q04828", "name": "AKR1C1", "organism": "Homo sapiens", "uniprot_id": "Q04828" }, { "function": "Muscle-specific type III intermediate filament essential for proper muscular structure and function. Plays a crucial role in maintaining the structure of sarcomeres, inter-connecting the Z-disks and forming the myofibrils, linking them not only to the sarcolemmal cytoskeleton, but also to the nucleus and mitochondria, thus providing strength for the muscle fiber during activity (By similarity). In adult striated muscle they form a fibrous network connecting myofibrils to each other and to the plasma membrane from the periphery of the Z-line structures (PubMed:25394388). May act as a sarcomeric microtubule-anchoring protein: specifically associates with detyrosinated tubulin-alpha chains, leading to buckled microtubules and mechanical resistance to contraction (PubMed:27102488). Required for nuclear membrane integrity, via anchoring at the cell tip and nuclear envelope, resulting in maintenance of microtubule-derived intracellular mechanical forces (PubMed:35959657). Contributes to the transcriptional regulation of the NKX2-5 gene in cardiac progenitor cells during a short period of cardiomyogenesis and in cardiac side population stem cells in the adult. Plays a role in maintaining an optimal conformation of nebulette (NEB) on heart muscle sarcomeres to bind and recruit cardiac alpha-actin (PubMed:27733623)", "gene_name": "Des", "glycan_count": 1, "glycosylation_sites": [], "id": "P31001", "name": "Desmin (Des)", "organism": "Mus musculus", "uniprot_id": "P31001" }, { "function": "Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Implicated in cytokinesis, receptor capping, and cell locomotion (PubMed:11942626, PubMed:2526655). In myoblasts, may regulate PIEZO1-dependent cortical actomyosin assembly involved in myotube formation (By similarity)", "gene_name": "MYL9", "glycan_count": 1, "glycosylation_sites": [], "id": "P24844", "name": "Myosin Light Chain 9 (Myl9)", "organism": "Homo sapiens", "uniprot_id": "P24844" }, { "function": "Regulatory light chain of myosin. Does not bind calcium", "gene_name": "MYL6", "glycan_count": 4, "glycosylation_sites": [], "id": "P60660", "name": "Myosin Light Chain 6 (Myl6)", "organism": "Homo sapiens", "uniprot_id": "P60660" }, { "function": "Innate immunity protein that plays several important functions in antimicrobial and antitumor defense systems. Acts as a pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria and thus provides bactericidal activity (PubMed:9707603). Forms an equimolar complex with heat shock protein HSPA1A and induces programmed cell death through apoptosis and necroptosis in tumor cell lines by activating the TNFR1 receptor on the target cell membrane (PubMed:21247889, PubMed:26183779). In addition, acts in complex with the Ca(2+)-binding protein S100A4 as a chemoattractant able to induce lymphocyte movement (PubMed:26654597). Mechanistically, this complex acts as a ligand of the chemotactic receptors CCR5 and CXCR3 which are present on the cells of the immune system (PubMed:30713770). Also promotes the activation of lymphocytes that become able to kill virus-infected cells as well as tumor cells by modulating the spectrum of their target-cell specificity (PubMed:28977785, PubMed:29083508). Induction of cytotoxicity on monocyte surface requires interaction with TREM1 receptor (PubMed:25595774, PubMed:28977785)", "gene_name": "PGLYRP1", "glycan_count": 0, "glycosylation_sites": [ { "position": 112, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O75594", "name": "Muscleblind-like Splicing Regulator 1 (Mbnl1)", "organism": "Homo sapiens", "uniprot_id": "O75594" }, { "function": "Peptide hormone that functions as endogenous ligand for the G-protein-coupled apelin receptor (APLNR/APJ), that plays a role in cadiovascular homeostasis (PubMed:10525157, PubMed:22810587, PubMed:35817871, PubMed:38428423). Functions as a balanced agonist activating both G(i) protein pathway and beta-arrestin pathway of APLNR (PubMed:22810587, PubMed:38428423). Downstream G proteins activation, apelin can inhibit cAMP production and activate key intracellular effectors such as ERKs (PubMed:22810587, PubMed:35817871, PubMed:38428423). On the other hand, APLNR activation induces beta-arrestin recruitment to the membrane leading to desensitization and internalization of the receptor (PubMed:22810587, PubMed:38428423). Apelin blunts cardiac hypertrophic induction from APLNR on response to pathological stimuli, but also induces myocardial hypertrophy under normal conditions (PubMed:22810587, PubMed:38428423). Apelin-36 dissociates more hardly than (pyroglu)apelin-13 from APLNR (By similarity). Involved in the regulation of cardiac precursor cell movements during gastrulation and heart morphogenesis (By similarity). Has an inhibitory effect on cytokine production in response to T-cell receptor/CD3 cross-linking; the oral intake of apelin in the colostrum and the milk might therefore modulate immune responses in neonates (By similarity). Plays a role in early coronary blood vessels formation (By similarity). Mediates myocardial contractility in an ERK1/2-dependent manner (By similarity). May also have a role in the central control of body fluid homeostasis by influencing vasopressin release and drinking behavior (By similarity)", "gene_name": "APLN", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9ULZ1", "name": "Apelin (Apln)", "organism": "Homo sapiens", "uniprot_id": "Q9ULZ1" }, { "function": "Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate, an important precursor of carotenoids and geranylated proteins", "gene_name": "GGPS1", "glycan_count": 0, "glycosylation_sites": [], "id": "O95749", "name": "Geranylgeranyl diphosphate synthase 1 (GGPS1)", "organism": "Homo sapiens", "uniprot_id": "O95749" }, { "function": "Catalyzes the condensation of acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is converted by HMG-CoA reductase (HMGCR) into mevalonate, a precursor for cholesterol synthesis", "gene_name": "HMGCS1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q01581", "name": "HMG-CoA synthase 1 (HMGCS1)", "organism": "Homo sapiens", "uniprot_id": "Q01581" }, { "function": "Reversible hydration of carbon dioxide", "gene_name": "CA3", "glycan_count": 1, "glycosylation_sites": [], "id": "P07451", "name": "Carbonic anhydrase 3 (CA3)", "organism": "Homo sapiens", "uniprot_id": "P07451" }, { "function": "Key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The size and extensibility of the cross-links are the main determinants of sarcomere extensibility properties of muscle. In non-muscle cells, seems to play a role in chromosome condensation and chromosome segregation during mitosis. Might link the lamina network to chromatin or nuclear actin, or both during interphase", "gene_name": "TTN", "glycan_count": 3, "glycosylation_sites": [], "id": "Q8WZ42", "name": "Titin", "organism": "Homo sapiens", "uniprot_id": "Q8WZ42" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UKA1/Q14896", "name": "Myosin binding protein C (MYBPC1/3)", "organism": "", "uniprot_id": "" }, { "function": "Binds and activates TEK/TIE2 receptor by inducing its dimerization and tyrosine phosphorylation. Plays an important role in the regulation of angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Required for normal angiogenesis and heart development during embryogenesis. After birth, activates or inhibits angiogenesis, depending on the context. Inhibits angiogenesis and promotes vascular stability in quiescent vessels, where endothelial cells have tight contacts. In quiescent vessels, ANGPT1 oligomers recruit TEK to cell-cell contacts, forming complexes with TEK molecules from adjoining cells, and this leads to preferential activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascades. In migrating endothelial cells that lack cell-cell adhesions, ANGT1 recruits TEK to contacts with the extracellular matrix, leading to the formation of focal adhesion complexes, activation of PTK2/FAK and of the downstream kinases MAPK1/ERK2 and MAPK3/ERK1, and ultimately to the stimulation of sprouting angiogenesis. Mediates blood vessel maturation/stability. Implicated in endothelial developmental processes later and distinct from that of VEGF. Appears to play a crucial role in mediating reciprocal interactions between the endothelium and surrounding matrix and mesenchyme", "gene_name": "ANGPT1", "glycan_count": 7, "glycosylation_sites": [ { "position": 92, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 122, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 154, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 243, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 295, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q15389", "name": "Angiopoietin (Ang)", "organism": "Homo sapiens", "uniprot_id": "Q15389" }, { "function": "Aggregates keratin intermediate filaments and promotes disulfide-bond formation among the intermediate filaments during terminal differentiation of mammalian epidermis", "gene_name": "FLG", "glycan_count": 1, "glycosylation_sites": [], "id": "P20930", "name": "Filaggrin", "organism": "Homo sapiens", "uniprot_id": "P20930" }, { "function": "Major keratinocyte cell envelope protein", "gene_name": "LORICRIN", "glycan_count": 1, "glycosylation_sites": [], "id": "P23490", "name": "Loricrin", "organism": "Homo sapiens", "uniprot_id": "P23490" }, { "function": "Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Responsible for cross-linking epidermal proteins during formation of the stratum corneum. Involved in cell proliferation (PubMed:26220141)", "gene_name": "TGM1", "glycan_count": 1, "glycosylation_sites": [], "id": "P22735", "name": "Transglutaminase-1", "organism": "Homo sapiens", "uniprot_id": "P22735" }, { "function": "Adapter protein that functions as a clathrin-associated sorting protein (CLASP) required for clathrin-mediated endocytosis of selected cargo proteins. Can bind and assemble clathrin, and binds simultaneously to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and cargos containing non-phosphorylated NPXY internalization motifs, such as the LDL receptor, to recruit them to clathrin-coated pits. Can function in clathrin-mediated endocytosis independently of the AP-2 complex. Involved in endocytosis of integrin beta-1; this function seems to redundant with the AP-2 complex and seems to require DAB2 binding to endocytosis accessory EH domain-containing proteins such as EPS15, EPS15L1 and ITSN1. Involved in endocytosis of cystic fibrosis transmembrane conductance regulator/CFTR. Involved in endocytosis of megalin/LRP2 lipoprotein receptor during embryonal development. Required for recycling of the TGF-beta receptor. Involved in CFTR trafficking to the late endosome. Involved in several receptor-mediated signaling pathways. Involved in TGF-beta receptor signaling and facilitates phosphorylation of the signal transducer SMAD2. Mediates TFG-beta-stimulated JNK activation. May inhibit the canoniocal Wnt/beta-catenin signaling pathway by stabilizing the beta-catenin destruction complex through a competing association with axin preventing its dephosphorylation through protein phosphatase 1 (PP1). Sequesters LRP6 towards clathrin-mediated endocytosis, leading to inhibition of Wnt/beta-catenin signaling. May activate non-canonical Wnt signaling. In cell surface growth factor/Ras signaling pathways proposed to inhibit ERK activation by interrupting the binding of GRB2 to SOS1 and to inhibit SRC by preventing its activating phosphorylation at 'Tyr-419'. Proposed to be involved in modulation of androgen receptor (AR) signaling mediated by SRC activation; seems to compete with AR for interaction with SRC. Plays a role in the CSF-1 signal transduction pathway. Plays a role in cellular differentiation. Involved in cell positioning and formation of visceral endoderm (VE) during embryogenesis and proposed to be required in the VE to respond to Nodal signaling coming from the epiblast. Required for the epithelial to mesenchymal transition, a process necessary for proper embryonic development. May be involved in myeloid cell differentiation and can induce macrophage adhesion and spreading. May act as a tumor suppressor", "gene_name": "DAB2", "glycan_count": 1, "glycosylation_sites": [], "id": "P98082", "name": "MUC1", "organism": "Homo sapiens", "uniprot_id": "P98082" }, { "function": "Part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linkling of collagen fibrils. Required for normal hydroxylation of lysine residues in type I collagen chains in skin, bone, tendon, aorta and cornea. Required for normal skin stability via its role in hydroxylation of lysine residues in collagen alpha chains and in collagen fibril assembly. Apparently not required for normal prolyl 3-hydroxylation on collagen chains, possibly because it functions redundantly with other prolyl 3-hydroxylases", "gene_name": "P3H3", "glycan_count": 2, "glycosylation_sites": [ { "position": 331, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 462, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8IVL6", "name": "MUC5AC", "organism": "Homo sapiens", "uniprot_id": "Q8IVL6" }, { "function": "Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid (By similarity). L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system and plays an important role in fast excitatory synaptic transmission (By similarity). Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse upon entry of monovalent and divalent cations such as sodium and calcium. The receptor then desensitizes rapidly and enters in a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of L-glutamate. Through complex formation with NSG1, GRIP1 and STX12 controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting (By similarity)", "gene_name": "Gria2", "glycan_count": 0, "glycosylation_sites": [ { "position": 256, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 370, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 406, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 413, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q61605", "name": "Defensin \u03b21 (Defb1)", "organism": "Mus musculus", "uniprot_id": "P23819" }, { "function": "Component of innate and adaptive immunity that recognizes and binds 23S rRNA from bacteria. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Specifically binds the 5'-CGGAAAGACC-3' sequence on bacterial 23S rRNA, a sequence also bound by MLS group antibiotics (including erythromycin). May also recognize vesicular stomatitis virus; however, these data require additional evidences", "gene_name": "Tlr13", "glycan_count": 6, "glycosylation_sites": [ { "position": 93, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 109, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 125, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 152, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 167, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 209, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 233, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 263, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 271, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 274, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 300, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 310, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 357, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 388, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 413, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 421, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 644, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 663, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 711, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 742, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6R5N8", "name": "Lactoferrin (Ltf)", "organism": "Mus musculus", "uniprot_id": "Q6R5N8" }, { "function": "Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G (PubMed:9126337). Modulates the innate immune response after bacterial infection (PubMed:12615907). Contributes to regulate the inflammatory and immune responses to the intracellular parasite L.major (PubMed:25030421). Down-regulates responses to bacterial lipopolysaccharide (LPS) (PubMed:12615907, PubMed:25030421, PubMed:9039268). Plays a role in regulating the activation of NF-kappa-B and inflammatory responses (PubMed:11017147, PubMed:12615907). Has antimicrobial activity against mycobacteria, but not against salmonella (PubMed:18322212). Contributes to normal resistance against infection by M.tuberculosis (PubMed:18322212). Required for normal resistance to L.major (PubMed:25030421). Required for normal wound healing, probably by preventing tissue damage by limiting protease activity (PubMed:11017147, PubMed:25030421). Together with ELANE, required for normal differentiation and proliferation of bone marrow myeloid cells (By similarity)", "gene_name": "Slpi", "glycan_count": 0, "glycosylation_sites": [], "id": "P97430", "name": "Secretory Leukocyte Peptidase Inhibitor (Slpi)", "organism": "Mus musculus", "uniprot_id": "P97430" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "fragment of P05067", "name": "Amyloid-beta (A\u03b2)", "organism": "", "uniprot_id": "" }, { "function": "Catalyzes the peptide bond hydrolysis in Xaa-His dipeptides, displaying the highest activity toward carnosine (beta-alanyl-L-histidine) and anserine (beta-alanyl-3-methyl-histidine)", "gene_name": "CNDP1", "glycan_count": 24, "glycosylation_sites": [ { "position": 322, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 382, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q96KN2", "name": "Carnosinase CN1", "organism": "Homo sapiens", "uniprot_id": "Q96KN2" }, { "function": "Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling (By similarity)", "gene_name": "EFNA3", "glycan_count": 15, "glycosylation_sites": [ { "position": 38, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 67, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 100, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P52797", "name": "Ephrin-A3", "organism": "Homo sapiens", "uniprot_id": "P52797" }, { "function": "Endoribonuclease that cleaves tRNAs and rRNAs (PubMed:29563550). Cleaves tRNAs 11 nucleotides from the 3'-terminus at the acceptor stem (PubMed:29563550). Does not act on tRNA(Sec) (PubMed:29563550). Able to restrict HIV-1 virus replication; ability to inhibit HIV-1 replication is dependent on endoribonuclease activity (PubMed:29563550)", "gene_name": "SLFN13", "glycan_count": 0, "glycosylation_sites": [], "id": "Q68D06", "name": "B7-H6", "organism": "Homo sapiens", "uniprot_id": "Q68D06" }, { "function": "ATP-independent molecular chaperone preventing the aggregation of misfolded and hydrophobic patches-containing proteins (PubMed:21636303). Functions as part of a cytosolic protein quality control complex, the BAG6/BAT3 complex, which maintains these client proteins in a soluble state and participates in their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation (PubMed:20516149, PubMed:21636303, PubMed:21743475, PubMed:28104892). The BAG6/BAT3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endoplasmic reticulum membrane. Recruited to ribosomes, it interacts with the transmembrane region of newly synthesized tail-anchored proteins and together with SGTA and ASNA1 mediates their delivery to the endoplasmic reticulum (PubMed:20516149, PubMed:20676083, PubMed:25535373, PubMed:28104892). Client proteins that cannot be properly delivered to the endoplasmic reticulum are ubiquitinated by RNF126, an E3 ubiquitin-protein ligase associated with BAG6 and are sorted to the proteasome (PubMed:24981174, PubMed:27193484, PubMed:28104892). SGTA which prevents the recruitment of RNF126 to BAG6 may negatively regulate the ubiquitination and the proteasomal degradation of client proteins (PubMed:23129660, PubMed:25179605, PubMed:27193484). Similarly, the BAG6/BAT3 complex also functions as a sorting platform for proteins of the secretory pathway that are mislocalized to the cytosol either delivering them to the proteasome for degradation or to the endoplasmic reticulum (PubMed:21743475). The BAG6/BAT3 complex also plays a role in the endoplasmic reticulum-associated degradation (ERAD), a quality control mechanism that eliminates unwanted proteins of the endoplasmic reticulum through their retrotranslocation to the cytosol and their targeting to the proteasome. It maintains these retrotranslocated proteins in an unfolded yet soluble state condition in the cytosol to ensure their proper delivery to the proteasome (PubMed:21636303). BAG6 is also required for selective ubiquitin-mediated degradation of defective nascent chain polypeptides by the proteasome. In this context, it may participate in the production of antigenic peptides and play a role in antigen presentation in immune response (By similarity). BAG6 is also involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. BAG6 may ensure the proper degradation of these proteins and thereby protects the endoplasmic reticulum from protein overload upon stress (PubMed:26565908). By inhibiting the polyubiquitination and subsequent proteasomal degradation of HSPA2 it may also play a role in the assembly of the synaptonemal complex during spermatogenesis (By similarity). Also positively regulates apoptosis by interacting with and stabilizing the proapoptotic factor AIFM1 (By similarity). By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway (PubMed:26692333)", "gene_name": "BAG6", "glycan_count": 2, "glycosylation_sites": [], "id": "P46379", "name": "BAG6 (BAT3)", "organism": "Homo sapiens", "uniprot_id": "P46379" }, { "function": "Glycosyltransferase that catalyzes the transfer of an N-acetylglucosamine (GlcNAc) moiety in beta1-6 linkage from UDP-GlcNAc onto mucin-type core 1 O-glycan to form the branched mucin-type core 2 O-glycan (PubMed:1329093, PubMed:23027862). The catalysis is metal ion-independent and occurs with inversion of the anomeric configuration of sugar donor (By similarity). Selectively involved in synthesis of mucin-type core 2 O-glycans that serve as scaffolds for the display of selectin ligand sialyl Lewis X epitope by myeloid cells, with an impact on homeostasis and recruitment to inflammatory sites (By similarity). Can also act on glycolipid substrates. Transfers GlcNAc moiety to GalGb4Cer globosides in a reaction step to the synthesis of stage-specific embryonic antigen 1 (SSEA-1) determinant (By similarity). Can use Galbeta1-3GalNAcalpha1- and Galbeta1-3GalNAcbeta1- oligosaccharide derivatives as acceptor substrates (By similarity)", "gene_name": "GCNT1", "glycan_count": 1, "glycosylation_sites": [ { "position": 58, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 95, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q02742", "name": "GCNT1 (Core-2 \u03b21,6-N-acetylglucosaminyltransferase)", "organism": "Homo sapiens", "uniprot_id": "Q02742" }, { "function": "A beta-galactoside alpha2-3 sialyltransferase involved in terminal sialylation of glycoproteins and glycolipids (PubMed:8288606, PubMed:8611500). Catalyzes the transfer of sialic acid (N-acetyl-neuraminic acid; Neu5Ac) from the nucleotide sugar donor CMP-Neu5Ac onto acceptor Galbeta-(1->3)-GalNAc- and Galbeta-(1->4)-GlcNAc-terminated glycoconjugates through an alpha2-3 linkage (PubMed:8288606, PubMed:8611500). Plays a major role in hemostasis. Responsible for sialylation of plasma VWF/von Willebrand factor, preventing its recognition by asialoglycoprotein receptors (ASGPR) and subsequent clearance. Regulates ASGPR-mediated clearance of platelets (By similarity). Participates in the biosynthesis of the sialyl Lewis X epitopes, both on O- and N-glycans, which are recognized by SELE/E-selectin, SELP/P-selectin and SELL/L-selectin. Essential for selectin-mediated rolling and adhesion of leukocytes during extravasation (PubMed:25498912). Contributes to adhesion and transendothelial migration of neutrophils likely through terminal sialylation of CXCR2 (By similarity). In glycosphingolipid biosynthesis, sialylates GM1 and GA1 gangliosides to form GD1a and GM1b, respectively (PubMed:8288606). Metabolizes brain c-series ganglioside GT1c forming GQ1c (By similarity). Synthesizes ganglioside LM1 (IV3Neu5Ac-nLc4Cer), a major structural component of peripheral nerve myelin (PubMed:8611500)", "gene_name": "ST3GAL4", "glycan_count": 4, "glycosylation_sites": [ { "position": 61, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 131, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 310, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 329, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q11206", "name": "ST3Gal4", "organism": "Homo sapiens", "uniprot_id": "Q11206" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03437 (IAV)", "name": "Hemagglutinin (HA)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P0DTC2 (SARS-CoV-2)", "name": "Spike protein (S)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P0DTC4 (SARS-CoV-2)", "name": "Envelope protein (E)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6X4T0 (PRRSV)", "name": "Glycoprotein 5 (GP5)", "organism": "", "uniprot_id": "" }, { "function": "Serine protease (PubMed:20977675, PubMed:28710277, PubMed:34562451). Cleaves the proform of PRSS8/prostasin to form the active protein (PubMed:34562451). Cleaves the proform of HGF to form the active protein which promotes MAPK signaling (PubMed:20977675). Promotes the formation of the stratum corneum and subsequently the epidermal barrier in embryos (By similarity)", "gene_name": "TMPRSS13", "glycan_count": 0, "glycosylation_sites": [ { "position": 255, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 292, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 405, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 445, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9BYE1", "name": "Interferon-induced transmembrane protein 3 (IFITM3)", "organism": "Homo sapiens", "uniprot_id": "Q9BYE2" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P59595 (SARS-CoV-2)", "name": "Nucleocapsid protein (NP)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6T2U2 (JEV)", "name": "Non-structural protein 2A (NS2A)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9QZQ8 (HCV)", "name": "Non-structural protein NS2", "organism": "", "uniprot_id": "" }, { "function": "Sorting receptor that directs several proteins to their correct location within the cell (Probable). Along with AP-1 complex, involved Golgi apparatus - endosome sorting (PubMed:17646382). Sorting receptor for APP, regulating its intracellular trafficking and processing into amyloidogenic-beta peptides. Retains APP in the trans-Golgi network, hence preventing its transit through late endosomes where amyloid beta peptides Abeta40 and Abeta42 are generated (PubMed:16174740, PubMed:16407538, PubMed:17855360, PubMed:24523320). May also sort newly produced amyloid-beta peptides to lysosomes for catabolism (PubMed:24523320). Does not affect APP trafficking from the endoplasmic reticulum to Golgi compartments (PubMed:17855360). Sorting receptor for the BDNF receptor NTRK2/TRKB that facilitates NTRK2 trafficking between synaptic plasma membranes, postsynaptic densities and cell soma, hence positively regulates BDNF signaling by controlling the intracellular location of its receptor (PubMed:23977241). Sorting receptor for GDNF that promotes GDNF regulated, but not constitutive secretion (PubMed:21994944). Sorting receptor for the GDNF-GFRA1 complex, directing it from the cell surface to endosomes. GDNF is then targeted to lysosomes and degraded, while its receptor GFRA1 recycles back to the cell membrane, resulting in a GDNF clearance pathway. The SORL1-GFRA1 complex further targets RET for endocytosis, but not for degradation, affecting GDNF-induced neurotrophic activities (PubMed:23333276). Sorting receptor for ERBB2/HER2. Regulates ERBB2 subcellular distribution by promoting its recycling after internalization from endosomes back to the plasma membrane, hence stimulating phosphoinositide 3-kinase (PI3K)-dependent ERBB2 signaling. In ERBB2-dependent cancer cells, promotes cell proliferation (PubMed:31138794). Sorting receptor for lipoprotein lipase LPL. Promotes LPL localization to endosomes and later to the lysosomes, leading to degradation of newly synthesized LPL (PubMed:21385844). Potential sorting receptor for APOA5, inducing APOA5 internalization to early endosomes, then to late endosomes, wherefrom a portion is sent to lysosomes and degradation, another portion is sorted to the trans-Golgi network (PubMed:18603531). Sorting receptor for the insulin receptor INSR. Promotes recycling of internalized INSR via the Golgi apparatus back to the cell surface, thereby preventing lysosomal INSR catabolism, increasing INSR cell surface expression and strengthening insulin signal reception in adipose tissue. Does not affect INSR internalization (PubMed:27322061). Plays a role in renal ion homeostasis, controlling the phospho-regulation of SLC12A1/NKCC2 by STK39/SPAK kinase and PPP3CB/calcineurin A beta phosphatase, possibly through intracellular sorting of STK39 and PPP3CB (By similarity). Stimulates, via the N-terminal ectodomain, the proliferation and migration of smooth muscle cells, possibly by increasing cell surface expression of the urokinase receptor uPAR/PLAUR. This may promote extracellular matrix proteolysis and hence facilitate cell migration (PubMed:14764453). By acting on the migration of intimal smooth muscle cells, may accelerate intimal thickening following vascular injury (PubMed:14764453). Promotes adhesion of monocytes (PubMed:23486467). Stimulates proliferation and migration of monocytes/macrophages (By similarity). Through its action on intimal smooth muscle cells and macrophages, may accelerate intimal thickening and macrophage foam cell formation in the process of atherosclerosis (By similarity). Regulates hypoxia-enhanced adhesion of hematopoietic stem and progenitor cells to the bone marrow stromal cells via a PLAUR-mediated pathway. This function is mediated by the N-terminal ectodomain (PubMed:23486467). Metabolic regulator, which functions to maintain the adequate balance between lipid storage and oxidation in response to changing environmental conditions, such as temperature and diet. The N-terminal ectodomain negatively regulates adipose tissue energy expenditure, acting through the inhibition the BMP/Smad pathway (By similarity). May regulate signaling by the heterodimeric neurotrophic cytokine CLCF1-CRLF1 bound to the CNTFR receptor by promoting the endocytosis of the tripartite complex CLCF1-CRLF1-CNTFR and lysosomal degradation (PubMed:26858303). May regulate IL6 signaling, decreasing cis signaling, possibly by interfering with IL6-binding to membrane-bound IL6R, while up-regulating trans signaling via soluble IL6R (PubMed:28265003)", "gene_name": "SORL1", "glycan_count": 99, "glycosylation_sites": [ { "position": 99, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 158, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 368, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 430, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 616, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 674, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 818, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 871, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1035, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1068, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1164, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1191, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1246, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1367, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1458, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1608, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1706, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1733, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1809, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1854, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1894, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1986, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2010, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2054, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2069, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2076, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2092, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q92673", "name": "NCAM2", "organism": "Homo sapiens", "uniprot_id": "Q92673" }, { "function": "Dual specificity kinase. Is activated by cytokines and environmental stress in vivo. Catalyzes the concomitant phosphorylation of a threonine and a tyrosine residue in the MAP kinase p38. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14", "gene_name": "MAP2K3", "glycan_count": 1, "glycosylation_sites": [], "id": "P46734", "name": "MAP2K3", "organism": "Homo sapiens", "uniprot_id": "P46734" }, { "function": "Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors (PubMed:34234773). Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin (CTTN) (Probable). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN) (PubMed:21411625). In addition to phosphorylating focal adhesion proteins, SRC is also active at the sites of cell-cell contact adherens junctions and phosphorylates substrates such as beta-catenin (CTNNB1), delta-catenin (CTNND1), and plakoglobin (JUP). Another type of cell-cell junction, the gap junction, is also a target for SRC, which phosphorylates connexin-43 (GJA1). SRC is implicated in regulation of pre-mRNA-processing and phosphorylates RNA-binding proteins such as KHDRBS1 (Probable). Phosphorylates PKP3 at 'Tyr-195' in response to reactive oxygen species, which may cause the release of PKP3 from desmosome cell junctions into the cytoplasm (PubMed:25501895). Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors (By similarity). Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1 (PubMed:11389730). Plays a role in EGF-mediated calcium-activated chloride channel activation (PubMed:18586953). Required for epidermal growth factor receptor (EGFR) internalization through phosphorylation of clathrin heavy chain (CLTC and CLTCL1) at 'Tyr-1477'. Involved in beta-arrestin (ARRB1 and ARRB2) desensitization through phosphorylation and activation of GRK2, leading to beta-arrestin phosphorylation and internalization. Has a critical role in the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal growth factor (Probable). Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus (PubMed:7853507). Plays an important role in osteoclastic bone resorption in conjunction with PTK2B/PYK2. Both the formation of a SRC-PTK2B/PYK2 complex and SRC kinase activity are necessary for this function. Recruited to activated integrins by PTK2B/PYK2, thereby phosphorylating CBL, which in turn induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function (PubMed:14585963, PubMed:8755529). Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase (PubMed:12615910). Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation (PubMed:16186108). Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-731' (PubMed:20100835, PubMed:21309750). Enhances RIGI-elicited antiviral signaling (PubMed:19419966). Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376' (PubMed:14585963). Phosphorylates BCAR1 at 'Tyr-128' (PubMed:22710723). Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity (PubMed:20525694). Phosphorylates synaptic vesicle protein synaptophysin (SYP) (By similarity). Involved in anchorage-independent cell growth (PubMed:19307596). Required for podosome formation (By similarity). Mediates IL6 signaling by activating YAP1-NOTCH pathway to induce inflammation-induced epithelial regeneration (PubMed:25731159). Phosphorylates OTUB1, promoting deubiquitination of RPTOR (PubMed:35927303). Phosphorylates caspase CASP8 at 'Tyr-380' which negatively regulates CASP8 processing and activation, down-regulating CASP8 proapoptotic function (PubMed:16619028)", "gene_name": "SRC", "glycan_count": 9, "glycosylation_sites": [], "id": "P12931", "name": "SRC", "organism": "Homo sapiens", "uniprot_id": "P12931" }, { "function": "Transcription factor that recognizes and binds to the AP-1 consensus motif 5'-TGA[GC]TCA-3' (PubMed:10995748, PubMed:22083952). Heterodimerizes with proteins of the FOS family to form an AP-1 transcription complex, thereby enhancing its DNA binding activity to the AP-1 consensus sequence 5'-TGA[GC]TCA-3' and enhancing its transcriptional activity (By similarity). Together with FOSB, plays a role in activation-induced cell death of T cells by binding to the AP-1 promoter site of FASLG/CD95L, and inducing its transcription in response to activation of the TCR/CD3 signaling pathway (PubMed:12618758). Promotes activity of NR5A1 when phosphorylated by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation (PubMed:17210646). Involved in activated KRAS-mediated transcriptional activation of USP28 in colorectal cancer (CRC) cells (PubMed:24623306). Binds to the USP28 promoter in colorectal cancer (CRC) cells (PubMed:24623306)", "gene_name": "JUN", "glycan_count": 2, "glycosylation_sites": [], "id": "P05412", "name": "JUN", "organism": "Homo sapiens", "uniprot_id": "P05412" }, { "function": "Essential for normal retinal maturation and development (By similarity). Acts as a retinal cell surface receptor for NXNL1 and plays an important role in NXNL1-mediated survival of retinal cone photoreceptors (PubMed:25957687). In association with glucose transporter SLC16A1/GLUT1 and NXNL1, promotes retinal cone survival by enhancing aerobic glycolysis and accelerating the entry of glucose into photoreceptors (PubMed:25957687). May act as a potent stimulator of IL6 secretion in multiple cell lines that include monocytes (PubMed:21620857)", "gene_name": "BSG", "glycan_count": 62, "glycosylation_sites": [ { "position": 160, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 268, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 302, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P35613", "name": "CD147", "organism": "Homo sapiens", "uniprot_id": "P35613" }, { "function": "IFN-induced antiviral host restriction factor which efficiently blocks the release of diverse mammalian enveloped viruses by directly tethering nascent virions to the membranes of infected cells. Acts as a direct physical tether, holding virions to the cell membrane and linking virions to each other. The tethered virions can be internalized by endocytosis and subsequently degraded or they can remain on the cell surface. In either case, their spread as cell-free virions is restricted (PubMed:18200009, PubMed:18342597, PubMed:19036818, PubMed:19879838, PubMed:20019814, PubMed:20399176, PubMed:20419159, PubMed:20940320, PubMed:21529378, PubMed:22520941, PubMed:37922253). Its target viruses belong to diverse families, including retroviridae: human immunodeficiency virus type 1 (HIV-1), human immunodeficiency virus type 2 (HIV-2), simian immunodeficiency viruses (SIVs), equine infectious anemia virus (EIAV), feline immunodeficiency virus (FIV), prototype foamy virus (PFV), Mason-Pfizer monkey virus (MPMV), human T-cell leukemia virus type 1 (HTLV-1), Rous sarcoma virus (RSV) and murine leukemia virus (MLV), flavivirideae: hepatitis C virus (HCV), filoviridae: ebola virus (EBOV) and marburg virus (MARV), arenaviridae: lassa virus (LASV) and machupo virus (MACV), herpesviridae: kaposis sarcoma-associated herpesvirus (KSHV), rhabdoviridae: vesicular stomatitis virus (VSV), orthomyxoviridae: influenza A virus, paramyxoviridae: nipah virus, and coronaviridae: SARS-CoV (PubMed:18200009, PubMed:18342597, PubMed:19179289, PubMed:19879838, PubMed:20399176, PubMed:20419159, PubMed:20686043, PubMed:20943977, PubMed:21529378, PubMed:21621240, PubMed:22520941, PubMed:26378163, PubMed:31199522). Can inhibit cell surface proteolytic activity of MMP14 causing decreased activation of MMP15 which results in inhibition of cell growth and migration (PubMed:22065321). Can stimulate signaling by LILRA4/ILT7 and consequently provide negative feedback to the production of IFN by plasmacytoid dendritic cells in response to viral infection (PubMed:19564354, PubMed:26172439). Plays a role in the organization of the subapical actin cytoskeleton in polarized epithelial cells. Isoform 1 and isoform 2 are both effective viral restriction factors but have differing antiviral and signaling activities (PubMed:23028328, PubMed:26172439). Isoform 2 is resistant to HIV-1 Vpu-mediated degradation and restricts HIV-1 viral budding in the presence of Vpu (PubMed:23028328, PubMed:26172439). Isoform 1 acts as an activator of NF-kappa-B and this activity is inhibited by isoform 2 (PubMed:23028328)", "gene_name": "BST2", "glycan_count": 25, "glycosylation_sites": [ { "position": 65, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 92, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q10589", "name": "CD317 (BST-2, tetherin, HM1.24)", "organism": "Homo sapiens", "uniprot_id": "Q10589" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "not mentioned", "name": "HHV-6 glycoprotein O (gO)", "organism": "", "uniprot_id": "" }, { "function": "ATP-dependent chaperone involved in the processing of proteins in the endoplasmic reticulum, regulating their transport (PubMed:23572575, PubMed:39509507). Together with MESD, acts as a modulator of the Wnt pathway by promoting the folding of LRP6, a coreceptor of the canonical Wnt pathway (PubMed:23572575, PubMed:39509507). When associated with CNPY3, required for proper folding of Toll-like receptors (PubMed:11584270). Promotes folding and trafficking of TLR4 to the cell surface (PubMed:11584270). May participate in the unfolding of cytosolic leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1 to facilitate their translocation into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) and secretion; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059)", "gene_name": "HSP90B1", "glycan_count": 66, "glycosylation_sites": [ { "position": 62, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 107, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 217, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 445, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 481, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 502, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P14625", "name": "gp96", "organism": "Homo sapiens", "uniprot_id": "P14625" }, { "function": "Capsid protein. Probably binds RNA and plays a role in packaging", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8JPX0", "name": "Lassa virus glycoprotein complex (GPC)", "organism": "Cucumber mosaic virus", "uniprot_id": "Q8JPX0" }, { "function": "May increase cell susceptibility to TNF-induced apoptosis", "gene_name": "PPP1R1C", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8WVI7", "name": "Phosphoglucomutase 3 (PGM3)", "organism": "Homo sapiens", "uniprot_id": "Q8WVI7" }, { "function": "Receptor that plays a role in T-cell activation, proliferation, survival and the maintenance of immune homeostasis (PubMed:1650475, PubMed:7568038). Functions not only as an amplifier of TCR signals but delivers unique signals that control intracellular biochemical events that alter the gene expression program of T-cells (PubMed:24665965). Stimulation upon engagement of its cognate ligands CD80 or CD86 increases proliferation and expression of various cytokines in particular IL2 production in both CD4(+) and CD8(+) T-cell subsets (PubMed:1650475, PubMed:35397202). Mechanistically, ligation induces recruitment of protein kinase C-theta/PRKCQ and GRB2 leading to NF-kappa-B activation via both PI3K/Akt-dependent and -independent pathways (PubMed:21964608, PubMed:24665965, PubMed:7568038). In conjunction with TCR/CD3 ligation and CD40L costimulation, enhances the production of IL4 and IL10 in T-cells (PubMed:8617933)", "gene_name": "CD28", "glycan_count": 4, "glycosylation_sites": [ { "position": 37, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 71, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 92, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 105, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 129, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P10747", "name": "CD28", "organism": "Homo sapiens", "uniprot_id": "P10747" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01857 (IgG1 heavy chain)", "name": "Immunoglobulin G (IgG)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01876 (IgA1 heavy chain)", "name": "Immunoglobulin A (IgA)", "organism": "", "uniprot_id": "" }, { "function": "Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to hepatocyte growth factor/HGF ligand. Regulates many physiological processes including proliferation, scattering, morphogenesis and survival. Ligand binding at the cell surface induces autophosphorylation of MET on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1, SRC, GRB2, STAT3 or the adapter GAB1. Recruitment of these downstream effectors by MET leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. The RAS-ERK activation is associated with the morphogenetic effects while PI3K/AKT coordinates prosurvival effects. During embryonic development, MET signaling plays a role in gastrulation, development and migration of neuronal precursors, angiogenesis and kidney formation. During skeletal muscle development, it is crucial for the migration of muscle progenitor cells and for the proliferation of secondary myoblasts (By similarity). In adults, participates in wound healing as well as organ regeneration and tissue remodeling. Also promotes differentiation and proliferation of hematopoietic cells. May regulate cortical bone osteogenesis (By similarity)", "gene_name": "MET", "glycan_count": 74, "glycosylation_sites": [ { "position": 45, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 106, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 149, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 202, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 399, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 405, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 582, "type": "O-linked (Man) threonine" }, { "position": 607, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 635, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 676, "type": "O-linked (Man) threonine" }, { "position": 761, "type": "O-linked (Man) threonine" }, { "position": 785, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 879, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 930, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08581", "name": "MET", "organism": "Homo sapiens", "uniprot_id": "P08581" }, { "function": "Electrogenic sodium/bicarbonate cotransporter with a Na(+):HCO3(-) stoichiometry varying from 1:2 to 1:3. May regulate bicarbonate influx/efflux at the basolateral membrane of cells and regulate intracellular pH", "gene_name": "SLC4A4", "glycan_count": 1, "glycosylation_sites": [ { "position": 597, "type": "N-linked (GalNAc) asparagine" }, { "position": 617, "type": "N-linked (GalNAc) asparagine" } ], "id": "Q9Y6R1", "name": "Sodium-glucose cotransporter-2 (SGLT2)", "organism": "Homo sapiens", "uniprot_id": "Q9Y6R1" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P08588/P07550", "name": "Beta-adrenergic receptor (ADRB1/ADRB2)", "organism": "", "uniprot_id": "" }, { "function": "Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen", "gene_name": "SERPINH1", "glycan_count": 52, "glycosylation_sites": [ { "position": 120, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 125, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P50454", "name": "SERPINH1", "organism": "Homo sapiens", "uniprot_id": "P50454" }, { "function": "Part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linkling of collagen fibrils (By similarity). Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens (PubMed:10686424, PubMed:15854030, PubMed:8621606). These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links (Probable)", "gene_name": "PLOD1", "glycan_count": 56, "glycosylation_sites": [ { "position": 163, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 197, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 538, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 686, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q02809", "name": "PLOD1", "organism": "Homo sapiens", "uniprot_id": "Q02809" }, { "function": "Involved in angiogenesis; promotes angiogenic sprouting. May have potent implications in lung endothelial cell-leukocyte interactions", "gene_name": "ESM1", "glycan_count": 0, "glycosylation_sites": [ { "position": 156, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" } ], "id": "Q9NQ30", "name": "ESM1", "organism": "Homo sapiens", "uniprot_id": "Q9NQ30" }, { "function": "Receptor tyrosine-protein kinase involved in numerous cellular mechanisms including cell proliferation, neuronal navigation, cell migration, and cell differentiation in response to glia cell line-derived growth family factors (GDNF, NRTN, ARTN, PSPN and GDF15) (PubMed:20064382, PubMed:20616503, PubMed:20702524, PubMed:21357690, PubMed:21454698, PubMed:24560924, PubMed:28846097, PubMed:28846099, PubMed:28953886, PubMed:31118272). In contrast to most receptor tyrosine kinases, RET requires not only its cognate ligands but also coreceptors, for activation (PubMed:21994944, PubMed:23333276, PubMed:28846097, PubMed:28846099, PubMed:28953886). GDNF ligands (GDNF, NRTN, ARTN, PSPN and GDF15) first bind their corresponding GDNFR coreceptors (GFRA1, GFRA2, GFRA3, GFRA4 and GFRAL, respectively), triggering RET autophosphorylation and activation, leading to activation of downstream signaling pathways, including the MAPK- and AKT-signaling pathways (PubMed:21994944, PubMed:23333276, PubMed:24560924, PubMed:25242331, PubMed:28846097, PubMed:28846099, PubMed:28953886). Acts as a dependence receptor via the GDNF-GFRA1 signaling: in the presence of the ligand GDNF in somatotrophs within pituitary, promotes survival and down regulates growth hormone (GH) production, but triggers apoptosis in absence of GDNF (PubMed:20616503, PubMed:21994944). Required for the molecular mechanisms orchestration during intestine organogenesis via the ARTN-GFRA3 signaling: involved in the development of enteric nervous system and renal organogenesis during embryonic life, and promotes the formation of Peyer's patch-like structures, a major component of the gut-associated lymphoid tissue (By similarity). Mediates, through interaction with GDF15-receptor GFRAL, GDF15-induced cell-signaling in the brainstem which triggers an aversive response, characterized by nausea, vomiting, and/or loss of appetite in response to various stresses (PubMed:28846097, PubMed:28846099, PubMed:28953886). Modulates cell adhesion via its cleavage by caspase in sympathetic neurons and mediates cell migration in an integrin (e.g. ITGB1 and ITGB3)-dependent manner (PubMed:20702524, PubMed:21357690). Also active in the absence of ligand, triggering apoptosis through a mechanism that requires receptor intracellular caspase cleavage (PubMed:21357690). Triggers the differentiation of rapidly adapting (RA) mechanoreceptors (PubMed:20064382). Involved in the development of the neural crest (By similarity). Regulates nociceptor survival and size (By similarity). Phosphorylates PTK2/FAK1 (PubMed:21454698)", "gene_name": "RET", "glycan_count": 4, "glycosylation_sites": [ { "position": 98, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 151, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 199, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 336, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 343, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 361, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 367, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 377, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 394, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 448, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 468, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 554, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 688, "type": "O-linked (GlcNAc) serine" } ], "id": "P07949", "name": "RET", "organism": "Homo sapiens", "uniprot_id": "P07949" }, { "function": "Neuronal receptor tyrosine kinase that is essentially and transiently expressed in specific regions of the central and peripheral nervous systems and plays an important role in the genesis and differentiation of the nervous system (PubMed:11121404, PubMed:11387242, PubMed:16317043, PubMed:17274988, PubMed:30061385, PubMed:34646012, PubMed:34819673). Also acts as a key thinness protein involved in the resistance to weight gain: in hypothalamic neurons, controls energy expenditure acting as a negative regulator of white adipose tissue lipolysis and sympathetic tone to fine-tune energy homeostasis (By similarity). Following activation by ALKAL2 ligand at the cell surface, transduces an extracellular signal into an intracellular response (PubMed:30061385, PubMed:33411331, PubMed:34646012, PubMed:34819673). In contrast, ALKAL1 is not a potent physiological ligand for ALK (PubMed:34646012). Ligand-binding to the extracellular domain induces tyrosine kinase activation, leading to activation of the mitogen-activated protein kinase (MAPK) pathway (PubMed:34819673). Phosphorylates almost exclusively at the first tyrosine of the Y-x-x-x-Y-Y motif (PubMed:15226403, PubMed:16878150). Induces tyrosine phosphorylation of CBL, FRS2, IRS1 and SHC1, as well as of the MAP kinases MAPK1/ERK2 and MAPK3/ERK1 (PubMed:15226403, PubMed:16878150). ALK activation may also be regulated by pleiotrophin (PTN) and midkine (MDK) (PubMed:11278720, PubMed:11809760, PubMed:12107166, PubMed:12122009). PTN-binding induces MAPK pathway activation, which is important for the anti-apoptotic signaling of PTN and regulation of cell proliferation (PubMed:11278720, PubMed:11809760, PubMed:12107166). MDK-binding induces phosphorylation of the ALK target insulin receptor substrate (IRS1), activates mitogen-activated protein kinases (MAPKs) and PI3-kinase, resulting also in cell proliferation induction (PubMed:12122009). Drives NF-kappa-B activation, probably through IRS1 and the activation of the AKT serine/threonine kinase (PubMed:15226403, PubMed:16878150). Recruitment of IRS1 to activated ALK and the activation of NF-kappa-B are essential for the autocrine growth and survival signaling of MDK (PubMed:15226403, PubMed:16878150)", "gene_name": "ALK", "glycan_count": 1, "glycosylation_sites": [ { "position": 169, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 244, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 285, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 324, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 411, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 424, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 445, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 563, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 571, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 627, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 709, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 808, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 863, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 864, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 886, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 986, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UM73", "name": "ALK", "organism": "Homo sapiens", "uniprot_id": "Q9UM73" }, { "function": "Catalyzes the transport of the major hydrophobic bile salts, such as taurine and glycine-conjugated cholic acid across the canalicular membrane of hepatocytes in an ATP-dependent manner, therefore participates in hepatic bile acid homeostasis and consequently to lipid homeostasis through regulation of biliary lipid secretion in a bile salts dependent manner (PubMed:15791618, PubMed:16332456, PubMed:18985798, PubMed:19228692, PubMed:20010382, PubMed:20398791, PubMed:22262466, PubMed:24711118, PubMed:29507376, PubMed:32203132). Transports taurine-conjugated bile salts more rapidly than glycine-conjugated bile salts (PubMed:16332456). Also transports non-bile acid compounds, such as pravastatin and fexofenadine in an ATP-dependent manner and may be involved in their biliary excretion (PubMed:15901796, PubMed:18245269)", "gene_name": "ABCB11", "glycan_count": 0, "glycosylation_sites": [ { "position": 109, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 116, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 122, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 125, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O95342", "name": "Bile salt export pump (BSEP)", "organism": "Homo sapiens", "uniprot_id": "O95342" }, { "function": "DEAD-box RNA helicase possibly involved in RNA degradation. Unwinds dsRNA in both 5'- and 3'-directions, has RNA-dependent ATPase activity", "gene_name": "cshA", "glycan_count": 0, "glycosylation_sites": [], "id": "P0A4D8", "name": "CRM197", "organism": "Streptococcus pneumoniae (strain ATCC BAA-255 / R6)", "uniprot_id": "P0A4D8" }, { "function": "Energy-dependent phospholipid efflux translocator that acts as a positive regulator of biliary lipid secretion. Functions as a floppase that translocates specifically phosphatidylcholine (PC) from the inner to the outer leaflet of the canalicular membrane bilayer into the canaliculi of hepatocytes. Translocation of PC makes the biliary phospholipids available for extraction into the canaliculi lumen by bile salt mixed micelles and therefore protects the biliary tree from the detergent activity of bile salts (PubMed:17523162, PubMed:21820390, PubMed:23468132, PubMed:24594635, PubMed:24723470, PubMed:24806754, PubMed:31873305, PubMed:7957936, PubMed:8898203, PubMed:9366571). Plays a role in the recruitment of phosphatidylcholine (PC), phosphatidylethanolamine (PE) and sphingomyelin (SM) molecules to nonraft membranes and to further enrichment of SM and cholesterol in raft membranes in hepatocytes (PubMed:23468132). Required for proper phospholipid bile formation (By similarity). Indirectly involved in cholesterol efflux activity from hepatocytes into the canalicular lumen in the presence of bile salts in an ATP-dependent manner (PubMed:24045840). Promotes biliary phospholipid secretion as canaliculi-containing vesicles from the canalicular plasma membrane (PubMed:28012258, PubMed:9366571). In cooperation with ATP8B1, functions to protect hepatocytes from the deleterious detergent activity of bile salts (PubMed:21820390). Does not confer multidrug resistance (By similarity)", "gene_name": "ABCB4", "glycan_count": 1, "glycosylation_sites": [ { "position": 91, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 97, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P21439", "name": "ABCB4", "organism": "Homo sapiens", "uniprot_id": "P21439" }, { "function": "Actin-binding protein that contains 2 major actin binding sites (PubMed:21685497, PubMed:23184945). Organizes filamentous actin into parallel bundles (PubMed:20393565, PubMed:21685497, PubMed:23184945). Plays a role in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers (PubMed:22155786). Important for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration (PubMed:20393565, PubMed:21685497, PubMed:23184945). Mediates reorganization of the actin cytoskeleton and axon growth cone collapse in response to NGF (PubMed:22155786)", "gene_name": "FSCN1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q16658", "name": "Fascin-1", "organism": "Homo sapiens", "uniprot_id": "Q16658" }, { "function": "Transcriptional regulator. Activates E box-dependent transcription in collaboration with TCF3/E47, but the activity is completely antagonized by the negative regulator of neurogenesis HES1. Plays a role in the differentiation of subsets of neural cells by activating E box-dependent transcription (By similarity)", "gene_name": "ATOH1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q92858", "name": "HMMR/CD168", "organism": "Homo sapiens", "uniprot_id": "Q92858" }, { "function": "Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases", "gene_name": "NCAPG", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9BPX3", "name": "NCAPG", "organism": "Homo sapiens", "uniprot_id": "Q9BPX3" }, { "function": "NADH-cytochrome b5 reductases are involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction", "gene_name": "CYB5R1", "glycan_count": 0, "glycosylation_sites": [], "id": "O95329", "name": "Thrombospondin-4 (THBS4)", "organism": "Homo sapiens", "uniprot_id": "Q9UHQ9" }, { "function": "", "gene_name": "GLT8D2", "glycan_count": 0, "glycosylation_sites": [ { "position": 234, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9H1C3", "name": "Collagen type XIX alpha 1 (COL19A1)", "organism": "Homo sapiens", "uniprot_id": "Q9H1C3" }, { "function": "Plays a role during the calcification of cartilage and the transition of cartilage to bone", "gene_name": "COL27A1", "glycan_count": 2, "glycosylation_sites": [ { "position": 271, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1769, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8IZC6", "name": "Collagen type XXV alpha 1 (COL25A1)", "organism": "Homo sapiens", "uniprot_id": "Q8IZC6" }, { "function": "Major connective tissue mitoattractant secreted by vascular endothelial cells. Promotes proliferation and differentiation of chondrocytes. Is involved in the stimulation of osteoblast differentiation and has a critical role in osteogenesis (PubMed:39414788). Mediates heparin- and divalent cation-dependent cell adhesion in many cell types including fibroblasts, myofibroblasts, endothelial and epithelial cells. Enhances fibroblast growth factor-induced DNA synthesis", "gene_name": "CCN2", "glycan_count": 2, "glycosylation_sites": [ { "position": 28, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 225, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P29279", "name": "Connective tissue growth factor (CTGF)", "organism": "Homo sapiens", "uniprot_id": "P29279" }, { "function": "Multifunctional ATP-dependent RNA helicase. The ATPase activity can be stimulated by various ribo-and deoxynucleic acids indicative for a relaxed substrate specificity. In vitro can unwind partially double-stranded DNA with a preference for 5'-single-stranded DNA overhangs. Binds RNA G-quadruplex (rG4s) structures, including those located in the 5'-UTR of NRAS mRNA. Involved in many cellular processes, which do not necessarily require its ATPase/helicase catalytic activities. Involved in transcription regulation. Positively regulates CDKN1A/WAF1/CIP1 transcription in an SP1-dependent manner, hence inhibits cell growth. This function requires its ATPase, but not helicase activity. CDKN1A up-regulation may be cell-type specific. Binds CDH1/E-cadherin promoter and represses its transcription. Potentiates HNF4A-mediated MTTP transcriptional activation; this function requires ATPase, but not helicase activity. Facilitates HNF4A acetylation, possibly catalyzed by CREBBP/EP300, thereby increasing the DNA-binding affinity of HNF4 to its response element. In addition, disrupts the interaction between HNF4 and SHP that forms inactive heterodimers and enhances the formation of active HNF4 homodimers. By promoting HNF4A-induced MTTP expression, may play a role in lipid homeostasis. May positively regulate TP53 transcription. Associates with mRNPs, predominantly with spliced mRNAs carrying an exon junction complex (EJC). Involved in the regulation of translation initiation. Not involved in the general process of translation, but promotes efficient translation of selected complex mRNAs, containing highly structured 5'-untranslated regions (UTR). This function depends on helicase activity. Might facilitate translation by resolving secondary structures of 5'-UTRs during ribosome scanning. Alternatively, may act prior to 43S ribosomal scanning and promote 43S pre-initiation complex entry to mRNAs exhibiting specific RNA motifs, by performing local remodeling of transcript structures located close to the cap moiety. Independently of its ATPase activity, promotes the assembly of functional 80S ribosomes and disassembles from ribosomes prior to the translation elongation process. Positively regulates the translation of cyclin E1/CCNE1 mRNA and consequently promotes G1/S-phase transition during the cell cycle. May activate TP53 translation. Required for endoplasmic reticulum stress-induced ATF4 mRNA translation. Independently of its ATPase/helicase activity, enhances IRES-mediated translation; this activity requires interaction with EIF4E. Independently of its ATPase/helicase activity, has also been shown specifically repress cap-dependent translation, possibly by acting on translation initiation factor EIF4E. Involved in innate immunity, acting as a viral RNA sensor. Binds viral RNAs and promotes the production of type I interferon (IFN-alpha and IFN-beta). Potentiate MAVS/RIGI-mediated induction of IFNB in early stages of infection (By similarity). Enhances IFNB1 expression via IRF3/IRF7 pathway and participates in NFKB activation in the presence of MAVS and TBK1 (PubMed:30475900). Involved in TBK1 and IKBKE-dependent IRF3 activation leading to IFNB induction, acts as a scaffolding adapter that links IKBKE and IRF3 and coordinates their activation. Involved in the TLR7/TLR8 signaling pathway leading to type I interferon induction, including IFNA4 production. In this context, acts as an upstream regulator of IRF7 activation by MAP3K14/NIK and CHUK/IKKA. Stimulates CHUK autophosphorylation and activation following physiological activation of the TLR7 and TLR8 pathways, leading to MAP3K14/CHUK-mediated activatory phosphorylation of IRF7. Also stimulates MAP3K14/CHUK-dependent NF-kappa-B signaling. Negatively regulates TNF-induced IL6 and IL8 expression, via the NF-kappa-B pathway. May act by interacting with RELA/p65 and trapping it in the cytoplasm. May also bind IFNB promoter; the function is independent of IRF3 (By similarity). Involved in both stress and inflammatory responses (PubMed:31511697). Independently of its ATPase/helicase activity, required for efficient stress granule assembly through its interaction with EIF4E, hence promotes survival in stressed cells (By similarity). Independently of its helicase activity, regulates NLRP3 inflammasome assembly through interaction with NLRP3 and hence promotes cell death by pyroptosis during inflammation. This function is independent of helicase activity. Therefore DDX3X availability may be used to interpret stress signals and choose between pro-survival stress granules and pyroptotic NLRP3 inflammasomes and serve as a live-or-die checkpoint in stressed cells (PubMed:31511697). In association with GSK3A/B, negatively regulates extrinsic apoptotic signaling pathway via death domain receptors, including TNFRSF10B, slowing down the rate of CASP3 activation following death receptor stimulation. Cleavage by caspases may inactivate DDX3X and relieve the inhibition. Independently of its ATPase/helicase activity, allosteric activator of CSNK1E. Stimulates CSNK1E-mediated phosphorylation of DVL2, thereby involved in the positive regulation of Wnt/beta-catenin signaling pathway. Also activates CSNK1A1 and CSNK1D in vitro, but it is uncertain if these targets are physiologically relevant. ATPase and casein kinase-activating functions are mutually exclusive. May be involved in mitotic chromosome segregation (By similarity)", "gene_name": "Ddx3x", "glycan_count": 1, "glycosylation_sites": [], "id": "Q62167", "name": "Dag1 (Dystroglycan 1)", "organism": "Mus musculus", "uniprot_id": "Q62167" }, { "function": "Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity", "gene_name": "Tnnt3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9QZ47", "name": "Sgcb (Sarcoglycan Beta)", "organism": "Mus musculus", "uniprot_id": "Q9QZ47" }, { "function": "Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity", "gene_name": "Tnnt3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9QZ46", "name": "Sgcd (Sarcoglycan Delta)", "organism": "Mus musculus", "uniprot_id": "Q9QZ47" }, { "function": "", "gene_name": "SRY", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9QZ45", "name": "Sgcg (Sarcoglycan Gamma)", "organism": "Microtus agrestis", "uniprot_id": "Q9QZ45" }, { "function": "Type I collagen is a member of group I collagen (fibrillar forming collagen)", "gene_name": "Col1a1", "glycan_count": 3, "glycosylation_sites": [ { "position": 56, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 254, "type": "O-linked (Gal...) hydroxylysine; alternate" }, { "position": 1097, "type": "O-linked (Gal...) hydroxylysine; alternate" }, { "position": 1354, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P11087", "name": "Collagen type I (Col1a1)", "organism": "Mus musculus", "uniprot_id": "P11087" }, { "function": "Collagen type III occurs in most soft connective tissues along with type I collagen. Involved in regulation of cortical development. Is the major ligand of ADGRG1 in the developing brain and binding to ADGRG1 inhibits neuronal migration and activates the RhoA pathway by coupling ADGRG1 to GNA13 and possibly GNA12", "gene_name": "COL3A1", "glycan_count": 22, "glycosylation_sites": [ { "position": 263, "type": "O-linked (Gal...) hydroxylysine; alternate" } ], "id": "P02461", "name": "Collagen type III (Col3a1)", "organism": "Homo sapiens", "uniprot_id": "P02461" }, { "function": "Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes (PubMed:18983167). May be involved in maintaining basal levels of the cyclic nucleotide and/or in the cAMP regulation of germ cell development (PubMed:18983167). Binding to RAF1 reduces RAF1 'Ser-259' inhibitory-phosphorylation and stimulates RAF1-dependent EGF-activated ERK-signaling (PubMed:23509299). Protects against cell death induced by hydrogen peroxide and staurosporine (PubMed:23509299)", "gene_name": "PDE8A", "glycan_count": 0, "glycosylation_sites": [], "id": "O60658", "name": "Phosphodiesterase 3B", "organism": "Homo sapiens", "uniprot_id": "O60658" }, { "function": "Constitutively active, non-selective divalent cation-conducting channel that is permeable to Ca(2+), Mn(2+), and Mg(2+), with a high permeability for Ca(2+). However, can be enhanced by increasing temperature and by ligands, including the endogenous neurosteroid pregnenolone sulfate and sphingosine-1 and suppressed by intracellular Mg(2+) (PubMed:12672799, PubMed:12672827, PubMed:32343227). Implicated in a variety of cellular processes, including insulin/peptide secretion, vascular constriction and dilation, noxious heat sensing, inflammatory and spontaneous pain sensitivity. In neurons of the dorsal root ganglia, functions as thermosensitive channel for the detection of noxious heat and spontaneous pain. Suggested to function as an ionotropic steroid receptor in beta-cell, indeed pregnenolone sulfate leads to Ca(2+) influx and enhanced insulin secretion. Mediates Zn(2+) uptake into the lumen of pancreatic beta cell secretory granules, thereby regulating insulin secretion (By similarity). Forms heteromultimeric ion channels with TRPM1 which are permeable for Ca(2+) and Zn(2+) ions (PubMed:21278253). Exists as multiple splice variants which differ significantly in their biophysical properties (By similarity)", "gene_name": "TRPM3", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9HCF6", "name": "Transient receptor potential cation channel subfamily M member 3 (TRPM3)", "organism": "Homo sapiens", "uniprot_id": "Q9HCF6" }, { "function": "Beta-galactosyltransferase that transfers beta-galactose to hydroxylysine residues of type I collagen (PubMed:19075007, PubMed:22216269, PubMed:27402836). By acting on collagen glycosylation, facilitates the formation of collagen triple helix (PubMed:27402836). Also involved in the biosynthesis of collagen type IV (PubMed:30412317)", "gene_name": "COLGALT1", "glycan_count": 31, "glycosylation_sites": [ { "position": 96, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 184, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 381, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8NBJ5", "name": "FCSK", "organism": "Homo sapiens", "uniprot_id": "Q8NBJ5" }, { "function": "Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins", "gene_name": "FUCA2", "glycan_count": 7, "glycosylation_sites": [ { "position": 171, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 239, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 377, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9BTY2", "name": "FUC1", "organism": "Homo sapiens", "uniprot_id": "Q9BTY2" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "engineered", "name": "Micro-dystrophin", "organism": "", "uniprot_id": "" }, { "function": "May be involved in the formation and stability of synapses as well as being involved in the clustering of nicotinic acetylcholine receptors", "gene_name": "DTNA", "glycan_count": 3, "glycosylation_sites": [], "id": "Q9Y4J8", "name": "Dystrobrevin", "organism": "Homo sapiens", "uniprot_id": "Q9Y4J8" }, { "function": "Serum endocuclease secreted into body fluids by a wide variety of exocrine and endocrine organs (PubMed:11241278, PubMed:2251263, PubMed:2277032). Expressed by non-hematopoietic tissues and preferentially cleaves protein-free DNA (By similarity). Among other functions, seems to be involved in cell death by apoptosis (PubMed:11241278). Binds specifically to G-actin and blocks actin polymerization (By similarity). Together with DNASE1L3, plays a key role in degrading neutrophil extracellular traps (NETs) (By similarity). NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (By similarity). Degradation of intravascular NETs by DNASE1 and DNASE1L3 is required to prevent formation of clots that obstruct blood vessels and cause organ damage following inflammation (By similarity)", "gene_name": "DNASE1", "glycan_count": 3, "glycosylation_sites": [ { "position": 40, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 128, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P24855", "name": "DNase I", "organism": "Homo sapiens", "uniprot_id": "P24855" }, { "function": "Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Isoform 1, isoform 2 and isoform 3 phosphorylate CAMK1 and CAMK4. Isoform 3 phosphorylates CAMK1D. Isoform 4, isoform 5 and isoform 6 lacking part of the calmodulin-binding domain are inactive. Efficiently phosphorylates 5'-AMP-activated protein kinase (AMPK) trimer, including that consisting of PRKAA1, PRKAB1 and PRKAG1. This phosphorylation is stimulated in response to Ca(2+) signals (By similarity). Seems to be involved in hippocampal activation of CREB1 (By similarity). May play a role in neurite growth. Isoform 3 may promote neurite elongation, while isoform 1 may promoter neurite branching", "gene_name": "CAMKK2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96RR4", "name": "Calcium/calmodulin-dependent protein kinase kinase 2 (CAMKK2)", "organism": "Homo sapiens", "uniprot_id": "Q96RR4" }, { "function": "Plays a role in vesicle-mediated secretory processes (PubMed:24843546). Required for normal accumulation of secretory vesicles in hippocampus, pituitary and pancreatic islets (By similarity). Required for the accumulation of normal levels of insulin-containing vesicles and preventing their degradation (PubMed:24843546). Plays a role in insulin secretion in response to glucose stimuli (PubMed:24843546). Required for normal accumulation of the neurotransmitters norepinephrine, dopamine and serotonin in the brain (By similarity). In females, but not in males, required for normal accumulation and secretion of pituitary hormones, such as luteinizing hormone (LH) and follicle-stimulating hormone (FSH) (By similarity). Required to maintain normal levels of renin expression and renin release (By similarity). Seems to lack intrinsic enzyme activity (By similarity). May regulate catalytic active protein-tyrosine phosphatases such as PTPRA through dimerization (By similarity)", "gene_name": "PTPRN", "glycan_count": 11, "glycosylation_sites": [ { "position": 441, "type": "O-linked (GalNAc...) threonine" }, { "position": 506, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 524, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q16849", "name": "DEP-1 (Density-enhanced phosphatase-1)", "organism": "Homo sapiens", "uniprot_id": "Q16849" }, { "function": "Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells (PubMed:25255767, PubMed:29581253). Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction (PubMed:29581253). In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA (PubMed:29925947). Plays a role in the assembly of the gamma-tubulin ring complex (gTuRC), which regulates the minus-end nucleation of alpha-beta tubulin heterodimers that grow into microtubule protafilaments (PubMed:39321809, PubMed:38609661). Part of the ACTR1A/ACTB filament around which the dynactin complex is built (By similarity). The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity)", "gene_name": "ACTB", "glycan_count": 3, "glycosylation_sites": [], "id": "P60709", "name": "Beta Actin", "organism": "Homo sapiens", "uniprot_id": "P60709" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "H2AM12 (M polyprotein)", "name": "Gc glycoprotein (Schmallenberg virus)", "organism": "", "uniprot_id": "" }, { "function": "Can mediate aggregation most likely through a homophilic molecular interaction", "gene_name": "ESAM", "glycan_count": 28, "glycosylation_sites": [ { "position": 108, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 169, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 213, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 236, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q96AP7", "name": "APJ receptor", "organism": "Homo sapiens", "uniprot_id": "Q96AP7" }, { "function": "Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFC and VEGFD, and plays an essential role in adult lymphangiogenesis and in the development of the vascular network and the cardiovascular system during embryonic development. Promotes proliferation, survival and migration of endothelial cells, and regulates angiogenic sprouting. Signaling by activated FLT4 leads to enhanced production of VEGFC, and to a lesser degree VEGFA, thereby creating a positive feedback loop that enhances FLT4 signaling. Modulates KDR signaling by forming heterodimers. The secreted isoform 3 may function as a decoy receptor for VEGFC and/or VEGFD and play an important role as a negative regulator of VEGFC-mediated lymphangiogenesis and angiogenesis. Binding of vascular growth factors to isoform 1 or isoform 2 leads to the activation of several signaling cascades; isoform 2 seems to be less efficient in signal transduction, because it has a truncated C-terminus and therefore lacks several phosphorylation sites. Mediates activation of the MAPK1/ERK2, MAPK3/ERK1 signaling pathway, of MAPK8 and the JUN signaling pathway, and of the AKT1 signaling pathway. Phosphorylates SHC1. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase. Promotes phosphorylation of MAPK8 at 'Thr-183' and 'Tyr-185', and of AKT1 at 'Ser-473'", "gene_name": "FLT4", "glycan_count": 5, "glycosylation_sites": [ { "position": 33, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 166, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 251, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 299, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 411, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 515, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 527, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 594, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 683, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 690, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 758, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P35916", "name": "VEGFR3", "organism": "Homo sapiens", "uniprot_id": "P35916" }, { "function": "Auxiliary protein of DNA polymerase delta and epsilon, is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand (PubMed:35585232). Induces a robust stimulatory effect on the 3'-5' exonuclease and 3'-phosphodiesterase, but not apurinic-apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2. Plays a key role in DNA damage response (DDR) by being conveniently positioned at the replication fork to coordinate DNA replication with DNA repair and DNA damage tolerance pathways (PubMed:24939902). Acts as a loading platform to recruit DDR proteins that allow completion of DNA replication after DNA damage and promote postreplication repair: Monoubiquitinated PCNA leads to recruitment of translesion (TLS) polymerases, while 'Lys-63'-linked polyubiquitination of PCNA is involved in error-free pathway and employs recombination mechanisms to synthesize across the lesion (PubMed:24695737)", "gene_name": "PCNA", "glycan_count": 2, "glycosylation_sites": [], "id": "P12004", "name": "PCNA", "organism": "Homo sapiens", "uniprot_id": "P12004" }, { "function": "Envelope glycoprotein that forms spikes at the surface of virion envelope and binds to the host cell entry receptors MYH9/NMMHC-IIA and MYH10/NMMHC-IIB, promoting the virus entry into host cells. Essential for the initial attachment to heparan sulfate moieties of the host cell surface proteoglycans. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell: following initial binding to its host cell entry receptors, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May be involved in the fusion between the virion envelope and the outer nuclear membrane during virion egress. Also plays a role, together with gK, in virus-induced cell-to-cell fusion (syncytia formation)", "gene_name": "gB", "glycan_count": 0, "glycosylation_sites": [ { "position": 87, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 141, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 398, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 430, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 489, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 674, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P06437", "name": "HSV-1 gB glycoprotein", "organism": "Human herpesvirus 1 (strain KOS)", "uniprot_id": "P06437" }, { "function": "Dopamine receptor whose activity is mediated by G proteins which activate adenylyl cyclase", "gene_name": "D1dr", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9QZQ9", "name": "PRV gB glycoprotein", "organism": "Mus musculus", "uniprot_id": "Q9QZQ9" }, { "function": "Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein", "gene_name": "rep", "glycan_count": 0, "glycosylation_sites": [], "id": "P0C6X7", "name": "HBV polymerase", "organism": "Severe acute respiratory syndrome coronavirus", "uniprot_id": "P0C6X7" }, { "function": "Component of the mechanistic target of rapamycin complex 1 (mTORC1), an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth (PubMed:12150925, PubMed:12150926, PubMed:12747827, PubMed:24403073, PubMed:26588989, PubMed:32561715, PubMed:37541260). In response to nutrients, growth factors or amino acids, mTORC1 is recruited to the lysosome membrane and promotes protein, lipid and nucleotide synthesis by phosphorylating several substrates, such as ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1) (PubMed:12150925, PubMed:12150926, PubMed:12747827, PubMed:24403073, PubMed:26588989, PubMed:37541260). In the same time, it inhibits catabolic pathways by phosphorylating the autophagy initiation components ULK1 and ATG13, as well as transcription factor TFEB, a master regulators of lysosomal biogenesis and autophagy (PubMed:12150925, PubMed:12150926, PubMed:12747827, PubMed:24403073, PubMed:32561715, PubMed:37541260). The mTORC1 complex is inhibited in response to starvation and amino acid depletion (PubMed:12150925, PubMed:12150926, PubMed:12747827, PubMed:24403073, PubMed:37541260). Within the mTORC1 complex, RPTOR acts both as a molecular adapter, which (1) mediates recruitment of mTORC1 to lysosomal membranes via interaction with small GTPases Rag (RagA/RRAGA, RagB/RRAGB, RagC/RRAGC and/or RagD/RRAGD), and a (2) substrate-specific adapter, which promotes substrate specificity by binding to TOS motif-containing proteins and direct them towards the active site of the MTOR kinase domain for phosphorylation (PubMed:12747827, PubMed:24403073, PubMed:26588989, PubMed:37541260). mTORC1 complex regulates many cellular processes, such as odontoblast and osteoclast differentiation or neuronal transmission (By similarity). mTORC1 complex in excitatory neuronal transmission is required for the prosocial behavior induced by the psychoactive substance lysergic acid diethylamide (LSD) (By similarity)", "gene_name": "RPTOR", "glycan_count": 2, "glycosylation_sites": [ { "position": 700, "type": "O-linked (GlcNAc) threonine" } ], "id": "Q8N122", "name": "Raptor", "organism": "Homo sapiens", "uniprot_id": "Q8N122" }, { "function": "Catalytic component of the TSC-TBC complex, a multiprotein complex that acts as a negative regulator of the canonical mTORC1 complex, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth (PubMed:12172553, PubMed:12271141, PubMed:12842888, PubMed:12906785, PubMed:15340059, PubMed:22819219, PubMed:24529379, PubMed:28215400, PubMed:33436626, PubMed:35772404). Within the TSC-TBC complex, TSC2 acts as a GTPase-activating protein (GAP) for the small GTPase RHEB, a direct activator of the protein kinase activity of mTORC1 (PubMed:12172553, PubMed:12820960, PubMed:12842888, PubMed:12906785, PubMed:15340059, PubMed:22819219, PubMed:24529379, PubMed:33436626). In absence of nutrients, the TSC-TBC complex inhibits mTORC1, thereby preventing phosphorylation of ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1) by the mTORC1 signaling (PubMed:12172553, PubMed:12271141, PubMed:12842888, PubMed:12906785, PubMed:22819219, PubMed:24529379, PubMed:28215400, PubMed:35772404). The TSC-TBC complex is inactivated in response to nutrients, relieving inhibition of mTORC1 (PubMed:12172553, PubMed:24529379). Involved in microtubule-mediated protein transport via its ability to regulate mTORC1 signaling (By similarity). Also stimulates the intrinsic GTPase activity of the Ras-related proteins RAP1A and RAB5 (By similarity)", "gene_name": "TSC2", "glycan_count": 2, "glycosylation_sites": [], "id": "P49815", "name": "TSC2", "organism": "Homo sapiens", "uniprot_id": "P49815" }, { "function": "Serine/threonine-protein kinase that acts downstream of mTOR signaling in response to growth factors and nutrients to promote cell proliferation, cell growth and cell cycle progression (PubMed:11500364, PubMed:12801526, PubMed:14673156, PubMed:15071500, PubMed:15341740, PubMed:16286006, PubMed:17052453, PubMed:17053147, PubMed:17936702, PubMed:18952604, PubMed:19085255, PubMed:19720745, PubMed:19935711, PubMed:19995915, PubMed:22017876, PubMed:23429703, PubMed:28178239). Regulates protein synthesis through phosphorylation of EIF4B, RPS6 and EEF2K, and contributes to cell survival by repressing the pro-apoptotic function of BAD (PubMed:11500364, PubMed:12801526, PubMed:14673156, PubMed:15071500, PubMed:15341740, PubMed:16286006, PubMed:17052453, PubMed:17053147, PubMed:17936702, PubMed:18952604, PubMed:19085255, PubMed:19720745, PubMed:19935711, PubMed:19995915, PubMed:22017876, PubMed:23429703, PubMed:28178239). Under conditions of nutrient depletion, the inactive form associates with the EIF3 translation initiation complex (PubMed:16286006). Upon mitogenic stimulation, phosphorylation by the mechanistic target of rapamycin complex 1 (mTORC1) leads to dissociation from the EIF3 complex and activation (PubMed:16286006). The active form then phosphorylates and activates several substrates in the pre-initiation complex, including the EIF2B complex and the cap-binding complex component EIF4B (PubMed:16286006). Also controls translation initiation by phosphorylating a negative regulator of EIF4A, PDCD4, targeting it for ubiquitination and subsequent proteolysis (PubMed:17053147). Promotes initiation of the pioneer round of protein synthesis by phosphorylating POLDIP3/SKAR (PubMed:15341740). In response to IGF1, activates translation elongation by phosphorylating EEF2 kinase (EEF2K), which leads to its inhibition and thus activation of EEF2 (PubMed:11500364). Also plays a role in feedback regulation of mTORC2 by mTORC1 by phosphorylating MAPKAP1/SIN1, MTOR and RICTOR, resulting in the inhibition of mTORC2 and AKT1 signaling (PubMed:15899889, PubMed:19720745, PubMed:19935711, PubMed:19995915). Also involved in feedback regulation of mTORC1 and mTORC2 by phosphorylating DEPTOR (PubMed:22017876). Mediates cell survival by phosphorylating the pro-apoptotic protein BAD and suppressing its pro-apoptotic function (By similarity). Phosphorylates mitochondrial URI1 leading to dissociation of a URI1-PPP1CC complex (PubMed:17936702). The free mitochondrial PPP1CC can then dephosphorylate RPS6KB1 at Thr-412, which is proposed to be a negative feedback mechanism for the RPS6KB1 anti-apoptotic function (PubMed:17936702). Mediates TNF-alpha-induced insulin resistance by phosphorylating IRS1 at multiple serine residues, resulting in accelerated degradation of IRS1 (PubMed:18952604). In cells lacking functional TSC1-2 complex, constitutively phosphorylates and inhibits GSK3B (PubMed:17052453). May be involved in cytoskeletal rearrangement through binding to neurabin (By similarity). Phosphorylates and activates the pyrimidine biosynthesis enzyme CAD, downstream of MTOR (PubMed:23429703). Following activation by mTORC1, phosphorylates EPRS and thereby plays a key role in fatty acid uptake by adipocytes and also most probably in interferon-gamma-induced translation inhibition (PubMed:28178239)", "gene_name": "RPS6KB1", "glycan_count": 1, "glycosylation_sites": [], "id": "P23443", "name": "S6K1", "organism": "Homo sapiens", "uniprot_id": "P23443" }, { "function": "Repressor of translation initiation that regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation. Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways", "gene_name": "EIF4EBP1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q13541", "name": "4EBP1", "organism": "Homo sapiens", "uniprot_id": "Q13541" }, { "function": "Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:17434132, PubMed:22748924, PubMed:26976582, PubMed:28727686, PubMed:34741373, PubMed:35395208). Recognizes and binds phosphorylated sites/phosphodegrons within target proteins and thereafter brings them to the SCF complex for ubiquitination (PubMed:17434132, PubMed:22748924, PubMed:26774286, PubMed:26976582, PubMed:28727686, PubMed:34741373). Identified substrates include cyclin-E (CCNE1 or CCNE2), DISC1, JUN, MYC, NOTCH1 released notch intracellular domain (NICD), NFE2L1, NOTCH2, MCL1, MLST8, RICTOR, and probably PSEN1 (PubMed:11565034, PubMed:11585921, PubMed:12354302, PubMed:14739463, PubMed:15103331, PubMed:17558397, PubMed:17873522, PubMed:22608923, PubMed:22748924, PubMed:25775507, PubMed:25897075, PubMed:26976582, PubMed:28007894, PubMed:28727686, PubMed:29149593, PubMed:34102342). Acts as a negative regulator of JNK signaling by binding to phosphorylated JUN and promoting its ubiquitination and subsequent degradation (PubMed:14739463). Involved in bone homeostasis and negative regulation of osteoclast differentiation (PubMed:29149593). Regulates the amplitude of the cyclic expression of hepatic core clock genes and genes involved in lipid and glucose metabolism via ubiquitination and proteasomal degradation of their transcriptional repressor NR1D1; CDK1-dependent phosphorylation of NR1D1 is necessary for SCF(FBXW7)-mediated ubiquitination (PubMed:27238018). Also able to promote 'Lys-63'-linked ubiquitination in response to DNA damage (PubMed:26774286). The SCF(FBXW7) complex facilitates double-strand break repair following phosphorylation by ATM: phosphorylation promotes localization to sites of double-strand breaks and 'Lys-63'-linked ubiquitination of phosphorylated XRCC4, enhancing DNA non-homologous end joining (PubMed:26774286)", "gene_name": "FBXW7", "glycan_count": 1, "glycosylation_sites": [], "id": "Q969H0", "name": "FBXW7", "organism": "Homo sapiens", "uniprot_id": "Q969H0" }, { "function": "Deubiquitinase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins (PubMed:18254724, PubMed:19135894, PubMed:22371489, PubMed:25944111, PubMed:29626158, PubMed:30914461, PubMed:37454738). May therefore play an important regulatory role at the level of protein turnover by preventing degradation of proteins through the removal of conjugated ubiquitin (PubMed:18254724, PubMed:19135894, PubMed:22371489, PubMed:25944111, PubMed:29626158, PubMed:30914461, PubMed:37454738). Specifically hydrolyzes 'Lys-11'-, followed by 'Lys-63'-, 'Lys-48'- and 'Lys-6'-linked polyubiquitins chains (PubMed:30914461). Essential component of TGF-beta/BMP signaling cascade (PubMed:19135894). Specifically deubiquitinates monoubiquitinated SMAD4, opposing the activity of E3 ubiquitin-protein ligase TRIM33 (PubMed:19135894). Deubiquitinates alkylation repair enzyme ALKBH3 (PubMed:25944111). OTUD4 recruits USP7 and USP9X to stabilize ALKBH3, thereby promoting the repair of alkylated DNA lesions (PubMed:25944111). Deubiquitinates RNA demethylase enzyme ALKBH5, promoting its stability (PubMed:37454738). Deubiquitinates mTORC2 complex component RICTOR at 'Lys-294' by removing 'Lys-63'-linked polyubiquitin chains, stabilizing RICTOR and enhancing its binding to MTOR, thus promoting mTORC2 complex assembly (PubMed:33378666). Regulates chromosome alignment and segregation in mitosis by regulating the localization of BIRC5/survivin to mitotic centromeres (PubMed:16322459). Involved in axonal growth and neuronal cell migration (PubMed:24607389). Regulates cellular clock function by enhancing the protein stability and transcriptional activity of the core circadian protein BMAL1 via its deubiquitinating activity (PubMed:29626158). Acts as a regulator of peroxisome import by mediating deubiquitination of PEX5: specifically deubiquitinates PEX5 monoubiquitinated at 'Cys-11' following its retrotranslocation into the cytosol, resetting PEX5 for a subsequent import cycle (PubMed:22371489). Deubiquitinates PEG10 (By similarity). Inhibits the activation of the Hippo signaling pathway via deubiquitination of AMOTL2 at 'Lys-347' and 'Lys-408' which prohibits its interaction with and activation of LATS2. Loss of LATS2 activation and subsequent loss of YAP1 phosphorylation results in an increase in YAP1-driven transcription of target genes (PubMed:26598551, PubMed:34404733)", "gene_name": "USP9X", "glycan_count": 1, "glycosylation_sites": [], "id": "Q93008", "name": "USP9X", "organism": "Homo sapiens", "uniprot_id": "Q93008" }, { "function": "Epidermis-specific type I keratin that plays a key role in skin. Acts as a regulator of innate immunity in response to skin barrier breach: required for some inflammatory checkpoint for the skin barrier maintenance", "gene_name": "KRT16", "glycan_count": 1, "glycosylation_sites": [], "id": "P08779", "name": "KRT16", "organism": "Homo sapiens", "uniprot_id": "P08779" }, { "function": "Required for the formation of keratin intermediate filaments in the basal epidermis and maintenance of the skin barrier in response to mechanical stress (By similarity). Regulates the recruitment of Langerhans cells to the epidermis, potentially by modulation of the abundance of macrophage chemotactic cytokines, macrophage inflammatory cytokines and CTNND1 localization in keratinocytes (By similarity)", "gene_name": "KRT5", "glycan_count": 1, "glycosylation_sites": [], "id": "P13647", "name": "KRT5", "organism": "Homo sapiens", "uniprot_id": "P13647" }, { "function": "Probably contributes to terminal cornification (PubMed:1380918). Associated with keratinocyte activation, proliferation and keratinization (PubMed:12598329). Required for maintenance of corneocytes and keratin filaments in suprabasal keratinocytes in the epidermis of the ear, potentially via moderation of expression and localization of keratins and their partner proteins (By similarity). Plays a role in the establishment of the epidermal barrier on plantar skin (By similarity)", "gene_name": "KRT2", "glycan_count": 1, "glycosylation_sites": [], "id": "P35908", "name": "KRT2", "organism": "Homo sapiens", "uniprot_id": "P35908" }, { "function": "May serve an important special function either in the mature palmar and plantar skin tissue or in the morphogenetic program of the formation of these tissues. Plays a role in keratin filament assembly", "gene_name": "KRT9", "glycan_count": 13, "glycosylation_sites": [], "id": "P35527", "name": "KRT9", "organism": "Homo sapiens", "uniprot_id": "P35527" }, { "function": "Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping", "gene_name": "MYH14", "glycan_count": 2, "glycosylation_sites": [], "id": "Q7Z406", "name": "MYH14", "organism": "Homo sapiens", "uniprot_id": "Q7Z406" }, { "function": "Transcription factor involved in the regulation of podocyte-expressed genes (PubMed:24042019, PubMed:28059119). Essential for the specification of dorsal limb fate at both the zeugopodal and autopodal levels", "gene_name": "LMX1B", "glycan_count": 0, "glycosylation_sites": [], "id": "O60663", "name": "LMX1B", "organism": "Homo sapiens", "uniprot_id": "O60663" }, { "function": "Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments. Inhibits beta-catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta-catenin through a CRM1-dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. Required for proper localization of non-farnesylated prelamin-A/C. Together with NEMP1, contributes to nuclear envelope stiffness in germ cells (PubMed:32923640). EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD", "gene_name": "EMD", "glycan_count": 3, "glycosylation_sites": [], "id": "P50402", "name": "Emerin", "organism": "Homo sapiens", "uniprot_id": "P50402" }, { "function": "Serine/threonine-protein kinase which phosphorylates a broad range of proteins involved in multiple processes such as neuronal plasticity, innate immunity, autophagy, and vesicle trafficking (PubMed:17114044, PubMed:20949042, PubMed:21850687, PubMed:22012985, PubMed:23395371, PubMed:24687852, PubMed:25201882, PubMed:26014385, PubMed:26824392, PubMed:27830463, PubMed:28720718, PubMed:29125462, PubMed:29127255, PubMed:29212815, PubMed:30398148, PubMed:30635421). Is a key regulator of RAB GTPases by regulating the GTP/GDP exchange and interaction partners of RABs through phosphorylation (PubMed:26824392, PubMed:28720718, PubMed:29125462, PubMed:29127255, PubMed:29212815, PubMed:30398148, PubMed:30635421). Phosphorylates RAB3A, RAB3B, RAB3C, RAB3D, RAB5A, RAB5B, RAB5C, RAB8A, RAB8B, RAB10, RAB12, RAB29, RAB35, and RAB43 (PubMed:23395371, PubMed:26824392, PubMed:28720718, PubMed:29125462, PubMed:29127255, PubMed:29212815, PubMed:30398148, PubMed:30635421, PubMed:38127736). Regulates the RAB3IP-catalyzed GDP/GTP exchange for RAB8A through the phosphorylation of 'Thr-72' on RAB8A (PubMed:26824392). Inhibits the interaction between RAB8A and GDI1 and/or GDI2 by phosphorylating 'Thr-72' on RAB8A (PubMed:26824392). Regulates primary ciliogenesis through phosphorylation of RAB8A and RAB10, which promotes SHH signaling in the brain (PubMed:29125462, PubMed:30398148). Together with RAB29, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose-6-phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner (PubMed:23395371). Regulates neuronal process morphology in the intact central nervous system (CNS) (PubMed:17114044). Plays a role in synaptic vesicle trafficking (PubMed:24687852). Plays an important role in recruiting SEC16A to endoplasmic reticulum exit sites (ERES) and in regulating ER to Golgi vesicle-mediated transport and ERES organization (PubMed:25201882). Positively regulates autophagy through a calcium-dependent activation of the CaMKK/AMPK signaling pathway (PubMed:22012985). The process involves activation of nicotinic acid adenine dinucleotide phosphate (NAADP) receptors, increase in lysosomal pH, and calcium release from lysosomes (PubMed:22012985). Phosphorylates PRDX3 (PubMed:21850687). By phosphorylating APP on 'Thr-743', which promotes the production and the nuclear translocation of the APP intracellular domain (AICD), regulates dopaminergic neuron apoptosis (PubMed:28720718). Acts as a positive regulator of innate immunity by mediating phosphorylation of RIPK2 downstream of NOD1 and NOD2, thereby enhancing RIPK2 activation (PubMed:27830463). Independent of its kinase activity, inhibits the proteasomal degradation of MAPT, thus promoting MAPT oligomerization and secretion (PubMed:26014385). In addition, has GTPase activity via its Roc domain which regulates LRRK2 kinase activity (PubMed:18230735, PubMed:26824392, PubMed:28720718, PubMed:29125462, PubMed:29212815). Recruited by RAB29/RAB7L1 to overloaded lysosomes where it phosphorylates and stabilizes RAB8A and RAB10 which promote lysosomal content release and suppress lysosomal enlargement through the EHBP1 and EHBP1L1 effector proteins (PubMed:30209220, PubMed:38227290)", "gene_name": "LRRK2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q5S007", "name": "Leucine-rich repeat kinase 2 (LRRK2)", "organism": "Homo sapiens", "uniprot_id": "Q5S007" }, { "function": "Plays an important role in B-cell response to antigen that acts both as a negative or positive coreceptor. Inhibits B-cell receptor (BCR) signaling in the absence of CR2 stimulation but engagement with CR2 and the BCR lead to a superior calcium response compared to CR2 and BCR costimulation (PubMed:30107486). May be involved in B-cell development and differentiation in peripheral lymphoid organs and may be useful markers of B-cell stages. May have an immunoregulatory role in marginal zone B-cells. May play a role in fertilization (By similarity)", "gene_name": "FCRL5", "glycan_count": 2, "glycosylation_sites": [ { "position": 383, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q96RD9", "name": "Fc\u03b1/\u03bc receptor (Fc\u03b1/\u03bcR)", "organism": "Homo sapiens", "uniprot_id": "Q96RD9" }, { "function": "ATP- and membrane-binding protein that controls membrane reorganization/tubulation upon ATP hydrolysis. In vitro causes vesiculation of endocytic membranes (PubMed:24019528). Acts in early endocytic membrane fusion and membrane trafficking of recycling endosomes (PubMed:15020713, PubMed:17233914, PubMed:20801876). Recruited to endosomal membranes upon nerve growth factor stimulation, indirectly regulates neurite outgrowth (By similarity). Plays a role in myoblast fusion (By similarity). Involved in the unidirectional retrograde dendritic transport of endocytosed BACE1 and in efficient sorting of BACE1 to axons implicating a function in neuronal APP processing (By similarity). Plays a role in the formation of the ciliary vesicle (CV), an early step in cilium biogenesis (PubMed:31615969). Proposed to be required for the fusion of distal appendage vesicles (DAVs) to form the CV by recruiting SNARE complex component SNAP29. Is required for recruitment of transition zone proteins CEP290, RPGRIP1L, TMEM67 and B9D2, and of IFT20 following DAV reorganization before Rab8-dependent ciliary membrane extension. Required for the loss of CCP110 form the mother centriole essential for the maturation of the basal body during ciliogenesis (PubMed:25686250)", "gene_name": "EHD1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H4M9", "name": "FKRP", "organism": "Homo sapiens", "uniprot_id": "Q9H4M9" }, { "function": "Has no esterase activity", "gene_name": "CES1P1", "glycan_count": 0, "glycosylation_sites": [ { "position": 80, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UKY3", "name": "POMT2", "organism": "Homo sapiens", "uniprot_id": "Q9UKY3" }, { "function": "Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA", "gene_name": "RNASE1", "glycan_count": 22, "glycosylation_sites": [ { "position": 27, "type": "N-linked (Glc) (glycation) lysine; in vitro" }, { "position": 33, "type": "N-linked (Glc) (glycation) lysine; in vitro" }, { "position": 60, "type": "N-linked (GlcNAc...) asparagine; partial" }, { "position": 63, "type": "N-linked (Glc) (glycation) lysine; in vitro" }, { "position": 67, "type": "N-linked (Glc) (glycation) lysine; in vitro" } ], "id": "P61823", "name": "RNase B", "organism": "Bos taurus", "uniprot_id": "P61823" }, { "function": "Plays a role in the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins (PubMed:16186509, PubMed:29997207, PubMed:37943610, PubMed:37943617). Enhances SYVN1 stability. Plays a role in LPL maturation and secretion. Required for normal differentiation of the pancreas epithelium, and for normal exocrine function and survival of pancreatic cells. May play a role in Notch signaling", "gene_name": "SEL1L", "glycan_count": 46, "glycosylation_sites": [ { "position": 195, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 217, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 272, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 431, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 608, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UBV2", "name": "GDP-mannose-4,6-dehydratase (GMD)", "organism": "Homo sapiens", "uniprot_id": "Q9UBV2" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P69905 (HBA1), P68871 (HBB)", "name": "Hemoglobin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P00686 (AMY2A, human)", "name": "Alpha-amylase", "organism": "", "uniprot_id": "" }, { "function": "Receptor for extracellular UDP > UTP > ATP. The activity of this receptor is mediated by G proteins which activate a phosphatidylinositol-calcium second messenger system", "gene_name": "P2RY6", "glycan_count": 0, "glycosylation_sites": [ { "position": 5, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q15077", "name": "P2Y6 receptor", "organism": "Homo sapiens", "uniprot_id": "Q15077" }, { "function": "Catalyzes the reversible phosphorylytic cleavage of uridine to uracil and ribose-1-phosphate which can then be utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis (PubMed:7488099). Shows broad substrate specificity and can also accept deoxyuridine and other analogous compounds (Probable)", "gene_name": "UPP1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q16831", "name": "UPP1 (Uridine Phosphorylase 1)", "organism": "Homo sapiens", "uniprot_id": "Q16831" }, { "function": "Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate (PubMed:11306702, PubMed:11494055). Does not phosphorylate deoxyribonucleosides or purine ribonucleosides (PubMed:11306702). Can use ATP or GTP as a phosphate donor (PubMed:11306702). Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4-thiouridine, 5-bromouridine, N(4)-acetylcytidine, N(4)-benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5-methylcytidine, and N(4)-anisoylcytidine (PubMed:11306702)", "gene_name": "UCK2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9BZX2", "name": "UCK2 (Uridine-cytidine kinase 2)", "organism": "Homo sapiens", "uniprot_id": "Q9BZX2" }, { "function": "Plays a role in lipoprotein-mediated cholesterol uptake in hepatocytes (PubMed:25732850). Binds cholesterol (PubMed:25732850). Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport (By similarity)", "gene_name": "FABP1", "glycan_count": 1, "glycosylation_sites": [], "id": "P07148", "name": "FABP1", "organism": "Homo sapiens", "uniprot_id": "P07148" }, { "function": "RNA-binding protein that binds to the 3'-UTR region of mRNAs and increases their stability (PubMed:14517288, PubMed:18285462, PubMed:31358969). Involved in embryonic stem cell (ESC) differentiation: preferentially binds mRNAs that are not methylated by N6-methyladenosine (m6A), stabilizing them, promoting ESC differentiation (By similarity). Has also been shown to be capable of binding to m6A-containing mRNAs and contributes to MYC stability by binding to m6A-containing MYC mRNAs (PubMed:32245947). Binds to poly-U elements and AU-rich elements (AREs) in the 3'-UTR of target mRNAs (PubMed:14731398, PubMed:17632515, PubMed:18285462, PubMed:23519412, PubMed:8626503). Binds avidly to the AU-rich element in FOS and IL3/interleukin-3 mRNAs. In the case of the FOS AU-rich element, binds to a core element of 27 nucleotides that contain AUUUA, AUUUUA, and AUUUUUA motifs. Binds preferentially to the 5'-UUUU[AG]UUU-3' motif in vitro (PubMed:8626503). With ZNF385A, binds the 3'-UTR of p53/TP53 mRNA to control their nuclear export induced by CDKN2A. Hence, may regulate p53/TP53 expression and mediate in part the CDKN2A anti-proliferative activity. May also bind with ZNF385A the CCNB1 mRNA (By similarity). Increases the stability of the leptin mRNA harboring an AU-rich element (ARE) in its 3' UTR (PubMed:29180010)", "gene_name": "ELAVL1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q15717", "name": "HuR (ELAVL1)", "organism": "Homo sapiens", "uniprot_id": "Q15717" }, { "function": "Required for the maintenance of uterine histoarchitecture and normal female reproductive lifespan (By similarity). May serve as a universal non-classical progesterone receptor in the uterus (Probable). Intracellular heme chaperone required for delivery of labile, or signaling heme, to the nucleus (By similarity). Plays a role in adipocyte function and systemic glucose homeostasis (PubMed:28111073). In brown fat, which has a high demand for heme, delivery of labile heme in the nucleus regulates the activity of heme-responsive transcriptional repressors such as NR1D1 and BACH1 (By similarity)", "gene_name": "PGRMC2", "glycan_count": 1, "glycosylation_sites": [ { "position": 15, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" } ], "id": "O15173", "name": "\u03b3-sarcoglycan", "organism": "Homo sapiens", "uniprot_id": "O15173" }, { "function": "", "gene_name": "PHTF1", "glycan_count": 2, "glycosylation_sites": [ { "position": 179, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 180, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 363, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 431, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 674, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 733, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UMS5", "name": "Neurofascin 155", "organism": "Homo sapiens", "uniprot_id": "Q9UMS5" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P27361/P28482", "name": "ERK1/2 (MAPK3/MAPK1)", "organism": "", "uniprot_id": "" }, { "function": "Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK14 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as pro-inflammatory cytokines or physical stress leading to direct activation of transcription factors. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases which are activated through phosphorylation and further phosphorylate additional targets. RPS6KA5/MSK1 and RPS6KA4/MSK2 can directly phosphorylate and activate transcription factors such as CREB1, ATF1, the NF-kappa-B isoform RELA/NFKB3, STAT1 and STAT3, but can also phosphorylate histone H3 and the nucleosomal protein HMGN1 (PubMed:9687510, PubMed:9792677). RPS6KA5/MSK1 and RPS6KA4/MSK2 play important roles in the rapid induction of immediate-early genes in response to stress or mitogenic stimuli, either by inducing chromatin remodeling or by recruiting the transcription machinery (PubMed:9687510, PubMed:9792677). On the other hand, two other kinase targets, MAPKAPK2/MK2 and MAPKAPK3/MK3, participate in the control of gene expression mostly at the post-transcriptional level, by phosphorylating ZFP36 (tristetraprolin) and ELAVL1, and by regulating EEF2K, which is important for the elongation of mRNA during translation. MKNK1/MNK1 and MKNK2/MNK2, two other kinases activated by p38 MAPKs, regulate protein synthesis by phosphorylating the initiation factor EIF4E2 (PubMed:11154262). MAPK14 also interacts with casein kinase II, leading to its activation through autophosphorylation and further phosphorylation of TP53/p53 (PubMed:10747897). In the cytoplasm, the p38 MAPK pathway is an important regulator of protein turnover. For example, CFLAR is an inhibitor of TNF-induced apoptosis whose proteasome-mediated degradation is regulated by p38 MAPK phosphorylation. In a similar way, MAPK14 phosphorylates the ubiquitin ligase SIAH2, regulating its activity towards EGLN3 (PubMed:17003045). MAPK14 may also inhibit the lysosomal degradation pathway of autophagy by interfering with the intracellular trafficking of the transmembrane protein ATG9 (PubMed:19893488). Another function of MAPK14 is to regulate the endocytosis of membrane receptors by different mechanisms that impinge on the small GTPase RAB5A. In addition, clathrin-mediated EGFR internalization induced by inflammatory cytokines and UV irradiation depends on MAPK14-mediated phosphorylation of EGFR itself as well as of RAB5A effectors (PubMed:16932740). Ectodomain shedding of transmembrane proteins is regulated by p38 MAPKs as well. In response to inflammatory stimuli, p38 MAPKs phosphorylate the membrane-associated metalloprotease ADAM17 (PubMed:20188673). Such phosphorylation is required for ADAM17-mediated ectodomain shedding of TGF-alpha family ligands, which results in the activation of EGFR signaling and cell proliferation. Another p38 MAPK substrate is FGFR1. FGFR1 can be translocated from the extracellular space into the cytosol and nucleus of target cells, and regulates processes such as rRNA synthesis and cell growth. FGFR1 translocation requires p38 MAPK activation. In the nucleus, many transcription factors are phosphorylated and activated by p38 MAPKs in response to different stimuli. Classical examples include ATF1, ATF2, ATF6, ELK1, PTPRH, DDIT3, TP53/p53 and MEF2C and MEF2A (PubMed:10330143, PubMed:9430721, PubMed:9858528). The p38 MAPKs are emerging as important modulators of gene expression by regulating chromatin modifiers and remodelers. The promoters of several genes involved in the inflammatory response, such as IL6, IL8 and IL12B, display a p38 MAPK-dependent enrichment of histone H3 phosphorylation on 'Ser-10' (H3S10ph) in LPS-stimulated myeloid cells. This phosphorylation enhances the accessibility of the cryptic NF-kappa-B-binding sites marking promoters for increased NF-kappa-B recruitment. Phosphorylates CDC25B and CDC25C which is required for binding to 14-3-3 proteins and leads to initiation of a G2 delay after ultraviolet radiation (PubMed:11333986). Phosphorylates TIAR following DNA damage, releasing TIAR from GADD45A mRNA and preventing mRNA degradation (PubMed:20932473). The p38 MAPKs may also have kinase-independent roles, which are thought to be due to the binding to targets in the absence of phosphorylation. Protein O-Glc-N-acylation catalyzed by the OGT is regulated by MAPK14, and, although OGT does not seem to be phosphorylated by MAPK14, their interaction increases upon MAPK14 activation induced by glucose deprivation. This interaction may regulate OGT activity by recruiting it to specific targets such as neurofilament H, stimulating its O-Glc-N-acylation. Required in mid-fetal development for the growth of embryo-derived blood vessels in the labyrinth layer of the placenta. Also plays an essential role in developmental and stress-induced erythropoiesis, through regulation of EPO gene expression (PubMed:10943842). Isoform MXI2 activation is stimulated by mitogens and oxidative stress and only poorly phosphorylates ELK1 and ATF2. Isoform EXIP may play a role in the early onset of apoptosis. Phosphorylates S100A9 at 'Thr-113' (PubMed:15905572). Phosphorylates NLRP1 downstream of MAP3K20/ZAK in response to UV-B irradiation and ribosome collisions, promoting activation of the NLRP1 inflammasome and pyroptosis (PubMed:35857590)", "gene_name": "MAPK14", "glycan_count": 1, "glycosylation_sites": [], "id": "Q16539", "name": "p38 MAPK (MAPK14)", "organism": "Homo sapiens", "uniprot_id": "Q16539" }, { "function": "Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses (PubMed:18626576, PubMed:9244310, PubMed:9252186, PubMed:9346484). Acts as a part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B on serine residues (PubMed:18626576, PubMed:35952808, PubMed:9244310, PubMed:9252186, PubMed:9346484). These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome (PubMed:18626576, PubMed:9244310, PubMed:9252186, PubMed:9346484). In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis (PubMed:18626576, PubMed:9244310, PubMed:9252186, PubMed:9346484). Negatively regulates the pathway by phosphorylating the scaffold protein TAXBP1 and thus promoting the assembly of the A20/TNFAIP3 ubiquitin-editing complex (composed of A20/TNFAIP3, TAX1BP1, and the E3 ligases ITCH and RNF11) (PubMed:21765415). Therefore, CHUK plays a key role in the negative feedback of NF-kappa-B canonical signaling to limit inflammatory gene activation. As part of the non-canonical pathway of NF-kappa-B activation, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B RelB-p52 complexes (PubMed:20501937). In turn, these complexes regulate genes encoding molecules involved in B-cell survival and lymphoid organogenesis. Also participates in the negative feedback of the non-canonical NF-kappa-B signaling pathway by phosphorylating and destabilizing MAP3K14/NIK. Within the nucleus, phosphorylates CREBBP and consequently increases both its transcriptional and histone acetyltransferase activities (PubMed:17434128). Modulates chromatin accessibility at NF-kappa-B-responsive promoters by phosphorylating histones H3 at 'Ser-10' that are subsequently acetylated at 'Lys-14' by CREBBP (PubMed:12789342). Additionally, phosphorylates the CREBBP-interacting protein NCOA3. Also phosphorylates FOXO3 and may regulate this pro-apoptotic transcription factor (PubMed:15084260). Phosphorylates RIPK1 at 'Ser-25' which represses its kinase activity and consequently prevents TNF-mediated RIPK1-dependent cell death (By similarity). Phosphorylates AMBRA1 following mitophagy induction, promoting AMBRA1 interaction with ATG8 family proteins and its mitophagic activity (PubMed:30217973)", "gene_name": "CHUK", "glycan_count": 2, "glycosylation_sites": [], "id": "O15111", "name": "IKK\u03b1 (CHUK)", "organism": "Homo sapiens", "uniprot_id": "O15111" }, { "function": "Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses (PubMed:20434986, PubMed:20797629, PubMed:21138416, PubMed:30337470, PubMed:9346484). Acts as a part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation (PubMed:9346484). Phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues (PubMed:20434986, PubMed:20797629, PubMed:21138416, PubMed:9346484). These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome (PubMed:20434986, PubMed:20797629, PubMed:21138416, PubMed:9346484). In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis (PubMed:20434986, PubMed:20797629, PubMed:21138416, PubMed:9346484). In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE (PubMed:11297557, PubMed:14673179, PubMed:20410276, PubMed:21138416). IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators since they exert a negative regulation on canonical IKKs (PubMed:11297557, PubMed:20410276, PubMed:21138416). Phosphorylates FOXO3, mediating the TNF-dependent inactivation of this pro-apoptotic transcription factor (PubMed:15084260). Also phosphorylates other substrates including NAA10, NCOA3, BCL10 and IRS1 (PubMed:17213322, PubMed:19716809). Phosphorylates RIPK1 at 'Ser-25' which represses its kinase activity and consequently prevents TNF-mediated RIPK1-dependent cell death (By similarity). Phosphorylates the C-terminus of IRF5, stimulating IRF5 homodimerization and translocation into the nucleus (PubMed:25326418). Following bacterial lipopolysaccharide (LPS)-induced TLR4 endocytosis, phosphorylates STAT1 at 'Thr-749' which restricts interferon signaling and anti-inflammatory responses and promotes innate inflammatory responses (PubMed:38621137). IKBKB-mediated phosphorylation of STAT1 at 'Thr-749' promotes binding of STAT1 to the ARID5A promoter, resulting in transcriptional activation of ARID5A and subsequent ARID5A-mediated stabilization of IL6 (PubMed:32209697). It also promotes binding of STAT1 to the IL12B promoter and activation of IL12B transcription (PubMed:32209697)", "gene_name": "IKBKB", "glycan_count": 1, "glycosylation_sites": [], "id": "O14920", "name": "IKK\u03b2 (IKBKB)", "organism": "Homo sapiens", "uniprot_id": "O14920" }, { "function": "Plays multiple roles in cell cycle progression, cytokinesis and apoptosis. Involved in pre-mRNA splicing in a kinase activity-dependent manner. Isoform 7 may act as a negative regulator of normal cell cycle progression", "gene_name": "CDK11B", "glycan_count": 1, "glycosylation_sites": [], "id": "P21127", "name": "PITSLRE (CDK11)", "organism": "Homo sapiens", "uniprot_id": "P21127" }, { "function": "Required for lipopolysaccharide (LPS)-induced, TLR4-mediated activation of the MAPK/ERK pathway in macrophages, thus being critical for production of the pro-inflammatory cytokine TNF-alpha (TNF) during immune responses. Involved in the regulation of T-helper cell differentiation and IFNG expression in T-cells. Involved in mediating host resistance to bacterial infection through negative regulation of type I interferon (IFN) production. In vitro, activates MAPK/ERK pathway in response to IL1 in an IRAK1-independent manner, leading to up-regulation of IL8 and CCL4. Transduces CD40 and TNFRSF1A signals that activate ERK in B-cells and macrophages, and thus may play a role in the regulation of immunoglobulin production. May also play a role in the transduction of TNF signals that activate JNK and NF-kappa-B in some cell types. In adipocytes, activates MAPK/ERK pathway in an IKBKB-dependent manner in response to IL1B and TNF, but not insulin, leading to induction of lipolysis. Plays a role in the cell cycle. Isoform 1 shows some transforming activity, although it is much weaker than that of the activated oncogenic variant", "gene_name": "MAP3K8", "glycan_count": 0, "glycosylation_sites": [], "id": "P41279", "name": "COT (MAP3K8)", "organism": "Homo sapiens", "uniprot_id": "P41279" }, { "function": "Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to low amino acid availability (PubMed:25329545, PubMed:32610081). Plays a role as an activator of the integrated stress response (ISR) required for adaptation to amino acid starvation (By similarity). EIF2S1/eIF-2-alpha phosphorylation in response to stress converts EIF2S1/eIF-2-alpha into a global protein synthesis inhibitor, leading to a global attenuation of cap-dependent translation, and thus to a reduced overall utilization of amino acids, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4, and hence allowing ATF4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion (PubMed:32610081). Binds uncharged tRNAs (By similarity). Required for the translational induction of protein kinase PRKCH following amino acid starvation (By similarity). Involved in cell cycle arrest by promoting cyclin D1 mRNA translation repression after the unfolded protein response pathway (UPR) activation or cell cycle inhibitor CDKN1A/p21 mRNA translation activation in response to amino acid deprivation (PubMed:26102367). Plays a role in the consolidation of synaptic plasticity, learning as well as formation of long-term memory (By similarity). Plays a role in neurite outgrowth inhibition (By similarity). Plays a proapoptotic role in response to glucose deprivation (By similarity). Promotes global cellular protein synthesis repression in response to UV irradiation independently of the stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) and p38 MAPK signaling pathways (By similarity). Plays a role in the antiviral response against alphavirus infection; impairs early viral mRNA translation of the incoming genomic virus RNA, thus preventing alphavirus replication (By similarity)", "gene_name": "EIF2AK4", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9P2K8", "name": "GCN2 (EIF2AK4)", "organism": "Homo sapiens", "uniprot_id": "Q9P2K8" }, { "function": "Forms part of a two-component regulatory system AfsQ1/AfsQ2 involved in secondary metabolism. May activate AfsQ1 by phosphorylation", "gene_name": "afsQ2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q04943", "name": "Anti-M\u00fcllerian hormone", "organism": "Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)", "uniprot_id": "Q04943" }, { "function": "Macrophage-restricted adhesion molecule that mediates sialic-acid dependent binding to lymphocytes, including granulocytes, monocytes, natural killer cells, B-cells and CD8 T-cells. Plays a crucial role in limiting bacterial dissemination by engaging sialylated bacteria to promote effective phagocytosis and antigen presentation for the adaptive immune response (PubMed:12940982, PubMed:33489013). Mediates the uptake of various enveloped viruses via sialic acid recognition and subsequently induces the formation of intracellular compartments filled with virions (VCCs) (PubMed:28129379). In turn, enhances macrophage-to-T-cell transmission of several viruses including HIV-1 or SARS-CoV-2 (PubMed:28129379, PubMed:34782760). Acts as an endocytic receptor mediating clathrin dependent endocytosis. Preferentially binds to alpha-2,3-linked sialic acid (PubMed:12940982). Binds to SPN/CD43 on T-cells (By similarity). May play a role in hemopoiesis. Plays a role in the inhibition of antiviral innate immune by promoting TBK1 degradation via TYROBP and TRIM27-mediated ubiquitination (PubMed:26358190)", "gene_name": "SIGLEC1", "glycan_count": 14, "glycosylation_sites": [ { "position": 159, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 265, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 339, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 499, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 697, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 726, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 730, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 741, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 886, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1138, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1251, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1462, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1476, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9BZZ2", "name": "SIGLEC1 (Sialic acid-binding Ig-like lectin 1)", "organism": "Homo sapiens", "uniprot_id": "Q9BZZ2" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P69905/P68871", "name": "Hemoglobin", "organism": "", "uniprot_id": "" }, { "function": "Component of N-methyl-D-aspartate (NMDA) receptors (NMDARs) that function as heterotetrameric, ligand-gated cation channels with high calcium permeability and voltage-dependent block by Mg(2+) (PubMed:21376300, PubMed:26875626, PubMed:26919761, PubMed:28126851, PubMed:28228639, PubMed:36959261, PubMed:7679115, PubMed:7681588, PubMed:7685113). NMDARs participate in synaptic plasticity for learning and memory formation by contributing to the long-term potentiation (LTP) (PubMed:26875626). Channel activation requires binding of the neurotransmitter L-glutamate to the GluN2 subunit, glycine or D-serine binding to the GluN1 subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+) (PubMed:21376300, PubMed:26875626, PubMed:26919761, PubMed:27164704, PubMed:28095420, PubMed:28105280, PubMed:28126851, PubMed:28228639, PubMed:36959261, PubMed:38538865, PubMed:7679115, PubMed:7681588, PubMed:7685113). NMDARs mediate simultaneously the potasium efflux and the influx of calcium and sodium (By similarity). Each GluN2 or GluN3 subunit confers differential attributes to channel properties, including activation, deactivation and desensitization kinetics, pH sensitivity, Ca2(+) permeability, and binding to allosteric modulators (PubMed:26875626, PubMed:26919761, PubMed:36309015, PubMed:38598639)", "gene_name": "GRIN1", "glycan_count": 3, "glycosylation_sites": [ { "position": 61, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 203, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 239, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 276, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 300, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 350, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 368, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 440, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 471, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 491, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 674, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 771, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q05586", "name": "GRIN1 (NMDA receptor subunit 1)", "organism": "Homo sapiens", "uniprot_id": "Q05586" }, { "function": "Component of N-methyl-D-aspartate (NMDA) receptors (NMDARs) that function as heterotetrameric, ligand-gated cation channels with high calcium permeability and voltage-dependent block by Mg(2+) (PubMed:24272827, PubMed:24863970, PubMed:26875626, PubMed:26919761, PubMed:27839871, PubMed:28095420, PubMed:28126851, PubMed:38538865, PubMed:8768735). Participates in synaptic plasticity for learning and memory formation by contributing to the long-term depression (LTD) of hippocampus membrane currents (By similarity). Channel activation requires binding of the neurotransmitter L-glutamate to the GluN2 subunit, glycine or D-serine binding to the GluN1 subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+) (PubMed:24272827, PubMed:24863970, PubMed:26875626, PubMed:26919761, PubMed:27839871, PubMed:28095420, PubMed:28126851, PubMed:38538865, PubMed:8768735). NMDARs mediate simultaneously the potasium efflux and the influx of calcium and sodium (By similarity). Each GluN2 subunit confers differential attributes to channel properties, including activation, deactivation and desensitization kinetics, pH sensitivity, Ca2(+) permeability, and binding to allosteric modulators (PubMed:26875626, PubMed:28095420, PubMed:28126851, PubMed:38538865, PubMed:8768735). In concert with DAPK1 at extrasynaptic sites, acts as a central mediator for stroke damage. Its phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity inducing injurious Ca2+ influx through them, resulting in an irreversible neuronal death (By similarity)", "gene_name": "GRIN2B", "glycan_count": 0, "glycosylation_sites": [ { "position": 74, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 341, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 348, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 444, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 491, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 542, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 688, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13224", "name": "GRIN2B (NMDA receptor subunit 2B)", "organism": "Homo sapiens", "uniprot_id": "Q13224" }, { "function": "Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid (PubMed:1311100, PubMed:20805473, PubMed:21172611, PubMed:28628100, PubMed:35675825). L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse upon entry of monovalent and divalent cations such as sodium and calcium. The receptor then desensitizes rapidly and enters in a transient inactive state, characterized by the presence of bound agonist (By similarity). In the presence of CACNG2 or CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of L-glutamate (PubMed:21172611). Resensitization is blocked by CNIH2 through interaction with CACNG8 in the CACNG8-containing AMPA receptors complex (PubMed:21172611). Calcium (Ca(2+)) permeability depends on subunits composition and, heteromeric channels containing edited GRIA2 subunit are calcium-impermeable. Also permeable to other divalents cations such as strontium(2+) and magnesium(2+) and monovalent cations such as potassium(1+) and lithium(1+) (By similarity)", "gene_name": "GRIA1", "glycan_count": 2, "glycosylation_sites": [ { "position": 63, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 249, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 257, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 363, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 401, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 406, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P42261", "name": "GRIA2 (AMPA receptor subunit 2)", "organism": "Homo sapiens", "uniprot_id": "P42261" }, { "function": "Ionotropic glutamate receptor that functions as a cation-permeable ligand-gated ion channel, gated by L-glutamate and the glutamatergic agonist kainic acid. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist (PubMed:7719709). In association with GRIK2, involved in presynaptic facilitation of glutamate release at hippocampal mossy fiber synapses (By similarity)", "gene_name": "GRIK3", "glycan_count": 0, "glycosylation_sites": [ { "position": 70, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 76, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 278, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 381, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 415, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 426, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 433, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 548, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 551, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 752, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13003", "name": "GRIK2 (Kainate receptor subunit 2)", "organism": "Homo sapiens", "uniprot_id": "Q13003" }, { "function": "Alpha subunit of the heteropentameric ligand-gated chloride channel gated by Gamma-aminobutyric acid (GABA), a major inhibitory neurotransmitter in the brain (PubMed:23909897, PubMed:25489750, PubMed:29950725, PubMed:30602789). GABA-gated chloride channels, also named GABA(A) receptors (GABAAR), consist of five subunits arranged around a central pore and contain GABA active binding site(s) located at the alpha and beta subunit interface(s) (PubMed:29950725, PubMed:30602789). When activated by GABA, GABAARs selectively allow the flow of chloride anions across the cell membrane down their electrochemical gradient (PubMed:23909897, PubMed:29950725, PubMed:30602789). Alpha-1/GABRA1-containing GABAARs are largely synaptic (By similarity). Chloride influx into the postsynaptic neuron following GABAAR opening decreases the neuron ability to generate a new action potential, thereby reducing nerve transmission (By similarity). GABAARs containing alpha-1 and beta-2 or -3 subunits exhibit synaptogenic activity; the gamma-2 subunit being necessary but not sufficient to induce rapid synaptic contacts formation (PubMed:23909897, PubMed:25489750). GABAARs function also as histamine receptor where histamine binds at the interface of two neighboring beta subunits and potentiates GABA response (By similarity). GABAARs containing alpha, beta and epsilon subunits also permit spontaneous chloride channel activity while preserving the structural information required for GABA-gated openings (By similarity). Alpha-1-mediated plasticity in the orbitofrontal cortex regulates context-dependent action selection (By similarity). Together with rho subunits, may also control neuronal and glial GABAergic transmission in the cerebellum (By similarity)", "gene_name": "GABRA1", "glycan_count": 13, "glycosylation_sites": [ { "position": 38, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 138, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P14867", "name": "GABRA1 (GABA-A receptor subunit alpha-1)", "organism": "Homo sapiens", "uniprot_id": "P14867" }, { "function": "Component of a heterodimeric G-protein coupled receptor for GABA, formed by GABBR1 and GABBR2 (PubMed:15617512, PubMed:18165688, PubMed:22660477, PubMed:24305054, PubMed:36103875, PubMed:9872316, PubMed:9872744). Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins (PubMed:18165688). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase (PubMed:10075644, PubMed:10773016, PubMed:10906333, PubMed:24305054, PubMed:9872744). Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis (PubMed:10075644). Calcium is required for high affinity binding to GABA (By similarity). Plays a critical role in the fine-tuning of inhibitory synaptic transmission (PubMed:9844003). Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials (PubMed:10075644, PubMed:22660477, PubMed:9844003, PubMed:9872316, PubMed:9872744). Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception (Probable). Activated by (-)-baclofen, cgp27492 and blocked by phaclofen (PubMed:24305054, PubMed:9844003, PubMed:9872316)", "gene_name": "GABBR1", "glycan_count": 0, "glycosylation_sites": [ { "position": 24, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 84, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 409, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 440, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 482, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 502, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 514, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UBS5", "name": "GABBR1 (GABA-B receptor subunit 1)", "organism": "Homo sapiens", "uniprot_id": "Q9UBS5" }, { "function": "An alpha chain of antigen-presenting major histocompatibility complex class II (MHCII) molecule. In complex with the beta chain HLA-DRB, displays antigenic peptides on professional antigen presenting cells (APCs) for recognition by alpha-beta T cell receptor (TCR) on HLA-DR-restricted CD4-positive T cells. This guides antigen-specific T-helper effector functions, both antibody-mediated immune response and macrophage activation, to ultimately eliminate the infectious agents and transformed cells (PubMed:15265931, PubMed:15322540, PubMed:17334368, PubMed:22327072, PubMed:24190431, PubMed:27591323, PubMed:29884618, PubMed:31495665, PubMed:8145819, PubMed:9075930). Typically presents extracellular peptide antigens of 10 to 30 amino acids that arise from proteolysis of endocytosed antigens in lysosomes (PubMed:8145819). In the tumor microenvironment, presents antigenic peptides that are primarily generated in tumor-resident APCs likely via phagocytosis of apoptotic tumor cells or macropinocytosis of secreted tumor proteins (PubMed:31495665). Presents peptides derived from intracellular proteins that are trapped in autolysosomes after macroautophagy, a mechanism especially relevant for T cell selection in the thymus and central immune tolerance (PubMed:17182262, PubMed:23783831). The selection of the immunodominant epitopes follows two processing modes: 'bind first, cut/trim later' for pathogen-derived antigenic peptides and 'cut first, bind later' for autoantigens/self-peptides (PubMed:25413013). The anchor residue at position 1 of the peptide N-terminus, usually a large hydrophobic residue, is essential for high affinity interaction with MHCII molecules (PubMed:8145819)", "gene_name": "HLA-DRA", "glycan_count": 88, "glycosylation_sites": [ { "position": 103, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 143, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01903", "name": "HLA-DR (MHC class II)", "organism": "Homo sapiens", "uniprot_id": "P01903" }, { "function": "Lacks dipeptidase activity and is unable to hydrolyze cystinyl-bis-glycine, leukotriene D4 and the beta-lactam antibiotic imipenem (PubMed:32325220). The absence of activity may be due to the inability of asparagine (instead of aspartate found in DPEP1/2) at position 359 to function as the acid/base catalyst and activate the nucleophilic water/hydroxide (PubMed:32325220). A tyrosine (instead of histidine) at position 269 reduces affinity for the beta zinc and may cause substrate steric hindrance (PubMed:32325220)", "gene_name": "DPEP3", "glycan_count": 0, "glycosylation_sites": [ { "position": 334, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9H4B8", "name": "PGM3", "organism": "Homo sapiens", "uniprot_id": "Q9H4B8" }, { "function": "Hydrolase that removes conjugated ubiquitin from target proteins and regulates various pathways such as the TGF-beta receptor signaling, NF-kappa-B and RNF41/NRDP1-PRKN pathways (PubMed:16005295, PubMed:17318178, PubMed:19576224, PubMed:19826004, PubMed:21947082, PubMed:22344298, PubMed:24852371). Acts as a key regulator of TGF-beta receptor signaling pathway, but the precise mechanism is still unclear: according to a report, acts by promoting deubiquitination of monoubiquitinated R-SMADs (SMAD1, SMAD2 and/or SMAD3), thereby alleviating inhibition of R-SMADs and promoting activation of TGF-beta target genes (PubMed:21947082). According to another reports, regulates the TGF-beta receptor signaling pathway by mediating deubiquitination and stabilization of TGFBR1, leading to an enhanced TGF-beta signal (PubMed:22344298). Able to mediate deubiquitination of monoubiquitinated substrates, 'Lys-27'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (PubMed:33093067). May also regulate gene expression and/or DNA repair through the deubiquitination of histone H2B (PubMed:24526689). Acts as an inhibitor of mitophagy by counteracting the action of parkin (PRKN): hydrolyzes cleavage of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains attached by parkin on target proteins such as MFN2, thereby reducing parkin's ability to drive mitophagy (PubMed:24852371). Acts as an associated component of COP9 signalosome complex (CSN) and regulates different pathways via this association: regulates NF-kappa-B by mediating deubiquitination of NFKBIA and deubiquitinates substrates bound to VCP (PubMed:16005295, PubMed:17318178, PubMed:19576224, PubMed:19826004). Involved in endosome organization by mediating deubiquitination of SQSTM1: ubiquitinated SQSTM1 forms a molecular bridge that restrains cognate vesicles in the perinuclear region and its deubiquitination releases target vesicles for fast transport into the cell periphery (PubMed:27368102). Acts as a negative regulator of antifungal immunity by mediating 'Lys-27'-linked deubiquitination of CARD9, thereby inactivating CARD9 (PubMed:33093067)", "gene_name": "USP15", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y4E8", "name": "OGA", "organism": "Homo sapiens", "uniprot_id": "Q9Y4E8" }, { "function": "Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron (PubMed:11121422, PubMed:19556236, PubMed:7703255). Affords protection against programmed cell death and this cytoprotective effect relies on its ability to catabolize free heme and prevent it from sensitizing cells to undergo apoptosis (PubMed:20055707)", "gene_name": "HMOX1", "glycan_count": 1, "glycosylation_sites": [], "id": "P09601", "name": "HMOX1", "organism": "Homo sapiens", "uniprot_id": "P09601" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q06210/Q9BYC2", "name": "GFAT1/GFAT2", "organism": "", "uniprot_id": "" }, { "function": "Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate", "gene_name": "KDM4C", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H3R0", "name": "GNPNAT1", "organism": "Homo sapiens", "uniprot_id": "Q9H3R0" }, { "function": "Catalyzes the last step in biosynthesis of uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) by converting UTP and glucosamine 1-phosphate (GlcNAc-1-P) to the sugar nucleotide (PubMed:9603950, PubMed:9765219). Also converts UTP and galactosamine 1-phosphate (GalNAc-1-P) into uridine diphosphate-N-acetylgalactosamine (UDP-GalNAc) (PubMed:9765219). In addition to its role in metabolism, acts as a regulator of innate immunity in response to virus infection by mediating pyrophosphorylation of IRF3: catalyzes pyrophosphorylation of IRF3 phosphorylated at 'Ser-386' by TBK1, promoting IRF3 dimerization and activation, leading to type I interferon responses (PubMed:36603579)", "gene_name": "UAP1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q16222", "name": "UAP1", "organism": "Homo sapiens", "uniprot_id": "Q16222" }, { "function": "LA-PF4 stimulates DNA synthesis, mitosis, glycolysis, intracellular cAMP accumulation, prostaglandin E2 secretion, and synthesis of hyaluronic acid and sulfated glycosaminoglycan. It also stimulates the formation and secretion of plasminogen activator by human synovial cells. NAP-2 is a ligand for CXCR1 and CXCR2, and NAP-2, NAP-2(73), NAP-2(74), NAP-2(1-66), and most potent NAP-2(1-63) are chemoattractants and activators for neutrophils. TC-1 and TC-2 are antibacterial proteins, in vitro released from activated platelet alpha-granules. CTAP-III(1-81) is more potent than CTAP-III desensitize chemokine-induced neutrophil activation", "gene_name": "PPBP", "glycan_count": 0, "glycosylation_sites": [], "id": "P02775", "name": "Haptocorrin (Transcobalamin I)", "organism": "Homo sapiens", "uniprot_id": "P02775" }, { "function": "Primary vitamin B12-binding and transport protein. Delivers cobalamin to cells", "gene_name": "TCN2", "glycan_count": 0, "glycosylation_sites": [], "id": "P20062", "name": "Transcobalamin II", "organism": "Homo sapiens", "uniprot_id": "P20062" }, { "function": "Calcium-independent phospholipase involved in phospholipid remodeling with implications in cellular membrane homeostasis, mitochondrial integrity and signal transduction. Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 or sn-2 position of phospholipids (phospholipase A1 and A2 activity respectively), producing lysophospholipids that are used in deacylation-reacylation cycles (PubMed:10092647, PubMed:10336645, PubMed:20886109, PubMed:9417066). Hydrolyzes both saturated and unsaturated long fatty acyl chains in various glycerophospholipid classes such as phosphatidylcholines, phosphatidylethanolamines and phosphatidates, with a preference for hydrolysis at sn-2 position (PubMed:10092647, PubMed:10336645, PubMed:20886109). Can further hydrolyze lysophospholipids carrying saturated fatty acyl chains (lysophospholipase activity) (PubMed:20886109). Upon oxidative stress, contributes to remodeling of mitochondrial phospholipids in pancreatic beta cells, in a repair mechanism to reduce oxidized lipid content (PubMed:23533611). Preferentially hydrolyzes oxidized polyunsaturated fatty acyl chains from cardiolipins, yielding monolysocardiolipins that can be reacylated with unoxidized fatty acyls to regenerate native cardiolipin species (By similarity). Hydrolyzes oxidized glycerophosphoethanolamines present in pancreatic islets, releasing oxidized polyunsaturated fatty acids such as hydroxyeicosatetraenoates (HETEs) (By similarity). Has thioesterase activity toward fatty-acyl CoA releasing CoA-SH known to facilitate fatty acid transport and beta-oxidation in mitochondria particularly in skeletal muscle (PubMed:20886109). Plays a role in regulation of membrane dynamics and homeostasis. Selectively hydrolyzes sn-2 arachidonoyl group in plasmalogen phospholipids, structural components of lipid rafts and myelin (By similarity). Regulates F-actin polymerization at the pseudopods, which is required for both speed and directionality of MCP1/CCL2-induced monocyte chemotaxis (PubMed:18208975). Targets membrane phospholipids to produce potent lipid signaling messengers. Generates lysophosphatidate (LPA, 1-acyl-glycerol-3-phosphate), which acts via G-protein receptors in various cell types (By similarity). Has phospholipase A2 activity toward platelet-activating factor (PAF, 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine), likely playing a role in inactivation of this potent pro-inflammatory signaling lipid (By similarity). In response to glucose, amplifies calcium influx in pancreatic beta cells to promote INS secretion (By similarity)", "gene_name": "PLA2G6", "glycan_count": 0, "glycosylation_sites": [], "id": "O60733", "name": "PLA2G6", "organism": "Homo sapiens", "uniprot_id": "O60733" }, { "function": "G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling inhibits adenylate cyclase activity", "gene_name": "GRM4", "glycan_count": 0, "glycosylation_sites": [ { "position": 98, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 301, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 454, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 484, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 569, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6ZMQ2", "name": "TGM6", "organism": "Homo sapiens", "uniprot_id": "Q14833" }, { "function": "Scaffold protein of the presynaptic cytomatrix at the active zone (CAZ) which is the place in the synapse where neurotransmitter is released (PubMed:12812759). After synthesis, participates in the formation of Golgi-derived membranous organelles termed Piccolo-Bassoon transport vesicles (PTVs) that are transported along axons to sites of nascent synaptic contacts (PubMed:19380881). At the presynaptic active zone, regulates the spatial organization of synaptic vesicle cluster, the protein complexes that execute membrane fusion and compensatory endocytosis (By similarity). Also functions in processes other than assembly such as the regulation of specific presynaptic protein ubiquitination by interacting with SIAH1 or the regulation of presynaptic autophagy by associating with ATG5 (By similarity). Also mediates synapse to nucleus communication leading to reconfiguration of gene expression by associating with the transcriptional corepressor CTBP1 and by subsequently reducing the size of its pool available for nuclear import (By similarity). Inhibits the activity of the proportion of DAO enzyme that localizes to the presynaptic active zone, which may modulate synaptic transmission (By similarity)", "gene_name": "BSN", "glycan_count": 1, "glycosylation_sites": [ { "position": 1343, "type": "O-linked (GlcNAc) threonine" }, { "position": 1384, "type": "O-linked (GlcNAc) threonine" }, { "position": 2314, "type": "O-linked (GlcNAc) threonine" }, { "position": 2691, "type": "O-linked (GlcNAc) threonine" }, { "position": 2936, "type": "O-linked (GlcNAc) threonine" } ], "id": "Q9UPA5", "name": "BSN", "organism": "Homo sapiens", "uniprot_id": "Q9UPA5" }, { "function": "E3 ubiquitin-protein ligase involved in different protein quality control pathways in the cytoplasm (PubMed:25582440, PubMed:29033132, PubMed:34893540, PubMed:37891180, PubMed:38030679, PubMed:38182926, PubMed:38297121). Component of the N-end rule pathway: ubiquitinates proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their degradation (PubMed:34893540, PubMed:37891180, PubMed:38030679). Recognizes both type-1 and type-2 N-degrons, containing positively charged amino acids (Arg, Lys and His) and bulky and hydrophobic amino acids, respectively (PubMed:38030679). Does not ubiquitinate proteins that are acetylated at the N-terminus (PubMed:37891180). Together with UBR5, part of a cytoplasm protein quality control pathway that prevents protein aggregation by catalyzing assembly of heterotypic 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on aggregated proteins, leading to substrate recognition by the segregase p97/VCP and degradation by the proteasome: UBR4 probably synthesizes mixed chains containing multiple linkages, while UBR5 is likely branching multiple 'Lys-48'-linked chains of substrates initially modified (PubMed:29033132). Together with KCMF1, part of a protein quality control pathway that catalyzes ubiquitination and degradation of proteins that have been oxidized in response to reactive oxygen species (ROS): recognizes proteins with an Arg-CysO3(H) degron at the N-terminus, and mediates assembly of heterotypic 'Lys-63'-/'Lys-27'-linked branched ubiquitin chains on oxidized proteins, leading to their degradation by autophagy (PubMed:34893540). Catalytic component of the SIFI complex, a multiprotein complex required to inhibit the mitochondrial stress response after a specific stress event has been resolved: ubiquitinates and degrades (1) components of the HRI-mediated signaling of the integrated stress response, such as DELE1 and EIF2AK1/HRI, as well as (2) unimported mitochondrial precursors (PubMed:38297121). Within the SIFI complex, UBR4 initiates ubiquitin chain that are further elongated or branched by KCMF1 (PubMed:38297121). Mediates ubiquitination of ACLY, leading to its subsequent degradation (PubMed:23932781). Together with clathrin, forms meshwork structures involved in membrane morphogenesis and cytoskeletal organization (PubMed:16214886)", "gene_name": "UBR4", "glycan_count": 4, "glycosylation_sites": [], "id": "Q5T4S7", "name": "UBR4", "organism": "Homo sapiens", "uniprot_id": "Q5T4S7" }, { "function": "Acts as a cell adhesion ligand for skin epithelial cells and fibroblasts", "gene_name": "COL22A1", "glycan_count": 2, "glycosylation_sites": [ { "position": 375, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8NFW1", "name": "COL22A1", "organism": "Homo sapiens", "uniprot_id": "Q8NFW1" }, { "function": "Neural extracellular matrix (ECM) protein involved in interactions with different cells and matrix components. These interactions can influence cellular behavior by either evoking a stable adhesion and differentiation, or repulsion and inhibition of neurite growth. Binding to cell surface gangliosides inhibits RGD-dependent integrin-mediated cell adhesion and results in an inhibition of PTK2/FAK1 (FAK) phosphorylation and cell detachment. Binding to membrane surface sulfatides results in a oligodendrocyte adhesion and differentiation. Interaction with CNTN1 induces a repulsion of neurons and an inhibition of neurite outgrowth. Interacts with SCN2B may play a crucial role in clustering and regulation of activity of sodium channels at nodes of Ranvier. TNR-linked chondroitin sulfate glycosaminoglycans are involved in the interaction with FN1 and mediate inhibition of cell adhesion and neurite outgrowth. The highly regulated addition of sulfated carbohydrate structure may modulate the adhesive properties of TNR over the course of development and during synapse maintenance (By similarity)", "gene_name": "TNR", "glycan_count": 2, "glycosylation_sites": [ { "position": 36, "type": "O-linked (GalNAc...) threonine" }, { "position": 37, "type": "O-linked (GalNAc...) threonine" }, { "position": 55, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 176, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 180, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 198, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 271, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 278, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 302, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 392, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 470, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 581, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 791, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 874, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1036, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1046, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1261, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q92752", "name": "TNR", "organism": "Homo sapiens", "uniprot_id": "Q92752" }, { "function": "Histone methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also weakly methylates 'Lys-27' of histone H3 (H3K27me). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. During G0 phase, it probably contributes to silencing of MYC- and E2F-responsive genes, suggesting a role in G0/G1 transition in cell cycle. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53. Represses the expression of mitochondrial function-related genes, perhaps by occupying their promoter regions, working in concert with probable chromatin reader BAZ2B (By similarity)", "gene_name": "EHMT1", "glycan_count": 5, "glycosylation_sites": [], "id": "Q9H9B1", "name": "CREG2", "organism": "Homo sapiens", "uniprot_id": "Q9H9B1" }, { "function": "Binds to and activates protein kinase PAK1 (PubMed:11459829). Plays a role in the regulation of cell morphology, cytoskeletal organization and focal adhesion assembly during cell migration (PubMed:11459829, PubMed:17620058, PubMed:18086875, PubMed:21834987). Also stimulates quiescent cells to reenter the cell cycle (PubMed:11459829). Has no detectable GTPase activity but its high intrinsic guanine nucleotide exchange activity suggests it is constitutively GTP-bound (PubMed:16472646)", "gene_name": "RHOU", "glycan_count": 0, "glycosylation_sites": [], "id": "Q7L0Q8", "name": "RHOF", "organism": "Homo sapiens", "uniprot_id": "Q7L0Q8" }, { "function": "Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides. In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. Involved in prostate tumor progression", "gene_name": "FOLH1", "glycan_count": 43, "glycosylation_sites": [ { "position": 51, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 76, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 121, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 140, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 153, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 195, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 336, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 459, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 476, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 638, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q04609", "name": "Prostate-specific membrane antigen (PSMA)", "organism": "Homo sapiens", "uniprot_id": "Q04609" }, { "function": "Growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration and also has effects on the permeability of blood vessels. May function in angiogenesis of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentiated lymphatic endothelium in adults. Binds and activates KDR/VEGFR2 and FLT4/VEGFR3 receptors", "gene_name": "VEGFC", "glycan_count": 3, "glycosylation_sites": [ { "position": 175, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 205, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 240, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P49767", "name": "Vascular endothelial growth factor C (VEGF-C)", "organism": "Homo sapiens", "uniprot_id": "P49767" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P05556/P05106", "name": "Integrin alpha-V beta-3 (\u03b1V\u03b23)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "AMY2A", "glycan_count": 1, "glycosylation_sites": [ { "position": 476, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P04746", "name": "Alanine transaminase (ALT)", "organism": "Homo sapiens", "uniprot_id": "P04746" }, { "function": "Transcription factor that plays a key role in the response to oxidative stress: binds to antioxidant response (ARE) elements present in the promoter region of many cytoprotective genes, such as phase 2 detoxifying enzymes, and promotes their expression, thereby neutralizing reactive electrophiles (PubMed:11035812, PubMed:19489739, PubMed:29018201, PubMed:31398338). In normal conditions, ubiquitinated and degraded in the cytoplasm by the BCR(KEAP1) complex (PubMed:11035812, PubMed:15601839, PubMed:29018201). In response to oxidative stress, electrophile metabolites inhibit activity of the BCR(KEAP1) complex, promoting nuclear accumulation of NFE2L2/NRF2, heterodimerization with one of the small Maf proteins and binding to ARE elements of cytoprotective target genes (PubMed:19489739, PubMed:29590092). The NFE2L2/NRF2 pathway is also activated in response to selective autophagy: autophagy promotes interaction between KEAP1 and SQSTM1/p62 and subsequent inactivation of the BCR(KEAP1) complex, leading to NFE2L2/NRF2 nuclear accumulation and expression of cytoprotective genes (PubMed:20452972). The NFE2L2/NRF2 pathway is also activated during the unfolded protein response (UPR), contributing to redox homeostasis and cell survival following endoplasmic reticulum stress (By similarity). May also be involved in the transcriptional activation of genes of the beta-globin cluster by mediating enhancer activity of hypersensitive site 2 of the beta-globin locus control region (PubMed:7937919). Also plays an important role in the regulation of the innate immune response and antiviral cytosolic DNA sensing. It is a critical regulator of the innate immune response and survival during sepsis by maintaining redox homeostasis and restraint of the dysregulation of pro-inflammatory signaling pathways like MyD88-dependent and -independent and TNF-alpha signaling (By similarity). Suppresses macrophage inflammatory response by blocking pro-inflammatory cytokine transcription and the induction of IL6 (By similarity). Binds to the proximity of pro-inflammatory genes in macrophages and inhibits RNA Pol II recruitment. The inhibition is independent of the NRF2-binding motif and reactive oxygen species level (By similarity). Represses antiviral cytosolic DNA sensing by suppressing the expression of the adapter protein STING1 and decreasing responsiveness to STING1 agonists while increasing susceptibility to infection with DNA viruses (PubMed:30158636). Once activated, limits the release of pro-inflammatory cytokines in response to human coronavirus SARS-CoV-2 infection and to virus-derived ligands through a mechanism that involves inhibition of IRF3 dimerization. Also inhibits both SARS-CoV-2 replication, as well as the replication of several other pathogenic viruses including Herpes Simplex Virus-1 and-2, Vaccinia virus, and Zika virus through a type I interferon (IFN)-independent mechanism (PubMed:33009401)", "gene_name": "NFE2L2", "glycan_count": 1, "glycosylation_sites": [ { "position": 462, "type": "N-linked (Glc) (glycation) lysine" }, { "position": 472, "type": "N-linked (Glc) (glycation) lysine" }, { "position": 487, "type": "N-linked (Glc) (glycation) lysine" }, { "position": 499, "type": "N-linked (Glc) (glycation) arginine" }, { "position": 569, "type": "N-linked (Glc) (glycation) arginine" }, { "position": 574, "type": "N-linked (Glc) (glycation) lysine" } ], "id": "Q16236", "name": "Nuclear factor erythroid 2-related factor 2 (Nrf2)", "organism": "Homo sapiens", "uniprot_id": "Q16236" }, { "function": "Integrin alpha-IIb/beta-3 is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. It recognizes the sequence R-G-D in a wide array of ligands. It recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain (By similarity). Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen (PubMed:9111081). This step leads to rapid platelet aggregation which physically plugs ruptured endothelial cell surface (By similarity)", "gene_name": "ITGA2B", "glycan_count": 4, "glycosylation_sites": [ { "position": 46, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 280, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 601, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 711, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 874, "type": "O-linked (GalNAc...) serine; in variant S-874" }, { "position": 878, "type": "O-linked (GalNAc...) serine" }, { "position": 962, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08514", "name": "Glycoprotein IIb/IIIa", "organism": "Homo sapiens", "uniprot_id": "P08514" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "various (e.g., MMP-9: P14780)", "name": "Matrix Metalloproteinases (MMPs)", "organism": "", "uniprot_id": "" }, { "function": "Binds CpG islands in promoters where the DNA is methylated at position 5 of cytosine within CpG dinucleotides (PubMed:9774669). Binds hemimethylated DNA as well (PubMed:10947852, PubMed:24307175). Recruits histone deacetylases and DNA methyltransferases to chromatin (PubMed:10471499, PubMed:10947852). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:16428440, PubMed:28977666). Acts as a transcriptional repressor and plays a role in gene silencing (PubMed:10471499, PubMed:10947852, PubMed:16415179). Functions as a scaffold protein, targeting GATAD2A and GATAD2B to chromatin to promote repression (PubMed:16415179). May enhance the activation of some unmethylated cAMP-responsive promoters (PubMed:12665568)", "gene_name": "MBD2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UBB5", "name": "Transcriptional intermediary factor 1-gamma (TIF1-\u03b3)", "organism": "Homo sapiens", "uniprot_id": "Q9UBB5" }, { "function": "Cleaves the vWF multimers in plasma into smaller forms thereby controlling vWF-mediated platelet thrombus formation", "gene_name": "ADAMTS13", "glycan_count": 16, "glycosylation_sites": [ { "position": 142, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 146, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 387, "type": "C-linked (Man) tryptophan" }, { "position": 399, "type": "O-linked (Fuc...) serine" }, { "position": 552, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 579, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 614, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 667, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 698, "type": "O-linked (Fuc...) serine" }, { "position": 707, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 757, "type": "O-linked (Fuc...) serine" }, { "position": 828, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 907, "type": "O-linked (Fuc...) serine" }, { "position": 965, "type": "O-linked (Fuc...) serine" }, { "position": 1027, "type": "O-linked (Fuc...) serine" }, { "position": 1087, "type": "O-linked (Fuc...) serine" }, { "position": 1235, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1354, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q76LX8", "name": "ADAMTS13", "organism": "Homo sapiens", "uniprot_id": "Q76LX8" }, { "function": "Trimeric GP1,2 complexes form the virion surface spikes and mediate the viral entry processes, with GP1 acting as the receptor-binding subunit and GP2 as the membrane fusion subunit. At later times of infection, down-regulates the expression of various host cell surface molecules that are essential for immune surveillance and cell adhesion (PubMed:11836430). Down-modulates several integrins including ITGA1, ITGA2, ITGA3, ITGA4, ITGA5, ITGA6, ITGAV and ITGB1 (PubMed:11112476). This decrease in cell adhesion molecules may lead to cell detachment, contributing to the disruption of blood vessel integrity and hemorrhages developed during infection (cytotoxicity) (Probable). Interacts with host TLR4 and thereby stimulates the differentiation and activation of monocytes leading to bystander death of T-lymphocytes (PubMed:28542576). Down-regulates as well the function of host natural killer cells (PubMed:30013549). Counteracts the antiviral effect of host BST2/tetherin that restricts release of progeny virions from infected cells (PubMed:26516900, PubMed:27707924, PubMed:29669839). However, cooperates with VP40 and host BST2 to activate canonical NF-kappa-B pathway in a manner dependent on neddylation (PubMed:28878074)", "gene_name": "GP", "glycan_count": 0, "glycosylation_sites": [ { "position": 40, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 204, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 228, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 238, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 257, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 268, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 296, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 317, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 333, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 346, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 386, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 413, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 436, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 454, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 462, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 563, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 618, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "Q05320", "name": "Ebola virus soluble glycoprotein (sGP)", "organism": "Zaire ebolavirus (strain Mayinga-76)", "uniprot_id": "Q05320" }, { "function": "Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection (By similarity). Interacts with host DPP4 to mediate virla entry", "gene_name": "S", "glycan_count": 0, "glycosylation_sites": [ { "position": 66, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 104, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 125, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 155, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 166, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 222, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 236, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 244, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 410, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 487, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 592, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 619, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 719, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 774, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 785, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 870, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1176, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1213, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1225, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1241, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1256, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1277, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1288, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "K9N5Q8", "name": "MERS-CoV spike protein", "organism": "Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012)", "uniprot_id": "K9N5Q8" }, { "function": "Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway (PubMed:23522008)", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [ { "position": 183, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 347, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 433, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 905, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 982, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1134, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1174, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 2301, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 2305, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 2457, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P29990", "name": "Dengue virus envelope protein (E-protein)", "organism": "Dengue virus type 2 (strain Thailand/16681/1984)", "uniprot_id": "P29990" }, { "function": "Plays a role in virus budding by binding to the host cell membrane and packages the viral RNA into a nucleocapsid that forms the core of the mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Inhibits the integrated stress response (ISR) in the infected cell (By similarity)", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [ { "position": 192, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 920, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 997, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "Q32ZE1", "name": "Zika virus envelope protein", "organism": "Zika virus", "uniprot_id": "Q32ZE1" }, { "function": "Methyltransferase: Displays a capping enzyme activity. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. The enzymatic reaction involves a covalent link between 7-methyl-GMP and the methyltransferase, whereas eukaryotic capping enzymes form a covalent complex only with GMP. Methyltransferase catalyzes transfer of a methyl group from S-adenosylmethionine to GTP and GDP to yield m(7)GTP or m(7)GDP. GDP is a better substrate than GTP. This enzyme also displays guanylyltransferase activity to form a covalent complex, methyltransferase-m(7)GMP, from which 7-methyl-GMP is transferred to the mRNA to create the cap structure", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6J8G2", "name": "Hepatitis E virus capsid protein", "organism": "Hepatitis E virus genotype 3 (isolate Swine/United States/swUS1)", "uniprot_id": "Q6J8G2" }, { "function": "A 50S ribosomal subunit assembly protein with GTPase activity, required for 50S subunit assembly at low temperatures, may also play a role in translation. Binds GTP and analogs. Binds the 70S ribosome between the 30S and 50S subunits, in a similar position as ribosome-bound EF-G; it contacts a number of ribosomal proteins, both rRNAs and the A-site tRNA", "gene_name": "bipA", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9ZLZ3", "name": "HopQ", "organism": "Helicobacter pylori (strain J99 / ATCC 700824)", "uniprot_id": "Q9ZLZ3" }, { "function": "May be necessary for the transcription, folding, export, or function of the cytotoxin", "gene_name": "cagA", "glycan_count": 0, "glycosylation_sites": [], "id": "P55980", "name": "CagA", "organism": "Helicobacter pylori (strain ATCC 700392 / 26695)", "uniprot_id": "P55980" }, { "function": "Common junctional plaque protein. The membrane-associated plaques are architectural elements in an important strategic position to influence the arrangement and function of both the cytoskeleton and the cells within the tissue. The presence of plakoglobin in both the desmosomes and in the intermediate junctions suggests that it plays a central role in the structure and function of submembranous plaques. Acts as a substrate for VE-PTP and is required by it to stimulate VE-cadherin function in endothelial cells. Can replace beta-catenin in E-cadherin/catenin adhesion complexes which are proposed to couple cadherins to the actin cytoskeleton (By similarity)", "gene_name": "JUP", "glycan_count": 12, "glycosylation_sites": [ { "position": 14, "type": "O-linked (GlcNAc) threonine" } ], "id": "P14923", "name": "gp210", "organism": "Homo sapiens", "uniprot_id": "P14923" }, { "function": "Together with PML, this tumor suppressor is a major constituent of the PML bodies, a subnuclear organelle involved in a large number of physiological processes including cell growth, differentiation and apoptosis. Functions as a transcriptional coactivator of ETS1 and ETS2 according to PubMed:11909962. Under certain conditions, it may also act as a corepressor of ETS1 preventing its binding to DNA according to PubMed:15247905. Through the regulation of ETS1 it may play a role in angiogenesis, controlling endothelial cell motility and invasion. Through interaction with the MRN complex it may be involved in the regulation of telomeres lengthening. May also regulate TP53-mediated transcription and through CASP8AP2, regulate FAS-mediated apoptosis. Also plays a role in infection by viruses, including human cytomegalovirus and Epstein-Barr virus, through mechanisms that may involve chromatin and/or transcriptional regulation", "gene_name": "SP100", "glycan_count": 2, "glycosylation_sites": [], "id": "P23497", "name": "sp100", "organism": "Homo sapiens", "uniprot_id": "P23497" }, { "function": "Component of the nuclear body, also known as nuclear domain 10, PML oncogenic domain, and KR body (PubMed:8910577). May be involved in the pathogenesis of acute promyelocytic leukemia and viral infection (PubMed:8910577). May play a role in chromatin-mediated regulation of gene expression although it does not bind to histone H3 tails (PubMed:24267382)", "gene_name": "SP140", "glycan_count": 0, "glycosylation_sites": [], "id": "Q13342", "name": "sp140", "organism": "Homo sapiens", "uniprot_id": "Q13342" }, { "function": "Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate", "gene_name": "LTF", "glycan_count": 254, "glycosylation_sites": [ { "position": 156, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 497, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 642, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 10, "type": "O-linked (GlcNAc) serine; alternate" } ], "id": "P02788", "name": "Lactoferrin", "organism": "Homo sapiens", "uniprot_id": "P02788" }, { "function": "Hormone that seems to suppress insulin ability to stimulate glucose uptake into adipose cells (By similarity). Potentially links obesity to diabetes (By similarity). Promotes chemotaxis in myeloid cells (PubMed:15064728)", "gene_name": "RETN", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9HD89", "name": "Resistin", "organism": "Homo sapiens", "uniprot_id": "Q9HD89" }, { "function": "Nicotinamide/nicotinate-nucleotide adenylyltransferase that acts as an axon maintenance factor (By similarity). Axon survival factor required for the maintenance of healthy axons: acts by delaying Wallerian axon degeneration, an evolutionarily conserved process that drives the loss of damaged axons (By similarity). Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP (PubMed:16118205, PubMed:17402747). Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate but with a lower efficiency (PubMed:16118205, PubMed:17402747). Cannot use triazofurin monophosphate (TrMP) as substrate (PubMed:16118205, PubMed:17402747). Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+) (PubMed:16118205, PubMed:17402747). For the pyrophosphorolytic activity prefers NAD(+), NADH and NaAD as substrates and degrades nicotinic acid adenine dinucleotide phosphate (NHD) less effectively (PubMed:16118205, PubMed:17402747). Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NaADP(+) (PubMed:16118205, PubMed:17402747). Also acts as an activator of ADP-ribosylation by supporting the catalytic activity of PARP16 and promoting mono-ADP-ribosylation of ribosomes by PARP16 (PubMed:34314702). May be involved in the maintenance of axonal integrity (By similarity)", "gene_name": "NMNAT2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9BZQ4", "name": "CRPPA (CDP-L-ribitol pyrophosphorylase A)", "organism": "Homo sapiens", "uniprot_id": "Q9BZQ4" }, { "function": "Component of a complex that binds and activates STK11/LKB1. In the complex, required to stabilize the interaction between CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta) and STK11/LKB1 (By similarity)", "gene_name": "CAB39L", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H9S4", "name": "FKRP (Fukutin-related protein)", "organism": "Homo sapiens", "uniprot_id": "Q9H9S4" }, { "function": "The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specificity and liver tropism. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis. The large envelope protein also assures fusion between virion membrane and endosomal membrane. In its internal conformation the protein plays a role in virion morphogenesis and mediates the contact with the nucleocapsid like a matrix protein", "gene_name": "S", "glycan_count": 0, "glycosylation_sites": [ { "position": 320, "type": "N-linked (GlcNAc...) asparagine; by host; partial" }, { "position": 4, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P03141", "name": "Hepatitis B e antigen (HBeAg)", "organism": "Hepatitis B virus genotype A2 subtype adw2 (strain Rutter 1979)", "uniprot_id": "P03141" }, { "function": "Self assembles to form an icosahedral capsid. Most capsids appear to be large particles with an icosahedral symmetry of T=4 and consist of 240 copies of capsid protein, though a fraction forms smaller T=3 particles consisting of 180 capsid proteins. Entering capsids are transported along microtubules to the nucleus. Phosphorylation of the capsid is thought to induce exposure of nuclear localization signal in the C-terminal portion of the capsid protein that allows binding to the nuclear pore complex via the importin (karyopherin-) alpha and beta. Capsids are imported in intact form through the nuclear pore into the nuclear basket, where it probably binds NUP153. Only capsids that contain the mature viral genome can release the viral DNA and capsid protein into the nucleoplasm. Immature capsids get stuck in the basket. Capsids encapsulate the pre-genomic RNA and the P protein. Pre-genomic RNA is reverse-transcribed into DNA while the capsid is still in the cytoplasm. The capsid can then either be directed to the nucleus, providing more genomes for transcription, or bud through the endoplasmic reticulum to provide new virions", "gene_name": "C", "glycan_count": 0, "glycosylation_sites": [], "id": "P03146", "name": "HBV core antigen (HBcAg)", "organism": "Hepatitis B virus genotype D subtype ayw (isolate France/Tiollais/1979)", "uniprot_id": "P03146" }, { "function": "Indispensable for the control of thyroid structure and metabolism", "gene_name": "TSHB", "glycan_count": 7, "glycosylation_sites": [ { "position": 43, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01222", "name": "Thyroid stimulating hormone (TSH)", "organism": "Homo sapiens", "uniprot_id": "P01222" }, { "function": "Stimulates the adrenal glands to release cortisol", "gene_name": "POMC", "glycan_count": 0, "glycosylation_sites": [ { "position": 71, "type": "O-linked (HexNAc...) threonine" }, { "position": 91, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01189", "name": "Adrenocorticotropic hormone (ACTH)", "organism": "Homo sapiens", "uniprot_id": "P01189" }, { "function": "Tyrosine-protein kinase that plays an essential role as cell surface receptor for neuregulins. Binds to neuregulin-1 (NRG1) and is activated by it; ligand-binding increases phosphorylation on tyrosine residues and promotes its association with the p85 subunit of phosphatidylinositol 3-kinase (PubMed:20682778). May also be activated by CSPG5 (PubMed:15358134). Involved in the regulation of myeloid cell differentiation (PubMed:27416908)", "gene_name": "ERBB3", "glycan_count": 21, "glycosylation_sites": [ { "position": 126, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 250, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 353, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 408, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 414, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 437, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 469, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 522, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 566, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 616, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P21860", "name": "HER3 (Human Epidermal Growth Factor Receptor 3)", "organism": "Homo sapiens", "uniprot_id": "P21860" }, { "function": "", "gene_name": "xprt", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9U6Y2", "name": "Echinococcus granulosus Antigen B", "organism": "Leishmania donovani", "uniprot_id": "Q9U6Y2" }, { "function": "Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability. Involved in the behavioral responses to ethyl acetate, anisole, hexanoic acid, and pyrazines", "gene_name": "Or59a", "glycan_count": 0, "glycosylation_sites": [ { "position": 62, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9U6Y1", "name": "Echinococcus granulosus Antigen 5", "organism": "Drosophila melanogaster", "uniprot_id": "P81923" }, { "function": "Tetrodotoxin-resistant channel that mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which sodium ions may pass in accordance with their electrochemical gradient. Plays a role in neuropathic pain mechanisms", "gene_name": "SCN10A", "glycan_count": 1, "glycosylation_sites": [ { "position": 284, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 288, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 312, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 335, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 819, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1312, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1328, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1336, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1686, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y5Y9", "name": "Na v 1.8 (SCN10A)", "organism": "Homo sapiens", "uniprot_id": "Q9Y5Y9" }, { "function": "Mediates the Na(+)-independent uptake of organic anions (PubMed:10358072, PubMed:15159445, PubMed:17412826). Shows broad substrate specificity, can transport both organic anions such as bile acid taurocholate (cholyltaurine) and conjugated steroids (dehydroepiandrosterone 3-sulfate, 17-beta-glucuronosyl estradiol, and estrone 3-sulfate), as well as eicosanoids (prostaglandin E2, thromboxane B2, leukotriene C4, and leukotriene E4), and thyroid hormones (T4/L-thyroxine, and T3/3,3',5'-triiodo-L-thyronine) (PubMed:10358072, PubMed:10601278, PubMed:10873595, PubMed:11159893, PubMed:12196548, PubMed:12568656, PubMed:15159445, PubMed:15970799, PubMed:16627748, PubMed:17412826, PubMed:19129463, PubMed:26979622). Can take up bilirubin glucuronides from plasma into the liver, contributing to the detoxification-enhancing liver-blood shuttling loop (PubMed:22232210). Involved in the clearance of endogenous and exogenous substrates from the liver (PubMed:10358072, PubMed:10601278). Transports coproporphyrin I and III, by-products of heme synthesis, and may be involved in their hepatic disposition (PubMed:26383540). May contribute to regulate the transport of organic compounds in testes across the blood-testis-barrier (Probable). Can transport HMG-CoA reductase inhibitors (also known as statins), such as pravastatin and pitavastatin, a clinically important class of hypolipidemic drugs (PubMed:10601278, PubMed:15159445, PubMed:15970799). May play an important role in plasma and tissue distribution of the structurally diverse chemotherapeutic drug methotrexate (PubMed:23243220). May also transport antihypertension agents, such as the angiotensin-converting enzyme (ACE) inhibitor prodrug enalapril, and the highly selective angiotensin II AT1-receptor antagonist valsartan, in the liver (PubMed:16624871, PubMed:16627748). Shows a pH-sensitive substrate specificity towards prostaglandin E2 and T4 which may be ascribed to the protonation state of the binding site and leads to a stimulation of substrate transport in an acidic microenvironment (PubMed:19129463). Hydrogencarbonate/HCO3(-) acts as the probable counteranion that exchanges for organic anions (PubMed:19129463)", "gene_name": "SLCO1B1", "glycan_count": 3, "glycosylation_sites": [ { "position": 130, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 134, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 432, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 503, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 516, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 617, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y6L6", "name": "OATP1B1 (SLCO1B1)", "organism": "Homo sapiens", "uniprot_id": "Q9Y6L6" }, { "function": "Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CCL2, CCL8, CCL13, CCL19, CCL21 and CCL25. Chemokine-binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalization. Plays an important role in controlling the migration of immune and cancer cells that express chemokine receptors CCR7 and CCR9, by reducing the availability of CCL19, CCL21, and CCL25 through internalization. Negatively regulates CXCR3-induced chemotaxis. Regulates T-cell development in the thymus", "gene_name": "ACKR4", "glycan_count": 0, "glycosylation_sites": [ { "position": 6, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 19, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NPB9", "name": "OATP1B3 (SLCO1B3)", "organism": "Homo sapiens", "uniprot_id": "Q9NPB9" }, { "function": "Promotes guanine-nucleotide exchange on ARF1 and ARF5. Promotes the activation of ARF factors through replacement of GDP with GTP", "gene_name": "CYTH4", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UIA0", "name": "OAT3 (SLC22A8)", "organism": "Homo sapiens", "uniprot_id": "Q9UIA0" }, { "function": "Secondary active transporter that functions as a Na(+)-independent organic anion (OA)/dicarboxylate antiporter where the uptake of one molecule of OA into the cell is coupled with an efflux of one molecule of intracellular dicarboxylate such as 2-oxoglutarate or glutarate (PubMed:11669456, PubMed:11907186, PubMed:14675047, PubMed:22108572, PubMed:23832370, PubMed:28534121, PubMed:9950961). Mediates the uptake of OA across the basolateral side of proximal tubule epithelial cells, thereby contributing to the renal elimination of endogenous OA from the systemic circulation into the urine (PubMed:9887087). Functions as a biopterin transporters involved in the uptake and the secretion of coenzymes tetrahydrobiopterin (BH4), dihydrobiopterin (BH2) and sepiapterin to urine, thereby determining baseline levels of blood biopterins (PubMed:28534121). Transports prostaglandin E2 (PGE2) and prostaglandin F2-alpha (PGF2-alpha) and may contribute to their renal excretion (PubMed:11907186). Also mediates the uptake of cyclic nucleotides such as cAMP and cGMP (PubMed:26377792). Involved in the transport of neuroactive tryptophan metabolites kynurenate (KYNA) and xanthurenate (XA) and may contribute to their secretion from the brain (PubMed:22108572, PubMed:23832370). May transport glutamate (PubMed:26377792). Also involved in the disposition of uremic toxins and potentially toxic xenobiotics by the renal organic anion secretory pathway, helping reduce their undesired toxicological effects on the body (PubMed:11669456, PubMed:14675047). Uremic toxins include the indoxyl sulfate (IS), hippurate/N-benzoylglycine (HA), indole acetate (IA), 3-carboxy-4- methyl-5-propyl-2-furanpropionate (CMPF) and urate (PubMed:14675047, PubMed:26377792). Xenobiotics include the mycotoxin ochratoxin (OTA) (PubMed:11669456). May also contribute to the transport of organic compounds in testes across the blood-testis-barrier (PubMed:35307651)", "gene_name": "SLC22A6", "glycan_count": 0, "glycosylation_sites": [ { "position": 39, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 56, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 92, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 97, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 113, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q4U2R8", "name": "OAT1 (SLC22A6)", "organism": "Homo sapiens", "uniprot_id": "Q4U2R8" }, { "function": "Electrogenic voltage-dependent transporter that mediates the transport of a variety of organic cations such as endogenous bioactive amines, cationic drugs and xenobiotics (PubMed:9260930, PubMed:9687576). Functions as a Na(+)-independent, bidirectional uniporter (PubMed:21128598, PubMed:9687576). Cation cellular uptake or release is driven by the electrochemical potential, i.e. membrane potential and concentration gradient (PubMed:15212162, PubMed:9260930, PubMed:9687576). However, may also engage electroneutral cation exchange when saturating concentrations of cation substrates are reached (By similarity). Predominantly expressed at the basolateral membrane of hepatocytes and proximal tubules and involved in the uptake and disposition of cationic compounds by hepatic and renal clearance from the blood flow (PubMed:15783073). Implicated in monoamine neurotransmitters uptake such as histamine, dopamine, adrenaline/epinephrine, noradrenaline/norepinephrine, serotonin and tyramine, thereby supporting a physiological role in the central nervous system by regulating interstitial concentrations of neurotransmitters (PubMed:16581093, PubMed:17460754, PubMed:9687576). Also capable of transporting dopaminergic neuromodulators cyclo(his-pro), salsolinol and N-methyl-salsolinol, thereby involved in the maintenance of dopaminergic cell integrity in the central nervous system (PubMed:17460754). Mediates the bidirectional transport of acetylcholine (ACh) at the apical membrane of ciliated cell in airway epithelium, thereby playing a role in luminal release of ACh from bronchial epithelium (PubMed:15817714). Also transports guanidine and endogenous monoamines such as vitamin B1/thiamine, creatinine and N-1-methylnicotinamide (NMN) (PubMed:12089365, PubMed:15212162, PubMed:17072098, PubMed:24961373, PubMed:9260930). Mediates the uptake and efflux of quaternary ammonium compound choline (PubMed:9260930). Mediates the bidirectional transport of polyamine agmatine and the uptake of polyamines putrescine and spermidine (PubMed:12538837, PubMed:21128598). Able to transport non-amine endogenous compounds such as prostaglandin E2 (PGE2) and prostaglandin F2-alpha (PGF2-alpha) (PubMed:11907186). Also involved in the uptake of xenobiotic 4-(4-(dimethylamino)styryl)-N-methylpyridinium (ASP) (PubMed:12395288, PubMed:16394027). May contribute to regulate the transport of organic compounds in testis across the blood-testis-barrier (Probable)", "gene_name": "SLC22A2", "glycan_count": 0, "glycosylation_sites": [ { "position": 72, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O15244", "name": "OCT2 (SLC22A2)", "organism": "Homo sapiens", "uniprot_id": "O15244" }, { "function": "Multidrug efflux pump that functions as a H(+)/organic cation antiporter (PubMed:16330770, PubMed:17509534). Plays a physiological role in the excretion of cationic compounds including endogenous metabolites, drugs, toxins through the kidney and liver, into urine and bile respectively (PubMed:16330770, PubMed:17495125, PubMed:17509534, PubMed:17582384, PubMed:18305230, PubMed:19158817, PubMed:21128598, PubMed:24961373). Mediates the efflux of endogenous compounds such as creatinine, vitamin B1/thiamine, agmatine and estrone-3-sulfate (PubMed:16330770, PubMed:17495125, PubMed:17509534, PubMed:17582384, PubMed:18305230, PubMed:19158817, PubMed:21128598, PubMed:24961373). May also contribute to regulate the transport of cationic compounds in testis across the blood-testis-barrier (Probable)", "gene_name": "SLC47A1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q96FL8", "name": "MATE1 (SLC47A1)", "organism": "Homo sapiens", "uniprot_id": "Q96FL8" }, { "function": "Symporter that cotransports neutral amino acids and sodium ions, coupled to an H(+) antiporter activity (PubMed:11243884). Releases L-glutamine and glycine from astroglial cells and may participate in the glutamate/GABA-L-glutamine cycle and the NMDA receptors activation (By similarity). In addition, contributes significantly to L-glutamine uptake in retina, namely in ganglion and Mueller cells therefore, participates in the retinal glutamate-glutamine cycle (By similarity). The transport activity is pH sensitive and Li(+) tolerant (PubMed:11243884). Moreover functions in both direction and is associated with large uncoupled fluxes of protons (By similarity). The transport is electroneutral coupled to the cotransport of 1 Na(+) and the antiport of 1 H(+) (By similarity). May have a particular importance for modulation of net hepatic glutamine flux (By similarity)", "gene_name": "SLC38A5", "glycan_count": 0, "glycosylation_sites": [ { "position": 226, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8WUX1", "name": "MATE2/K (SLC47A2)", "organism": "Homo sapiens", "uniprot_id": "Q8WUX1" }, { "function": "Lipase that primarily hydrolyzes triglycerides and galactosylglycerides (PubMed:15287741, PubMed:17401110, PubMed:18702514, PubMed:19451396, PubMed:20083229, PubMed:21865348, PubMed:26494624). In neonates, may play a major role in pancreatic digestion of dietary fats such as milk fat globules enriched in long-chain triglycerides (PubMed:19824014, PubMed:21652702, PubMed:23732775). Hydrolyzes short-, medium- and long-chain fatty acyls in triglycerides without apparent positional specificity (PubMed:15287741, PubMed:17401110, PubMed:18702514, PubMed:21652702, PubMed:21865348). Can completely deacylate triacylglycerols (PubMed:21865348). When the liver matures and bile salt synthesis increases, likely functions mainly as a galactolipase and monoacylglycerol lipase. Hydrolyzes monogalactosyldiglycerols (MGDG) and digalactosyldiacylglycerols (DGDG) present in a plant-based diet, releasing long-chain polyunsaturated fatty acids (PubMed:15287741, PubMed:17401110, PubMed:18702514, PubMed:20083229, PubMed:26494624). Hydrolyzes medium- and long-chain fatty acyls in galactolipids (PubMed:18702514, PubMed:20083229). May act together with LIPF to hydrolyze partially digested triglycerides (PubMed:23732775). Hydrolyzes long-chain monoglycerides with high efficiency (PubMed:17401110, PubMed:21652702, PubMed:23732775). In cytotoxic T cells, contributes to perforin-dependent cell lysis, but is unlikely to mediate direct cytotoxicity (By similarity). Also has low phospholipase activity (PubMed:17401110, PubMed:18702514). In neurons, required for the localization of the phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) to neurite tips through acyl chain remodeling of membrane phospholipids (By similarity). The resulting OPPC-rich lipid membrane domain recruits the t-SNARE protein STX4 by selectively interacting with the STX4 transmembrane domain and this promotes surface expression of the dopamine transporter SLC6A3/DAT at neurite tips by facilitating fusion of SLC6A3-containing transport vesicles with the plasma membrane (By similarity)", "gene_name": "PNLIPRP2", "glycan_count": 0, "glycosylation_sites": [ { "position": 353, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 428, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P54317", "name": "Lipase", "organism": "Homo sapiens", "uniprot_id": "P54317" }, { "function": "Troponin I is the inhibitory subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity", "gene_name": "TNNI2", "glycan_count": 0, "glycosylation_sites": [], "id": "P48788", "name": "Fast skeletal muscle troponin I (TNNI2)", "organism": "Homo sapiens", "uniprot_id": "P48788" }, { "function": "Muscle contraction", "gene_name": "MYH8", "glycan_count": 0, "glycosylation_sites": [], "id": "P13535", "name": "Myosin heavy chain 2 (MYH2)", "organism": "Homo sapiens", "uniprot_id": "P13535" }, { "function": "Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore", "gene_name": "HA", "glycan_count": 0, "glycosylation_sites": [ { "position": 24, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 38, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 54, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 97, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 181, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 301, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 499, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P03437", "name": "Hemagglutinin (HA)", "organism": "Influenza A virus (strain A/Aichi/2/1968 H3N2)", "uniprot_id": "P03437" }, { "function": "Component of intercellular desmosome junctions (PubMed:34368962). Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion (PubMed:19717567)", "gene_name": "DSG1", "glycan_count": 2, "glycosylation_sites": [ { "position": 36, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 110, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 180, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q02413", "name": "Desmoglein-1 (Dsg1)", "organism": "Homo sapiens", "uniprot_id": "Q02413" }, { "function": "Component of the cornified envelope of keratinocytes. May link the cornified envelope to desmosomes and intermediate filaments", "gene_name": "EVPL", "glycan_count": 1, "glycosylation_sites": [], "id": "Q92817", "name": "Envoplakin (EVPL)", "organism": "Homo sapiens", "uniprot_id": "Q92817" }, { "function": "Major high molecular weight protein of desmosomes. Regulates profibrotic gene expression in cardiomyocytes via activation of the MAPK14/p38 MAPK signaling cascade and increase in TGFB1 protein abundance (By similarity)", "gene_name": "DSP", "glycan_count": 3, "glycosylation_sites": [], "id": "P15924", "name": "Desmoplakin (DSP)", "organism": "Homo sapiens", "uniprot_id": "P15924" }, { "function": "Component of the cornified envelope of keratinocytes. May link the cornified envelope to desmosomes and intermediate filaments. May act as a localization signal in PKB/AKT-mediated signaling", "gene_name": "PPL", "glycan_count": 1, "glycosylation_sites": [], "id": "O60437", "name": "Periplakin (PPL)", "organism": "Homo sapiens", "uniprot_id": "O60437" }, { "function": "", "gene_name": "DST", "glycan_count": 2, "glycosylation_sites": [], "id": "Q03001-7", "name": "Bullous Pemphigoid Antigen 1 (BP230)", "organism": "Homo sapiens", "uniprot_id": "Q03001-7" }, { "function": "Plays a role as a regulator of Rho activity during cytokinesis. May play a role in junctional plaques", "gene_name": "PKP4", "glycan_count": 1, "glycosylation_sites": [], "id": "Q99569", "name": "Plakophilin-4 (PKP4)", "organism": "Homo sapiens", "uniprot_id": "Q99569" }, { "function": "Plays a role in cellular signaling via Rho-related GTP-binding proteins and subsequent activation of transcription factor SRF (By similarity). Targets TJP1 to cell junctions. In cortical neurons, may play a role in glutaminergic signal transduction through interaction with the NMDA receptor subunit GRIN1 (By similarity)", "gene_name": "MYZAP", "glycan_count": 2, "glycosylation_sites": [], "id": "P0CAP1", "name": "MYZAP", "organism": "Homo sapiens", "uniprot_id": "P0CAP1" }, { "function": "Contributes to the regulation of alternative splicing of pre-mRNAs", "gene_name": "ARVCF", "glycan_count": 2, "glycosylation_sites": [], "id": "O00192", "name": "ARVCF", "organism": "Homo sapiens", "uniprot_id": "O00192" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01857 (IgG1 heavy chain, as adalimumab is a recombinant human IgG1 monoclonal antibody)", "name": "Adalimumab", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "ansB", "glycan_count": 0, "glycosylation_sites": [], "id": "P00805", "name": "Asparaginase (PEG-asparaginase)", "organism": "Escherichia coli (strain K12)", "uniprot_id": "P00805" }, { "function": "Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems", "gene_name": "SOD2", "glycan_count": 3, "glycosylation_sites": [], "id": "P04179", "name": "Superoxide dismutase 2 (SOD2)", "organism": "Homo sapiens", "uniprot_id": "P04179" }, { "function": "Has 3'-5' poly(A) exoribonuclease activity for synthetic poly(A) RNA substrate (PubMed:19276069, PubMed:20634287, PubMed:31439799). Its function seems to be partially redundant with that of CNOT8 (PubMed:19605561). Catalytic component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation (PubMed:19276069, PubMed:20634287, PubMed:31439799). During miRNA-mediated repression the complex also seems to act as translational repressor during translational initiation (PubMed:20065043). Additional complex functions may be a consequence of its influence on mRNA expression (PubMed:19276069, PubMed:23236473). Associates with members of the BTG family such as TOB1 and BTG2 and is required for their anti-proliferative activity (PubMed:19276069, PubMed:23236473)", "gene_name": "CNOT7", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UIV1", "name": "Kidney Injury Molecule-1 (KIM-1)", "organism": "Homo sapiens", "uniprot_id": "Q9UIV1" }, { "function": "Isoform A binds to IL-18 and inhibits its activity. Functions as an inhibitor of the early TH1 cytokine response", "gene_name": "IL18BP", "glycan_count": 13, "glycosylation_sites": [ { "position": 53, "type": "O-linked (GalNAc...) serine" }, { "position": 79, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 94, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 103, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 147, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "O95998", "name": "Interleukin-18 Binding Protein (IL-18BP)", "organism": "Homo sapiens", "uniprot_id": "O95998" }, { "function": "Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268)", "gene_name": "IGHE", "glycan_count": 106, "glycosylation_sites": [ { "position": 21, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 49, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 99, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 146, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 252, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 264, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 275, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01854", "name": "Immunoglobulin E", "organism": "Homo sapiens", "uniprot_id": "P01854" }, { "function": "Associates with the organic matrix of bone and cartilage. Thought to act as an inhibitor of bone formation", "gene_name": "MGP", "glycan_count": 0, "glycosylation_sites": [], "id": "P08493", "name": "Matrix Gla Protein (MGP)", "organism": "Homo sapiens", "uniprot_id": "P08493" }, { "function": "Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin", "gene_name": "PLAU", "glycan_count": 19, "glycosylation_sites": [ { "position": 38, "type": "O-linked (Fuc) threonine" }, { "position": 322, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P00749", "name": "Urokinase-type plasminogen activator (uPA)", "organism": "Homo sapiens", "uniprot_id": "P00749" }, { "function": "Metalloprotease which cleaves aggrecan, a cartilage proteoglycan, at the '1938-Glu-|-Leu-1939' site (within the chondroitin sulfate attachment domain), and may be involved in its turnover (By similarity). Also cleaves COMP (PubMed:39672391). Has angiogenic inhibitor activity (PubMed:10438512). May play a critical role in follicular rupture (By similarity)", "gene_name": "ADAMTS1", "glycan_count": 4, "glycosylation_sites": [ { "position": 547, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 720, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 764, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UHI8", "name": "ADAMTS-1", "organism": "Homo sapiens", "uniprot_id": "Q9UHI8" }, { "function": "Key element of the urea cycle converting L-arginine to urea and L-ornithine, which is further metabolized into metabolites proline and polyamides that drive collagen synthesis and bioenergetic pathways critical for cell proliferation, respectively; the urea cycle takes place primarily in the liver and, to a lesser extent, in the kidneys", "gene_name": "ARG1", "glycan_count": 1, "glycosylation_sites": [], "id": "P05089", "name": "Arginase-1 (Arg-1)", "organism": "Homo sapiens", "uniprot_id": "P05089" }, { "function": "Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6 (PubMed:22000856). DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease (PubMed:17143291). Inhibits the pro-apoptotic function of KREMEN1 in a Wnt-independent manner, and has anti-apoptotic activity (By similarity)", "gene_name": "DKK1", "glycan_count": 1, "glycosylation_sites": [ { "position": 61, "type": "O-linked (GalNAc...) serine" }, { "position": 256, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O94907", "name": "DKK1", "organism": "Homo sapiens", "uniprot_id": "O94907" }, { "function": "Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Acts in the canonical Wnt signaling pathway by promoting beta-catenin-dependent transcriptional activation (PubMed:23499309, PubMed:23656646, PubMed:26902720, PubMed:28528193). In some developmental processes, is also a ligand for the coreceptor RYK, thus triggering Wnt signaling (By similarity). Plays an essential role in the development of the embryonic brain and central nervous system (CNS) (By similarity). Has a role in osteoblast function, bone development and bone homeostasis (PubMed:23499309, PubMed:23656646)", "gene_name": "WNT1", "glycan_count": 0, "glycosylation_sites": [ { "position": 29, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 316, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 346, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 359, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P04628", "name": "Wnt1", "organism": "Homo sapiens", "uniprot_id": "P04628" }, { "function": "Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family (PubMed:20093360, PubMed:21244856, PubMed:24841207, PubMed:26902720). Required for normal embryonic mesoderm development and formation of caudal somites. Required for normal morphogenesis of the developing neural tube (By similarity). Mediates self-renewal of the stem cells at the bottom on intestinal crypts (in vitro) (PubMed:26902720)", "gene_name": "WNT3A", "glycan_count": 3, "glycosylation_sites": [ { "position": 87, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 298, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P56704", "name": "Wnt3a", "organism": "Homo sapiens", "uniprot_id": "P56704" }, { "function": "Ligand for members of the frizzled family of seven transmembrane receptors. Can activate or inhibit canonical Wnt signaling, depending on receptor context. In the presence of FZD4, activates beta-catenin signaling. In the presence of ROR2, inhibits the canonical Wnt pathway by promoting beta-catenin degradation through a GSK3-independent pathway which involves down-regulation of beta-catenin-induced reporter gene expression (By similarity). Suppression of the canonical pathway allows chondrogenesis to occur and inhibits tumor formation. Stimulates cell migration. Decreases proliferation, migration, invasiveness and clonogenicity of carcinoma cells and may act as a tumor suppressor (PubMed:15735754). Mediates motility of melanoma cells (PubMed:17426020). Required during embryogenesis for extension of the primary anterior-posterior axis and for outgrowth of limbs and the genital tubercle. Inhibits type II collagen expression in chondrocytes (By similarity)", "gene_name": "WNT5A", "glycan_count": 11, "glycosylation_sites": [ { "position": 114, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 120, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 312, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 326, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P41221", "name": "Wnt5a", "organism": "Homo sapiens", "uniprot_id": "P41221" }, { "function": "Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome-sized signalosomes (PubMed:11357136, PubMed:11448771, PubMed:15778503, PubMed:16341017, PubMed:16513652, PubMed:17326769, PubMed:17400545, PubMed:19107203, PubMed:19293931, PubMed:19801552, PubMed:28341812). Cell-surface coreceptor of Wnt/beta-catenin signaling, which plays a pivotal role in bone formation (PubMed:11357136, PubMed:11448771, PubMed:15778503, PubMed:16341017, PubMed:16513652, PubMed:17326769, PubMed:17400545, PubMed:19107203, PubMed:19293931, PubMed:19801552, PubMed:28341812). The Wnt-induced Fzd/LRP6 coreceptor complex recruits DVL1 polymers to the plasma membrane which, in turn, recruits the AXIN1/GSK3B-complex to the cell surface promoting the formation of signalosomes and inhibiting AXIN1/GSK3-mediated phosphorylation and destruction of beta-catenin (PubMed:16513652). Required for posterior patterning of the epiblast during gastrulation (By similarity)", "gene_name": "LRP6", "glycan_count": 4, "glycosylation_sites": [ { "position": 42, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 81, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 281, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 433, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 486, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 692, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 859, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 865, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 926, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1039, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O75581", "name": "LRP6", "organism": "Homo sapiens", "uniprot_id": "O75581" }, { "function": "May be a coreceptor along with FZD8 of Wnt proteins, such as WNT1, WNT3, WNT3A and WNT5A. Involved in neuron differentiation, axon guidance, corpus callosum establishment and neurite outgrowth. In response to WNT3 stimulation, receptor C-terminal cleavage occurs in its transmembrane region and allows the C-terminal intracellular product to translocate from the cytoplasm to the nucleus where it plays a crucial role in neuronal development", "gene_name": "RYK", "glycan_count": 2, "glycosylation_sites": [ { "position": 139, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 174, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 178, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 182, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 209, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P34925", "name": "Ryk", "organism": "Homo sapiens", "uniprot_id": "P34925" }, { "function": "Netrins control guidance of CNS commissural axons and peripheral motor axons. Its association with either DCC or some UNC5 receptors will lead to axon attraction or repulsion, respectively. Binding to UNC5C might cause dissociation of UNC5C from polymerized TUBB3 in microtubules and thereby lead to increased microtubule dynamics and axon repulsion (PubMed:28483977). Involved in dorsal root ganglion axon projection towards the spinal cord (PubMed:28483977). It also serves as a survival factor via its association with its receptors which prevent the initiation of apoptosis. Involved in tumorigenesis by regulating apoptosis (PubMed:15343335)", "gene_name": "NTN1", "glycan_count": 4, "glycosylation_sites": [ { "position": 95, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 116, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 131, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 417, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O95631", "name": "Netrin-1", "organism": "Homo sapiens", "uniprot_id": "O95631" }, { "function": "Binds to WNT proteins and inhibits their activities. May be involved in mesoderm segmentation", "gene_name": "WIF1", "glycan_count": 0, "glycosylation_sites": [ { "position": 88, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 245, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y5W5", "name": "Wif1", "organism": "Homo sapiens", "uniprot_id": "Q9Y5W5" }, { "function": "Key decatenating enzyme that alters DNA topology by binding to two double-stranded DNA molecules, generating a double-stranded break in one of the strands, passing the intact strand through the broken strand, and religating the broken strand (PubMed:17567603, PubMed:18790802, PubMed:22013166, PubMed:22323612). May play a role in regulating the period length of BMAL1 transcriptional oscillation (By similarity)", "gene_name": "TOP2A", "glycan_count": 3, "glycosylation_sites": [], "id": "P11388", "name": "Scleroderma Antibody-70 (SCL-70, Topoisomerase I)", "organism": "Homo sapiens", "uniprot_id": "P11388" }, { "function": "Major component of the virion core that undergoes proteolytic processing during the immature virion (IV) to mature virion (MV) transition. Essential for the formation of a structurally normal core", "gene_name": "OPG129", "glycan_count": 0, "glycosylation_sites": [], "id": "P20643", "name": "Vaccinia virus F13L (p37)", "organism": "Vaccinia virus (strain Copenhagen)", "uniprot_id": "P20643" }, { "function": "Cytokine that plays a critical role in modulating tissue responses during inflammation (PubMed:17204547). Plays an essential role in the regeneration of epithelial cells to maintain barrier function after injury and for the prevention of further tissue damage (PubMed:17204547). Unlike most of the cytokines, has no effect on immune cells. Signals through a heterodimeric receptor composed of two subunits, the specific receptor IL22RA1 which is present on non-immune cells in many organs and the shared subunit IL10RB (PubMed:10875937, PubMed:18599299). Ligation of IL22RA1 with IL22 induces activation of the tyrosine kinases JAK1 and TYK2, which in turn activates STAT3. In turn, promotes cell survival and proliferation through STAT3, ERK1/2 and PI3K/AKT pathways (PubMed:25793261, PubMed:31311100). Promotes phosphorylation of GSK3B at 'Ser-9' and CTTN (By similarity). Promotes epithelial cell spreading (By similarity)", "gene_name": "IL22", "glycan_count": 0, "glycosylation_sites": [ { "position": 54, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 68, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 97, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9GZX6", "name": "IL-22", "organism": "Homo sapiens", "uniprot_id": "Q9GZX6" }, { "function": "Tyrosine-protein kinase that acts as a cell-surface receptor for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA and PDGFB, and plays an essential role in the regulation of embryonic development, cell proliferation, survival, differentiation, chemotaxis and migration. Plays an essential role in blood vessel development by promoting proliferation, migration and recruitment of pericytes and smooth muscle cells to endothelial cells. Plays a role in the migration of vascular smooth muscle cells and the formation of neointima at vascular injury sites. Required for normal development of the cardiovascular system. Required for normal recruitment of pericytes (mesangial cells) in the kidney glomerulus, and for normal formation of a branched network of capillaries in kidney glomeruli. Promotes rearrangement of the actin cytoskeleton and the formation of membrane ruffles. Binding of its cognate ligands - homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFD -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PLCG1, PIK3R1, PTPN11, RASA1/GAP, CBL, SHC1 and NCK1. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the activation of protein kinase C. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to the activation of the AKT1 signaling pathway. Phosphorylation of SHC1, or of the C-terminus of PTPN11, creates a binding site for GRB2, resulting in the activation of HRAS, RAF1 and down-stream MAP kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation and activation of SRC family kinases. Promotes phosphorylation of PDCD6IP/ALIX and STAM. Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor", "gene_name": "PDGFRB", "glycan_count": 5, "glycosylation_sites": [ { "position": 45, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 89, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 103, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 215, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 230, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 292, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 307, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 354, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 371, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 468, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 479, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P09619", "name": "PDGFR\u03b2", "organism": "Homo sapiens", "uniprot_id": "P09619" }, { "function": "The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (PubMed:33795473). TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (PubMed:33795473). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:33795473). The TFIID complex structure can be divided into 3 modules TFIID-A, TFIID-B, and TFIID-C (PubMed:33795473). TAF6 homodimer connects TFIID modules, forming a rigid core (PubMed:33795473)", "gene_name": "TAF6", "glycan_count": 2, "glycosylation_sites": [], "id": "P49848", "name": "EXT1", "organism": "Homo sapiens", "uniprot_id": "P49848" }, { "function": "Glycosyltransferase forming with EXT1 the heterodimeric heparan sulfate polymerase which catalyzes the elongation of the heparan sulfate glycan backbone (PubMed:22660413, PubMed:36402845, PubMed:36593275). Glycan backbone extension consists in the alternating transfer of (1->4)-beta-D-GlcA and (1->4)-alpha-D-GlcNAc residues from their respective UDP-sugar donors. Both EXT1 and EXT2 are required for the full activity of the polymerase since EXT1 bears the N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase activity within the complex while EXT2 carries the glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity (PubMed:36402845, PubMed:36593275). Heparan sulfate proteoglycans are ubiquitous components of the extracellular matrix and play an important role in tissue homeostasis and signaling (PubMed:19344451, PubMed:22660413)", "gene_name": "EXT2", "glycan_count": 2, "glycosylation_sites": [ { "position": 288, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 637, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q93063", "name": "EXT2", "organism": "Homo sapiens", "uniprot_id": "Q93063" }, { "function": "Component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis", "gene_name": "STAG1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q8WVM7", "name": "COG7", "organism": "Homo sapiens", "uniprot_id": "Q8WVM7" }, { "function": "Pulmonary surfactant-associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces. SP-B increases the collapse pressure of palmitic acid to nearly 70 millinewtons per meter", "gene_name": "SFTPB", "glycan_count": 0, "glycosylation_sites": [ { "position": 129, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 311, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P07988", "name": "Surfactant protein B (SFTPB)", "organism": "Homo sapiens", "uniprot_id": "P07988" }, { "function": "Pulmonary surfactant associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces", "gene_name": "SFTPC", "glycan_count": 0, "glycosylation_sites": [], "id": "P11686", "name": "Surfactant protein C (SFTPC)", "organism": "Homo sapiens", "uniprot_id": "P11686" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P35247/P35242", "name": "Surfactant protein A (SFTPA1/2)", "organism": "", "uniprot_id": "" }, { "function": "Actin-binding protein that enhances membrane ruffling and RAC activation. Enhances the actin-bundling activity of LCP1. Binds calcium. Plays a role in RAC signaling and in phagocytosis. May play a role in macrophage activation and function. Promotes the proliferation of vascular smooth muscle cells and of T-lymphocytes. Enhances lymphocyte migration. Plays a role in vascular inflammation", "gene_name": "AIF1", "glycan_count": 0, "glycosylation_sites": [], "id": "P55008", "name": "Ionized calcium-binding adapter molecule 1 (IBA-1)", "organism": "Homo sapiens", "uniprot_id": "P55008" }, { "function": "Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell", "gene_name": "Rpl34", "glycan_count": 0, "glycosylation_sites": [], "id": "P11250", "name": "Measles virus fusion (F) glycoprotein", "organism": "Rattus norvegicus", "uniprot_id": "P11250" }, { "function": "Tyrosine-protein kinase that acts as a cell-surface receptor for CSF1 and IL34 and plays an essential role in the regulation of survival, proliferation and differentiation of hematopoietic precursor cells, especially mononuclear phagocytes, such as macrophages and monocytes. Promotes the release of pro-inflammatory chemokines in response to IL34 and CSF1, and thereby plays an important role in innate immunity and in inflammatory processes. Plays an important role in the regulation of osteoclast proliferation and differentiation, the regulation of bone resorption, and is required for normal bone and tooth development. Required for normal male and female fertility, and for normal development of milk ducts and acinar structures in the mammary gland during pregnancy. Promotes reorganization of the actin cytoskeleton, regulates formation of membrane ruffles, cell adhesion and cell migration, and promotes cancer cell invasion. Activates several signaling pathways in response to ligand binding, including the ERK1/2 and the JNK pathway (PubMed:20504948, PubMed:30982609). Phosphorylates PIK3R1, PLCG2, GRB2, SLA2 and CBL. Activation of PLCG2 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, that then lead to the activation of protein kinase C family members, especially PRKCD. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leads to activation of the AKT1 signaling pathway. Activated CSF1R also mediates activation of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1, and of the SRC family kinases SRC, FYN and YES1. Activated CSF1R transmits signals both via proteins that directly interact with phosphorylated tyrosine residues in its intracellular domain, or via adapter proteins, such as GRB2. Promotes activation of STAT family members STAT3, STAT5A and/or STAT5B. Promotes tyrosine phosphorylation of SHC1 and INPP5D/SHIP-1. Receptor signaling is down-regulated by protein phosphatases, such as INPP5D/SHIP-1, that dephosphorylate the receptor and its downstream effectors, and by rapid internalization of the activated receptor. In the central nervous system, may play a role in the development of microglia macrophages (PubMed:30982608)", "gene_name": "CSF1R", "glycan_count": 32, "glycosylation_sites": [ { "position": 45, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 73, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 153, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 240, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 275, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 302, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 335, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 353, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 412, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 428, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 480, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P07333", "name": "Colony-stimulating factor 1 receptor (CSF1R)", "organism": "Homo sapiens", "uniprot_id": "P07333" }, { "function": "Multidomain scaffolding Mg(2+)-independent protein kinase that catalyzes the phosphotransfer from ATP to proteins such as NRXN1, and plays a role in synaptic transmembrane protein anchoring and ion channel trafficking (PubMed:18423203). Contributes to neural development and regulation of gene expression via interaction with the transcription factor TBR1. Binds to cell-surface proteins, including amyloid precursor protein, neurexins and syndecans. May mediate a link between the extracellular matrix and the actin cytoskeleton via its interaction with syndecan and with the actin/spectrin-binding protein 4.1. Component of the LIN-10-LIN-2-LIN-7 complex, which associates with the motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B along microtubules (By similarity)", "gene_name": "CASK", "glycan_count": 2, "glycosylation_sites": [], "id": "O14936", "name": "LIN2 (CASK)", "organism": "Homo sapiens", "uniprot_id": "O14936" }, { "function": "Plays a role in establishing and maintaining the asymmetric distribution of channels and receptors at the plasma membrane of polarized cells. Forms membrane-associated multiprotein complexes that may regulate delivery and recycling of proteins to the correct membrane domains. The tripartite complex composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 associates with the motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B along microtubules (By similarity). This complex may have the potential to couple synaptic vesicle exocytosis to cell adhesion in brain. Ensures the proper localization of GRIN2B (subunit 2B of the NMDA receptor) to neuronal postsynaptic density and may function in localizing synaptic vesicles at synapses where it is recruited by beta-catenin and cadherin. Required to localize Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 to the basolateral membrane of epithelial cells", "gene_name": "LIN7C", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NUP9", "name": "LIN7A", "organism": "Homo sapiens", "uniprot_id": "Q9NUP9" }, { "function": "Catalyzes the oxidation of the less abundant 1,2-dihydro-beta-NAD(P) and 1,6-dihydro-beta-NAD(P) to form beta-NAD(P)(+). The enzyme hormone is secreted by the kidney, and circulates in blood and modulates cardiac function and systemic blood pressure. Lowers blood pressure in vivo by decreasing cardiac contractility and heart rate and preventing a compensatory increase in peripheral vascular tone, suggesting a causal link to the increased plasma catecholamine and heightened cardiovascular risk. High concentrations of catecholamines activate plasma renalase and promotes its secretion and synthesis", "gene_name": "RNLS", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NUP8", "name": "LIN7B", "organism": "Homo sapiens", "uniprot_id": "Q5VYX0" }, { "function": "tRNA methylase which 2'-O-methylates cytidine(4) in tRNA(Pro) and tRNA(Gly)(GCC), and adenosine(4) in tRNA(His)", "gene_name": "TRMT13", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NUP7", "name": "LIN7C", "organism": "Homo sapiens", "uniprot_id": "Q9NUP7" }, { "function": "Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone", "gene_name": "NDUFB8", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UQF3", "name": "LIN10 (MINT1/APBA1)", "organism": "Homo sapiens", "uniprot_id": "O95169" }, { "function": "General activator of RNA polymerase III transcription. Factor exclusively required for RNA polymerase III transcription of genes with promoter elements upstream of the initiation sites (PubMed:11040218, PubMed:11121026, PubMed:11564744, PubMed:26638071). Contributes to the regulation of gene expression; functions as activator in the absence of oxidative stress (PubMed:26638071). Down-regulates expression of target genes in response to oxidative stress (PubMed:26638071). Overexpression protects cells against apoptosis in response to oxidative stress (PubMed:26638071)", "gene_name": "BRF2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9HAW0", "name": "Sclerostin", "organism": "Homo sapiens", "uniprot_id": "Q9HAW0" }, { "function": "Binds anionic lipids and gangliosides at acidic pH", "gene_name": "EPDR1", "glycan_count": 2, "glycosylation_sites": [ { "position": 130, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 182, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UM22", "name": "Osteoactivin", "organism": "Homo sapiens", "uniprot_id": "Q9UM22" }, { "function": "Bone protein that constitutes 1-2% of the total bone protein, and which acts as a negative regulator of bone formation (PubMed:3019668, PubMed:6967872). Functions to limit bone formation without impairing bone resorption or mineralization (By similarity). It binds strongly to apatite and calcium (PubMed:6967872)", "gene_name": "BGLAP", "glycan_count": 0, "glycosylation_sites": [], "id": "P02818", "name": "Osteocalcin", "organism": "Homo sapiens", "uniprot_id": "P02818" }, { "function": "Acts specifically as a negative regulator of skeletal muscle growth", "gene_name": "MSTN", "glycan_count": 1, "glycosylation_sites": [ { "position": 71, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O14793", "name": "Myostatin", "organism": "Homo sapiens", "uniprot_id": "O14793" }, { "function": "High-affinity receptor for interleukin-15 (PubMed:8530383). Can signal both in cis and trans where IL15R from one subset of cells presents IL15 to neighboring IL2RG-expressing cells (By similarity). In neutrophils, binds and activates kinase SYK in response to IL15 stimulation (PubMed:15123770). In neutrophils, required for IL15-induced phagocytosis in a SYK-dependent manner (PubMed:15123770). Expression of different isoforms may alter or interfere with signal transduction (PubMed:10480910)", "gene_name": "IL15RA", "glycan_count": 2, "glycosylation_sites": [ { "position": 137, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13261", "name": "IL-15", "organism": "Homo sapiens", "uniprot_id": "Q13261" }, { "function": "Mediates beneficial effects of muscular exercise. Induces browning of white adipose tissue by stimulating UCP1 expression, at least in part, via the nuclear receptor PPARA", "gene_name": "FNDC5", "glycan_count": 0, "glycosylation_sites": [ { "position": 87, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 132, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8NAU1", "name": "Irisin (FNDC5)", "organism": "Homo sapiens", "uniprot_id": "Q8NAU1" }, { "function": "Aminopeptidase which catalyzes the hydrolysis of amino acid residues from the N-terminus of peptide or protein substrates", "gene_name": "AOPEP", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8N6M6", "name": "Musclin", "organism": "Homo sapiens", "uniprot_id": "Q8N6M6" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04578 (gp120, HIV-1)", "name": "gp120/gp41", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6YMS4 (DENV)", "name": "Envelope glycoprotein (E)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03437 (Influenza A)", "name": "Hemagglutinin (HA)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q05320 (Ebola virus)", "name": "Glycoprotein (GP)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6Y2C6", "name": "Griffithsin (GRFT)", "organism": "Hepacivirus hominis", "uniprot_id": "Q6Y2C6" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NNX6/Q9H2X3", "name": "DC-SIGN/L-SIGN", "organism": "", "uniprot_id": "" }, { "function": "Saposin-A and saposin-C stimulate the hydrolysis of glucosylceramide by beta-glucosylceramidase (EC 3.2.1.45) and galactosylceramide by beta-galactosylceramidase (EC 3.2.1.46). Saposin-C apparently acts by combining with the enzyme and acidic lipid to form an activated complex, rather than by solubilizing the substrate", "gene_name": "PSAP", "glycan_count": 293, "glycosylation_sites": [ { "position": 80, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 101, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 215, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 332, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 426, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P07602", "name": "Prosaposin (PSAP)", "organism": "Homo sapiens", "uniprot_id": "P07602" }, { "function": "Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate, AA, C20:4(n-6)), with a particular role in the inflammatory response (PubMed:11939906, PubMed:16373578, PubMed:19540099, PubMed:22942274, PubMed:26859324, PubMed:27226593, PubMed:7592599, PubMed:7947975, PubMed:9261177). The cyclooxygenase activity oxygenates AA to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide prostaglandin H2 (PGH2), the precursor of all 2-series prostaglandins and thromboxanes (PubMed:16373578, PubMed:22942274, PubMed:26859324, PubMed:27226593, PubMed:7592599, PubMed:7947975, PubMed:9261177). This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons (PubMed:16373578, PubMed:22942274, PubMed:26859324, PubMed:27226593, PubMed:7592599, PubMed:7947975, PubMed:9261177). Similarly catalyzes successive cyclooxygenation and peroxidation of dihomo-gamma-linoleate (DGLA, C20:3(n-6)) and eicosapentaenoate (EPA, C20:5(n-3)) to corresponding PGH1 and PGH3, the precursors of 1- and 3-series prostaglandins (PubMed:11939906, PubMed:19540099). In an alternative pathway of prostanoid biosynthesis, converts 2-arachidonoyl lysophopholipids to prostanoid lysophopholipids, which are then hydrolyzed by intracellular phospholipases to release free prostanoids (PubMed:27642067). Metabolizes 2-arachidonoyl glycerol yielding the glyceryl ester of PGH2, a process that can contribute to pain response (PubMed:22942274). Generates lipid mediators from n-3 and n-6 polyunsaturated fatty acids (PUFAs) via a lipoxygenase-type mechanism. Oxygenates PUFAs to hydroperoxy compounds and then reduces them to corresponding alcohols (PubMed:11034610, PubMed:11192938, PubMed:9048568, PubMed:9261177). Plays a role in the generation of resolution phase interaction products (resolvins) during both sterile and infectious inflammation (PubMed:12391014). Metabolizes docosahexaenoate (DHA, C22:6(n-3)) to 17R-HDHA, a precursor of the D-series resolvins (RvDs) (PubMed:12391014). As a component of the biosynthetic pathway of E-series resolvins (RvEs), converts eicosapentaenoate (EPA, C20:5(n-3)) primarily to 18S-HEPE that is further metabolized by ALOX5 and LTA4H to generate 18S-RvE1 and 18S-RvE2 (PubMed:21206090). In vascular endothelial cells, converts docosapentaenoate (DPA, C22:5(n-3)) to 13R-HDPA, a precursor for 13-series resolvins (RvTs) shown to activate macrophage phagocytosis during bacterial infection (PubMed:26236990). In activated leukocytes, contributes to oxygenation of hydroxyeicosatetraenoates (HETE) to diHETES (5,15-diHETE and 5,11-diHETE) (PubMed:22068350, PubMed:26282205). Can also use linoleate (LA, (9Z,12Z)-octadecadienoate, C18:2(n-6)) as substrate and produce hydroxyoctadecadienoates (HODEs) in a regio- and stereospecific manner, being (9R)-HODE ((9R)-hydroxy-(10E,12Z)-octadecadienoate) and (13S)-HODE ((13S)-hydroxy-(9Z,11E)-octadecadienoate) its major products (By similarity). During neuroinflammation, plays a role in neuronal secretion of specialized preresolving mediators (SPMs) 15R-lipoxin A4 that regulates phagocytic microglia (By similarity)", "gene_name": "PTGS2", "glycan_count": 16, "glycosylation_sites": [ { "position": 53, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 130, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 396, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 580, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P35354", "name": "COX-2 (PTGS2)", "organism": "Homo sapiens", "uniprot_id": "P35354" }, { "function": "Positively regulates the transcription of MYCNOS in neuroblastoma cells", "gene_name": "MYCN", "glycan_count": 1, "glycosylation_sites": [], "id": "P04198", "name": "N-MYC", "organism": "Homo sapiens", "uniprot_id": "P04198" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Q0Q8 (PEDV S protein, reference)", "name": "Spike (S) glycoprotein", "organism": "", "uniprot_id": "" }, { "function": "Transcriptional regulator. May participate in transcriptional regulation through the recruitment of SETDB1 histone methyltransferase and subsequent modification of local chromatin structure", "gene_name": "ERG", "glycan_count": 1, "glycosylation_sites": [], "id": "P11308", "name": "ERG", "organism": "Homo sapiens", "uniprot_id": "P11308" }, { "function": "May be involved in neural development. Involved in regulation of osteoblast function and bone formation. Involved in matrix vesicle release by osteoblasts; this function seems to involve maintenance of the actin cytoskeleton. May be involved in cellular trafficking of SERT and thereby in regulation of serotonin uptake", "gene_name": "GPM6B", "glycan_count": 1, "glycosylation_sites": [ { "position": 73, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 177, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13491", "name": "M6a", "organism": "Homo sapiens", "uniprot_id": "Q13491" }, { "function": "Cell surface protein involved in cell-cell-interactions via its interactions with neurexin family members. Plays a role in synapse function and synaptic signal transmission, and may mediate its effects by clustering other synaptic proteins. May promote the initial formation of synapses, but is not essential for this. May also play a role in glia-glia or glia-neuron interactions in the developing peripheral nervous system (By similarity)", "gene_name": "NLGN3", "glycan_count": 0, "glycosylation_sites": [ { "position": 98, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 545, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NZ94", "name": "Neuroligin-3 (NLGN3)", "organism": "Homo sapiens", "uniprot_id": "Q9NZ94" }, { "function": "The exact function of MAP2 is unknown but MAPs may stabilize the microtubules against depolymerization. They also seem to have a stiffening effect on microtubules", "gene_name": "MAP2", "glycan_count": 1, "glycosylation_sites": [], "id": "P11137", "name": "MAP2", "organism": "Homo sapiens", "uniprot_id": "P11137" }, { "function": "Catalyzes the conversion of L-tyrosine to L-dihydroxyphenylalanine (L-Dopa), the rate-limiting step in the biosynthesis of catecholamines, dopamine, noradrenaline, and adrenaline. Uses tetrahydrobiopterin and molecular oxygen to convert tyrosine to L-Dopa (PubMed:15287903, PubMed:1680128, PubMed:17391063, PubMed:24753243, PubMed:34922205, PubMed:8528210, Ref.18). In addition to tyrosine, is able to catalyze the hydroxylation of phenylalanine and tryptophan with lower specificity (By similarity). Positively regulates the regression of retinal hyaloid vessels during postnatal development (By similarity)", "gene_name": "TH", "glycan_count": 0, "glycosylation_sites": [], "id": "P07101", "name": "Tyrosine hydroxylase", "organism": "Homo sapiens", "uniprot_id": "P07101" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P08514 (ITGA2B), P05106 (ITGB3)", "name": "Glycoprotein IIb/IIIa", "organism": "", "uniprot_id": "" }, { "function": "Cytosolic dehydrogenase that catalyzes the irreversible oxidation of a wide range of aldehydes to their corresponding carboxylic acid (PubMed:12941160, PubMed:15623782, PubMed:17175089, PubMed:19296407, PubMed:25450233, PubMed:26373694). Functions downstream of retinol dehydrogenases and catalyzes the oxidation of retinaldehyde into retinoic acid, the second step in the oxidation of retinol/vitamin A into retinoic acid (By similarity). This pathway is crucial to control the levels of retinol and retinoic acid, two important molecules which excess can be teratogenic and cytotoxic (By similarity). Also oxidizes aldehydes resulting from lipid peroxidation like (E)-4-hydroxynon-2-enal/HNE, malonaldehyde and hexanal that form protein adducts and are highly cytotoxic. By participating for instance to the clearance of (E)-4-hydroxynon-2-enal/HNE in the lens epithelium prevents the formation of HNE-protein adducts and lens opacification (PubMed:12941160, PubMed:15623782, PubMed:19296407). Also functions downstream of fructosamine-3-kinase in the fructosamine degradation pathway by catalyzing the oxidation of 3-deoxyglucosone, the carbohydrate product of fructosamine 3-phosphate decomposition, which is itself a potent glycating agent that may react with lysine and arginine side-chains of proteins (PubMed:17175089). Also has an aminobutyraldehyde dehydrogenase activity and is probably part of an alternative pathway for the biosynthesis of GABA/4-aminobutanoate in midbrain, thereby playing a role in GABAergic synaptic transmission (By similarity)", "gene_name": "ALDH1A1", "glycan_count": 1, "glycosylation_sites": [], "id": "P00352", "name": "ALDH1A1", "organism": "Homo sapiens", "uniprot_id": "P00352" }, { "function": "Transcription factor that forms a trimeric complex with OCT4 on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206 (By similarity). Binds to the proximal enhancer region of NANOG (By similarity). Critical for early embryogenesis and for embryonic stem cell pluripotency (PubMed:18035408). Downstream SRRT target that mediates the promotion of neural stem cell self-renewal (By similarity). Keeps neural cells undifferentiated by counteracting the activity of proneural proteins and suppresses neuronal differentiation (By similarity). May function as a switch in neuronal development (By similarity)", "gene_name": "SOX2", "glycan_count": 2, "glycosylation_sites": [], "id": "P48431", "name": "SOX2", "organism": "Homo sapiens", "uniprot_id": "P48431" }, { "function": "Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3'). Forms a trimeric complex with SOX2 or SOX15 on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206. Critical for early embryogenesis and for embryonic stem cell pluripotency", "gene_name": "POU5F1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q01860", "name": "OCT4 (POU5F1)", "organism": "Homo sapiens", "uniprot_id": "Q01860" }, { "function": "Binds to chondroitin sulfate on the cell surface to provide virion attachment to target cell", "gene_name": "OPG105", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8V4Y0", "name": "B6R", "organism": "Monkeypox virus (strain Zaire-96-I-16)", "uniprot_id": "Q8V4Y0" }, { "function": "Acts with RNA polymerase to initiate transcription from early gene promoters. Is recruited by the RPO-associated protein of 94 kDa RAP94/OPG109 to form the early transcription complex, which also contains the core RNA polymerase. ETF heterodimer binds to early gene promoters", "gene_name": "E6R", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8V4Y2", "name": "H3L", "organism": "Monkeypox virus (strain Zaire-96-I-16)", "uniprot_id": "Q8V4Y2" }, { "function": "", "gene_name": "E1R", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8V4Y7", "name": "J3R/J1L", "organism": "Monkeypox virus (strain Zaire-96-I-16)", "uniprot_id": "Q8V4Y7" }, { "function": "Late protein which is part of a large complex required for early virion morphogenesis. This complex participates in the formation of virosomes and the incorporation of virosomal contents into nascent immature virions", "gene_name": "E3R", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8V4Y5", "name": "E4R", "organism": "Monkeypox virus (strain Zaire-96-I-16)", "uniprot_id": "Q8V4Y5" }, { "function": "", "gene_name": "E9R", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8V4X9", "name": "A40L", "organism": "Monkeypox virus (strain Zaire-96-I-16)", "uniprot_id": "Q8V4X9" }, { "function": "", "gene_name": "E7R", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8V4Y1", "name": "B9R", "organism": "Monkeypox virus (strain Zaire-96-I-16)", "uniprot_id": "Q8V4Y1" }, { "function": "Multifunctional protein required for genome uncoating and replication. Major viral uncoating protein that is required for the release of the viral genome from incoming viral cores containing the viral DNA genome. Possesses an ATPase activity that is required for hexamerization and uncoating", "gene_name": "E5R", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8V4Y3", "name": "C2L", "organism": "Monkeypox virus (strain Zaire-96-I-16)", "uniprot_id": "Q8V4Y3" }, { "function": "Late protein which is part of a large complex required for early virion morphogenesis. This complex participates in the formation of virosomes and the incorporation of virosomal contents into nascent immature virions", "gene_name": "E2L", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8V4Y6", "name": "F8L", "organism": "Monkeypox virus (strain Zaire-96-I-16)", "uniprot_id": "Q8V4Y6" }, { "function": "The B subunit pentameric ring directs the A subunit to its target by binding to the GM1 gangliosides present on the surface of the intestinal epithelial cells. It can bind five GM1 gangliosides. It has no toxic activity by itself", "gene_name": "ctxB", "glycan_count": 0, "glycosylation_sites": [], "id": "P01556", "name": "Cholera toxin B subunit (CTB)", "organism": "Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)", "uniprot_id": "P01556" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P08514/P23219", "name": "GPIIb/IIIa (Integrin \u03b1IIb\u03b23)", "organism": "", "uniprot_id": "" }, { "function": "Receptor for thrombopoietin that regulates hematopoietic stem cell renewal, megakaryocyte differentiation, and platelet formation. Upon activation by THPO, induces rapid tyrosine phosphorylation and activation of JAK2, providing docking sites for many signaling proteins such as STAT5, SHIP/INPP5D, GRB2, SOS1 and PI3K (PubMed:15899890, PubMed:37633268). In turn, These signaling cascades lead to the proliferation, survival, and differentiation of megakaryocytes, ultimately leading to increased platelet production", "gene_name": "MPL", "glycan_count": 1, "glycosylation_sites": [ { "position": 117, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 178, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 298, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 358, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P40238", "name": "Thrombopoietin receptor (MPL)", "organism": "Homo sapiens", "uniprot_id": "P40238" }, { "function": "Isomerase that catalyzes the conversion of PGH2 into the more stable prostaglandin E2 (PGE2) (in vitro) (PubMed:12804604, PubMed:17585783, PubMed:18198127). The biological function and the GSH-dependent property of PTGES2 is still under debate (PubMed:17585783, PubMed:18198127). In vivo, PTGES2 could form a complex with GSH and heme and would not participate in PGE2 synthesis but would catalyze the degradation of prostaglandin E2 H2 (PGH2) to 12(S)-hydroxy-5(Z),8(E),10(E)-heptadecatrienoic acid (HHT) and malondialdehyde (MDA) (By similarity) (PubMed:17585783)", "gene_name": "PTGES2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H7Z7", "name": "CLEC-2", "organism": "Homo sapiens", "uniprot_id": "Q9H7Z7" }, { "function": "The GPIb-V-IX complex functions as the vWF receptor and mediates vWF-dependent platelet adhesion to blood vessels. The adhesion of platelets to injured vascular surfaces in the arterial circulation is a critical initiating event in hemostasis", "gene_name": "GP5", "glycan_count": 6, "glycosylation_sites": [ { "position": 51, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 181, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 243, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 267, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 298, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 312, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 385, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 499, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P40197", "name": "Soluble glycoprotein V (sGPV)", "organism": "Homo sapiens", "uniprot_id": "P40197" }, { "function": "Bifunctional inositol kinase that acts in concert with the IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4 (PubMed:17690096, PubMed:17702752, PubMed:21222653, PubMed:29590114). PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, exocytosis, insulin signaling and neutrophil activation (PubMed:17690096, PubMed:17702752, PubMed:21222653, PubMed:29590114). Phosphorylates inositol hexakisphosphate (InsP6) at position 1 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4 (PubMed:17690096, PubMed:17702752). Alternatively, phosphorylates PP-InsP5 at position 1, produced by IP6Ks from InsP6, to produce (PP)2-InsP4 (PubMed:17690096, PubMed:17702752). Required for normal hearing (PubMed:29590114)", "gene_name": "PPIP5K2", "glycan_count": 1, "glycosylation_sites": [], "id": "O43314", "name": "DUSP9", "organism": "Homo sapiens", "uniprot_id": "O43314" }, { "function": "Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis", "gene_name": "AGT", "glycan_count": 1, "glycosylation_sites": [ { "position": 38, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 161, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 295, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 319, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01019", "name": "AGT (Angiotensinogen)", "organism": "Homo sapiens", "uniprot_id": "P01019" }, { "function": "Receptor for angiotensin II, a vasoconstricting peptide (PubMed:28379944, PubMed:29967536, PubMed:31899086, PubMed:8185599). Signals primarily via a non-canonical G-protein- and beta-arrestin independent pathways (PubMed:28379944). Cooperates with MTUS1 to inhibit ERK2 activation and cell proliferation (PubMed:15123706)", "gene_name": "AGTR2", "glycan_count": 0, "glycosylation_sites": [ { "position": 4, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 13, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 24, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 29, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 34, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P50052", "name": "AGTR2 (Angiotensin II receptor type 2)", "organism": "Homo sapiens", "uniprot_id": "P50052" }, { "function": "Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations (By similarity). Regulates receptor-mediated endocytosis (PubMed:10393179, PubMed:10557078)", "gene_name": "EPN1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9Y6I3", "name": "MTUS1", "organism": "Homo sapiens", "uniprot_id": "Q9Y6I3" }, { "function": "Tyrosine phosphatase enzyme that plays important roles in controlling immune signaling pathways and fundamental physiological processes such as hematopoiesis (PubMed:14739280, PubMed:29925997). Dephosphorylates and negatively regulate several receptor tyrosine kinases (RTKs) such as EGFR, PDGFR and FGFR, thereby modulating their signaling activities (PubMed:21258366, PubMed:9733788). When recruited to immunoreceptor tyrosine-based inhibitory motif (ITIM)-containing receptors such as immunoglobulin-like transcript 2/LILRB1, programmed cell death protein 1/PDCD1, CD3D, CD22, CLEC12A and other receptors involved in immune regulation, initiates their dephosphorylation and subsequently inhibits downstream signaling events (PubMed:11907092, PubMed:14739280, PubMed:37932456, PubMed:38166031). Modulates the signaling of several cytokine receptors including IL-4 receptor (PubMed:9065461). Additionally, targets multiple cytoplasmic signaling molecules including STING1, LCK or STAT1 among others involved in diverse cellular processes including modulation of T-cell activation or cGAS-STING signaling (PubMed:34811497, PubMed:38532423). Within the nucleus, negatively regulates the activity of some transcription factors such as NFAT5 via direct dephosphorylation. Also acts as a key transcriptional regulator of hepatic gluconeogenesis by controlling recruitment of RNA polymerase II to the PCK1 promoter together with STAT5A (PubMed:37595871)", "gene_name": "PTPN6", "glycan_count": 2, "glycosylation_sites": [], "id": "P29350", "name": "PTPN6", "organism": "Homo sapiens", "uniprot_id": "P29350" }, { "function": "Tumor suppressor serine/threonine-protein kinase involved in synaptic plasticity, centriole duplication and G1/S phase transition. Polo-like kinases act by binding and phosphorylating proteins that are already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates CPAP, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1 and SYNGAP1. Plays a key role in synaptic plasticity and memory by regulating the Ras and Rap protein signaling: required for overactivity-dependent spine remodeling by phosphorylating the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 leading to their degradation by the proteasome. Conversely, phosphorylates the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1, promoting their activity. Also regulates synaptic plasticity independently of kinase activity, via its interaction with NSF that disrupts the interaction between NSF and the GRIA2 subunit of AMPARs, leading to a rapid rundown of AMPAR-mediated current that occludes long term depression. Required for procentriole formation and centriole duplication by phosphorylating CPAP and NPM1, respectively. Its induction by p53/TP53 suggests that it may participate in the mitotic checkpoint following stress", "gene_name": "PLK2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NYY3", "name": "PLK2", "organism": "Homo sapiens", "uniprot_id": "Q9NYY3" }, { "function": "Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Inhibits the transactivation function of HIF-1A under both normoxic and hypoxia-mimicking conditions. The interaction with EMAP2 increases the proteasome-mediated HIF-1A degradation under the hypoxic conditions. Plays a role in hepatitis C virus internal ribosome entry site-mediated translation. Mediates nuclear translocation of the androgen receptor (AR) and thereby enhances androgen-mediated transactivation. Promotes MAVS degradation and thereby negatively regulates MAVS-mediated innate immune response", "gene_name": "PSMA7", "glycan_count": 1, "glycosylation_sites": [ { "position": 130, "type": "O-linked (GlcNAc) serine" } ], "id": "O14818", "name": "PSMA7", "organism": "Homo sapiens", "uniprot_id": "O14818" }, { "function": "Protein tyrosine-protein phosphatase required for T-cell activation through the antigen receptor. Acts as a positive regulator of T-cell coactivation upon binding to DPP4. The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Upon T-cell activation, recruits and dephosphorylates SKAP1 and FYN (By similarity). Dephosphorylates LYN, and thereby modulates LYN activity. Interacts with CLEC10A at antigen presenting cell-T cell contact; CLEC10A on immature dendritic cells recognizes Tn antigen-carrying PTPRC/CD45 receptor on effector T cells and modulates T cell activation threshold to limit autoreactivity", "gene_name": "Ptprc", "glycan_count": 8, "glycosylation_sites": [ { "position": 66, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 152, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 163, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 209, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 213, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 220, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 255, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 260, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 292, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 313, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 324, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 349, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 418, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 429, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 459, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 491, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P06800", "name": "CD45", "organism": "Mus musculus", "uniprot_id": "P06800" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q60681", "name": "CD148", "organism": "", "uniprot_id": "Q60681" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P11453", "name": "C5a", "organism": "", "uniprot_id": "P11453" }, { "function": "Has chemotactic activity for neutrophils. Contributes to neutrophil activation during inflammation (By similarity). Hematoregulatory chemokine, which, in vitro, suppresses hematopoietic progenitor cell proliferation. KC(5-72) shows a highly enhanced hematopoietic activity", "gene_name": "Cxcl1", "glycan_count": 0, "glycosylation_sites": [], "id": "P12850", "name": "CXCL1", "organism": "Mus musculus", "uniprot_id": "P12850" }, { "function": "Cytokine with a wide variety of biological functions in immunity, tissue regeneration, and metabolism (Probable). Binds to IL6R, then the complex associates to the signaling subunit IL6ST/gp130 to trigger the intracellular IL6-signaling pathway (PubMed:8910279). The interaction with the membrane-bound IL6R and IL6ST stimulates 'classic signaling', whereas the binding of IL6 and soluble IL6R to IL6ST stimulates 'trans-signaling'. Alternatively, 'cluster signaling' occurs when membrane-bound IL6:IL6R complexes on transmitter cells activate IL6ST receptors on neighboring receiver cells (PubMed:27893700)", "gene_name": "Il6", "glycan_count": 0, "glycosylation_sites": [], "id": "P08505", "name": "IL-6", "organism": "Mus musculus", "uniprot_id": "P08505" }, { "function": "Acts as a substrate for the production of iodinated thyroid hormones thyroxine (T4) and triiodothyronine (T3) (By similarity). The synthesis of T3 and T4 involves iodination of selected tyrosine residues of TG/thyroglobulin followed by their oxidative coupling (By similarity). Following TG re-internalization and lysosomal-mediated proteolysis, T3 and T4 are released from the polypeptide backbone leading to their secretion into the bloodstream (By similarity). One dimer produces 7 thyroid hormone molecules (By similarity)", "gene_name": "TG", "glycan_count": 1, "glycosylation_sites": [ { "position": 110, "type": "N-linked (GlcNAc...) (complex) asparagine; alternate" }, { "position": 110, "type": "N-linked (GlcNAc...) (hybrid) asparagine; alternate" }, { "position": 483, "type": "N-linked (GlcNAc...) (complex) asparagine; alternate" }, { "position": 483, "type": "N-linked (GlcNAc...) (hybrid) asparagine; alternate" }, { "position": 495, "type": "N-linked (GlcNAc...) (complex) asparagine; alternate" }, { "position": 495, "type": "N-linked (GlcNAc...) (hybrid) asparagine; alternate" }, { "position": 853, "type": "N-linked (GlcNAc...) (complex) asparagine; alternate" }, { "position": 853, "type": "N-linked (GlcNAc...) (hybrid) asparagine; alternate" }, { "position": 947, "type": "N-linked (GlcNAc...) (complex) asparagine; alternate" }, { "position": 947, "type": "N-linked (GlcNAc...) (hybrid) asparagine; alternate" }, { "position": 1140, "type": "N-linked (GlcNAc...) (complex) asparagine; alternate" }, { "position": 1140, "type": "N-linked (GlcNAc...) (hybrid) asparagine; alternate" }, { "position": 1365, "type": "N-linked (GlcNAc...) (high mannose) asparagine" }, { "position": 1776, "type": "N-linked (GlcNAc...) (complex) asparagine; alternate" }, { "position": 1776, "type": "N-linked (GlcNAc...) (hybrid) asparagine; alternate" }, { "position": 1870, "type": "N-linked (GlcNAc...) (complex) asparagine; alternate" }, { "position": 1870, "type": "N-linked (GlcNAc...) (hybrid) asparagine; alternate" }, { "position": 2014, "type": "N-linked (GlcNAc...) (high mannose) asparagine" }, { "position": 2123, "type": "N-linked (GlcNAc...) (high mannose) asparagine" }, { "position": 2251, "type": "N-linked (GlcNAc...) (complex) asparagine; alternate" }, { "position": 2251, "type": "N-linked (GlcNAc...) (hybrid) asparagine; alternate" }, { "position": 2296, "type": "N-linked (GlcNAc...) (high mannose) asparagine" } ], "id": "P01267", "name": "Thyroglobulin (Tg)", "organism": "Bos taurus", "uniprot_id": "P01267" }, { "function": "Stress-activated serine/threonine-protein kinase involved in cytokine production, endocytosis, reorganization of the cytoskeleton, cell migration, cell cycle control, chromatin remodeling, DNA damage response and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. Phosphorylates ALOX5, CDC25B, CDC25C, CEP131, ELAVL1, HNRNPA0, HSP27/HSPB1, KRT18, KRT20, LIMK1, LSP1, PABPC1, PARN, PDE4A, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Phosphorylates HSF1; leading to the interaction with HSP90 proteins and inhibiting HSF1 homotrimerization, DNA-binding and transactivation activities (PubMed:16278218). Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to the dissociation of HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impairment of their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins ELAVL1, HNRNPA0, PABPC1 and TTP/ZFP36, leading to the regulation of the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity, leading to inhibition of dependent degradation of ARE-containing transcripts. Phosphorylates CEP131 in response to cellular stress induced by ultraviolet irradiation which promotes binding of CEP131 to 14-3-3 proteins and inhibits formation of novel centriolar satellites (PubMed:26616734). Also involved in late G2/M checkpoint following DNA damage through a process of post-transcriptional mRNA stabilization: following DNA damage, relocalizes from nucleus to cytoplasm and phosphorylates HNRNPA0 and PARN, leading to stabilization of GADD45A mRNA. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3", "gene_name": "MAPKAPK2", "glycan_count": 0, "glycosylation_sites": [], "id": "P49137", "name": "Malic Enzyme 1 (ME1)", "organism": "Homo sapiens", "uniprot_id": "P49137" }, { "function": "RNA reader protein, which recognizes and binds specific RNAs, thereby regulating RNA metabolic processes, such as pre-mRNA splicing, circular RNA (circRNA) formation, mRNA export, mRNA stability and/or translation (PubMed:10535969, PubMed:11297509, PubMed:11917126, PubMed:12467586, PubMed:15568022, PubMed:31868295, PubMed:36088389). Involved in various cellular processes, such as mRNA storage into stress granules, apoptosis, lipid deposition, interferon response, glial cell fate and development (PubMed:10535969, PubMed:11297509, PubMed:11917126, PubMed:12467586, PubMed:15568022, PubMed:31868295). Binds to the 5'-NACUAAY-N(1,20)-UAAY-3' RNA core sequence (PubMed:16041388). Acts as a mRNA modification reader that specifically recognizes and binds mRNA transcripts modified by internal N(7)-methylguanine (m7G) (By similarity). Promotes the formation of circular RNAs (circRNAs) during the epithelial to mesenchymal transition and in cardiomyocytes: acts by binding to sites flanking circRNA-forming exons (PubMed:37272356). CircRNAs are produced by back-splicing circularization of pre-mRNAs (PubMed:37272356). Plays a central role in myelinization via 3 distinct mechanisms (PubMed:10864952, PubMed:11917126, PubMed:12467586, PubMed:15568022, PubMed:20956316, PubMed:21253564). First, acts by protecting and promoting stability of target mRNAs such as MBP, SIRT2 and CDKN1B, which promotes oligodendrocyte differentiation (PubMed:10864952, PubMed:15568022, PubMed:28188285). Second, participates in mRNA transport by regulating the nuclear export of MBP mRNA (PubMed:12467586). Finally, indirectly regulates mRNA splicing of MAG pre-mRNA during oligodendrocyte differentiation by acting as a negative regulator of MAG exon 12 alternative splicing: acts by binding to HNRNPA1 mRNA splicing factor, preventing its translation (PubMed:11917126, PubMed:20956316, PubMed:21253564). Involved in microglia differentiation and remyelination by regulating microexon alternative splicing of the Rho GTPase pathway (PubMed:33045062, PubMed:33378678). Involved in macrophage differentiation: promotes monocyte differentiation by regulating pre-mRNA splicing in naive peripheral blood monocytes (PubMed:36088389). Acts as an important regulator of muscle development: required for the contractile function of cardiomyocytes by regulating alternative splicing of cardiomyocyte transcripts (PubMed:33397958, PubMed:36627242). Acts as a negative regulator of thermogenesis by decreasing stability, nuclear export and translation of mRNAs encoding PPARGC1A and UCP1 (PubMed:31868295). Also required for visceral endoderm function and blood vessel development (PubMed:11892011, PubMed:16470614). May also play a role in smooth muscle development (PubMed:14706070). In addition to its RNA-binding activity, also acts as a nuclear transcription coactivator for SREBF2/SREBP2 (PubMed:33942715, PubMed:34021134)", "gene_name": "Qki", "glycan_count": 0, "glycosylation_sites": [], "id": "Q61110", "name": "Type 1 Deiodinase (D1)", "organism": "Mus musculus", "uniprot_id": "Q9QYS9" }, { "function": "Cytokine with a wide variety of biological functions in immunity, tissue regeneration, and metabolism. Binds to IL6R, then the complex associates to the signaling subunit IL6ST/gp130 to trigger the intracellular IL6-signaling pathway. The interaction with the membrane-bound IL6R and IL6ST stimulates 'classic signaling', whereas the binding of IL6 and soluble IL6R to IL6ST stimulates 'trans-signaling'. Alternatively, 'cluster signaling' occurs when membrane-bound IL6:IL6R complexes on transmitter cells activate IL6ST receptors on neighboring receiver cells", "gene_name": "Il6", "glycan_count": 0, "glycosylation_sites": [], "id": "P20607", "name": "Interleukin-6 (IL-6)", "organism": "Rattus norvegicus", "uniprot_id": "P20607" }, { "function": "Cytokine that can act as a growth factor for activated T and NK cells, enhance the lytic activity of NK/lymphokine-activated killer cells, and stimulate the production of IFN-gamma by resting PBMC", "gene_name": "IL12B", "glycan_count": 5, "glycosylation_sites": [ { "position": 135, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 222, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 319, "type": "C-linked (Man) tryptophan" } ], "id": "P29460", "name": "Interleukin-10 (IL-10)", "organism": "Homo sapiens", "uniprot_id": "P29460" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01750", "name": "CD4", "organism": "Mus musculus", "uniprot_id": "P01750" }, { "function": "Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c (By similarity). The 2 core subunits UQCRC1/QCR1 and UQCRC2/QCR2 are homologous to the 2 mitochondrial-processing peptidase (MPP) subunits beta-MPP and alpha-MPP respectively, and they seem to have preserved their MPP processing properties (By similarity). May be involved in the in situ processing of UQCRFS1 into the mature Rieske protein and its mitochondrial targeting sequence (MTS)/subunit 9 when incorporated into complex III (Probable). Seems to play an important role in the maintenance of proper mitochondrial function in nigral dopaminergic neurons (PubMed:33141179)", "gene_name": "UQCRC1", "glycan_count": 4, "glycosylation_sites": [], "id": "P31930", "name": "UQCRC1", "organism": "Homo sapiens", "uniprot_id": "P31930" }, { "function": "Cytokine constitutively present intracellularly in nearly all resting non-hematopoietic cells that plays an important role in inflammation and bridges the innate and adaptive immune systems (PubMed:26439902). After binding to its receptor IL1R1 together with its accessory protein IL1RAP, forms the high affinity interleukin-1 receptor complex (PubMed:17507369, PubMed:2950091). Signaling involves the recruitment of adapter molecules such as MYD88, IRAK1 or IRAK4 (PubMed:17507369). In turn, mediates the activation of NF-kappa-B and the three MAPK pathways p38, p42/p44 and JNK pathways (PubMed:14687581). Within the cell, acts as an alarmin and cell death results in its liberation in the extracellular space after disruption of the cell membrane to induce inflammation and alert the host to injury or damage (PubMed:15679580). In addition to its role as a danger signal, which occurs when the cytokine is passively released by cell necrosis, directly senses DNA damage and acts as a signal for genotoxic stress without loss of cell integrity (PubMed:26439902)", "gene_name": "IL1A", "glycan_count": 0, "glycosylation_sites": [ { "position": 102, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 141, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01583", "name": "IL-1\u03b1", "organism": "Homo sapiens", "uniprot_id": "P01583" }, { "function": "Part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linking of collagen fibrils. Required for normal bone density and normal skin stability via its role in hydroxylation of lysine residues in collagen alpha chains and in collagen fibril assembly", "gene_name": "P3H4", "glycan_count": 13, "glycosylation_sites": [ { "position": 361, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q92791", "name": "RHAMM (CD168)", "organism": "Homo sapiens", "uniprot_id": "Q92791" }, { "function": "ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds, and xenobiotics from cells. Lipophilic anion transporter that mediates ATP-dependent transport of glucuronide conjugates such as estradiol-17-beta-o-glucuronide and GSH conjugates such as leukotriene C4 (LTC4) (PubMed:12527806, PubMed:15256465). May contribute to regulate the transport of organic compounds in testes across the blood-testis-barrier (Probable). Mediates multidrug resistance (MDR) in cancer cells by preventing the intracellular accumulation of certain antitumor drugs, such as, docetaxel and paclitaxel (PubMed:15256465, PubMed:23087055). Does not transport glycocholic acid, taurocholic acid, MTX, folic acid, cAMP, or cGMP (PubMed:12527806)", "gene_name": "ABCC10", "glycan_count": 2, "glycosylation_sites": [], "id": "Q5T3U5", "name": "ABCC10 (MRP7)", "organism": "Homo sapiens", "uniprot_id": "Q5T3U5" }, { "function": "Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis (PubMed:20627126, PubMed:21364656, PubMed:25778398, PubMed:28218735, PubMed:9859993). Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis (PubMed:16322459). Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules (PubMed:20826784). Involved in the recruitment of CPC to centromeres during early mitosis via association with histone H3 phosphorylated at 'Thr-3' (H3pT3) during mitosis (PubMed:20929775). The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules (PubMed:18591255). May counteract a default induction of apoptosis in G2/M phase (PubMed:9859993). The acetylated form represses STAT3 transactivation of target gene promoters (PubMed:20826784). May play a role in neoplasia (PubMed:10626797). Inhibitor of CASP3 and CASP7 (PubMed:21536684). Essential for the maintenance of mitochondrial integrity and function (PubMed:25778398). Isoform 2 and isoform 3 do not appear to play vital roles in mitosis (PubMed:12773388, PubMed:16291752). Isoform 3 shows a marked reduction in its anti-apoptotic effects when compared with the displayed wild-type isoform (PubMed:10626797)", "gene_name": "BIRC5", "glycan_count": 0, "glycosylation_sites": [], "id": "O15392", "name": "Survivin (BIRC5)", "organism": "Homo sapiens", "uniprot_id": "O15392" }, { "function": "Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, copper homeostasis, mitogenic kinase signaling, cell proliferation, as well as cell invasion and metastasis (PubMed:11257230, PubMed:11257231, PubMed:11447297, PubMed:12121969, PubMed:12620238, PubMed:17560374, PubMed:17967870, PubMed:19473982, PubMed:20154138, PubMed:22103349, PubMed:9230442). Acts as a direct caspase inhibitor (PubMed:11257230, PubMed:11257231, PubMed:12620238). Directly bind to the active site pocket of CASP3 and CASP7 and obstructs substrate entry (PubMed:11257230, PubMed:11257231, PubMed:16352606, PubMed:16916640). Inactivates CASP9 by keeping it in a monomeric, inactive state (PubMed:12620238). Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and the target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, RIPK2, MAP3K2/MEKK2, DIABLO/SMAC, AIFM1, CCS, PTEN and BIRC5/survivin (PubMed:17560374, PubMed:17967870, PubMed:19473982, PubMed:20154138, PubMed:22103349, PubMed:22607974, PubMed:29452636, PubMed:30026309). Acts as an important regulator of innate immunity by mediating 'Lys-63'-linked polyubiquitination of RIPK2 downstream of NOD1 and NOD2, thereby transforming RIPK2 into a scaffolding protein for downstream effectors, ultimately leading to activation of the NF-kappa-B and MAP kinases signaling (PubMed:19667203, PubMed:22607974, PubMed:29452636, PubMed:30026309). 'Lys-63'-linked polyubiquitination of RIPK2 also promotes recruitment of the LUBAC complex to RIPK2 (PubMed:22607974, PubMed:29452636). Regulates the BMP signaling pathway and the SMAD and MAP3K7/TAK1 dependent pathways leading to NF-kappa-B and JNK activation (PubMed:17560374). Ubiquitination of CCS leads to enhancement of its chaperone activity toward its physiologic target, SOD1, rather than proteasomal degradation (PubMed:20154138). Ubiquitination of MAP3K2/MEKK2 and AIFM1 does not lead to proteasomal degradation (PubMed:17967870, PubMed:22103349). Plays a role in copper homeostasis by ubiquitinating COMMD1 and promoting its proteasomal degradation (PubMed:14685266). Can also function as E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation (PubMed:21145488). Ubiquitinates and therefore mediates the proteasomal degradation of BCL2 in response to apoptosis (PubMed:29020630). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner (PubMed:22095281). Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8 (PubMed:22095281). Acts as a positive regulator of Wnt signaling and ubiquitinates TLE1, TLE2, TLE3, TLE4 and AES (PubMed:22304967). Ubiquitination of TLE3 results in inhibition of its interaction with TCF7L2/TCF4 thereby allowing efficient recruitment and binding of the transcriptional coactivator beta-catenin to TCF7L2/TCF4 that is required to initiate a Wnt-specific transcriptional program (PubMed:22304967)", "gene_name": "XIAP", "glycan_count": 1, "glycosylation_sites": [], "id": "P98170", "name": "XIAP", "organism": "Homo sapiens", "uniprot_id": "P98170" }, { "function": "Apoptotic regulator capable of exerting proapoptotic and anti-apoptotic activities and plays crucial roles in apoptosis, cell proliferation, and cell cycle control (PubMed:11024045, PubMed:11084335, PubMed:11162435, PubMed:16729033, PubMed:17294084). Its anti-apoptotic activity is mediated through the inhibition of CASP3, CASP7 and CASP9, as well as by its E3 ubiquitin-protein ligase activity (PubMed:11024045, PubMed:16729033). As it is a weak caspase inhibitor, its anti-apoptotic activity is thought to be due to its ability to ubiquitinate DIABLO/SMAC targeting it for degradation thereby promoting cell survival (PubMed:16729033). May contribute to caspase inhibition, by blocking the ability of DIABLO/SMAC to disrupt XIAP/BIRC4-caspase interactions (PubMed:16729033). Protects against apoptosis induced by TNF or by chemical agents such as adriamycin, etoposide or staurosporine (PubMed:11084335, PubMed:11162435, PubMed:11865055). Suppression of apoptosis is mediated by activation of MAPK8/JNK1, and possibly also of MAPK9/JNK2 (PubMed:11865055). This activation depends on TAB1 and MAP3K7/TAK1 (PubMed:11865055). In vitro, inhibits CASP3 and proteolytic activation of pro-CASP9 (PubMed:11024045)", "gene_name": "BIRC7", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96CA5", "name": "Livin (BIRC7)", "organism": "Homo sapiens", "uniprot_id": "Q96CA5" }, { "function": "May play a role in tumor angiogenesis", "gene_name": "PLXDC2", "glycan_count": 30, "glycosylation_sites": [ { "position": 103, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 160, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6UX71", "name": "CMTM6", "organism": "Homo sapiens", "uniprot_id": "Q6UX71" }, { "function": "Membrane-anchored forms may play a role in cellular adhesion", "gene_name": "MSLN", "glycan_count": 31, "glycosylation_sites": [ { "position": 57, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 388, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 496, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 523, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13421", "name": "MASP1", "organism": "Homo sapiens", "uniprot_id": "Q13421" }, { "function": "Pore-forming component of the membrane attack complex (MAC), a multiprotein complex activated by the complement cascade, which inserts into a target cell membrane and forms a pore, leading to target cell membrane rupture and cell lysis (PubMed:22832194, PubMed:26841837, PubMed:26841934, PubMed:27052168, PubMed:30552328, PubMed:6177822, PubMed:9212048, PubMed:9634479). The MAC is initiated by proteolytic cleavage of C5 into complement C5b in response to the classical, alternative, lectin and GZMK complement pathways (PubMed:9212048, PubMed:9634479). The complement pathways consist in a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system (PubMed:9212048, PubMed:9634479). Constitutes the pore-forming subunit of the MAC complex: during MAC assembly, C9 associates with the C5b8 intermediate complex, and polymerizes to complete the pore (PubMed:26841934, PubMed:30111885, PubMed:30552328, PubMed:34752492, PubMed:4055801, PubMed:6177822)", "gene_name": "C9", "glycan_count": 56, "glycosylation_sites": [ { "position": 48, "type": "C-linked (Man) tryptophan" }, { "position": 51, "type": "C-linked (Man) tryptophan; partial" }, { "position": 277, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 415, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P02748", "name": "C9", "organism": "Homo sapiens", "uniprot_id": "P02748" }, { "function": "Directly regulates filament dynamics and has been implicated in a number of complex developmental and morphological processes, including mRNA localization and the establishment of cell polarity", "gene_name": "CAP1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q01518", "name": "CAP1", "organism": "Homo sapiens", "uniprot_id": "Q01518" }, { "function": "F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Plays a role in the regulation of cell morphology and cytoskeletal organization. Forms, with CAPZB, the barbed end of the fast growing ends of actin filaments in the dynactin complex and stabilizes dynactin structure. The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity)", "gene_name": "CAPZB", "glycan_count": 1, "glycosylation_sites": [], "id": "P47756", "name": "CAPZB", "organism": "Homo sapiens", "uniprot_id": "P47756" }, { "function": "Neural cell adhesion molecule involved in the dynamics of cell adhesion and in the generation of transmembrane signals at tyrosine kinase receptors. During brain development, critical in multiple processes, including neuronal migration, axonal growth and fasciculation, and synaptogenesis. In the mature brain, plays a role in the dynamics of neuronal structure and function, including synaptic plasticity", "gene_name": "L1CAM", "glycan_count": 58, "glycosylation_sites": [ { "position": 100, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 203, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 247, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 294, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 433, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 479, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 490, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 505, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 588, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 671, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 726, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 777, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 825, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 849, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 876, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 979, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1022, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1030, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1071, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1105, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P32004", "name": "L1CAM", "organism": "Homo sapiens", "uniprot_id": "P32004" }, { "function": "ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). During leukocyte trans-endothelial migration, ICAM1 engagement promotes the assembly of endothelial apical cups through ARHGEF26/SGEF and RHOG activation (By similarity)", "gene_name": "Icam1", "glycan_count": 7, "glycosylation_sites": [ { "position": 47, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 185, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 204, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 267, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 311, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 362, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 388, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 409, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 456, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 469, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P13597", "name": "ICAM-1 (Intercellular adhesion molecule 1)", "organism": "Mus musculus", "uniprot_id": "P13597" }, { "function": "Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, neuronal growth cone collapse and cell migration (By similarity)", "gene_name": "DPYSL4", "glycan_count": 1, "glycosylation_sites": [], "id": "O14531", "name": "NG2 (Neural/glial antigen 2; CSPG4)", "organism": "Homo sapiens", "uniprot_id": "O14531" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9JKC6/Q9JKC7", "name": "YM1/2 (Chitinase-like proteins)", "organism": "", "uniprot_id": "" }, { "function": "Required for oligodendrocyte and motor neuron specification in the spinal cord, as well as for the development of somatic motor neurons in the hindbrain (PubMed:11955448, PubMed:12121626, PubMed:16908628). Functions together with ZNF488 to promote oligodendrocyte differentiation (PubMed:16908628). Cooperates with OLIG1 to establish the pMN domain of the embryonic neural tube (PubMed:11955448, PubMed:12121626). Antagonist of V2 interneuron and of NKX2-2-induced V3 interneuron development (PubMed:11955448, PubMed:12121626)", "gene_name": "Olig2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9EQW6", "name": "OLIG2", "organism": "Mus musculus", "uniprot_id": "Q9EQW6" }, { "function": "Required for brain and eye development. Promotes the disassembly of phosphorylated vimentin intermediate filaments (IF) during mitosis and may play a role in the trafficking and distribution of IF proteins and other cellular factors to daughter cells during progenitor cell division. Required for survival, renewal and mitogen-stimulated proliferation of neural progenitor cells (By similarity)", "gene_name": "NES", "glycan_count": 1, "glycosylation_sites": [], "id": "P48681", "name": "Nestin", "organism": "Homo sapiens", "uniprot_id": "P48681" }, { "function": "Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Down-regulates basal and activated transcription. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Inhibits transcriptional activation of PAX3 and ETS1 through direct protein-protein interactions. Modulates PAX5 activity; the function seems to involve CREBBP. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Acts as a histone chaperone that facilitates deposition of histone H3.3. Acts as a targeting component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Does not affect the ATPase activity of ATRX but alleviates its transcription repression activity. Upon neuronal activation associates with regulatory elements of selected immediate early genes where it promotes deposition of histone H3.3 which may be linked to transcriptional induction of these genes. Required for the recruitment of histone H3.3:H4 dimers to PML-nuclear bodies (PML-NBs); the process is independent of ATRX and facilitated by ASF1A; PML-NBs are suggested to function as regulatory sites for the incorporation of newly synthesized histone H3.3 into chromatin. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Plays a role as a positive regulator of the heat shock transcription factor HSF1 activity during the stress protein response (By similarity)", "gene_name": "Daxx", "glycan_count": 0, "glycosylation_sites": [], "id": "O35613", "name": "Dcx (Doublecortin)", "organism": "Mus musculus", "uniprot_id": "O35613" }, { "function": "Reduces disulfideprotein thioredoxin (Trx) to its dithiol-containing form. Homodimeric flavoprotein involved in the regulation of cellular redox reactions, growth and differentiation. Contains a selenocysteine residue at the C-terminal active site that is essential for catalysis. Also has reductase activity on hydrogen peroxide (H2O2)", "gene_name": "Txnrd1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9JMH6", "name": "NeuN (Rbfox3)", "organism": "Mus musculus", "uniprot_id": "Q9JMH6" }, { "function": "ATP-dependent transporter of the ATP-binding cassette (ABC) family that binds and hydrolyzes ATP to enable active transport of various substrates including many drugs, toxicants and endogenous compound across cell membranes (PubMed:10359813, PubMed:11581266, PubMed:15083066). Transports glucuronide conjugates such as bilirubin diglucuronide, estradiol-17-beta-o-glucuronide and GSH conjugates such as leukotriene C4 (LTC4) (PubMed:11581266, PubMed:15083066). Transports also various bile salts (taurocholate, glycocholate, taurochenodeoxycholate-3-sulfate, taurolithocholate- 3-sulfate) (By similarity). Does not contribute substantially to bile salt physiology but provides an alternative route for the export of bile acids and glucuronides from cholestatic hepatocytes (By similarity). May contribute to regulate the transport of organic compounds in testes across the blood-testis-barrier (Probable). Can confer resistance to various anticancer drugs, methotrexate, tenoposide and etoposide, by decreasing accumulation of these drugs in cells (PubMed:10359813, PubMed:11581266)", "gene_name": "ABCC3", "glycan_count": 2, "glycosylation_sites": [ { "position": 18, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1006, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1007, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O15438", "name": "Multidrug resistance-associated protein 2 (MRP2)", "organism": "Homo sapiens", "uniprot_id": "O15438" }, { "function": "As a major transporter of conjugated bile salts from plasma into the hepatocyte, it plays a key role in the enterohepatic circulation of bile salts necessary for the solubilization and absorption of dietary fat and fat-soluble vitamins (PubMed:14660639, PubMed:24867799, PubMed:34060352, PubMed:8132774). It is strictly dependent on the extracellular presence of sodium (PubMed:14660639, PubMed:24867799, PubMed:34060352, PubMed:8132774). It exhibits broad substrate specificity and transports various bile acids, such as taurocholate, cholate, as well as non-bile acid organic compounds, such as estrone sulfate (PubMed:14660639, PubMed:34060352). Works collaboratively with the ileal transporter (NTCP2), the organic solute transporter (OST), and the bile salt export pump (BSEP), to ensure efficacious biological recycling of bile acids during enterohepatic circulation (PubMed:33222321)", "gene_name": "SLC10A1", "glycan_count": 0, "glycosylation_sites": [ { "position": 5, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 11, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q14973", "name": "Na+-taurocholate cotransporting polypeptide (NTCP)", "organism": "Homo sapiens", "uniprot_id": "Q14973" }, { "function": "Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen", "gene_name": "SOD3", "glycan_count": 91, "glycosylation_sites": [ { "position": 107, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 229, "type": "N-linked (Glc) (glycation) lysine; in vitro" }, { "position": 230, "type": "N-linked (Glc) (glycation) lysine; in vitro" } ], "id": "P08294", "name": "Superoxide dismutase (SOD)", "organism": "Homo sapiens", "uniprot_id": "P08294" }, { "function": "Phosphorylation-dependent transcription factor that stimulates transcription upon binding to the DNA cAMP response element (CRE), a sequence present in many viral and cellular promoters (By similarity). Transcription activation is enhanced by the TORC coactivators which act independently of Ser-119 phosphorylation (PubMed:14536081). Involved in different cellular processes including the synchronization of circadian rhythmicity and the differentiation of adipose cells (By similarity). Regulates the expression of apoptotic and inflammatory response factors in cardiomyocytes in response to ERFE-mediated activation of AKT signaling (By similarity)", "gene_name": "CREB1", "glycan_count": 3, "glycosylation_sites": [], "id": "P16220", "name": "CREB", "organism": "Homo sapiens", "uniprot_id": "P16220" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q13131/Q9Y478", "name": "AMPK (PRKAA1/2)", "organism": "", "uniprot_id": "" }, { "function": "Chemokine released during platelet aggregation that plays a role in different biological processes including hematopoiesis, cell proliferation, differentiation, and activation (PubMed:29930254, PubMed:9531587). Acts via different functional receptors including CCR1, CXCR3A or CXCR3B (PubMed:18174362, PubMed:29930254). Upon interaction with CXCR3A receptor, induces activated T-lymphocytes migration mediated via downstream Ras/extracellular signal-regulated kinase (ERK) signaling (PubMed:18174362, PubMed:24469069). Neutralizes the anticoagulant effect of heparin by binding more strongly to heparin than to the chondroitin-4-sulfate chains of the carrier molecule. Plays a role in the inhibition of hematopoiesis and in the maintenance of hematopoietic stem cell (HSC) quiescence (PubMed:9531587). Chemotactic for neutrophils and monocytes via CCR1 (PubMed:29930254). Inhibits endothelial cell proliferation. In cooperation with toll-like receptor 8/TLR8, induces chromatin remodeling and activates inflammatory gene expression via the TBK1-IRF5 axis (PubMed:35701499). In addition, induces myofibroblast differentiation and collagen synthesis in different precursor cells, including endothelial cells, by stimulating endothelial-to-mesenchymal transition (PubMed:34986347). Interacts with thrombomodulin/THBD to enhance the activation of protein C and thus potentiates its anticoagulant activity (PubMed:9395524)", "gene_name": "PF4", "glycan_count": 0, "glycosylation_sites": [], "id": "P02776", "name": "Platelet Factor 4 (PF4)", "organism": "Homo sapiens", "uniprot_id": "P02776" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P05109/P06702", "name": "S100A8/A9 (Calprotectin)", "organism": "", "uniprot_id": "" }, { "function": "Endothelial cell receptor that plays a critical role in regulating several physiological processes including hemostasis, coagulation, fibrinolysis, inflammation, and angiogenesis (PubMed:10761923). Acts as a cofactor for thrombin activation of protein C/PROC on the surface of vascular endothelial cells leading to initiation of the activated protein C anticoagulant pathway (PubMed:29323190, PubMed:33836597, PubMed:9395524). Also accelerates the activation of the plasma carboxypeptidase B2/CPB2, which catalyzes removal of C-terminal basic amino acids from its substrates including kinins or anaphylatoxins leading to fibrinolysis inhibition (PubMed:26663133). Plays critical protective roles in changing the cleavage specificity of protease-activated receptor 1/PAR1, inhibiting endothelial cell permeability and inflammation (By similarity). Suppresses inflammation distinctly from its anticoagulant cofactor activity by sequestering HMGB1 thereby preventing it from engaging cellular receptors such as RAGE and contributing to the inflammatory response (PubMed:15841214)", "gene_name": "THBD", "glycan_count": 2, "glycosylation_sites": [ { "position": 47, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 115, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 116, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 382, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 409, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 490, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 492, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" } ], "id": "P07204", "name": "Thrombomodulin (TM)", "organism": "Homo sapiens", "uniprot_id": "P07204" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P13612/P05556", "name": "Integrin \u03b14\u03b21 (VLA-4)", "organism": "", "uniprot_id": "" }, { "function": "Cell adhesion leukocyte receptor expressed by mucosal venules, helps to direct lymphocyte traffic into mucosal tissues including the Peyer patches and the intestinal lamina propria. It can bind both integrin alpha-4/beta-7 and L-selectin, regulating both the passage and retention of leukocytes. Isoform 2, lacking the mucin-like domain, may be specialized in supporting integrin alpha-4/beta-7-dependent adhesion strengthening, independent of L-selectin binding", "gene_name": "MADCAM1", "glycan_count": 2, "glycosylation_sites": [ { "position": 83, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13477", "name": "MadCAM-1", "organism": "Homo sapiens", "uniprot_id": "Q13477" }, { "function": "May regulate the dynamics and distribution of mitochondria in neural cells", "gene_name": "ARMCX6", "glycan_count": 0, "glycosylation_sites": [], "id": "Q7L4S7", "name": "SGLT2", "organism": "Homo sapiens", "uniprot_id": "Q7L4S7" }, { "function": "Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides (PubMed:17889651, PubMed:21078852). Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. May also activate immune cells and promote apoptosis in response to the lipid moiety of lipoproteins (PubMed:10426995, PubMed:10426996). Recognizes mycoplasmal macrophage-activating lipopeptide-2kD (MALP-2), soluble tuberculosis factor (STF), phenol-soluble modulin (PSM) and B.burgdorferi outer surface protein A lipoprotein (OspA-L) cooperatively with TLR6 (PubMed:11441107). Stimulation of monocytes in vitro with M.tuberculosis PstS1 induces p38 MAPK and ERK1/2 activation primarily via this receptor, but also partially via TLR4 (PubMed:16622205). MAPK activation in response to bacterial peptidoglycan also occurs via this receptor (PubMed:16622205). Acts as a receptor for M.tuberculosis lipoproteins LprA, LprG, LpqH and PstS1, some lipoproteins are dependent on other coreceptors (TLR1, CD14 and/or CD36); the lipoproteins act as agonists to modulate antigen presenting cell functions in response to the pathogen (PubMed:19362712). M.tuberculosis HSP70 (dnaK) but not HSP65 (groEL-2) acts via this protein to stimulate NF-kappa-B expression (PubMed:15809303). Recognizes M.tuberculosis major T-antigen EsxA (ESAT-6) which inhibits downstream MYD88-dependent signaling (shown in mouse) (By similarity). Forms activation clusters composed of several receptors depending on the ligand, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Forms the cluster TLR2:TLR6:CD14:CD36 in response to diacylated lipopeptides and TLR2:TLR1:CD14 in response to triacylated lipopeptides (PubMed:16880211). Required for normal uptake of M.tuberculosis, a process that is inhibited by M.tuberculosis LppM (By similarity)", "gene_name": "TLR2", "glycan_count": 16, "glycosylation_sites": [ { "position": 114, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 199, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 414, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 442, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O60603", "name": "Toll-like receptor 2 (TLR2)", "organism": "Homo sapiens", "uniprot_id": "O60603" }, { "function": "Abundant protease in the cytosolic granules of cytotoxic T-cells and NK-cells which activates caspase-independent pyroptosis when delivered into the target cell through the immunological synapse (PubMed:12819770, PubMed:32299851, PubMed:3257574, PubMed:3262682, PubMed:3263427). It cleaves after Lys or Arg (PubMed:12819770, PubMed:32299851). Once delivered into the target cell, acts by catalyzing cleavage of gasdermin-B (GSDMB), releasing the pore-forming moiety of GSDMB, thereby triggering pyroptosis and target cell death (PubMed:32299851, PubMed:34022140, PubMed:36157507, PubMed:36899106). Cleaves APEX1 after 'Lys-31' and destroys its oxidative repair activity (PubMed:12524539). Cleaves the nucleosome assembly protein SET after 'Lys-189', which disrupts its nucleosome assembly activity and allows the SET complex to translocate into the nucleus to nick and degrade the DNA (PubMed:11555662, PubMed:12628186, PubMed:16818237)", "gene_name": "GZMA", "glycan_count": 8, "glycosylation_sites": [ { "position": 170, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P12544", "name": "Granzyme A", "organism": "Homo sapiens", "uniprot_id": "P12544" }, { "function": "Receptor for extracellular adenine nucleotides such as ADP (PubMed:25822790, PubMed:9038354, PubMed:9442040). In platelets, binding to ADP leads to mobilization of intracellular calcium ions via activation of phospholipase C, a change in platelet shape, and ultimately platelet aggregation (PubMed:9442040)", "gene_name": "P2RY1", "glycan_count": 0, "glycosylation_sites": [ { "position": 11, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 27, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 113, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 197, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P47900", "name": "P2Y1 receptor", "organism": "Homo sapiens", "uniprot_id": "P47900" }, { "function": "High affinity receptor that binds the activated thrombin, leading to calcium release from intracellular stores (PubMed:1672265, PubMed:8136362). The thrombin-activated receptor signaling pathway is mediated through PTX-insensitive G proteins, activation of phospholipase C resulting in the production of 1D-myo-inositol 1,4,5-trisphosphate (InsP3) which binds to InsP3 receptors causing calcium release from the stores (By similarity). In astrocytes, the calcium released into the cytosol allows the Ca(2+)-dependent release of L-glutamate into the synaptic cleft through BEST1, that targets the neuronal postsynaptic GRIN2A/NMDAR receptor resulting in the synaptic plasticity regulation (By similarity). May play a role in platelets activation and in vascular development (PubMed:10079109). Mediates up-regulation of pro-inflammatory cytokines, such as MCP-1/CCL2 and IL6, triggered by coagulation factor Xa (F10) in cardiac fibroblasts and umbilical vein endothelial cells (PubMed:30568593, PubMed:34831181)", "gene_name": "F2R", "glycan_count": 4, "glycosylation_sites": [ { "position": 35, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 62, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 75, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 250, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 259, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P25116", "name": "Thrombin receptor (PAR-1)", "organism": "Homo sapiens", "uniprot_id": "P25116" }, { "function": "Cytokine that in its homotrimeric form binds to TNFRSF1A/TNFR1, TNFRSF1B/TNFBR and TNFRSF14/HVEM (PubMed:9462508). In its heterotrimeric form with LTB binds to TNFRSF3/LTBR (PubMed:24248355). Lymphotoxin is produced by lymphocytes and is cytotoxic for a wide range of tumor cells in vitro and in vivo", "gene_name": "LTA", "glycan_count": 10, "glycosylation_sites": [ { "position": 41, "type": "O-linked (GalNAc...) threonine; partial" }, { "position": 96, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01374", "name": "TNF-\u03b2", "organism": "Homo sapiens", "uniprot_id": "P01374" }, { "function": "Catalyzes the reduction of hydroperoxides in a glutathione-dependent manner thus regulating cellular redox homeostasis (PubMed:11115402, PubMed:36608588). Can reduce small soluble hydroperoxides such as H2O2, cumene hydroperoxide and tert-butyl hydroperoxide, as well as several fatty acid-derived hydroperoxides (PubMed:11115402, PubMed:36608588). In platelets catalyzes the reduction of 12-hydroperoxyeicosatetraenoic acid, the primary product of the arachidonate 12-lipoxygenase pathway (PubMed:11115402)", "gene_name": "GPX1", "glycan_count": 1, "glycosylation_sites": [], "id": "P07203", "name": "Glutathione peroxidase", "organism": "Homo sapiens", "uniprot_id": "P07203" }, { "function": "Catalytic subunit of the phagocyte NADPH oxidase complex that mediates the transfer of electrons from cytosolic NADPH to O2 to produce the superoxide anion (O2(-)) (PubMed:15338276, PubMed:36241643, PubMed:36413210, PubMed:38355798). In the activated complex, electrons are first transferred from NADPH to flavin adenine dinucleotide (FAD) and subsequently transferred via two heme molecules to molecular oxygen, producing superoxide through an outer-sphere reaction (Probable) (PubMed:38355798). Activation of the NADPH oxidase complex is initiated by the assembly of cytosolic subunits of the NADPH oxidase complex with the core NADPH oxidase complex to form a complex at the plasma membrane or phagosomal membrane (PubMed:19028840, PubMed:38355798). This activation process is initiated by phosphorylation dependent binding of the cytosolic NCF1/p47-phox subunit to the C-terminus of CYBA/p22-phox (By similarity). NADPH oxidase complex assembly is impaired through interaction with NRROS (By similarity)", "gene_name": "CYBB", "glycan_count": 10, "glycosylation_sites": [ { "position": 132, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 149, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 240, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P04839", "name": "Nox-2 (NADPH oxidase 2)", "organism": "Homo sapiens", "uniprot_id": "P04839" }, { "function": "Regulates glucokinase (GCK) by forming an inactive complex with this enzyme (PubMed:23621087, PubMed:23733961). Acts by promoting GCK recruitment to the nucleus, possibly to provide a reserve of GCK that can be quickly released in the cytoplasm after a meal (PubMed:10456334). The affinity of GCKR for GCK is modulated by fructose metabolites: GCKR with bound fructose 6-phosphate has increased affinity for GCK, while GCKR with bound fructose 1-phosphate has strongly decreased affinity for GCK and does not inhibit GCK activity (PubMed:23621087, PubMed:23733961)", "gene_name": "GCKR", "glycan_count": 0, "glycosylation_sites": [], "id": "Q14397", "name": "GCKR", "organism": "Homo sapiens", "uniprot_id": "Q14397" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6ZVQ5", "name": "MBOAT7", "organism": "", "uniprot_id": "Q6ZVQ5" }, { "function": "May play a major role in the structural organization and calcification of developing enamel (PubMed:18252228). May play a role in keratin cytoskeleton disassembly by recruiting CSNK1A1 to keratin filaments. Thereby, it may regulate epithelial cell migration (PubMed:23902688)", "gene_name": "FAM83H", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6ZRV2", "name": "TM6SF2", "organism": "Homo sapiens", "uniprot_id": "Q6ZRV2" }, { "function": "Cell adhesion protein that is required for normal responses to cell-cell contacts in brain and in the peripheral nervous system. Plays a role in neurite outgrowth in response to contactin binding. Plays a role in mediating cell-cell contacts between Schwann cells and axons. Plays a role in the formation and maintenance of the nodes of Ranvier on myelinated axons. Nodes of Ranvier contain clustered sodium channels that are crucial for the saltatory propagation of action potentials along myelinated axons. During development, nodes of Ranvier are formed by the fusion of two heminodes. Required for normal clustering of sodium channels at heminodes; not required for the formation of mature nodes with normal sodium channel clusters. Required, together with GLDN, for maintaining NFASC and sodium channel clusters at mature nodes of Ranvier", "gene_name": "NRCAM", "glycan_count": 72, "glycosylation_sites": [ { "position": 83, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 223, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 245, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 251, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 276, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 314, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 433, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 507, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 619, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 716, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 802, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 858, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 993, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1009, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1019, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1072, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1083, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1115, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q92823", "name": "NCAN", "organism": "Homo sapiens", "uniprot_id": "Q92823" }, { "function": "Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate", "gene_name": "FDPS", "glycan_count": 0, "glycosylation_sites": [], "id": "P08836", "name": "ALT (Alanine Aminotransferase)", "organism": "Gallus gallus", "uniprot_id": "P08836" }, { "function": "Receptor for TNFSF13/APRIL and TNFSF13B/TALL1/BAFF/BLYS that binds both ligands with similar high affinity. Mediates calcineurin-dependent activation of NF-AT, as well as activation of NF-kappa-B and AP-1. Involved in the stimulation of B- and T-cell function and the regulation of humoral immunity", "gene_name": "TNFRSF13B", "glycan_count": 0, "glycosylation_sites": [ { "position": 128, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O14836", "name": "TNFRSF13B (TACI)", "organism": "Homo sapiens", "uniprot_id": "O14836" }, { "function": "The GPIb-V-IX complex functions as the vWF receptor and mediates vWF-dependent platelet adhesion to blood vessels. The adhesion of platelets to injured vascular surfaces in the arterial circulation is a critical initiating event in hemostasis. GP-IX may provide for membrane insertion and orientation of GP-Ib", "gene_name": "GP9", "glycan_count": 0, "glycosylation_sites": [ { "position": 60, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P14770", "name": "CD42a (GP9)", "organism": "Homo sapiens", "uniprot_id": "P14770" }, { "function": "Integrin alpha-V/beta-3 (ITGAV:ITGB3) is a receptor for cytotactin, fibronectin, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin, vitronectin and von Willebrand factor. Integrin alpha-IIb/beta-3 (ITGA2B:ITGB3) is a receptor for fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. Integrins alpha-IIb/beta-3 and alpha-V/beta-3 recognize the sequence R-G-D in a wide array of ligands. Integrin alpha-IIb/beta-3 recognizes the sequence H-H-L-G-G-G-A-K-Q-A-G-D-V in fibrinogen gamma chain (By similarity). Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen (PubMed:9111081). This step leads to rapid platelet aggregation which physically plugs ruptured endothelial surface. Fibrinogen binding enhances SELP expression in activated platelets (By similarity). ITGAV:ITGB3 binds to fractalkine (CX3CL1) and acts as its coreceptor in CX3CR1-dependent fractalkine signaling (PubMed:23125415, PubMed:24789099). ITGAV:ITGB3 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling (PubMed:20682778). ITGAV:ITGB3 binds to FGF1 and this binding is essential for FGF1 signaling (PubMed:18441324). ITGAV:ITGB3 binds to FGF2 and this binding is essential for FGF2 signaling (PubMed:28302677). ITGAV:ITGB3 binds to IGF1 and this binding is essential for IGF1 signaling (PubMed:19578119). ITGAV:ITGB3 binds to IGF2 and this binding is essential for IGF2 signaling (PubMed:28873464). ITGAV:ITGB3 binds to IL1B and this binding is essential for IL1B signaling (PubMed:29030430). ITGAV:ITGB3 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1 (PubMed:18635536, PubMed:25398877). ITGAV:ITGB3 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1 (PubMed:12807887). In brain, plays a role in synaptic transmission and plasticity. Involved in the regulation of the serotonin neurotransmission, is required to localize to specific compartments within the synapse the serotonin receptor SLC6A4 and for an appropriate reuptake of serotonin. Controls excitatory synaptic strength by regulating GRIA2-containing AMPAR endocytosis, which affects AMPAR abundance and composition (By similarity). ITGAV:ITGB3 act as a receptor for CD40LG (PubMed:31331973). ITGAV:ITGB3 acts as a receptor for IBSP and promotes cell adhesion and migration to IBSP (PubMed:10640428)", "gene_name": "ITGB3", "glycan_count": 31, "glycosylation_sites": [ { "position": 125, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 346, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 397, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 478, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 585, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 680, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P05106", "name": "Integrin subunit beta 3 (ITGB3)", "organism": "Homo sapiens", "uniprot_id": "P05106" }, { "function": "Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to form an insoluble fibrin matrix. Has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways", "gene_name": "FGG", "glycan_count": 109, "glycosylation_sites": [ { "position": 78, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 334, "type": "N-linked (GlcNAc...) asparagine; in variant Asahi" } ], "id": "P02679", "name": "Fibrinogen gamma chain (FGG)", "organism": "Homo sapiens", "uniprot_id": "P02679" }, { "function": "Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics and cell shape. Part of the striatin-interacting phosphatase and kinase (STRIPAK) complexes. STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling. Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation", "gene_name": "STRIP1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q5VSL9", "name": "Platelet endothelial aggregation receptor 1 (PEAR1)", "organism": "Homo sapiens", "uniprot_id": "Q5VSL9" }, { "function": "Bactericidal C-type lectin which acts exclusively against Gram-positive bacteria and mediates bacterial killing by binding to surface-exposed carbohydrate moieties of peptidoglycan. Restricts bacterial colonization of the intestinal epithelial surface and consequently limits activation of adaptive immune responses by the microbiota", "gene_name": "REG3G", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6UW15", "name": "Regenerating islet-derived protein 3 gamma (Reg3\u03b3)", "organism": "Homo sapiens", "uniprot_id": "Q6UW15" }, { "function": "", "gene_name": "SSMEM1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8WWF3", "name": "Mucin 5AC (MUC5AC)", "organism": "Homo sapiens", "uniprot_id": "Q8WWF3" }, { "function": "Contributes to the lung's defense against inhaled microorganisms, organic antigens and toxins. Interacts with compounds such as bacterial lipopolysaccharides, oligosaccharides and fatty acids and modulates leukocyte action in immune response. May participate in the extracellular reorganization or turnover of pulmonary surfactant. Binds strongly maltose residues and to a lesser extent other alpha-glucosyl moieties", "gene_name": "SFTPD", "glycan_count": 0, "glycosylation_sites": [ { "position": 90, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P35247", "name": "Surfactant Protein D (SP-D)", "organism": "Homo sapiens", "uniprot_id": "P35247" }, { "function": "Promotes spermatogenesis and ovulation by stimulating the testes and ovaries to synthesize steroids", "gene_name": "LHB", "glycan_count": 32, "glycosylation_sites": [ { "position": 50, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01229", "name": "Luteinizing Hormone (LH)", "organism": "Homo sapiens", "uniprot_id": "P01229" }, { "function": "Stimulates the secretion of gonadotropins; it stimulates the secretion of both luteinizing and follicle-stimulating hormones", "gene_name": "GNRH1", "glycan_count": 0, "glycosylation_sites": [], "id": "P01148", "name": "Gonadotropin-Releasing Hormone (GnRH)", "organism": "Homo sapiens", "uniprot_id": "P01148" }, { "function": "ABCG5 and ABCG8 form an obligate heterodimer that mediates Mg(2+)- and ATP-dependent sterol transport across the cell membrane. Plays an essential role in the selective transport of the dietary cholesterol in and out of the enterocytes and in the selective sterol excretion by the liver into bile (PubMed:11099417, PubMed:11452359, PubMed:15054092, PubMed:27144356). Required for normal sterol homeostasis (PubMed:11099417, PubMed:11452359, PubMed:15054092). The heterodimer with ABCG5 has ATPase activity (PubMed:16893193, PubMed:20210363, PubMed:27144356)", "gene_name": "ABCG8", "glycan_count": 0, "glycosylation_sites": [ { "position": 619, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9H221", "name": "ABCG8", "organism": "Homo sapiens", "uniprot_id": "Q9H221" }, { "function": "ATP-dependent transporter of the ATP-binding cassette (ABC) family that may be involved in the cellular efflux of sterols, in particular cholesterol and desmosterol (a cholesterol precursor), to high-density lipoprotein (HDL) (PubMed:15240127, PubMed:33141061). May play an important role in the removal of amyloid-beta peptides from brain, in a process that can be antagonized by desmosterol. However it is unclear whether ABCG4 can directly transport amyloid-beta peptides or whether peptide export may be facilitated due to changes in the membrane lipid environment (By similarity). Induces apoptosis in various cells (PubMed:27228027)", "gene_name": "ABCG4", "glycan_count": 0, "glycosylation_sites": [ { "position": 422, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9H172", "name": "ABCG1", "organism": "Homo sapiens", "uniprot_id": "Q9H172" }, { "function": "Central enzyme in the extracellular metabolism of plasma lipoproteins. Synthesized mainly in the liver and secreted into plasma where it converts cholesterol and phosphatidylcholines (lecithins) to cholesteryl esters and lysophosphatidylcholines on the surface of high and low density lipoproteins (HDLs and LDLs) (PubMed:10329423, PubMed:19065001, PubMed:26195816). The cholesterol ester is then transported back to the liver. Has a preference for plasma 16:0-18:2 or 18:O-18:2 phosphatidylcholines (PubMed:8820107). Also produced in the brain by primary astrocytes, and esterifies free cholesterol on nascent APOE-containing lipoproteins secreted from glia and influences cerebral spinal fluid (CSF) APOE- and APOA1 levels. Together with APOE and the cholesterol transporter ABCA1, plays a key role in the maturation of glial-derived, nascent lipoproteins. Required for remodeling high-density lipoprotein particles into their spherical forms (PubMed:10722751). Catalyzes the hydrolysis of 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine (platelet-activating factor or PAF) to 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF) (PubMed:8016111). Also catalyzes the transfer of the acetate group from PAF to 1-hexadecanoyl-sn-glycero-3-phosphocholine forming lyso-PAF (PubMed:8016111). Catalyzes the esterification of (24S)-hydroxycholesterol (24(S)OH-C), also known as cerebrosterol to produce 24(S)OH-C monoesters (PubMed:24620755)", "gene_name": "LCAT", "glycan_count": 28, "glycosylation_sites": [ { "position": 44, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 108, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 296, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 408, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 431, "type": "O-linked (GalNAc...) threonine" }, { "position": 433, "type": "O-linked (GalNAc...) serine" } ], "id": "P04180", "name": "LCAT", "organism": "Homo sapiens", "uniprot_id": "P04180" }, { "function": "Ligand for CXCR2 (By similarity). Has chemotactic activity for neutrophils. May play a role in inflammation and exert its effects on endothelial cells in an autocrine fashion. In vitro, the processed form GRO-gamma(5-73) shows a fivefold higher chemotactic activity for neutrophilic granulocytes", "gene_name": "CXCL3", "glycan_count": 0, "glycosylation_sites": [], "id": "P19876", "name": "CETP", "organism": "Homo sapiens", "uniprot_id": "P19876" }, { "function": "Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals. Dephosphorylates and activates transcription factor NFATC1. Dephosphorylates and inactivates transcription factor ELK1. Dephosphorylates DARPP32", "gene_name": "PPP3CC", "glycan_count": 1, "glycosylation_sites": [], "id": "P48454", "name": "Calcineurin", "organism": "Homo sapiens", "uniprot_id": "P48454" }, { "function": "Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays contrasting roles in cell death and cell survival by functioning as a pro-apoptotic protein during DNA damage-induced apoptosis, but acting as an anti-apoptotic protein during cytokine receptor-initiated cell death, is involved in tumor suppression as well as survival of several cancers, is required for oxygen radical production by NADPH oxidase and acts as positive or negative regulator in platelet functional responses (PubMed:21406692, PubMed:21810427). Negatively regulates B cell proliferation and also has an important function in self-antigen induced B cell tolerance induction (By similarity). Upon DNA damage, activates the promoter of the death-promoting transcription factor BCLAF1/Btf to trigger BCLAF1-mediated p53/TP53 gene transcription and apoptosis (PubMed:21406692, PubMed:21810427). In response to oxidative stress, interact with and activate CHUK/IKKA in the nucleus, causing the phosphorylation of p53/TP53 (PubMed:21406692, PubMed:21810427). In the case of ER stress or DNA damage-induced apoptosis, can form a complex with the tyrosine-protein kinase ABL1 which trigger apoptosis independently of p53/TP53 (PubMed:21406692, PubMed:21810427). In cytosol can trigger apoptosis by activating MAPK11 or MAPK14, inhibiting AKT1 and decreasing the level of X-linked inhibitor of apoptosis protein (XIAP), whereas in nucleus induces apoptosis via the activation of MAPK8 or MAPK9. Upon ionizing radiation treatment, is required for the activation of the apoptosis regulators BAX and BAK, which trigger the mitochondrial cell death pathway. Can phosphorylate MCL1 and target it for degradation which is sufficient to trigger for BAX activation and apoptosis. Is required for the control of cell cycle progression both at G1/S and G2/M phases. Mediates phorbol 12-myristate 13-acetate (PMA)-induced inhibition of cell cycle progression at G1/S phase by up-regulating the CDK inhibitor CDKN1A/p21 and inhibiting the cyclin CCNA2 promoter activity. In response to UV irradiation can phosphorylate CDK1, which is important for the G2/M DNA damage checkpoint activation (By similarity). Can protect glioma cells from the apoptosis induced by TNFSF10/TRAIL, probably by inducing increased phosphorylation and subsequent activation of AKT1 (PubMed:15774464). Is highly expressed in a number of cancer cells and promotes cell survival and resistance against chemotherapeutic drugs by inducing cyclin D1 (CCND1) and hyperphosphorylation of RB1, and via several pro-survival pathways, including NF-kappa-B, AKT1 and MAPK1/3 (ERK1/2). Involved in antifungal immunity by mediating phosphorylation and activation of CARD9 downstream of C-type lectin receptors activation, promoting interaction between CARD9 and BCL10, followed by activation of NF-kappa-B and MAP kinase p38 pathways (By similarity). Can also act as tumor suppressor upon mitogenic stimulation with PMA or TPA. In N-formyl-methionyl-leucyl-phenylalanine (fMLP)-treated cells, is required for NCF1 (p47-phox) phosphorylation and activation of NADPH oxidase activity, and regulates TNF-elicited superoxide anion production in neutrophils, by direct phosphorylation and activation of NCF1 or indirectly through MAPK1/3 (ERK1/2) signaling pathways (PubMed:19801500). May also play a role in the regulation of NADPH oxidase activity in eosinophil after stimulation with IL5, leukotriene B4 or PMA (PubMed:11748588). In collagen-induced platelet aggregation, acts a negative regulator of filopodia formation and actin polymerization by interacting with and negatively regulating VASP phosphorylation (PubMed:16940418). Downstream of PAR1, PAR4 and CD36/GP4 receptors, regulates differentially platelet dense granule secretion; acts as a positive regulator in PAR-mediated granule secretion, whereas it negatively regulates CD36/GP4-mediated granule release (PubMed:19587372). Phosphorylates MUC1 in the C-terminal and regulates the interaction between MUC1 and beta-catenin (PubMed:11877440). The catalytic subunit phosphorylates 14-3-3 proteins (YWHAB, YWHAZ and YWHAH) in a sphingosine-dependent fashion (By similarity). Phosphorylates ELAVL1 in response to angiotensin-2 treatment (PubMed:18285462). Phosphorylates mitochondrial phospholipid scramblase 3 (PLSCR3), resulting in increased cardiolipin expression on the mitochondrial outer membrane which facilitates apoptosis (PubMed:12649167). Phosphorylates SMPD1 which induces SMPD1 secretion (PubMed:17303575)", "gene_name": "PRKCD", "glycan_count": 0, "glycosylation_sites": [], "id": "Q05655", "name": "Protein Kinase C delta (PKC\u03b4)", "organism": "Homo sapiens", "uniprot_id": "Q05655" }, { "function": "Inhibits urokinase-type plasminogen activator. The monocyte derived PAI-2 is distinct from the endothelial cell-derived PAI-1", "gene_name": "SERPINB2", "glycan_count": 0, "glycosylation_sites": [ { "position": 75, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 115, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 339, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P05120", "name": "SERPINB2", "organism": "Homo sapiens", "uniprot_id": "P05120" }, { "function": "Functions in lipid transport from the endoplasmic reticulum and is involved in a wide array of cellular functions probably through regulation of the biogenesis of lipid microdomains at the plasma membrane. Involved in the regulation of different receptors it plays a role in BDNF signaling and EGF signaling. Also regulates ion channels like the potassium channel and could modulate neurotransmitter release. Plays a role in calcium signaling through modulation together with ANK2 of the ITP3R-dependent calcium efflux at the endoplasmic reticulum. Plays a role in several other cell functions including proliferation, survival and death. Originally identified for its ability to bind various psychoactive drugs it is involved in learning processes, memory and mood alteration (PubMed:16472803, PubMed:9341151). Necessary for proper mitochondrial axonal transport in motor neurons, in particular the retrograde movement of mitochondria. Plays a role in protecting cells against oxidative stress-induced cell death via its interaction with RNF112 (By similarity)", "gene_name": "SIGMAR1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q99720", "name": "Sigma-1 receptor (S1R)", "organism": "Homo sapiens", "uniprot_id": "Q99720" }, { "function": "Phosphatidylserine receptor that plays an important functional role in regulatory B-cells homeostasis including generation, expansion and suppressor functions (By similarity). As P-selectin/SELPLG ligand, plays a specialized role in activated but not naive T-cell trafficking during inflammatory responses (PubMed:24703780). Controls thereby T-cell accumulation in the inflamed central nervous system (CNS) and the induction of autoimmune disease (PubMed:24703780). Also regulates expression of various anti-inflammatory cytokines and co-inhibitory ligands including IL10 (By similarity). Acts as a regulator of T-cell proliferation (By similarity). May play a role in kidney injury and repair (PubMed:17471468)", "gene_name": "HAVCR1", "glycan_count": 5, "glycosylation_sites": [ { "position": 65, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 263, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 277, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 291, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q96D42", "name": "KIM-1 (Havcr1)", "organism": "Homo sapiens", "uniprot_id": "Q96D42" }, { "function": "Barrier-forming claudin. Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity", "gene_name": "CLDN3", "glycan_count": 0, "glycosylation_sites": [], "id": "O15551", "name": "Claudin-3", "organism": "Homo sapiens", "uniprot_id": "O15551" }, { "function": "Can associate with other claudins to regulate tight junction structural and functional strand dynamics (PubMed:35773259, PubMed:36008380). May coassemble with CLDN8 into tight junction strands containing anion-selective channels that convey paracellular chloride permeability in renal collecting ducts (By similarity) (PubMed:36008380). May integrate into CLDN3 strands to modulate localized tight junction barrier properties (PubMed:35773259, PubMed:36008380). May disrupt strand assembly of channel-forming CLDN2 and CLDN15 and inhibit cation conductance (PubMed:35773259, PubMed:36008380). Cannot form tight junction strands on its own (PubMed:35773259, PubMed:36008380)", "gene_name": "CLDN4", "glycan_count": 0, "glycosylation_sites": [], "id": "O14493", "name": "Claudin-4", "organism": "Homo sapiens", "uniprot_id": "O14493" }, { "function": "Plays a major role in tight junction-specific obliteration of the intercellular space", "gene_name": "CLDN7", "glycan_count": 0, "glycosylation_sites": [], "id": "O95471", "name": "Claudin-7", "organism": "Homo sapiens", "uniprot_id": "O95471" }, { "function": "Binds to photoactivated, phosphorylated RHO and terminates RHO signaling via G-proteins by competing with G-proteins for the same binding site on RHO (By similarity). May play a role in preventing light-dependent degeneration of retinal photoreceptor cells (PubMed:9565049)", "gene_name": "SAG", "glycan_count": 0, "glycosylation_sites": [], "id": "P10523", "name": "Arrestin (S-antigen)", "organism": "Homo sapiens", "uniprot_id": "P10523" }, { "function": "Acts as a calcium sensor and regulates phototransduction of cone and rod photoreceptor cells (By similarity). Modulates light sensitivity of cone photoreceptor in dark and dim conditions (By similarity). In response to high Ca(2+) levels induced by low light levels, prolongs RHO/rhodopsin activation in rod photoreceptor cells by binding to and inhibiting GRK1-mediated phosphorylation of RHO/rhodopsin (By similarity). Plays a role in scotopic vision/enhances vision in dim light by enhancing signal transfer between rod photoreceptors and rod bipolar cells (By similarity). Improves rod photoreceptor sensitivity in dim light and mediates response of rod photoreceptors to facilitate detection of change and motion in bright light (By similarity)", "gene_name": "RCVRN", "glycan_count": 0, "glycosylation_sites": [], "id": "P35243", "name": "Recoverin", "organism": "Homo sapiens", "uniprot_id": "P35243" }, { "function": "Photoreceptor required for image-forming vision at low light intensity (PubMed:7846071, PubMed:8107847). Required for photoreceptor cell viability after birth (PubMed:12566452, PubMed:2215617). Light-induced isomerization of the chromophore 11-cis-retinal to all-trans-retinal triggers a conformational change that activates signaling via G-proteins (PubMed:26200343, PubMed:28524165, PubMed:28753425, PubMed:8107847). Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by the arrestin SAG and terminates signaling (PubMed:26200343, PubMed:28524165)", "gene_name": "RHO", "glycan_count": 23, "glycosylation_sites": [ { "position": 2, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 15, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08100", "name": "Rhodopsin", "organism": "Homo sapiens", "uniprot_id": "P08100" }, { "function": "This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the initial and rate limiting step in the cascade of reactions leading to melanin production from tyrosine (By similarity). In addition to hydroxylating tyrosine to DOPA (3,4-dihydroxyphenylalanine), also catalyzes the oxidation of DOPA to DOPA-quinone, and possibly the oxidation of DHI (5,6-dihydroxyindole) to indole-5,6 quinone (PubMed:28661582)", "gene_name": "TYR", "glycan_count": 0, "glycosylation_sites": [ { "position": 86, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 111, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 161, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 230, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 337, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 371, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P14679", "name": "Tyrosinase", "organism": "Homo sapiens", "uniprot_id": "P14679" }, { "function": "Soluble retinoid carrier essential the proper function of both rod and cone photoreceptors. Participates in the regeneration of active 11-cis-retinol and 11-cis-retinaldehyde, from the inactive 11-trans products of the rhodopsin photocycle and in the de novo synthesis of these retinoids from 11-trans metabolic precursors. The cycling of retinoids between photoreceptor and adjacent pigment epithelium cells is known as the 'visual cycle'", "gene_name": "RLBP1", "glycan_count": 1, "glycosylation_sites": [], "id": "P12271", "name": "Interphotoreceptor retinoid-binding protein (IRBP)", "organism": "Homo sapiens", "uniprot_id": "P12271" }, { "function": "S100A8 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. It can induce neutrophil chemotaxis and adhesion. Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions. The intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase. Also participates in regulatory T-cell differentiation together with CD69 (PubMed:26296369). Activates NADPH-oxidase by facilitating the enzyme complex assembly at the cell membrane, transferring arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX. The extracellular functions involve pro-inflammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities. Its pro-inflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER). Binding to TLR4 and AGER activates the MAP-kinase and NF-kappa-B signaling pathways resulting in the amplification of the pro-inflammatory cascade. Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth. Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3. Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK. Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants. Can act as a potent amplifier of inflammation in autoimmunity as well as in cancer development and tumor spread. The iNOS-S100A8/A9 transnitrosylase complex directs selective inflammatory stimulus-dependent S-nitrosylation of GAPDH and probably multiple targets such as ANXA5, EZR, MSN and VIM by recognizing a [IL]-x-C-x-x-[DE] motif; S100A8 seems to contribute to S-nitrosylation site selectivity", "gene_name": "S100A8", "glycan_count": 1, "glycosylation_sites": [], "id": "P05109", "name": "Protein S100-A8", "organism": "Homo sapiens", "uniprot_id": "P05109" }, { "function": "S100A9 is a calcium- and zinc-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response (PubMed:12626582, PubMed:15331440, PubMed:16258195, PubMed:19122197, PubMed:20103766, PubMed:21325622, PubMed:8423249). It can induce neutrophil chemotaxis, adhesion, can increase the bactericidal activity of neutrophils by promoting phagocytosis via activation of SYK, PI3K/AKT, and ERK1/2 and can induce degranulation of neutrophils by a MAPK-dependent mechanism (PubMed:12626582, PubMed:15331440, PubMed:20103766). Predominantly found as calprotectin (S100A8/A9) which has a wide plethora of intra- and extracellular functions (PubMed:16258195, PubMed:19122197, PubMed:8423249). The intracellular functions include: facilitating leukocyte arachidonic acid trafficking and metabolism, modulation of the tubulin-dependent cytoskeleton during migration of phagocytes and activation of the neutrophilic NADPH-oxidase (PubMed:15331440, PubMed:21325622). Also participates in regulatory T-cell differentiation together with CD69 (PubMed:26296369). Activates NADPH-oxidase by facilitating the enzyme complex assembly at the cell membrane, transferring arachidonic acid, an essential cofactor, to the enzyme complex and S100A8 contributes to the enzyme assembly by directly binding to NCF2/P67PHOX (PubMed:15642721, PubMed:22808130). The extracellular functions involve pro-inflammatory, antimicrobial, oxidant-scavenging and apoptosis-inducing activities (PubMed:19534726, PubMed:8423249). Its pro-inflammatory activity includes recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration (PubMed:15598812, PubMed:21487906). Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation endproducts (AGER) (PubMed:19402754). Binding to TLR4 and AGER activates the MAP-kinase and NF-kappa-B signaling pathways resulting in the amplification of the pro-inflammatory cascade (PubMed:19402754, PubMed:22804476). Has antimicrobial activity towards bacteria and fungi and exerts its antimicrobial activity probably via chelation of Zn(2+) which is essential for microbial growth (PubMed:19087201). Can induce cell death via autophagy and apoptosis and this occurs through the cross-talk of mitochondria and lysosomes via reactive oxygen species (ROS) and the process involves BNIP3 (PubMed:19935772). Can regulate neutrophil number and apoptosis by an anti-apoptotic effect; regulates cell survival via ITGAM/ITGB and TLR4 and a signaling mechanism involving MEK-ERK (PubMed:22363402). Its role as an oxidant scavenger has a protective role in preventing exaggerated tissue damage by scavenging oxidants (PubMed:21912088, PubMed:22489132). Can act as a potent amplifier of inflammation in autoimmunity as well as in cancer development and tumor spread (PubMed:16258195). Has transnitrosylase activity; in oxidatively-modified low-densitity lipoprotein (LDL(ox))-induced S-nitrosylation of GAPDH on 'Cys-247' proposed to transfer the NO moiety from NOS2/iNOS to GAPDH via its own S-nitrosylated Cys-3 (PubMed:25417112). The iNOS-S100A8/A9 transnitrosylase complex is proposed to also direct selective inflammatory stimulus-dependent S-nitrosylation of multiple targets such as ANXA5, EZR, MSN and VIM by recognizing a [IL]-x-C-x-x-[DE] motif (PubMed:25417112)", "gene_name": "S100A9", "glycan_count": 1, "glycosylation_sites": [], "id": "P06702", "name": "Protein S100-A9", "organism": "Homo sapiens", "uniprot_id": "P06702" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P0C0L4/P0C0L5", "name": "Complement C4-B/C4A", "organism": "", "uniprot_id": "" }, { "function": "Prenylcysteine oxidase that cleaves the thioether bond of prenyl-L-cysteines, such as farnesylcysteine and geranylgeranylcysteine (PubMed:10585463, PubMed:11078725, PubMed:12186880). Only active against free prenylcysteines and not prenylcysteine residues within prenylated proteins or peptides (By similarity). Involved in the final step in the degradation of prenylated proteins, by degrading prenylcysteines after the protein has been degraded (PubMed:10585463)", "gene_name": "PCYOX1", "glycan_count": 66, "glycosylation_sites": [ { "position": 196, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 323, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 353, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UHG3", "name": "IL-19", "organism": "Homo sapiens", "uniprot_id": "Q9UHG3" }, { "function": "Multifunctional cytokine mainly produced by T-cells that plays a regulatory role in immune response, tissue homeostasis, host defense, and oncogenesis (PubMed:25168428, PubMed:27687232). Possesses antiviral functions and induces the type I interferon response during influenza infection (PubMed:27687232). Signals through two receptor complexes IL20RA/IL20RB or IL20RB/IL22RA1 (PubMed:11706020, PubMed:30111632). In turn, stimulates the JAK1-STAT3 and MAPK pathways and promotes the secretion of pro-inflammatory mediators including IL8 and MMP1 (PubMed:25168428). Intracellularly, maintains endoplasmic reticulum homeostasis by restricting the eIF2alpha-CHOP pathway-mediated stress signal (By similarity). In addition, acts as a quality control mechanism for the ubiquitin proteasome system by alerting the cell to proteasome dysfunction through activation of PKR/EIF2AK2 (By similarity)", "gene_name": "IL24", "glycan_count": 0, "glycosylation_sites": [ { "position": 85, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 99, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 126, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13007", "name": "IL-24", "organism": "Homo sapiens", "uniprot_id": "Q13007" }, { "function": "May play a role in local mechanisms of mucosal immunity and seems to have a pro-inflammatory function. May play a role in inflammatory bowel disease. Activates STAT1 and STAT3, MAPK1/3 (ERK1/2), JUN and AKT. Induces expression of SOCS3, TNF-alpha and IL-8, secretion of IL-8 and IL-10 and surface expression of ICAM1. Decreases proliferation of intestinal epithelial cells. Is inhibited by heparin", "gene_name": "IL26", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NPH9", "name": "IL-26", "organism": "Homo sapiens", "uniprot_id": "Q9NPH9" }, { "function": "Single-stranded DNA-specific cytidine deaminase. Involved in somatic hypermutation (SHM), gene conversion, and class-switch recombination (CSR) in B-lymphocytes by deaminating C to U during transcription of Ig-variable (V) and Ig-switch (S) region DNA. Required for several crucial steps of B-cell terminal differentiation necessary for efficient antibody responses (PubMed:18722174, PubMed:21385873, PubMed:21518874, PubMed:27716525). May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation (PubMed:21496894)", "gene_name": "AICDA", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9GZX7", "name": "IL-20RA", "organism": "Homo sapiens", "uniprot_id": "Q9GZX7" }, { "function": "The IL20RA/IL20RB dimer is a receptor for IL19, IL20 and IL24. The IL22RA1/IL20RB dimer is a receptor for IL20 and IL24", "gene_name": "IL20RB", "glycan_count": 1, "glycosylation_sites": [ { "position": 40, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 134, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6UXL0", "name": "IL-20RB", "organism": "Homo sapiens", "uniprot_id": "Q6UXL0" }, { "function": "Component of the receptor for IL20, IL22 and IL24. Component of IL22 receptor formed by IL22RA1 and IL10RB enabling IL22 signaling via JAK/STAT pathways. IL22 also induces activation of MAPK1/MAPK3 and Akt kinases pathways. Component of one of the receptor for IL20 and IL24 formed by IL22RA1 and IL20RB also signaling through STATs activation. Mediates IL24 antiangiogenic activity as well as IL24 inhibitory effect on endothelial cell tube formation and differentiation", "gene_name": "IL22RA1", "glycan_count": 1, "glycosylation_sites": [ { "position": 80, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 172, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8N6P7", "name": "IL-22RA1", "organism": "Homo sapiens", "uniprot_id": "Q8N6P7" }, { "function": "A cytochrome P450 monooxygenase involved in the metabolism of retinoates (RAs), the active metabolites of vitamin A, and critical signaling molecules in animals (PubMed:14532297). RAs exist as at least four different isomers: all-trans-RA (atRA), 9-cis-RA, 13-cis-RA, and 9,13-dicis-RA, where atRA is considered to be the biologically active isomer, although 9-cis-RA and 13-cis-RA also have activity (Probable). Catalyzes the oxidation of atRA primarily at C-4 (PubMed:14532297). Oxidation of atRA limits its biological activity and initiates a degradative process leading to its eventual elimination, thereby contributes to the regulation of atRA homeostasis and signaling (Probable). Able to metabolize other RAs such as 9-cis with high efficiency (PubMed:14532297). Can oxidize all-trans-13,14-dihydroretinoate (DRA) to metabolites which could include all-trans-4-oxo-DRA, all-trans-4-hydroxy-DRA, all-trans-5,8-epoxy-DRA, and all-trans-18-hydroxy-DRA (By similarity). Shares sequence similarity with other CYP26 family members, but has higher affinity to 9-cis-RA and is much less sensitive to the inhibitory effects of ketoconazole (PubMed:14532297). In cooperation with Cyp26a1, contributes to the CNS patterning and the development of regions of higher visual acuity (By similarity)", "gene_name": "CYP26C1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6V0L0", "name": "CD36", "organism": "Homo sapiens", "uniprot_id": "Q6V0L0" }, { "function": "Binds activated protein C. Enhances protein C activation by the thrombin-thrombomodulin complex; plays a role in the protein C pathway controlling blood coagulation", "gene_name": "PROCR", "glycan_count": 15, "glycosylation_sites": [ { "position": 47, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 64, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 136, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 172, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UNN8", "name": "SRA-1 (SCARA1)", "organism": "Homo sapiens", "uniprot_id": "Q9UNN8" }, { "function": "Pro-inflammatory cytokine primarily involved in epithelial barrier repair, polarized T-helper 1 (Th1) cell and natural killer (NK) cell immune responses (PubMed:10653850). Upon binding to IL18R1 and IL18RAP, forms a signaling ternary complex which activates NF-kappa-B, triggering synthesis of inflammatory mediators (PubMed:14528293, PubMed:25500532, PubMed:37993714). Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T-helper 1 (Th1) cells and natural killer (NK) cells (PubMed:10653850). Involved in transduction of inflammation downstream of pyroptosis: its mature form is specifically released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore (PubMed:33883744)", "gene_name": "IL18", "glycan_count": 1, "glycosylation_sites": [], "id": "Q14116", "name": "IL-18", "organism": "Homo sapiens", "uniprot_id": "Q14116" }, { "function": "Major thyroid hormone transport protein in serum", "gene_name": "SERPINA7", "glycan_count": 41, "glycosylation_sites": [ { "position": 36, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 99, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 116, "type": "N-linked (GlcNAc...) asparagine; in variant Gary" }, { "position": 165, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 253, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P05543", "name": "Thyroxine-binding globulin (TBG)", "organism": "Homo sapiens", "uniprot_id": "P05543" }, { "function": "Receptor for the C-terminal sequence motif K-D-E-L that is present on endoplasmic reticulum resident proteins and that mediates their recycling from the Golgi back to the endoplasmic reticulum", "gene_name": "KDELR1", "glycan_count": 0, "glycosylation_sites": [], "id": "P24390", "name": "Deiodinase type 1 (DIO1)", "organism": "Homo sapiens", "uniprot_id": "P24390" }, { "function": "Plays a crucial role in the metabolism of thyroid hormones (TH) and has specific roles in TH activation and inactivation by deiodination (PubMed:12586771, PubMed:11108274, PubMed:10403186, PubMed:18821722). Catalyzes the deiodination of L-thyroxine (T4) to 3,5,3'-triiodothyronine (T3), 3,3',5'-triiodothyronine (rT3) to 3,3'-diiodothyronine (3,3'-T2) and 3',5'-diiodothyronine (3',5'-T2) to 3'-monoiodothyronine (3'-T1) via outer-ring deiodination (ORD) (PubMed:12586771, PubMed:11108274, PubMed:10403186, PubMed:18821722, PubMed:18339710). Catalyzes the phenolic ring deiodinations of 3,3',5'-triiodothyronamine and 3',5'- diiodothyronamine (PubMed:18339710)", "gene_name": "DIO2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q92813", "name": "Deiodinase type 2 (DIO2)", "organism": "Homo sapiens", "uniprot_id": "Q92813" }, { "function": "Receptor for netrin required for axon guidance. Mediates axon repulsion of neuronal growth cones in the developing nervous system upon ligand binding. Axon repulsion in growth cones may be caused by its association with DCC that may trigger signaling for repulsion (By similarity). Functions as a netrin receptor that negatively regulates vascular branching during angiogenesis. Mediates retraction of tip cell filopodia on endothelial growth cones in response to netrin (By similarity). It also acts as a dependence receptor required for apoptosis induction when not associated with netrin ligand (PubMed:12598906). Mediates apoptosis by activating DAPK1. In the absence of NTN1, activates DAPK1 by reducing its autoinhibitory phosphorylation at Ser-308 thereby increasing its catalytic activity (By similarity)", "gene_name": "UNC5B", "glycan_count": 3, "glycosylation_sites": [ { "position": 222, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 347, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8IZJ1", "name": "Deiodinase type 3 (DIO3)", "organism": "Homo sapiens", "uniprot_id": "Q8IZJ1" }, { "function": "Gp-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to von Willebrand factor, which is already bound to the subendothelium", "gene_name": "GP1BB", "glycan_count": 1, "glycosylation_sites": [ { "position": 66, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P13224", "name": "Platelet glycoprotein Ib beta chain", "organism": "Homo sapiens", "uniprot_id": "P13224" }, { "function": "Functions as a transport protein in the blood stream. Binds various hydrophobic ligands in the interior of its beta-barrel domain. Also binds synthetic drugs and influences their distribution and availability. Appears to function in modulating the activity of the immune system during the acute-phase reaction", "gene_name": "ORM2", "glycan_count": 148, "glycosylation_sites": [ { "position": 33, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 56, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 72, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 93, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 103, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P19652", "name": "Alpha-1-acid glycoprotein 2", "organism": "Homo sapiens", "uniprot_id": "P19652" }, { "function": "Multifunctional protein that plays a critical role in regulating the availability of IGFs such as IGF1 and IGF2 to their receptors and thereby regulates IGF-mediated cellular processes including cell migration, proliferation, differentiation or apoptosis in a cell-type specific manner (PubMed:11397844, PubMed:15972819). Also plays a positive role in cell migration by interacting with integrin ITGA5:ITGB1 through its RGD motif (PubMed:7504269). Mechanistically, binding to integrins leads to activation of focal adhesion kinase/PTK2 and stimulation of the mitogen-activated protein kinase (MAPK) pathway (PubMed:11397844). Regulates cardiomyocyte apoptosis by suppressing HIF-1alpha/HIF1A ubiquitination and subsequent degradation (By similarity)", "gene_name": "IGFBP1", "glycan_count": 0, "glycosylation_sites": [], "id": "P08833", "name": "Insulin-like growth factor binding protein 1 (IGFBP1)", "organism": "Homo sapiens", "uniprot_id": "P08833" }, { "function": "Increases ligand-dependent transcriptional activity of AR and other nuclear hormone receptors", "gene_name": "ZMIZ2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8NF64", "name": "Membrane progesterone receptor beta (mPR\u03b2/PAQR8)", "organism": "Homo sapiens", "uniprot_id": "Q8NF64" }, { "function": "Transcriptional activator involved in the development of insulin-producting beta cells in the endocrine pancreas (By similarity). May also be involved in specifying diencephalic neuromeric boundaries, and in controlling the expression of genes that play a role in axonal guidance. Binds to elements within the NEUROD1 promoter (By similarity)", "gene_name": "NKX2-2", "glycan_count": 0, "glycosylation_sites": [], "id": "O95096", "name": "Heart and neural crest derivatives-expressed transcript 2 (HAND2)", "organism": "Homo sapiens", "uniprot_id": "O95096" }, { "function": "Acts as a transcriptional repressor (PubMed:10688654, PubMed:24359566). Transcriptional repression may be mediated through recruitment of histone deacetylases to target promoters (PubMed:10688654). May play a role in myeloid maturation and in the development and/or maintenance of other differentiated tissues. Probable substrate-recognition component of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:14528312)", "gene_name": "ZBTB16", "glycan_count": 0, "glycosylation_sites": [], "id": "Q05516", "name": "Zinc finger and BTB domain-containing 16 (ZBTB16)", "organism": "Homo sapiens", "uniprot_id": "Q05516" }, { "function": "", "gene_name": "PSG1", "glycan_count": 1, "glycosylation_sites": [ { "position": 61, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 111, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 199, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 259, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 268, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 303, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P11464", "name": "PSG1", "organism": "Homo sapiens", "uniprot_id": "P11464" }, { "function": "", "gene_name": "PSG2", "glycan_count": 1, "glycosylation_sites": [ { "position": 61, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 111, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 199, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P11465", "name": "PSG3", "organism": "Homo sapiens", "uniprot_id": "P11465" }, { "function": "", "gene_name": "PSG4", "glycan_count": 1, "glycosylation_sites": [ { "position": 104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 111, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 199, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 268, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 299, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 303, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q00888", "name": "PSG7", "organism": "Homo sapiens", "uniprot_id": "Q00888" }, { "function": "", "gene_name": "PSG6", "glycan_count": 0, "glycosylation_sites": [ { "position": 61, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 103, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 110, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 198, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 267, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 302, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 386, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q00889", "name": "PSG8", "organism": "Homo sapiens", "uniprot_id": "Q00889" }, { "function": "Hydrolyzes all ester bonds in triglyceride and displays a high affinity for triolein. For unsaturated substrates having long fatty acyl chains (C18:2 cis-9, cis-12 and C18:3 cis-9, cis-12, cis-15) GCL I shows higher specific activity than GCL II, whereas GCL II shows higher specific activity against saturated substrates having short fatty acid chains (C8, C10, C12 and C14)", "gene_name": "LIP2", "glycan_count": 0, "glycosylation_sites": [ { "position": 302, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 383, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q00890", "name": "PSG9", "organism": "Geotrichum candidum", "uniprot_id": "P22394" }, { "function": "Cell adhesion protein that mediates homophilic cell adhesion in a calcium-independent manner (By similarity). Plays a role as coinhibitory receptor in immune response, insulin action and also functions as an activator during angiogenesis (PubMed:18424730, PubMed:23696226, PubMed:25363763). Its coinhibitory receptor function is phosphorylation- and PTPN6 -dependent, which in turn, suppress signal transduction of associated receptors by dephosphorylation of their downstream effectors. Plays a role in immune response, of T cells, natural killer (NK) and neutrophils (PubMed:18424730, PubMed:23696226). Upon TCR/CD3 complex stimulation, inhibits TCR-mediated cytotoxicity by blocking granule exocytosis by mediating homophilic binding to adjacent cells, allowing interaction with and phosphorylation by LCK and interaction with the TCR/CD3 complex which recruits PTPN6 resulting in dephosphorylation of CD247 and ZAP70 (PubMed:18424730). Also inhibits T cell proliferation and cytokine production through inhibition of JNK cascade and plays a crucial role in regulating autoimmunity and anti-tumor immunity by inhibiting T cell through its interaction with HAVCR2 (PubMed:25363763). Upon natural killer (NK) cells activation, inhibit KLRK1-mediated cytolysis of CEACAM1-bearing tumor cells by trans-homophilic interactions with CEACAM1 on the target cell and lead to cis-interaction between CEACAM1 and KLRK1, allowing PTPN6 recruitment and then VAV1 dephosphorylation (PubMed:23696226). Upon neutrophils activation negatively regulates IL1B production by recruiting PTPN6 to a SYK-TLR4-CEACAM1 complex, that dephosphorylates SYK, reducing the production of reactive oxygen species (ROS) and lysosome disruption, which in turn, reduces the activity of the inflammasome. Down-regulates neutrophil production by acting as a coinhibitory receptor for CSF3R by down-regulating the CSF3R-STAT3 pathway through recruitment of PTPN6 that dephosphorylates CSF3R (By similarity). Also regulates insulin action by promoting INS clearance and regulating lipogenesis in liver through regulating insulin signaling (By similarity). Upon INS stimulation, undergoes phosphorylation by INSR leading to INS clearance by increasing receptor-mediated insulin endocytosis. This inernalization promotes interaction with FASN leading to receptor-mediated insulin degradation and to reduction of FASN activity leading to negative regulation of fatty acid synthesis. INSR-mediated phosphorylation also provokes a down-regulation of cell proliferation through SHC1 interaction resulting in decrease coupling of SHC1 to the MAPK3/ERK1-MAPK1/ERK2 and phosphatidylinositol 3-kinase pathways (By similarity). Functions as activator in angiogenesis by promoting blood vessel remodeling through endothelial cell differentiation and migration and in arteriogenesis by increasing the number of collateral arteries and collateral vessel calibers after ischemia. Also regulates vascular permeability through the VEGFR2 signaling pathway resulting in control of nitric oxide production (By similarity). Down-regulates cell growth in response to EGF through its interaction with SHC1 that mediates interaction with EGFR resulting in decrease coupling of SHC1 to the MAPK3/ERK1-MAPK1/ERK2 pathway (By similarity). Negatively regulates platelet aggregation by decreasing platelet adhesion on type I collagen through the GPVI-FcRgamma complex (By similarity). Inhibits cell migration and cell scattering through interaction with FLNA; interferes with the interaction of FLNA with RALA (PubMed:16291724). Mediates bile acid transport activity in a phosphorylation dependent manner (By similarity). Negatively regulates osteoclastogenesis (By similarity)", "gene_name": "CEACAM1", "glycan_count": 47, "glycosylation_sites": [ { "position": 104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 111, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 115, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 152, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 182, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 197, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 208, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 224, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 232, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 254, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 274, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 288, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 292, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 302, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 309, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 345, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 351, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 363, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 378, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 405, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P13688", "name": "CEACAM1", "organism": "Homo sapiens", "uniprot_id": "P13688" }, { "function": "Cell surface glycoprotein that plays a role in cell adhesion in a calcium-independent manner (PubMed:11590190, PubMed:2022629, PubMed:8776764). Mediates heterophilic cell adhesion with other carcinoembryonic antigen-related cell adhesion molecules, such as CEACAM6 (PubMed:11590190, PubMed:2022629, PubMed:8776764). Heterophilic interaction with CEACAM8 occurs in activated neutrophils (PubMed:8776764)", "gene_name": "CEACAM8", "glycan_count": 10, "glycosylation_sites": [ { "position": 104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 111, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 115, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 152, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 173, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 197, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 224, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 256, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 274, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 288, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 309, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P31997", "name": "CEACAM8", "organism": "Homo sapiens", "uniprot_id": "P31997" }, { "function": "Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids", "gene_name": "MT1A", "glycan_count": 0, "glycosylation_sites": [], "id": "P04731", "name": "MT1A", "organism": "Homo sapiens", "uniprot_id": "P04731" }, { "function": "Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids", "gene_name": "MT2A", "glycan_count": 2, "glycosylation_sites": [], "id": "P02795", "name": "MT2A", "organism": "Homo sapiens", "uniprot_id": "P02795" }, { "function": "Binds heavy metals. Contains three zinc and three copper atoms per polypeptide chain and only a negligible amount of cadmium. Inhibits survival and neurite formation of cortical neurons in vitro", "gene_name": "MT3", "glycan_count": 0, "glycosylation_sites": [], "id": "P25713", "name": "MT3", "organism": "Homo sapiens", "uniprot_id": "P25713" }, { "function": "Transmembrane serine/threonine kinase forming with the TGF-beta type I serine/threonine kinase receptor, TGFBR1, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and thus regulates a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and activation of TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways", "gene_name": "TGFBR2", "glycan_count": 12, "glycosylation_sites": [ { "position": 70, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 94, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 154, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P37173", "name": "TGFBR2", "organism": "Homo sapiens", "uniprot_id": "P37173" }, { "function": "Transcription factor that acts as a transcriptional activator (PubMed:24886874, PubMed:26543203). Binds cooperatively with POU3F2/BRN2 or POU3F1/OCT6 to gene promoters, which enhances transcriptional activation (By similarity). Acts as a transcriptional activator of TEAD2 by binding to its gene promoter and first intron (By similarity). Plays a redundant role with SOX4 and SOX12 in cell survival of developing tissues such as the neural tube, branchial arches and somites, thereby contributing to organogenesis (By similarity)", "gene_name": "SOX11", "glycan_count": 1, "glycosylation_sites": [], "id": "P35716", "name": "SOX4", "organism": "Homo sapiens", "uniprot_id": "P35716" }, { "function": "Component of some SCF (SKP1-cullin-F-box) protein ligase complex that plays a central role in iron homeostasis by promoting the ubiquitination and subsequent degradation of IREB2/IRP2 (PubMed:19762596, PubMed:19762597). The C-terminal domain of FBXL5 contains a redox-sensitive [2Fe-2S] cluster that, upon oxidation, promotes binding to IRP2 to effect its oxygen-dependent degradation (PubMed:32126207). Under iron deficiency conditions, the N-terminal hemerythrin-like (Hr) region, which contains a diiron metal center, cannot bind iron and undergoes conformational changes that destabilize the FBXL5 protein and cause its ubiquitination and degradation (PubMed:19762596, PubMed:19762597). When intracellular iron levels start rising, the Hr region is stabilized (PubMed:19762596, PubMed:19762597). Additional increases in iron levels facilitate the assembly and incorporation of a redox active [2Fe-2S] cluster in the C-terminal domain (PubMed:32126207). Only when oxygen level is high enough to maintain the cluster in its oxidized state can FBXL5 recruit IRP2 as a substrate for polyubiquination and degradation (PubMed:32126207). Promotes ubiquitination and subsequent degradation of the dynactin complex component DCTN1 (PubMed:17532294). Within the nucleus, promotes the ubiquitination of SNAI1; preventing its interaction with DNA and promoting its degradation (PubMed:24157836). Negatively regulates DNA damage response by mediating the ubiquitin-proteasome degradation of the DNA repair protein NABP2 (PubMed:25249620)", "gene_name": "FBXL5", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UKA1", "name": "FBXO3", "organism": "Homo sapiens", "uniprot_id": "Q9UKA1" }, { "function": "Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types", "gene_name": "CDH12", "glycan_count": 2, "glycosylation_sites": [ { "position": 256, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 456, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 537, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 545, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P55289", "name": "Neural cadherin (N-cadherin)", "organism": "Homo sapiens", "uniprot_id": "P55289" }, { "function": "Phosphoinositide-3-kinase (PI3K) phosphorylates phosphatidylinositol (PI) and its phosphorylated derivatives at position 3 of the inositol ring to produce 3-phosphoinositides (PubMed:15135396, PubMed:23936502, PubMed:28676499). Uses ATP and PtdIns(4,5)P2 (phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3) (PubMed:15135396, PubMed:28676499). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Participates in cellular signaling in response to various growth factors. Involved in the activation of AKT1 upon stimulation by receptor tyrosine kinases ligands such as EGF, insulin, IGF1, VEGFA and PDGF. Involved in signaling via insulin-receptor substrate (IRS) proteins. Essential in endothelial cell migration during vascular development through VEGFA signaling, possibly by regulating RhoA activity. Required for lymphatic vasculature development, possibly by binding to RAS and by activation by EGF and FGF2, but not by PDGF. Regulates invadopodia formation through the PDPK1-AKT1 pathway. Participates in cardiomyogenesis in embryonic stem cells through a AKT1 pathway. Participates in vasculogenesis in embryonic stem cells through PDK1 and protein kinase C pathway. In addition to its lipid kinase activity, it displays a serine-protein kinase activity that results in the autophosphorylation of the p85alpha regulatory subunit as well as phosphorylation of other proteins such as 4EBP1, H-Ras, the IL-3 beta c receptor and possibly others (PubMed:23936502, PubMed:28676499). Plays a role in the positive regulation of phagocytosis and pinocytosis (By similarity)", "gene_name": "PIK3CA", "glycan_count": 0, "glycosylation_sites": [], "id": "P42336", "name": "PI3K (PIK3CA)", "organism": "Homo sapiens", "uniprot_id": "P42336" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q02583", "name": "NTRK1", "organism": "", "uniprot_id": "Q02583" }, { "function": "Tumor suppressor that is a key regulator of the G1/S transition of the cell cycle (PubMed:10499802). The hypophosphorylated form binds transcription regulators of the E2F family, preventing transcription of E2F-responsive genes (PubMed:10499802). Both physically blocks E2Fs transactivating domain and recruits chromatin-modifying enzymes that actively repress transcription (PubMed:10499802). Cyclin and CDK-dependent phosphorylation of RB1 induces its dissociation from E2Fs, thereby activating transcription of E2F responsive genes and triggering entry into S phase (PubMed:10499802). RB1 also promotes the G0-G1 transition upon phosphorylation and activation by CDK3/cyclin-C (PubMed:15084261). Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex (By similarity)", "gene_name": "RB1", "glycan_count": 2, "glycosylation_sites": [], "id": "P06400", "name": "RB1", "organism": "Homo sapiens", "uniprot_id": "P06400" }, { "function": "Ser/Thr-kinase component of cyclin D-CDK4 (DC) complexes that phosphorylate and inhibit members of the retinoblastoma (RB) protein family including RB1 and regulate the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complexes and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals. Also phosphorylates SMAD3 in a cell-cycle-dependent manner and represses its transcriptional activity. Component of the ternary complex, cyclin D/CDK4/CDKN1B, required for nuclear translocation and activity of the cyclin D-CDK4 complex", "gene_name": "CDK4", "glycan_count": 1, "glycosylation_sites": [], "id": "P11802", "name": "CDK4", "organism": "Homo sapiens", "uniprot_id": "P11802" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P29460 (IL23A), Q9NPF7 (IL12B)", "name": "Interleukin-23 (IL-23)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "Mrps31", "glycan_count": 0, "glycosylation_sites": [], "id": "Q61733", "name": "Kir4.1", "organism": "Mus musculus", "uniprot_id": "Q61733" }, { "function": "Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient (PubMed:1325650, PubMed:17021166, PubMed:28256214, PubMed:29844171). Implicated in the regulation of hippocampal replay occurring within sharp wave ripples (SPW-R) important for memory (By similarity)", "gene_name": "SCN2A", "glycan_count": 1, "glycosylation_sites": [ { "position": 212, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 285, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 291, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 297, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 303, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 308, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 340, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1368, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1382, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1393, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q99250", "name": "Nav1.2", "organism": "Homo sapiens", "uniprot_id": "Q99250" }, { "function": "Pore-forming subunit of a voltage-gated sodium channel complex assuming opened or closed conformations in response to the voltage difference across membranes and through which sodium ions selectively pass along their electrochemical gradient (PubMed:24874546, PubMed:25239001, PubMed:25725044, PubMed:26900580, PubMed:29726066, PubMed:33245860, PubMed:36696443, PubMed:36823201). Contributes to neuronal excitability by regulating action potential threshold and propagation (PubMed:24874546, PubMed:25239001, PubMed:25725044, PubMed:26900580, PubMed:29726066, PubMed:33245860, PubMed:36696443, PubMed:36823201)", "gene_name": "SCN8A", "glycan_count": 2, "glycosylation_sites": [ { "position": 215, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 289, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 295, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 308, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 326, "type": "N-linked (GlcNAc...) (high mannose) asparagine" }, { "position": 1358, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1372, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1383, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UQD0", "name": "Nav1.6", "organism": "Homo sapiens", "uniprot_id": "Q9UQD0" }, { "function": "Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents (PubMed:12181424, PubMed:15454078, PubMed:15863612, PubMed:16299511, PubMed:17224476, PubMed:20953164, PubMed:23677916, PubMed:24728418, PubMed:26253506, PubMed:27218670, PubMed:29078335, PubMed:29742403, PubMed:30023270, PubMed:30172029, PubMed:34163037, PubMed:8099908). Mediates influx of calcium ions into the cytoplasm, and thereby triggers calcium release from the sarcoplasm (By similarity). Plays an important role in excitation-contraction coupling in the heart. Required for normal heart development and normal regulation of heart rhythm (PubMed:15454078, PubMed:15863612, PubMed:17224476, PubMed:24728418, PubMed:26253506). Required for normal contraction of smooth muscle cells in blood vessels and in the intestine. Essential for normal blood pressure regulation via its role in the contraction of arterial smooth muscle cells (PubMed:28119464). Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group (Probable)", "gene_name": "CACNA1C", "glycan_count": 2, "glycosylation_sites": [ { "position": 153, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 328, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1436, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1487, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13936", "name": "Cav1.2", "organism": "Homo sapiens", "uniprot_id": "Q13936" }, { "function": "Pore-forming subunit of the mechanosensitive non-specific cation Piezo channel required for rapidly adapting mechanically activated (MA) currents and has a key role in sensing touch and tactile pain (PubMed:23479567, PubMed:23695678, PubMed:25955826, PubMed:37590348). Piezo channels are homotrimeric three-blade propeller-shaped structures that utilize a cap-motion and plug-and-latch mechanism to gate their ion-conducting pathways (PubMed:37590348). Generates currents characterized by a linear current-voltage relationship that are sensitive to ruthenium red and gadolinium (By similarity). Conductance to monovalent alkali ions is highest for K(+), intermediate for Na(+) and lowest for Li(+) (PubMed:25955826). Divalent ions except for Mn(2+) permeate the channel but more slowly than the monovalent ions and they also reduce K(+) currents (PubMed:25955826). Plays a key role in epithelial cell adhesion by maintaining integrin activation through R-Ras recruitment to the ER, most probably in its activated state, and subsequent stimulation of calpain signaling (PubMed:20016066). In inner ear hair cells, PIEZO1/2 subunits may constitute part of the mechanotransducer (MET) non-selective cation channel complex where they may act as pore-forming ion-conducting component in the complex (By similarity). In the kidney, may contribute to the detection of intraluminal pressure changes and to urine flow sensing (By similarity). Acts as a shear-stress sensor that promotes endothelial cell organization and alignment in the direction of blood flow through calpain activation (PubMed:25119035). Plays a key role in blood vessel formation and vascular structure in both development and adult physiology (By similarity). Acts as a sensor of phosphatidylserine (PS) flipping at the plasma membrane and governs morphogenesis of muscle cells (By similarity). In myoblasts, flippase-mediated PS enrichment at the inner leaflet of plasma membrane triggers channel activation and Ca2+ influx followed by Rho GTPases signal transduction, leading to assembly of cortical actomyosin fibers and myotube formation (PubMed:29799007)", "gene_name": "PIEZO1", "glycan_count": 11, "glycosylation_sites": [ { "position": 295, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2294, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q92508", "name": "Piezo1", "organism": "Homo sapiens", "uniprot_id": "Q92508" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y6U6", "name": "NCX3", "organism": "", "uniprot_id": "Q9Y6U6" }, { "function": "Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient", "gene_name": "KCNA3", "glycan_count": 1, "glycosylation_sites": [ { "position": 279, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P22001", "name": "Kv1.3", "organism": "Homo sapiens", "uniprot_id": "P22001" }, { "function": "Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid (PubMed:20614889, PubMed:31300657, PubMed:8003671). L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system and plays an important role in fast excitatory synaptic transmission (PubMed:14687553). Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse upon entry of monovalent and divalent cations such as sodium and calcium (PubMed:20614889, PubMed:8003671). The receptor then desensitizes rapidly and enters in a transient inactive state, characterized by the presence of bound agonist (By similarity). In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of L-glutamate (By similarity). Through complex formation with NSG1, GRIP1 and STX12 controls the intracellular fate of AMPAR and the endosomal sorting of the GRIA2 subunit toward recycling and membrane targeting (By similarity)", "gene_name": "GRIA2", "glycan_count": 0, "glycosylation_sites": [ { "position": 256, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 370, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 406, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 413, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P42262", "name": "AMPAR (GluA2)", "organism": "Homo sapiens", "uniprot_id": "P42262" }, { "function": "ATP-gated nonselective transmembrane cation channel that requires high millimolar concentrations of ATP for activation (PubMed:17483156, PubMed:25281740, PubMed:9038151). Upon ATP binding, it rapidly opens to allow the influx of small cations Na(+) and Ca(2+), and the K(+) efflux (PubMed:17483156, PubMed:20453110, PubMed:28235784, PubMed:39262850). Also has the ability to form a large pore in the cell membrane, allowing the passage of large cationic molecules (PubMed:17483156). In microglia, may mediate NADPH transport across the plasma membrane (PubMed:39142135). In immune cells, P2RX7 acts as a molecular sensor in pathological inflammatory states by detecting and responding to high local concentrations of extracellar ATP. In microglial cells, P2RX7 activation leads to the release of pro-inflammatory cytokines, such as IL-1beta and IL-18, through the activation of the NLRP3 inflammasome and caspase-1 (PubMed:26877061). Cooperates with KCNK6 to activate NLRP3 inflammasome (By similarity). Activates death pathways leading to apoptosis and autophagy (PubMed:21821797, PubMed:23303206, PubMed:28326637). Activates death pathways leading to pyroptosis (By similarity)", "gene_name": "P2RX7", "glycan_count": 11, "glycosylation_sites": [ { "position": 187, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 202, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 213, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 241, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 284, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q99572", "name": "P2X7R", "organism": "Homo sapiens", "uniprot_id": "Q99572" }, { "function": "Part of the insoluble cornified cell envelope (CE) of stratified squamous epithelia", "gene_name": "IVL", "glycan_count": 1, "glycosylation_sites": [], "id": "P07476", "name": "Involucrin", "organism": "Homo sapiens", "uniprot_id": "P07476" }, { "function": "Type I keratin involved in the formation and maintenance of various skin appendages, specifically in determining shape and orientation of hair (By similarity). Required for the correct growth of hair follicles, in particular for the persistence of the anagen (growth) state (By similarity). Modulates the function of TNF-alpha in the specific context of hair cycling. Regulates protein synthesis and epithelial cell growth through binding to the adapter protein SFN and by stimulating Akt/mTOR pathway (By similarity). Involved in tissue repair. May be a marker of basal cell differentiation in complex epithelia and therefore indicative of a certain type of epithelial 'stem cells'. Acts as a promoter of epithelial proliferation by acting a regulator of immune response in skin: promotes Th1/Th17-dominated immune environment contributing to the development of basaloid skin tumors (By similarity). May act as an autoantigen in the immunopathogenesis of psoriasis, with certain peptide regions being a major target for autoreactive T-cells and hence causing their proliferation", "gene_name": "KRT17", "glycan_count": 1, "glycosylation_sites": [], "id": "Q04695", "name": "Keratin 17 (K17)", "organism": "Homo sapiens", "uniprot_id": "Q04695" }, { "function": "Transcriptional activator that recognizes and binds to the DNA sequence 5'-[AG]TAAA[TC]A-3' and regulates different processes, such as apoptosis and autophagy (PubMed:10102273, PubMed:16751106, PubMed:21329882, PubMed:30513302). Acts as a positive regulator of autophagy in skeletal muscle: in starved cells, enters the nucleus following dephosphorylation and binds the promoters of autophagy genes, such as GABARAP1L, MAP1LC3B and ATG12, thereby activating their expression, resulting in proteolysis of skeletal muscle proteins (By similarity). Triggers apoptosis in the absence of survival factors, including neuronal cell death upon oxidative stress (PubMed:10102273, PubMed:16751106). Participates in post-transcriptional regulation of MYC: following phosphorylation by MAPKAPK5, promotes induction of miR-34b and miR-34c expression, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent its translation (PubMed:21329882). In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription (PubMed:23283301). In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription. Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). Also acts as a key regulator of regulatory T-cells (Treg) differentiation by activating expression of FOXP3 (PubMed:30513302)", "gene_name": "FOXO3", "glycan_count": 2, "glycosylation_sites": [], "id": "O43524", "name": "FOXO3", "organism": "Homo sapiens", "uniprot_id": "O43524" }, { "function": "Hydrolyzes rapidly the acetylcholine neurotransmitter released into the synaptic cleft allowing to terminate the signal transduction at the neuromuscular junction. Role in neuronal apoptosis", "gene_name": "ACHE", "glycan_count": 2, "glycosylation_sites": [ { "position": 296, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 381, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 495, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P22303", "name": "Acetylcholinesterase (AChE)", "organism": "Homo sapiens", "uniprot_id": "P22303" }, { "function": "Catalyzes the reversible conversion of beta-D-fructose 1,6-bisphosphate (FBP) into two triose phosphate and plays a key role in glycolysis and gluconeogenesis (By similarity). In addition, may also function as scaffolding protein (By similarity)", "gene_name": "Aldoa", "glycan_count": 1, "glycosylation_sites": [], "id": "P05064", "name": "ALT (Alanine aminotransferase)", "organism": "Mus musculus", "uniprot_id": "P05064" }, { "function": "Retinol-binding protein that mediates retinol transport in blood plasma (PubMed:5541771). Delivers retinol from the liver stores to the peripheral tissues (Probable). Transfers the bound all-trans retinol to STRA6, that then facilitates retinol transport across the cell membrane (PubMed:22665496)", "gene_name": "RBP4", "glycan_count": 0, "glycosylation_sites": [], "id": "P02753", "name": "Retinol-binding protein (RBP)", "organism": "Homo sapiens", "uniprot_id": "P02753" }, { "function": "Triosephosphate isomerase is an extremely efficient metabolic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis and gluconeogenesis", "gene_name": "Tpi1", "glycan_count": 1, "glycosylation_sites": [], "id": "P48500", "name": "GIP receptor", "organism": "Rattus norvegicus", "uniprot_id": "P48500" }, { "function": "Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism (PubMed:17307971, PubMed:17712357). In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation (PubMed:17307971, PubMed:17712357). AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators (PubMed:17307971, PubMed:17712357). Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively (PubMed:7959015). Promotes lipolysis of lipid droplets by mediating phosphorylation of isoform 1 of CHKA (CHKalpha2) (PubMed:34077757). Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3 (By similarity). Involved in insulin receptor/INSR internalization (PubMed:25687571). AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160 (By similarity). Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A (PubMed:11518699, PubMed:11554766, PubMed:15866171, PubMed:17711846, PubMed:18184930). Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm (By similarity). In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription (By similarity). Acts as a key regulator of cell growth and proliferation by phosphorylating FNIP1, TSC2, RPTOR, WDR24 and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2 (PubMed:14651849, PubMed:20160076, PubMed:21205641). Also phosphorylates and inhibits GATOR2 subunit WDR24 in response to nutrient limitation, leading to suppress glucose-mediated mTORC1 activation (PubMed:36732624). In response to energetic stress, phosphorylates FNIP1, inactivating the non-canonical mTORC1 signaling, thereby promoting nuclear translocation of TFEB and TFE3, and inducing transcription of lysosomal or autophagy genes (PubMed:37079666). In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1 (PubMed:21205641). In that process, it also activates WDR45/WIPI4 (PubMed:28561066). Phosphorylates CASP6, thereby preventing its autoprocessing and subsequent activation (PubMed:32029622). AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it (By similarity). May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it (By similarity). Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin (PubMed:17486097). Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1 (PubMed:12519745, PubMed:20074060). Plays an important role in the differential regulation of pro-autophagy (composed of PIK3C3, BECN1, PIK3R4 and UVRAG or ATG14) and non-autophagy (composed of PIK3C3, BECN1 and PIK3R4) complexes, in response to glucose starvation (By similarity). Can inhibit the non-autophagy complex by phosphorylating PIK3C3 and can activate the pro-autophagy complex by phosphorylating BECN1 (By similarity). Upon glucose starvation, promotes ARF6 activation in a kinase-independent manner leading to cell migration (PubMed:36017701). Upon glucose deprivation mediates the phosphorylation of ACSS2 at 'Ser-659', which exposes the nuclear localization signal of ACSS2, required for its interaction with KPNA1 and nuclear translocation (PubMed:28552616). Upon stress, regulates mitochondrial fragmentation through phosphorylation of MTFR1L (PubMed:36367943)", "gene_name": "PRKAA2", "glycan_count": 4, "glycosylation_sites": [], "id": "P54646", "name": "AMPK", "organism": "Homo sapiens", "uniprot_id": "P54646" }, { "function": "Ligand-activated transcription factor. Key regulator of lipid metabolism. Activated by the endogenous ligand 1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphocholine (16:0/18:1-GPC). Activated by oleylethanolamide, a naturally occurring lipid that regulates satiety. Receptor for peroxisome proliferators such as hypolipidemic drugs and fatty acids. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as a transcription activator for the ACOX1 and P450 genes. Transactivation activity requires heterodimerization with RXRA and is antagonized by NR2C2. May be required for the propagation of clock information to metabolic pathways regulated by PER2", "gene_name": "PPARA", "glycan_count": 0, "glycosylation_sites": [], "id": "Q07869", "name": "PPAR-\u03b1", "organism": "Homo sapiens", "uniprot_id": "Q07869" }, { "function": "Ligand-activated transcription factor. Receptor for bile acids (BAs) such as chenodeoxycholic acid (CDCA), lithocholic acid, deoxycholic acid (DCA) and allocholic acid (ACA). Plays a essential role in BA homeostasis through the regulation of genes involved in BA synthesis, conjugation and enterohepatic circulation. Also regulates lipid and glucose homeostasis and is involved innate immune response (PubMed:10334992, PubMed:10334993, PubMed:21383957, PubMed:22820415). The FXR-RXR heterodimer binds predominantly to farnesoid X receptor response elements (FXREs) containing two inverted repeats of the consensus sequence 5'-AGGTCA-3' in which the monomers are spaced by 1 nucleotide (IR-1) but also to tandem repeat DR1 sites with lower affinity, and can be activated by either FXR or RXR-specific ligands. It is proposed that monomeric nuclear receptors such as NR5A2/LRH-1 bound to coregulatory nuclear responsive element (NRE) halfsites located in close proximity to FXREs modulate transcriptional activity (By similarity). In the liver activates transcription of the corepressor NR0B2 thereby indirectly inhibiting CYP7A1 and CYP8B1 (involved in BA synthesis) implicating at least in part histone demethylase KDM1A resulting in epigenomic repression, and SLC10A1/NTCP (involved in hepatic uptake of conjugated BAs). Activates transcription of the repressor MAFG (involved in regulation of BA synthesis) (By similarity). Activates transcription of SLC27A5/BACS and BAAT (involved in BA conjugation), ABCB11/BSEP (involved in bile salt export) by directly recruiting histone methyltransferase CARM1, and ABCC2/MRP2 (involved in secretion of conjugated BAs) and ABCB4 (involved in secretion of phosphatidylcholine in the small intestine) (PubMed:12754200, PubMed:15471871, PubMed:17895379). Activates transcription of SLC27A5/BACS and BAAT (involved in BA conjugation), ABCB11/BSEP (involved in bile salt export) by directly recruiting histone methyltransferase CARM1, and ABCC2/MRP2 (involved in secretion of conjugated BAs) and ABCB4 (involved in secretion of phosphatidylcholine in the small intestine) (PubMed:10514450, PubMed:15239098, PubMed:16269519). In the intestine activates FGF19 expression and secretion leading to hepatic CYP7A1 repression (PubMed:12815072, PubMed:19085950). The function also involves the coordinated induction of hepatic KLB/beta-klotho expression (By similarity). Regulates transcription of liver UGT2B4 and SULT2A1 involved in BA detoxification; binding to the UGT2B4 promoter seems to imply a monomeric transactivation independent of RXRA (PubMed:12806625, PubMed:16946559). Modulates lipid homeostasis by activating liver NR0B2/SHP-mediated repression of SREBF1 (involved in de novo lipogenesis), expression of PLTP (involved in HDL formation), SCARB1 (involved in HDL hepatic uptake), APOE, APOC1, APOC4, PPARA (involved in beta-oxidation of fatty acids), VLDLR and SDC1 (involved in the hepatic uptake of LDL and IDL remnants), and inhibiting expression of MTTP (involved in VLDL assembly (PubMed:12554753, PubMed:12660231, PubMed:15337761). Increases expression of APOC2 (promoting lipoprotein lipase activity implicated in triglyceride clearance) (PubMed:11579204). Transrepresses APOA1 involving a monomeric competition with NR2A1 for binding to a DR1 element (PubMed:11927623, PubMed:21804189). Also reduces triglyceride clearance by inhibiting expression of ANGPTL3 and APOC3 (both involved in inhibition of lipoprotein lipase) (PubMed:12891557). Involved in glucose homeostasis by modulating hepatic gluconeogenesis through activation of NR0B2/SHP-mediated repression of respective genes. Modulates glycogen synthesis (inducing phosphorylation of glycogen synthase kinase-3) (By similarity). Modulates glucose-stimulated insulin secretion and is involved in insulin resistance (PubMed:20447400). Involved in intestinal innate immunity. Plays a role in protecting the distal small intestine against bacterial overgrowth and preservation of the epithelial barrier (By similarity). Down-regulates inflammatory cytokine expression in several types of immune cells including macrophages and mononuclear cells (PubMed:21242261). Mediates trans-repression of TLR4-induced cytokine expression; the function seems to require its sumoylation and prevents N-CoR nuclear receptor corepressor clearance from target genes such as IL1B and NOS2 (PubMed:19864602). Involved in the TLR9-mediated protective mechanism in intestinal inflammation. Plays an anti-inflammatory role in liver inflammation; proposed to inhibit pro-inflammatory (but not antiapoptotic) NF-kappa-B signaling) (By similarity)", "gene_name": "NR1H4", "glycan_count": 0, "glycosylation_sites": [], "id": "Q96RI1", "name": "FXR", "organism": "Homo sapiens", "uniprot_id": "Q96RI1" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P06756/P05556", "name": "Integrin \u03b1v\u03b23", "organism": "", "uniprot_id": "" }, { "function": "The biological function of avidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of avidin)", "gene_name": "AVD", "glycan_count": 2, "glycosylation_sites": [ { "position": 41, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P02701", "name": "Avidin", "organism": "Gallus gallus", "uniprot_id": "P02701" }, { "function": "The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin)", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P22629", "name": "Streptavidin", "organism": "Streptomyces avidinii", "uniprot_id": "P22629" }, { "function": "E3 ubiquitin-protein ligase. Together with the phosphatase EPM2A/laforin, appears to be involved in the clearance of toxic polyglucosan and protein aggregates via multiple pathways. In complex with EPM2A/laforin and HSP70, suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS). Ubiquitinates the glycogen-targeting protein phosphatase subunits PPP1R3C/PTG and PPP1R3D in a laforin-dependent manner and targets them for proteasome-dependent degradation, thus decreasing glycogen accumulation. Polyubiquitinates EPM2A/laforin and ubiquitinates AGL and targets them for proteasome-dependent degradation. Also promotes proteasome-independent protein degradation through the macroautophagy pathway", "gene_name": "NHLRC1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q6VVB1", "name": "Holocarboxylase synthetase (HCS)", "organism": "Homo sapiens", "uniprot_id": "Q6VVB1" }, { "function": "Catalytic release of biotin from biocytin, the product of biotin-dependent carboxylases degradation", "gene_name": "BTD", "glycan_count": 63, "glycosylation_sites": [ { "position": 119, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 150, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 203, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 349, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 402, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 489, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P43251", "name": "Biotinidase (BT)", "organism": "Homo sapiens", "uniprot_id": "P43251" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q04206/Q04207", "name": "NF-\u03baB (p50/p65)", "organism": "", "uniprot_id": "" }, { "function": "Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK1/ERK2 and MAPK3/ERK1 are the 2 MAPKs which play an important role in the MAPK/ERK cascade. They participate also in a signaling cascade initiated by activated KIT and KITLG/SCF. Depending on the cellular context, the MAPK/ERK cascade mediates diverse biological functions such as cell growth, adhesion, survival and differentiation through the regulation of transcription, translation, cytoskeletal rearrangements. The MAPK/ERK cascade also plays a role in initiation and regulation of meiosis, mitosis, and postmitotic functions in differentiated cells by phosphorylating a number of transcription factors. About 160 substrates have already been discovered for ERKs. Many of these substrates are localized in the nucleus, and seem to participate in the regulation of transcription upon stimulation. However, other substrates are found in the cytosol as well as in other cellular organelles, and those are responsible for processes such as translation, mitosis and apoptosis. Moreover, the MAPK/ERK cascade is also involved in the regulation of the endosomal dynamics, including lysosome processing and endosome cycling through the perinuclear recycling compartment (PNRC); as well as in the fragmentation of the Golgi apparatus during mitosis. The substrates include transcription factors (such as ATF2, BCL6, ELK1, ERF, FOS, HSF4 or SPZ1), cytoskeletal elements (such as CANX, CTTN, GJA1, MAP2, MAPT, PXN, SORBS3 or STMN1), regulators of apoptosis (such as BAD, BTG2, CASP9, DAPK1, IER3, MCL1 or PPARG), regulators of translation (such as EIF4EBP1 and FXR1) and a variety of other signaling-related molecules (like ARHGEF2, DCC, FRS2 or GRB10). Protein kinases (such as RAF1, RPS6KA1/RSK1, RPS6KA3/RSK2, RPS6KA2/RSK3, RPS6KA6/RSK4, SYK, MKNK1/MNK1, MKNK2/MNK2, RPS6KA5/MSK1, RPS6KA4/MSK2, MAPKAPK3 or MAPKAPK5) and phosphatases (such as DUSP1, DUSP4, DUSP6 or DUSP16) are other substrates which enable the propagation the MAPK/ERK signal to additional cytosolic and nuclear targets, thereby extending the specificity of the cascade. Mediates phosphorylation of TPR in response to EGF stimulation. May play a role in the spindle assembly checkpoint. Phosphorylates PML and promotes its interaction with PIN1, leading to PML degradation. Phosphorylates CDK2AP2 (By similarity). Phosphorylates phosphoglycerate kinase PGK1 under hypoxic conditions to promote its targeting to the mitochondrion and suppress the formation of acetyl-coenzyme A from pyruvate (PubMed:26942675)", "gene_name": "MAPK1", "glycan_count": 1, "glycosylation_sites": [], "id": "P28482", "name": "Mitogen-activated protein kinase 1 (MAPK1)", "organism": "Homo sapiens", "uniprot_id": "P28482" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P08253/P14780", "name": "Matrix metalloproteinase-2/9 (MMP-2/9)", "organism": "", "uniprot_id": "" }, { "function": "Functions as an interleukin receptor which binds interleukin-12 with low affinity and is involved in IL12 transduction. Associated with IL12RB2 it forms a functional, high affinity receptor for IL12. Also associates with IL23R to form the interleukin-23 receptor which functions in IL23 signal transduction probably through activation of the Jak-Stat signaling cascade", "gene_name": "IL12RB1", "glycan_count": 0, "glycosylation_sites": [ { "position": 121, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 329, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 346, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 352, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 442, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 456, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P42701", "name": "IL12RB1", "organism": "Homo sapiens", "uniprot_id": "P42701" }, { "function": "Growth factor active in angiogenesis and endothelial cell growth, stimulating their proliferation and migration. It binds to the receptor FLT1/VEGFR-1. Isoform PlGF-2 binds NRP1/neuropilin-1 and NRP2/neuropilin-2 in a heparin-dependent manner. Also promotes cell tumor growth", "gene_name": "PGF", "glycan_count": 0, "glycosylation_sites": [ { "position": 33, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 101, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P49763", "name": "PGF", "organism": "Homo sapiens", "uniprot_id": "P49763" }, { "function": "High-capacity urate transporter, which may play a role in the urate reabsorption by proximal tubules (PubMed:18327257, PubMed:18701466, PubMed:22647630, PubMed:28083649, PubMed:36749388). May have a residual high-affinity, low-capacity glucose and fructose transporter activity (PubMed:18327257, PubMed:18701466, PubMed:18842065). Transports urate at rates 45- to 60-fold faster than glucose (PubMed:18842065). Does not transport galactose (PubMed:28083649). May mediate small uptake of adenine but not of other nucleobases (PubMed:22647630)", "gene_name": "SLC2A9", "glycan_count": 0, "glycosylation_sites": [ { "position": 90, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NRM0", "name": "GLUT9", "organism": "Homo sapiens", "uniprot_id": "Q9NRM0" }, { "function": "Functions as a Na(+)-independent bidirectional multispecific transporter (PubMed:11327718, PubMed:18216183, PubMed:21446918, PubMed:28945155). Contributes to the renal and hepatic elimination of endogenous organic compounds from the systemic circulation into the urine and bile, respectively (PubMed:11327718, PubMed:25904762). Capable of transporting a wide range of purine and pyrimidine nucleobases, nucleosides and nucleotides, with cGMP, 2'deoxyguanosine and GMP being the preferred substrates (PubMed:11327718, PubMed:18216183, PubMed:26377792, PubMed:28945155). Functions as a pH- and chloride-independent cGMP bidirectional facilitative transporter that can regulate both intracellular and extracellular levels of cGMP and may be involved in cGMP signaling pathways (PubMed:18216183, PubMed:26377792). Mediates orotate/glutamate bidirectional exchange and most likely display a physiological role in hepatic release of glutamate into the blood (PubMed:21446918). Involved in renal secretion and possible reabsorption of creatinine (PubMed:25904762, PubMed:28945155). Able to uptake prostaglandin E2 (PGE2) and may contribute to PGE2 renal excretion (Probable). Also transports alpha-ketoglutarate and urate (PubMed:11327718, PubMed:26377792). Apart from the orotate/glutamate exchange, the counterions for the uptake of other SLC22A7/OAT2 substrates remain to be identified (PubMed:26377792)", "gene_name": "SLC22A7", "glycan_count": 2, "glycosylation_sites": [ { "position": 91, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y694", "name": "OAT3", "organism": "Homo sapiens", "uniprot_id": "Q9Y694" }, { "function": "Component of the ankyrin-1 complex, a multiprotein complex involved in the stability and shape of the erythrocyte membrane (PubMed:35835865). Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane", "gene_name": "GYPA", "glycan_count": 28, "glycosylation_sites": [ { "position": 21, "type": "O-linked (GalNAc...) serine" }, { "position": 22, "type": "O-linked (GalNAc...) threonine" }, { "position": 23, "type": "O-linked (GalNAc...) threonine" }, { "position": 29, "type": "O-linked (GalNAc...) threonine" }, { "position": 30, "type": "O-linked (GalNAc...) serine" }, { "position": 31, "type": "O-linked (GalNAc...) threonine" }, { "position": 32, "type": "O-linked (GalNAc...) serine" }, { "position": 36, "type": "O-linked (GalNAc...) threonine" }, { "position": 38, "type": "O-linked (GalNAc...) serine" }, { "position": 41, "type": "O-linked (GalNAc...) serine" }, { "position": 44, "type": "O-linked (GalNAc...) threonine" }, { "position": 45, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 52, "type": "O-linked (GalNAc...) threonine" }, { "position": 56, "type": "O-linked (GalNAc...) threonine" }, { "position": 63, "type": "O-linked (GalNAc...) serine" }, { "position": 66, "type": "O-linked (GalNAc...) serine" }, { "position": 69, "type": "O-linked (GalNAc...) threonine" } ], "id": "P02724", "name": "Glycophorin A (GPA)", "organism": "Homo sapiens", "uniprot_id": "P02724" }, { "function": "Its primary physiological function is unclear. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May promote myelin homeostasis through acting as an agonist for ADGRG6 receptor. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro) (By similarity). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or Zn(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity)", "gene_name": "PRNP", "glycan_count": 14, "glycosylation_sites": [ { "position": 181, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 197, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P04156", "name": "Prion protein (PrP)", "organism": "Homo sapiens", "uniprot_id": "P04156" }, { "function": "Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways (PubMed:15696159, PubMed:16511572, PubMed:36732624). Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif (PubMed:15696159, PubMed:16511572, PubMed:36732624). Binding generally results in the modulation of the activity of the binding partner (PubMed:16511572). Promotes inactivation of WDR24 component of the GATOR2 complex by binding to phosphorylated WDR24 (PubMed:36732624). Participates in the positive regulation of NMDA glutamate receptor activity by promoting the L-glutamate secretion through interaction with BEST1 (PubMed:29121962). Reduces keratinocyte intercellular adhesion, via interacting with PKP1 and sequestering it in the cytoplasm, thereby reducing its incorporation into desmosomes (PubMed:29678907). Plays a role in mitochondrial protein catabolic process (also named MALM) that promotes the degradation of damaged proteins inside mitochondria (PubMed:22532927)", "gene_name": "YWHAG", "glycan_count": 2, "glycosylation_sites": [], "id": "P61981", "name": "14-3-3 gamma protein", "organism": "Homo sapiens", "uniprot_id": "P61981" }, { "function": "Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol", "gene_name": "COMT", "glycan_count": 1, "glycosylation_sites": [], "id": "P21964", "name": "COMT (Catechol-O-methyltransferase)", "organism": "Homo sapiens", "uniprot_id": "P21964" }, { "function": "Catalyzes the oxidative deamination of primary and some secondary amines such as neurotransmitters, and exogenous amines including the tertiary amine, neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), with concomitant reduction of oxygen to hydrogen peroxide and participates in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues (PubMed:11049757, PubMed:11134050, PubMed:20493079, PubMed:8316221, PubMed:8665924). Preferentially degrades benzylamine and phenylethylamine (PubMed:11049757, PubMed:11134050, PubMed:20493079, PubMed:8316221, PubMed:8665924)", "gene_name": "MAOB", "glycan_count": 1, "glycosylation_sites": [], "id": "P27338", "name": "MAO-B (Monoamine oxidase B)", "organism": "Homo sapiens", "uniprot_id": "P27338" }, { "function": "Buffers cytosolic calcium. May stimulate a membrane Ca(2+)-ATPase and a 3',5'-cyclic nucleotide phosphodiesterase", "gene_name": "Calb1", "glycan_count": 1, "glycosylation_sites": [], "id": "P12658", "name": "Calbindin", "organism": "Mus musculus", "uniprot_id": "P12658" }, { "function": "Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth (By similarity). Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G-proteins (PubMed:10926528, PubMed:11972040, PubMed:12044163, PubMed:16586416, PubMed:16908857, PubMed:17060607, PubMed:17449675, PubMed:18818650, PubMed:21389983, PubMed:22198838, PubMed:23579341, PubMed:25205354, PubMed:27458239). Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by the arrestin SAG and terminates signaling (PubMed:1396673, PubMed:15111114)", "gene_name": "RHO", "glycan_count": 7, "glycosylation_sites": [ { "position": 2, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 15, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P02699", "name": "Rhodopsin", "organism": "Bos taurus", "uniprot_id": "P02699" }, { "function": "Involved in the biosynthetic pathway of cholesterol", "gene_name": "ACAT2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9BWD1", "name": "Dehydrodolichyl diphosphate synthase subunit (DHDDS)", "organism": "Homo sapiens", "uniprot_id": "Q9BWD1" }, { "function": "Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. In the lumen of the endoplasmic reticulum, adds the first glucose residue from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide intermediate Man(9)GlcNAc(2)-PP-Dol to produce Glc(1)Man(9)GlcNAc(2)-PP-Dol. Glc(1)Man(9)GlcNAc(2)-PP-Dol is a substrate for ALG8, the following enzyme in the biosynthetic pathway", "gene_name": "ALG6", "glycan_count": 0, "glycosylation_sites": [ { "position": 59, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y672", "name": "ALG6", "organism": "Homo sapiens", "uniprot_id": "Q9Y672" }, { "function": "Plays a role in the regulation of glomerular permeability, acting probably as a linker between the plasma membrane and the cytoskeleton", "gene_name": "NPHS2", "glycan_count": 0, "glycosylation_sites": [ { "position": 287, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NP85", "name": "Podocin", "organism": "Homo sapiens", "uniprot_id": "Q9NP85" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01876 (IgA1), P01877/P0DOX2 (IgA2)", "name": "Immunoglobulin A (IgA)", "organism": "", "uniprot_id": "" }, { "function": "Converts sphingomyelin to ceramide (PubMed:12563314, PubMed:1840600, PubMed:18815062, PubMed:25339683, PubMed:25920558, PubMed:27659707, PubMed:33163980). Exists as two enzymatic forms that arise from alternative trafficking of a single protein precursor, one that is targeted to the endolysosomal compartment, whereas the other is released extracellularly (PubMed:20807762, PubMed:21098024, PubMed:9660788). However, in response to various forms of stress, lysosomal exocytosis may represent a major source of the secretory form (PubMed:12563314, PubMed:20530211, PubMed:20807762, PubMed:22573858, PubMed:9393854)", "gene_name": "SMPD1", "glycan_count": 6, "glycosylation_sites": [ { "position": 88, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 177, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 337, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 397, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 505, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 522, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P17405", "name": "Acid sphingomyelinase (ASM)", "organism": "Homo sapiens", "uniprot_id": "P17405" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01225|P01215", "name": "Follicle-stimulating hormone (FSH, CGA|FSHB)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01229|P01229", "name": "Luteinizing hormone (LH, CGA|LHB)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01215|P01233|Q9UBR2", "name": "Human Chorionic Gonadotropin (hCG, CGA|CGB3|CGB7)", "organism": "", "uniprot_id": "" }, { "function": "Has antibacterial activity", "gene_name": "DEFB123", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8N688", "name": "Beta-defensin 104 (DEFB104A)", "organism": "Homo sapiens", "uniprot_id": "Q8N688" }, { "function": "Involved in controlling patterning and neuronal circuit formation at the laminar, cellular, subcellular and synaptic levels. Promotes neurite outgrowth of both axons and dendrites", "gene_name": "NTNG1", "glycan_count": 2, "glycosylation_sites": [ { "position": 133, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 320, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 406, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 433, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y2I2", "name": "Neurotrimin (NTM)", "organism": "Homo sapiens", "uniprot_id": "Q9Y2I2" }, { "function": "Immunoregulatory receptor which inhibits the T-cell response (PubMed:24691993). May promote differentiation of embryonic stem cells, by inhibiting BMP4 signaling (By similarity). May stimulate MMP14-mediated MMP2 activation (PubMed:20666777)", "gene_name": "VSIR", "glycan_count": 15, "glycosylation_sites": [ { "position": 49, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 91, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 128, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9H7M9", "name": "V-set and immunoglobulin domain-containing protein 4 (VSIG4)", "organism": "Homo sapiens", "uniprot_id": "Q9H7M9" }, { "function": "Mediates inactivation of the lipoprotein lipase LPL, and thereby plays a role in the regulation of triglyceride clearance from the blood serum and in lipid metabolism (PubMed:19270337, PubMed:21398697, PubMed:27929370, PubMed:29899144). May also play a role in regulating glucose homeostasis and insulin sensitivity (Probable). Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage (PubMed:14583458, PubMed:17068295). Upon heterologous expression, inhibits the adhesion of endothelial cell to the extracellular matrix (ECM), and inhibits the reorganization of the actin cytoskeleton, formation of actin stress fibers and focal adhesions in endothelial cells that have adhered to ANGPTL4-containing ECM (in vitro) (PubMed:17068295). Depending on context, may modulate tumor-related angiogenesis (By similarity)", "gene_name": "ANGPTL4", "glycan_count": 25, "glycosylation_sites": [ { "position": 177, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9BY76", "name": "ANGPTL4", "organism": "Homo sapiens", "uniprot_id": "Q9BY76" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "varies by strain; e.g., P03468 for H3N2", "name": "Influenza virus neuraminidase (NA)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P05019 (chicken, if inferred from UniProt)", "name": "Insulin-like growth factor-1 (IGF-1)", "organism": "", "uniprot_id": "" }, { "function": "Participates in the regulation of synaptic vesicle docking and fusion through interaction with GTP-binding proteins (By similarity). Essential for neurotransmission and binds syntaxin, a component of the synaptic vesicle fusion machinery probably in a 1:1 ratio. Can interact with syntaxins 1, 2, and 3 but not syntaxin 4. Involved in the release of neurotransmitters from neurons through interacting with SNARE complex component STX1A and mediating the assembly of the SNARE complex at synaptic membranes (By similarity). May play a role in determining the specificity of intracellular fusion reactions", "gene_name": "STXBP1", "glycan_count": 1, "glycosylation_sites": [], "id": "P61764", "name": "STXBP1", "organism": "Homo sapiens", "uniprot_id": "P61764" }, { "function": "Pore-forming subunit of Nav1.1, a voltage-gated sodium (Nav) channel that directly mediates the depolarizing phase of action potentials in excitable membranes. Navs, also called VGSCs (voltage-gated sodium channels) or VDSCs (voltage-dependent sodium channels), operate by switching between closed and open conformations depending on the voltage difference across the membrane. In the open conformation they allow Na(+) ions to selectively pass through the pore, along their electrochemical gradient. The influx of Na(+) ions provokes membrane depolarization, initiating the propagation of electrical signals throughout cells and tissues (PubMed:14672992). By regulating the excitability of neurons, ensures that they respond appropriately to synaptic inputs, maintaining the balance between excitation and inhibition in brain neural circuits (By similarity). Nav1.1 plays a role in controlling the excitability and action potential propagation from somatosensory neurons, thereby contributing to the sensory perception of mechanically-induced pain (By similarity)", "gene_name": "SCN1A", "glycan_count": 1, "glycosylation_sites": [ { "position": 211, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 284, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 295, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 301, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 306, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 338, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1378, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1392, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1403, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P35498", "name": "SCN1A", "organism": "Homo sapiens", "uniprot_id": "P35498" }, { "function": "Pore-forming subunit of the voltage-gated potassium (Kv) M-channel which is responsible for the M-current, a key controller of neuronal excitability (PubMed:24277843, PubMed:28793216, PubMed:9836639). M-channel is composed of pore-forming subunits KCNQ2 and KCNQ3 assembled as heterotetramers (PubMed:10781098, PubMed:14534157, PubMed:32884139, PubMed:37857637, PubMed:9836639). The native M-current has a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs (PubMed:14534157, PubMed:28793216, PubMed:9836639). KCNQ2-KCNQ3 M-channel is selectively permeable in vitro to other cations besides potassium, in decreasing order of affinity K(+) > Rb(+) > Cs(+) > Na(+) (PubMed:28793216). M-channel association with SLC5A3/SMIT1 alters channel ion selectivity, increasing Na(+) and Cs(+) permeation relative to K(+) (PubMed:28793216). Suppressed by activation of the muscarinic acetylcholine receptor CHRM1 (PubMed:10684873, PubMed:10713961)", "gene_name": "KCNQ2", "glycan_count": 1, "glycosylation_sites": [], "id": "O43526", "name": "KCNQ2", "organism": "Homo sapiens", "uniprot_id": "O43526" }, { "function": "Endonuclease that cooperates with the MRE11-RAD50-NBN (MRN) complex in DNA-end resection, the first step of double-strand break (DSB) repair through the homologous recombination (HR) pathway (PubMed:17965729, PubMed:19202191, PubMed:19759395, PubMed:20064462, PubMed:23273981, PubMed:26721387, PubMed:27814491, PubMed:27889449, PubMed:30787182). HR is restricted to S and G2 phases of the cell cycle and preferentially repairs DSBs resulting from replication fork collapse (PubMed:17965729, PubMed:19202191, PubMed:23273981, PubMed:27814491, PubMed:27889449, PubMed:30787182). Key determinant of DSB repair pathway choice, as it commits cells to HR by preventing classical non-homologous end-joining (NHEJ) (PubMed:19202191). Specifically promotes the endonuclease activity of the MRN complex to clear DNA ends containing protein adducts: recruited to DSBs by NBN following phosphorylation by CDK1, and promotes the endonuclease activity of MRE11 to clear protein-DNA adducts and generate clean double-strand break ends (PubMed:27814491, PubMed:27889449, PubMed:30787182, PubMed:33836577). Functions downstream of the MRN complex and ATM, promotes ATR activation and its recruitment to DSBs in the S/G2 phase facilitating the generation of ssDNA (PubMed:16581787, PubMed:17965729, PubMed:19759395, PubMed:20064462). Component of the BRCA1-RBBP8 complex that regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage (PubMed:15485915, PubMed:16818604). During immunoglobulin heavy chain class-switch recombination, promotes microhomology-mediated alternative end joining (A-NHEJ) and plays an essential role in chromosomal translocations (By similarity). Binds preferentially to DNA Y-junctions and to DNA substrates with blocked ends and promotes intermolecular DNA bridging (PubMed:30601117)", "gene_name": "RBBP8", "glycan_count": 1, "glycosylation_sites": [], "id": "Q99708", "name": "ATN1", "organism": "Homo sapiens", "uniprot_id": "Q99708" }, { "function": "Hyperpolarization-activated ion channel that is permeable to sodium and potassium ions. Displays lower selectivity for K(+) over Na(+) ions (PubMed:10228147, PubMed:22006928). Contributes to the native pacemaker currents in heart (If) and in neurons (Ih) (PubMed:10228147, PubMed:10524219). Can also transport ammonium in the distal nephron (By similarity). Involved in the initiation of neuropathic pain in sensory neurons (By similarity)", "gene_name": "HCN2", "glycan_count": 1, "glycosylation_sites": [ { "position": 407, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UL51", "name": "HCN2", "organism": "Homo sapiens", "uniprot_id": "Q9UL51" }, { "function": "Has neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons. Binds, in a calcium-dependent manner, to cultured neocortical neurons and promotes cell survival (By similarity)", "gene_name": "ENO2", "glycan_count": 1, "glycosylation_sites": [], "id": "P09104", "name": "Neuron Specific Enolase (NSE)", "organism": "Homo sapiens", "uniprot_id": "P09104" }, { "function": "Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins", "gene_name": "GFPT2", "glycan_count": 0, "glycosylation_sites": [], "id": "O94808", "name": "GFPT2", "organism": "Homo sapiens", "uniprot_id": "O94808" }, { "function": "Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface", "gene_name": "ASGR1", "glycan_count": 0, "glycosylation_sites": [ { "position": 79, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 147, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P07306", "name": "ASGR1", "organism": "Homo sapiens", "uniprot_id": "P07306" }, { "function": "Unknown. Cellular response protein to viral infection", "gene_name": "GOLM1", "glycan_count": 61, "glycosylation_sites": [ { "position": 109, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 144, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 398, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8NBJ4", "name": "Golgi Protein 73 (GP73)", "organism": "Homo sapiens", "uniprot_id": "Q8NBJ4" }, { "function": "Lineage-specific cytokine affecting the proliferation and maturation of megakaryocytes from their committed progenitor cells. It acts at a late stage of megakaryocyte development. It may be the major physiological regulator of circulating platelets", "gene_name": "THPO", "glycan_count": 32, "glycosylation_sites": [ { "position": 22, "type": "O-linked (GalNAc...) serine" }, { "position": 58, "type": "O-linked (GalNAc...) threonine" }, { "position": 131, "type": "O-linked (GalNAc...) threonine" }, { "position": 179, "type": "O-linked (GalNAc...) threonine" }, { "position": 180, "type": "O-linked (GalNAc...) threonine" }, { "position": 184, "type": "O-linked (GalNAc...) serine" }, { "position": 197, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 206, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 213, "type": "O-linked (GalNAc...) threonine" }, { "position": 234, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 255, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 265, "type": "O-linked (GalNAc...) serine" }, { "position": 340, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 348, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P40225", "name": "Thrombopoietin (TPO)", "organism": "Homo sapiens", "uniprot_id": "P40225" }, { "function": "Acts as a lysosomal receptor for glucosylceramidase (GBA1) targeting", "gene_name": "SCARB2", "glycan_count": 116, "glycosylation_sites": [ { "position": 45, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 68, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 105, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 206, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 224, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 249, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 304, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 325, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 412, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 430, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q14108", "name": "SCARB2", "organism": "Homo sapiens", "uniprot_id": "Q14108" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P24807 (human)", "name": "CD24", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q96LC7 (human)", "name": "Siglec-10 (human)/Siglec-G (mouse/pig)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "various (host/viral)", "name": "Neuraminidase", "organism": "", "uniprot_id": "" }, { "function": "Inactive precursor of the viral replicase, which is activated by cleavages carried out by the viral protease nsP2", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8JUX6", "name": "E1 glycoprotein", "organism": "Chikungunya virus (strain S27-African prototype)", "uniprot_id": "Q8JUX6" }, { "function": "", "gene_name": "ie-1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8JUX7", "name": "E2 glycoprotein", "organism": "Anticarsia gemmatalis nuclear polyhedrosis virus", "uniprot_id": "Q8JUX7" }, { "function": "Constant region of immunoglobulin light chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268)", "gene_name": "IGKC", "glycan_count": 1, "glycosylation_sites": [], "id": "P01834", "name": "Kappa light chain", "organism": "Homo sapiens", "uniprot_id": "P01834" }, { "function": "Functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs. Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. Involved in the maturation of both CD4(+) and CD8(+) cells in the thymus. Important for follicular differentiation and possibly cell fate selection within the follicle. During cerebellar development, functions as a receptor for neuronal DNER and is involved in the differentiation of Bergmann glia. Represses neuronal and myogenic differentiation. May play an essential role in postimplantation development, probably in some aspect of cell specification and/or differentiation. May be involved in mesoderm development, somite formation and neurogenesis. May enhance HIF1A function by sequestering HIF1AN away from HIF1A. Required for the THBS4 function in regulating protective astrogenesis from the subventricular zone (SVZ) niche after injury. Involved in determination of left/right symmetry by modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO)", "gene_name": "NOTCH1", "glycan_count": 14, "glycosylation_sites": [ { "position": 41, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 65, "type": "O-linked (Glc...) serine" }, { "position": 73, "type": "O-linked (Fuc...) threonine" }, { "position": 116, "type": "O-linked (Fuc...) threonine" }, { "position": 146, "type": "O-linked (Glc...) serine" }, { "position": 194, "type": "O-linked (Fuc...) threonine" }, { "position": 232, "type": "O-linked (Fuc...) threonine; alternate" }, { "position": 232, "type": "O-linked (GalNAc...) threonine; alternate" }, { "position": 311, "type": "O-linked (Fuc...) threonine" }, { "position": 341, "type": "O-linked (Glc...) serine" }, { "position": 349, "type": "O-linked (Fuc...) threonine" }, { "position": 378, "type": "O-linked (Glc...) serine" }, { "position": 435, "type": "O-linked (Glc...) serine" }, { "position": 458, "type": "O-linked (Glc...) serine" }, { "position": 466, "type": "O-linked (Fuc...) threonine" }, { "position": 496, "type": "O-linked (Glc...) serine" }, { "position": 534, "type": "O-linked (Glc...) serine" }, { "position": 609, "type": "O-linked (Glc...) serine" }, { "position": 617, "type": "O-linked (Fuc...) threonine" }, { "position": 647, "type": "O-linked (Glc...) serine" }, { "position": 692, "type": "O-linked (Fuc...) threonine" }, { "position": 722, "type": "O-linked (Glc...) serine" }, { "position": 759, "type": "O-linked (Glc...) serine" }, { "position": 767, "type": "O-linked (Fuc...) threonine" }, { "position": 784, "type": "O-linked (GlcNAc) serine" }, { "position": 797, "type": "O-linked (Glc...) serine" }, { "position": 805, "type": "O-linked (Fuc...) threonine" }, { "position": 921, "type": "O-linked (Fuc) serine" }, { "position": 951, "type": "O-linked (Glc...) serine" }, { "position": 959, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 997, "type": "O-linked (Fuc...) threonine" }, { "position": 1027, "type": "O-linked (Glc...) serine" }, { "position": 1035, "type": "O-linked (Fuc...) threonine" }, { "position": 1065, "type": "O-linked (Glc...) serine" }, { "position": 1159, "type": "O-linked (Fuc...) threonine" }, { "position": 1179, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1189, "type": "O-linked (Glc...) serine" }, { "position": 1197, "type": "O-linked (Fuc...) threonine" }, { "position": 1241, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1273, "type": "O-linked (Glc...) serine" }, { "position": 1362, "type": "O-linked (Fuc...) threonine" }, { "position": 1379, "type": "O-linked (GlcNAc...) threonine" }, { "position": 1402, "type": "O-linked (Fuc...) threonine; alternate" }, { "position": 1402, "type": "O-linked (GalNAc...) threonine; alternate" }, { "position": 1489, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1587, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1725, "type": "O-linked (GalNAc...) threonine" } ], "id": "P46531", "name": "NOTCH1", "organism": "Homo sapiens", "uniprot_id": "P46531" }, { "function": "Transcription factor that is involved in the regulation of muscle stem cells proliferation, playing a role in myogenesis and muscle regeneration", "gene_name": "PAX7", "glycan_count": 1, "glycosylation_sites": [], "id": "P23759", "name": "PAX7", "organism": "Homo sapiens", "uniprot_id": "P23759" }, { "function": "Multifunctional protein that plays a critical role in regulating the availability of IGFs such as IGF1 and IGF2 to their receptors and thereby regulates IGF-mediated cellular processes including proliferation, differentiation, and apoptosis in a cell-type specific manner (PubMed:18563800, PubMed:38796567). Functions coordinately with receptor protein tyrosine phosphatase beta/PTPRB and the IGF1 receptor to regulate IGF1-mediated signaling by stimulating the phosphorylation of PTEN leading to its inactivation and AKT1 activation (PubMed:22869525). Plays a positive role in cell migration via interaction with integrin alpha5/ITGA5 through an RGD motif (PubMed:16569642). Additionally, interaction with ITGA5/ITGB1 enhances the adhesion of endothelial progenitor cells to endothelial cells (PubMed:26076738). Upon mitochondrial damage, facilitates apoptosis with ITGA5 of podocytes, and then activates the phosphorylation of focal adhesion kinase (FAK)-mediated mitochondrial injury (PubMed:38796567)", "gene_name": "IGFBP2", "glycan_count": 3, "glycosylation_sites": [], "id": "P18065", "name": "IGFBP2", "organism": "Homo sapiens", "uniprot_id": "P18065" }, { "function": "Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids (PubMed:31416931). Phospholipid translocation also seems to be implicated in vesicle formation and in uptake of lipid signaling molecules. In vitro, its ATPase activity is selectively and stereospecifically stimulated by phosphatidylserine (PS) (PubMed:31416931). The flippase complex ATP8A1:TMEM30A seems to play a role in regulation of cell migration probably involving flippase-mediated translocation of phosphatidylethanolamine (PE) at the cell membrane (By similarity). Acts as aminophospholipid translocase at the cell membrane in neuronal cells (By similarity)", "gene_name": "ATP8A1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y2Q0", "name": "ATP11A", "organism": "Homo sapiens", "uniprot_id": "Q9Y2Q0" }, { "function": "Multifunctional protein that is involved in the regulation of many processes including cell proliferation, apoptosis, cell cycle progression or transcription (PubMed:18039846, PubMed:20015864). Regulates the proliferation of neuronal stem cells, differentiation of leukemic cells and progression from G1 to S phase of the cell cycle. As negative regulator of caspase-3-dependent apoptosis, may act as an antagonist of ANP32A in regulating tissue homeostasis (PubMed:20015864). Exhibits histone chaperone properties, able to recruit histones to certain promoters, thus regulating the transcription of specific genes (PubMed:18039846, PubMed:20538007). Also plays an essential role in the nucleocytoplasmic transport of specific mRNAs via the uncommon nuclear mRNA export receptor XPO1/CRM1 (PubMed:17178712). Participates in the regulation of adequate adaptive immune responses by acting on mRNA expression and cell proliferation (By similarity)", "gene_name": "ANP32B", "glycan_count": 2, "glycosylation_sites": [], "id": "Q92688", "name": "ANP32B", "organism": "Homo sapiens", "uniprot_id": "Q92688" }, { "function": "Accelerates the intermembrane transfer of various glycolipids. Catalyzes the transfer of various glycosphingolipids between membranes but does not catalyze the transfer of phospholipids. May be involved in the intracellular translocation of glucosylceramides", "gene_name": "GLTP", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NZD2", "name": "COL11A2", "organism": "Homo sapiens", "uniprot_id": "Q9NZD2" }, { "function": "Catalyzes the regio and stereo-specific incorporation of molecular oxygen into free and esterified polyunsaturated fatty acids generating lipid hydroperoxides that can be further reduced to the corresponding hydroxy species (PubMed:17493578, PubMed:18311922, PubMed:1851637, PubMed:32404334, PubMed:8319693, PubMed:8500694). Mainly converts arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate) to the specific bioactive lipid (12S)-hydroperoxyeicosatetraenoate/(12S)-HPETE (PubMed:17493578, PubMed:22984144, PubMed:24282679, PubMed:8319693, PubMed:8500694). Through the production of bioactive lipids like (12S)-HPETE it regulates different biological processes including platelet activation (PubMed:8319693, PubMed:8500694). It can also catalyze the epoxidation of double bonds of polyunsaturated fatty acids such as (14S)-hydroperoxy-docosahexaenoate/(14S)-HPDHA resulting in the formation of (13S,14S)-epoxy-DHA (PubMed:23504711). Furthermore, it may participate in the sequential oxidations of DHA ((4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate) to generate specialized pro-resolving mediators (SPMs) like resolvin D5 ((7S,17S)-diHPDHA) and (7S,14S)-diHPDHA, that actively down-regulate the immune response and have anti-aggregation properties with platelets (PubMed:32404334). An additional function involves a multistep process by which it transforms leukotriene A4/LTA4 into the bioactive lipids lipoxin A4/LXA4 and lipoxin B4/LXB4, both are vasoactive and LXA4 may regulate neutrophil function via occupancy of specific recognition sites (PubMed:8250832). Can also peroxidize linoleate ((9Z,12Z)-octadecadienoate) to (13S)-hydroperoxyoctadecadienoate/ (13S-HPODE) (By similarity). Due to its role in regulating both the expression of the vascular endothelial growth factor (VEGF, an angiogenic factor involved in the survival and metastasis of solid tumors) and the expression of integrin beta-1 (known to affect tumor cell migration and proliferation), it can be regarded as protumorigenic (PubMed:16638750, PubMed:22237009, PubMed:9751607). Important for cell survival, as it may play a role not only in proliferation but also in the prevention of apoptosis in vascular smooth muscle cells (PubMed:23578768)", "gene_name": "ALOX12", "glycan_count": 1, "glycosylation_sites": [], "id": "P18054", "name": "ALOX12", "organism": "Homo sapiens", "uniprot_id": "P18054" }, { "function": "Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components", "gene_name": "LAMA2", "glycan_count": 114, "glycosylation_sites": [ { "position": 55, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 89, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 303, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 363, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 380, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 470, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 746, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1061, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1597, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1614, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1700, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1810, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1901, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1916, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1920, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2017, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2028, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2045, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2126, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2240, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2360, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2435, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2478, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2551, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2558, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2648, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2868, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2893, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P24043", "name": "Laminin-\u03b12 (LAMA2)", "organism": "Homo sapiens", "uniprot_id": "P24043" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Complex: LAMA2/LAMB1/LAMC1", "name": "Laminin-211 (merosin)", "organism": "", "uniprot_id": "" }, { "function": "Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruits SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides", "gene_name": "FKBP1A", "glycan_count": 1, "glycosylation_sites": [], "id": "P62942", "name": "Tacrolimus-binding protein (FKBP12)", "organism": "Homo sapiens", "uniprot_id": "P62942" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P16070 (rat)", "name": "CD44", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04233 (rat)", "name": "CD74", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P10923 (rat)", "name": "SPP1 (Osteopontin)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P09544 (rat)", "name": "Wnt1", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q62876 (rat)", "name": "AdipoQ (Adiponectin)", "organism": "", "uniprot_id": "" }, { "function": "Low affinity receptor for N-formyl-methionyl peptides, which are powerful neutrophils chemotactic factors. Binding of FMLP to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. Acts as a receptor for humanin (PubMed:15465011)", "gene_name": "FPR3", "glycan_count": 0, "glycosylation_sites": [ { "position": 4, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 10, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P25089", "name": "Formyl Peptide Receptor 2 (FPR2)", "organism": "Homo sapiens", "uniprot_id": "P25089" }, { "function": "Non-receptor tyrosine kinase which mediates signal transduction downstream of a variety of transmembrane receptors including classical immunoreceptors like the B-cell receptor (BCR). Regulates several biological processes including innate and adaptive immunity, cell adhesion, osteoclast maturation, platelet activation and vascular development (PubMed:12387735, PubMed:33782605). Assembles into signaling complexes with activated receptors at the plasma membrane via interaction between its SH2 domains and the receptor tyrosine-phosphorylated ITAM domains. The association with the receptor can also be indirect and mediated by adapter proteins containing ITAM or partial hemITAM domains. The phosphorylation of the ITAM domains is generally mediated by SRC subfamily kinases upon engagement of the receptor. More rarely signal transduction via SYK could be ITAM-independent. Direct downstream effectors phosphorylated by SYK include DEPTOR, VAV1, PLCG1, PI-3-kinase, LCP2 and BLNK (PubMed:12456653, PubMed:15388330, PubMed:34634301, PubMed:8657103). Initially identified as essential in B-cell receptor (BCR) signaling, it is necessary for the maturation of B-cells most probably at the pro-B to pre-B transition (PubMed:12456653). Activated upon BCR engagement, it phosphorylates and activates BLNK an adapter linking the activated BCR to downstream signaling adapters and effectors. It also phosphorylates and activates PLCG1 and the PKC signaling pathway. It also phosphorylates BTK and regulates its activity in B-cell antigen receptor (BCR)-coupled signaling. In addition to its function downstream of BCR also plays a role in T-cell receptor signaling. Also plays a crucial role in the innate immune response to fungal, bacterial and viral pathogens. It is for instance activated by the membrane lectin CLEC7A. Upon stimulation by fungal proteins, CLEC7A together with SYK activates immune cells inducing the production of ROS. Also activates the inflammasome and NF-kappa-B-mediated transcription of chemokines and cytokines in presence of pathogens. Regulates neutrophil degranulation and phagocytosis through activation of the MAPK signaling cascade (By similarity). Required for the stimulation of neutrophil phagocytosis by IL15 (PubMed:15123770). Also mediates the activation of dendritic cells by cell necrosis stimuli. Also involved in mast cells activation. Involved in interleukin-3/IL3-mediated signaling pathway in basophils (By similarity). Also functions downstream of receptors mediating cell adhesion (PubMed:12387735). Relays for instance, integrin-mediated neutrophils and macrophages activation and P-selectin receptor/SELPG-mediated recruitment of leukocytes to inflammatory loci. Also plays a role in non-immune processes. It is for instance involved in vascular development where it may regulate blood and lymphatic vascular separation. It is also required for osteoclast development and function. Functions in the activation of platelets by collagen, mediating PLCG2 phosphorylation and activation. May be coupled to the collagen receptor by the ITAM domain-containing FCER1G. Also activated by the membrane lectin CLEC1B that is required for activation of platelets by PDPN/podoplanin. Involved in platelet adhesion being activated by ITGB3 engaged by fibrinogen. Together with CEACAM20, enhances production of the cytokine CXCL8/IL-8 via the NFKB pathway and may thus have a role in the intestinal immune response (By similarity)", "gene_name": "SYK", "glycan_count": 1, "glycosylation_sites": [], "id": "P43405", "name": "Spleen tyrosine kinase (SYK)", "organism": "Homo sapiens", "uniprot_id": "P43405" }, { "function": "Co-chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp60, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (PubMed:11422376, PubMed:1346131, PubMed:7912672). The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable)", "gene_name": "HSPE1", "glycan_count": 1, "glycosylation_sites": [], "id": "P61604", "name": "Heat Shock Protein Family E Member 1 (HSPE1)", "organism": "Homo sapiens", "uniprot_id": "P61604" }, { "function": "Co-chaperone and adapter protein that connects different classes of molecular chaperones including heat shock proteins 70 (HSP70s), e.g. HSPA1A/HSP70 or HSPA8/HSC70, and small heat shock proteins (sHSPs), e.g. HSPB8 (PubMed:27884606, PubMed:30559338). Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from HSP70s, thereby triggering client protein release (PubMed:27884606, PubMed:30559338). Nucleotide release is mediated via BAG3 binding to the nucleotide-binding domain (NBD) of HSP70s, whereas client release is mediated via binding to the substrate-binding domain (SBD) (PubMed:27474739, PubMed:9873016). Has anti-apoptotic activity (PubMed:10597216). Plays a role in the HSF1 nucleocytoplasmic transport (PubMed:26159920)", "gene_name": "BAG3", "glycan_count": 2, "glycosylation_sites": [], "id": "O95817", "name": "BCL2-associated athanogene 3 (BAG3)", "organism": "Homo sapiens", "uniprot_id": "O95817" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04494 (EHV-1 gB, inferred from literature)", "name": "Glycoprotein B (gB)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01857 (mink, inferred)", "name": "IgG", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01871 (mink, inferred)", "name": "IgM", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P13612 (human, inferred)", "name": "Integrin VLA-4", "organism": "", "uniprot_id": "" }, { "function": "Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (PubMed:2001362, PubMed:20676357, PubMed:21245143, PubMed:21593166, PubMed:25678563). Exerts a strong chemotactic effect on leukocytes partly through activation of one of its membrane receptors BSG/CD147, initiating a signaling cascade that culminates in MAPK/ERK activation (PubMed:11943775, PubMed:21245143). Activates endothelial cells (ECs) in a pro-inflammatory manner by stimulating activation of NF-kappa-B and ERK, JNK and p38 MAP-kinases and by inducing expression of adhesion molecules including SELE and VCAM1 (PubMed:15130913). Induces apoptosis in ECs by promoting the FOXO1-dependent expression of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis (PubMed:31063815). In response to oxidative stress, initiates proapoptotic and antiapoptotic signaling in ECs via activation of NF-kappa-B and AKT1 and up-regulation of antiapoptotic protein BCL2 (PubMed:23180369). Negatively regulates MAP3K5/ASK1 kinase activity, autophosphorylation and oxidative stress-induced apoptosis mediated by MAP3K5/ASK1 (PubMed:26095851). Necessary for the assembly of TARDBP in heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and regulates TARDBP binding to RNA UG repeats and TARDBP-dependent expression of HDAC6, ATG7 and VCP which are involved in clearance of protein aggregates (PubMed:25678563). Plays an important role in platelet activation and aggregation (By similarity). Regulates calcium mobilization and integrin ITGA2B:ITGB3 bidirectional signaling via increased ROS production as well as by facilitating the interaction between integrin and the cell cytoskeleton (By similarity). Binds heparan sulfate glycosaminoglycans (PubMed:11943775). Inhibits replication of influenza A virus (IAV) (PubMed:19207730). Inhibits ITCH/AIP4-mediated ubiquitination of matrix protein 1 (M1) of IAV by impairing the interaction of ITCH/AIP4 with M1, followed by the suppression of the nuclear export of M1, and finally reduction of the replication of IAV (PubMed:22347431, PubMed:30328013)", "gene_name": "PPIA", "glycan_count": 8, "glycosylation_sites": [ { "position": 108, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P62937", "name": "Cyclophilin A (CypA)", "organism": "Homo sapiens", "uniprot_id": "P62937" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "not assigned (AMDV structural protein)", "name": "VP2", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P20839 (human, inferred)", "name": "Inosine monophosphate dehydrogenase (IMPDH)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P19838 (human, inferred)", "name": "NF-\u03baB", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P00738 (human)", "name": "Haptoglobin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q13753 (human)", "name": "Zonulin (Prehaptoglobin-2)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01584 (human)", "name": "IL-1\u03b2", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P05231 (human)", "name": "IL-6", "organism": "", "uniprot_id": "" }, { "function": "Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal lung alveolar septum formation during embryogenesis, normal development of the gastrointestinal tract, normal development of Leydig cells and spermatogenesis. Required for normal oligodendrocyte development and normal myelination in the spinal cord and cerebellum. Plays an important role in wound healing. Signaling is modulated by the formation of heterodimers with PDGFB (By similarity)", "gene_name": "PDGFA", "glycan_count": 0, "glycosylation_sites": [ { "position": 134, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P04085", "name": "Platelet-derived growth factor-AA (PDGF-AA)", "organism": "Homo sapiens", "uniprot_id": "P04085" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P16070 (human)", "name": "CD44", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P15692 (human)", "name": "VEGFA", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P08254 (human)", "name": "MMP-3", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P14780 (human)", "name": "MMP-9", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P12931 (human)", "name": "c-Src", "organism": "", "uniprot_id": "" }, { "function": "Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl-epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin", "gene_name": "F13A1", "glycan_count": 3, "glycosylation_sites": [ { "position": 614, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P00488", "name": "Factor XIII", "organism": "Homo sapiens", "uniprot_id": "P00488" }, { "function": "Secreted lysophospholipase D that hydrolyzes lysophospholipids to produce the signaling molecule lysophosphatidic acid (LPA) in extracellular fluids (PubMed:12354767, PubMed:14500380, PubMed:15769751, PubMed:26371182, PubMed:27754931). Its major substrate is lysophosphatidylcholine (PubMed:12176993, PubMed:14500380, PubMed:27754931). Can also act on sphingosylphosphorylcholine producing sphingosine-1-phosphate, a modulator of cell motility (PubMed:14500380). Can hydrolyze, in vitro, bis-pNPP, to some extent pNP-TMP, and barely ATP (PubMed:12176993, PubMed:15769751). Involved in several motility-related processes such as angiogenesis and neurite outgrowth. Acts as an angiogenic factor by stimulating migration of smooth muscle cells and microtubule formation (PubMed:11559573). Stimulates migration of melanoma cells, probably via a pertussis toxin-sensitive G protein (PubMed:1733949). May have a role in induction of parturition (PubMed:12176993). Possible involvement in cell proliferation and adipose tissue development (Probable). Required for LPA production in activated platelets, cleaves the sn-1 lysophospholipids to generate sn-1 lysophosphatidic acids containing predominantly 18:2 and 20:4 fatty acids (PubMed:21393252). Shows a preference for the sn-1 to the sn-2 isomer of 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF) (PubMed:21393252)", "gene_name": "ENPP2", "glycan_count": 18, "glycosylation_sites": [ { "position": 54, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 411, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 525, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 807, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13822", "name": "Autotaxin (ATX)", "organism": "Homo sapiens", "uniprot_id": "Q13822" }, { "function": "Receptor for lysophosphatidic acid (LPA) (PubMed:19306925, PubMed:25025571, PubMed:26091040, PubMed:9070858). Plays a role in the reorganization of the actin cytoskeleton, cell migration, differentiation and proliferation, and thereby contributes to the responses to tissue damage and infectious agents. Activates downstream signaling cascades via the G(i)/G(o), G(12)/G(13), and G(q) families of heteromeric G proteins. Signaling inhibits adenylyl cyclase activity and decreases cellular cAMP levels (PubMed:26091040). Signaling triggers an increase of cytoplasmic Ca(2+) levels (PubMed:19656035, PubMed:19733258, PubMed:26091040). Activates RALA; this leads to the activation of phospholipase C (PLC) and the formation of inositol 1,4,5-trisphosphate (PubMed:19306925). Signaling mediates activation of down-stream MAP kinases (By similarity). Contributes to the regulation of cell shape. Promotes Rho-dependent reorganization of the actin cytoskeleton in neuronal cells and neurite retraction (PubMed:26091040). Promotes the activation of Rho and the formation of actin stress fibers (PubMed:26091040). Promotes formation of lamellipodia at the leading edge of migrating cells via activation of RAC1 (By similarity). Through its function as LPA receptor, plays a role in chemotaxis and cell migration, including responses to injury and wounding (PubMed:18066075, PubMed:19656035, PubMed:19733258). Plays a role in triggering inflammation in response to bacterial lipopolysaccharide (LPS) via its interaction with CD14. Promotes cell proliferation in response to LPA (By similarity). Inhibits the intracellular ciliogenesis pathway in response to LPA and through AKT1 activation (PubMed:31204173). Required for normal skeleton development. May play a role in osteoblast differentiation. Required for normal brain development. Required for normal proliferation, survival and maturation of newly formed neurons in the adult dentate gyrus. Plays a role in pain perception and in the initiation of neuropathic pain (By similarity)", "gene_name": "LPAR1", "glycan_count": 1, "glycosylation_sites": [ { "position": 27, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 35, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q92633", "name": "Lysophosphatidic Acid Receptor 1 (LPAR1)", "organism": "Homo sapiens", "uniprot_id": "Q92633" }, { "function": "Receptor for lysophosphatidic acid (LPA), a mediator of diverse cellular activities. May play a role in the development of ovarian cancer. Seems to be coupled to the G(i)/G(o) and G(q) families of heteromeric G proteins", "gene_name": "LPAR3", "glycan_count": 2, "glycosylation_sites": [ { "position": 15, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 172, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UBY5", "name": "Lysophosphatidic Acid Receptor 3 (LPAR3)", "organism": "Homo sapiens", "uniprot_id": "Q9UBY5" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q13464/Q9H2A7", "name": "Rho-associated protein kinase (ROCK1/ROCK2)", "organism": "", "uniprot_id": "" }, { "function": "Thiol protease that acts as a major effector caspase involved in the execution phase of apoptosis (PubMed:18723680, PubMed:20566630, PubMed:23650375, PubMed:35338844, PubMed:35446120, PubMed:7596430). Following cleavage and activation by initiator caspases (CASP8, CASP9 and/or CASP10), mediates execution of apoptosis by catalyzing cleavage of many proteins (PubMed:18723680, PubMed:20566630, PubMed:23650375, PubMed:7596430). At the onset of apoptosis, it proteolytically cleaves poly(ADP-ribose) polymerase PARP1 at a '216-Asp-|-Gly-217' bond (PubMed:10497198, PubMed:16374543, PubMed:7596430, PubMed:7774019). Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain (By similarity). Cleaves and activates caspase-6, -7 and -9 (CASP6, CASP7 and CASP9, respectively) (PubMed:7596430). Cleaves and inactivates interleukin-18 (IL18) (PubMed:37993714, PubMed:9334240). Involved in the cleavage of huntingtin (PubMed:8696339). Triggers cell adhesion in sympathetic neurons through RET cleavage (PubMed:21357690). Cleaves and inhibits serine/threonine-protein kinase AKT1 in response to oxidative stress (PubMed:23152800). Acts as an inhibitor of type I interferon production during virus-induced apoptosis by mediating cleavage of antiviral proteins CGAS, IRF3 and MAVS, thereby preventing cytokine overproduction (PubMed:30878284). Also involved in pyroptosis by mediating cleavage and activation of gasdermin-E (GSDME) (PubMed:35338844, PubMed:35446120). Cleaves XRCC4 and phospholipid scramblase proteins XKR4, XKR8 and XKR9, leading to promote phosphatidylserine exposure on apoptotic cell surface (PubMed:23845944, PubMed:33725486). Cleaves BIRC6 following inhibition of BIRC6-caspase binding by DIABLO/SMAC (PubMed:36758104, PubMed:36758106)", "gene_name": "CASP3", "glycan_count": 1, "glycosylation_sites": [], "id": "P42574", "name": "Caspase-3", "organism": "Homo sapiens", "uniprot_id": "P42574" }, { "function": "Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction (PubMed:19617626, PubMed:21531719, PubMed:2400579). Proteolytically cleaves CTBP1 at 'Asn-375', 'Gly-387' and 'His-409' (PubMed:23707407). Cleaves and activates caspase-7 (CASP7) (PubMed:19617626)", "gene_name": "CAPN1", "glycan_count": 2, "glycosylation_sites": [], "id": "P07384", "name": "Calpain", "organism": "Homo sapiens", "uniprot_id": "P07384" }, { "function": "Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins", "gene_name": "rpn-3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q04908", "name": "Anti-M\u00fcllerian Hormone (AMH)", "organism": "Caenorhabditis elegans", "uniprot_id": "Q04908" }, { "function": "Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix", "gene_name": "SGCA", "glycan_count": 0, "glycosylation_sites": [ { "position": 174, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 246, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q16586", "name": "Alpha-sarcoglycan (SGCA)", "organism": "Homo sapiens", "uniprot_id": "Q16586" }, { "function": "Has acyl-CoA thioesterase activity towards medium and long-chain (C14 to C18) fatty acyl-CoA substrates, and probably plays a role in mitochondrial fatty acid metabolism. Plays a role in the apoptotic process, possibly via its regulation of AKT1 activity. According to PubMed:11598301, inhibits AKT1 phosphorylation and activity. According to PubMed:17615157, enhances AKT1 activity by favoring its phosphorylation and translocation to plasma membrane", "gene_name": "THEM4", "glycan_count": 0, "glycosylation_sites": [], "id": "Q5T1C6", "name": "Cavin-4", "organism": "Homo sapiens", "uniprot_id": "Q5T1C6" }, { "function": "", "gene_name": "MAN2B2", "glycan_count": 28, "glycosylation_sites": [ { "position": 226, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 249, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 294, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 336, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 516, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 608, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 670, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 675, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 748, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 808, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 812, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 890, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y2E5", "name": "GALGT2 (Beta-1,4-N-acetylgalactosaminyltransferase 2)", "organism": "Homo sapiens", "uniprot_id": "Q9Y2E5" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P23229/P05106", "name": "Integrin alphaVbeta6", "organism": "", "uniprot_id": "" }, { "function": "ATP-dependent annealing helicase that binds selectively to fork DNA relative to ssDNA or dsDNA and catalyzes the rewinding of the stably unwound DNA. Rewinds single-stranded DNA bubbles that are stably bound by replication protein A (RPA). Acts throughout the genome to reanneal stably unwound DNA, performing the opposite reaction of many enzymes, such as helicases and polymerases, that unwind DNA. May play an important role in DNA damage response by acting at stalled replication forks", "gene_name": "SMARCAL1", "glycan_count": 3, "glycosylation_sites": [], "id": "Q9NZC9", "name": "SMARCAL1", "organism": "Homo sapiens", "uniprot_id": "Q9NZC9" }, { "function": "Lipoprotein-associated calcium-independent phospholipase A2 involved in phospholipid catabolism during inflammatory and oxidative stress response (PubMed:10066756, PubMed:16371369, PubMed:17090529, PubMed:2040620, PubMed:7700381, PubMed:8624782). At the lipid-aqueous interface, hydrolyzes the ester bond of fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) (PubMed:10504265, PubMed:2040620). Specifically targets phospholipids with a short-chain fatty acyl group at sn-2 position (PubMed:2040620). Can hydrolyze phospholipids with long fatty acyl chains, only if they carry oxidized functional groups (PubMed:2040620, PubMed:8624782). Hydrolyzes and inactivates platelet-activating factor (PAF, 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine), a potent pro-inflammatory signaling lipid that acts through PTAFR on various innate immune cells (PubMed:10066756, PubMed:10504265, PubMed:11590221, PubMed:16371369, PubMed:18434304, PubMed:7592717, PubMed:7700381, PubMed:8624782, PubMed:8675689). Hydrolyzes oxidatively truncated phospholipids carrying an aldehyde group at omega position, preventing their accumulation in low-density lipoprotein (LDL) particles and uncontrolled pro-inflammatory effects (PubMed:2040620, PubMed:7700381). As part of high-density lipoprotein (HDL) particles, can hydrolyze phospholipids having long-chain fatty acyl hydroperoxides at sn-2 position and protect against potential accumulation of these oxylipins in the vascular wall (PubMed:17090529). Catalyzes the release from membrane phospholipids of F2-isoprostanes, lipid biomarkers of cellular oxidative damage (PubMed:16371369)", "gene_name": "PLA2G7", "glycan_count": 0, "glycosylation_sites": [ { "position": 423, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 433, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13093", "name": "PLA2R", "organism": "Homo sapiens", "uniprot_id": "Q13093" }, { "function": "ATP-dependent transporter of the ATP-binding cassette (ABC) family involved in the transport of very long chain fatty acid (VLCFA)-CoA from the cytosol to the peroxisome lumen (PubMed:11248239, PubMed:15682271, PubMed:16946495, PubMed:18757502, PubMed:21145416, PubMed:23671276, PubMed:29397936, PubMed:33500543). Coupled to the ATP-dependent transporter activity also has a fatty acyl-CoA thioesterase activity (ACOT) and hydrolyzes VLCFA-CoA into VLCFA prior their ATP-dependent transport into peroxisomes, the ACOT activity is essential during this transport process (PubMed:29397936, PubMed:33500543). Thus, plays a role in regulation of VLCFAs and energy metabolism namely, in the degradation and biosynthesis of fatty acids by beta-oxidation, mitochondrial function and microsomal fatty acid elongation (PubMed:21145416, PubMed:23671276). Involved in several processes; namely, controls the active myelination phase by negatively regulating the microsomal fatty acid elongation activity and may also play a role in axon and myelin maintenance. Also controls the cellular response to oxidative stress by regulating mitochondrial functions such as mitochondrial oxidative phosphorylation and depolarization. And finally controls the inflammatory response by positively regulating peroxisomal beta-oxidation of VLCFAs (By similarity)", "gene_name": "ABCD1", "glycan_count": 0, "glycosylation_sites": [ { "position": 214, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P33897", "name": "Adrenoleukodystrophy protein (ALDP)", "organism": "Homo sapiens", "uniprot_id": "P33897" }, { "function": "ATP-dependent transporter of the ATP-binding cassette (ABC) family involved in the transport of very long chain fatty acid (VLCFA)-CoA from the cytosol to the peroxisome lumen (PubMed:21145416, PubMed:29397936). Like ABCD1 seems to have fatty acyl-CoA thioesterase (ACOT) and ATPase activities, according to this model, VLCFA-CoA as free VLCFA is transpoted in an ATP-dependent manner into peroxisomes after the hydrolysis of VLCFA-CoA mediated by the ACOT activity of ABCD2 (Probable) (PubMed:29397936). Shows overlapping substrate specificities with ABCD1 toward saturated fatty acids (FA) and monounsaturated FA (MUFA) but has a distinct substrate preference for shorter VLCFA (C22:0) and polyunsaturated fatty acid (PUFA) such as C22:6-CoA and C24:6-CoA (in vitro) (PubMed:21145416). Thus, may play a role in regulation of VLCFAs and energy metabolism namely, in the degradation and biosynthesis of fatty acids by beta-oxidation (PubMed:21145416)", "gene_name": "ABCD2", "glycan_count": 0, "glycosylation_sites": [ { "position": 190, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 227, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UBJ2", "name": "Adrenoleukodystrophy-related protein (ALDR)", "organism": "Homo sapiens", "uniprot_id": "Q9UBJ2" }, { "function": "Broad substrate specificity ATP-dependent transporter of the ATP-binding cassette (ABC) family that catalyzes the transport of long-chain fatty acids (LCFA)-CoA, dicarboxylic acids-CoA, long-branched-chain fatty acids-CoA and bile acids from the cytosol to the peroxisome lumen for beta-oxydation (PubMed:11248239, PubMed:24333844, PubMed:25168382, PubMed:29397936). Has fatty acyl-CoA thioesterase and ATPase activities (PubMed:29397936). Probably hydrolyzes fatty acyl-CoAs into free fatty acids prior to their ATP-dependent transport into peroxisomes (By similarity). Thus, play a role in regulation of LCFAs and energy metabolism namely, in the degradation and biosynthesis of fatty acids by beta-oxidation (PubMed:24333844, PubMed:25944712)", "gene_name": "ABCD3", "glycan_count": 1, "glycosylation_sites": [ { "position": 12, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 106, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 206, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P28288", "name": "PMP70", "organism": "Homo sapiens", "uniprot_id": "P28288" }, { "function": "Ligand for the T-cell-specific cell surface receptor ICOS. Acts as a costimulatory signal for T-cell proliferation and cytokine secretion (PubMed:11007762, PubMed:11023515, PubMed:30498080). Also induces B-cell proliferation and differentiation into plasma cells. Could play an important role in mediating local tissue responses to inflammatory conditions, as well as in modulating the secondary immune response by co-stimulating memory T-cell function (By similarity). In endothelial cells, required for proper neutrophil transmigration in response to chemoattractants, such as CXCL8/IL8 or N-formyl-methionyl peptides (fMLP) (PubMed:30498080)", "gene_name": "ICOSLG", "glycan_count": 12, "glycosylation_sites": [ { "position": 70, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 137, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 173, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 186, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 225, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O75144", "name": "ICOSLG", "organism": "Homo sapiens", "uniprot_id": "O75144" }, { "function": "Catalyzes the citrullination/deimination of arginine residues of proteins such as histones, thereby playing a key role in histone code and regulation of stem cell maintenance (PubMed:15339660, PubMed:15345777, PubMed:16567635, PubMed:21245532). Citrullinates histone H1 at 'Arg-54' (to form H1R54ci), histone H3 at 'Arg-2', 'Arg-8', 'Arg-17' and/or 'Arg-26' (to form H3R2ci, H3R8ci, H3R17ci, H3R26ci, respectively) and histone H4 at 'Arg-3' (to form H4R3ci) (PubMed:15339660, PubMed:15345777, PubMed:16567635, PubMed:21245532). Acts as a key regulator of stem cell maintenance by mediating citrullination of histone H1: citrullination of 'Arg-54' of histone H1 (H1R54ci) results in H1 displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance (PubMed:15339660, PubMed:15345777, PubMed:16567635, PubMed:21245532). Promotes profound chromatin decondensation during the innate immune response to infection in neutrophils by mediating formation of H1R54ci (PubMed:18209087). Required for the formation of neutrophil extracellular traps (NETs); NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (By similarity). Citrullination of histone H3 prevents their methylation by CARM1 and HRMT1L2/PRMT1 and represses transcription (PubMed:15345777). Citrullinates EP300/P300 at 'Arg-2142', which favors its interaction with NCOA2/GRIP1 (PubMed:15731352)", "gene_name": "PADI4", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UM07", "name": "PADI4", "organism": "Homo sapiens", "uniprot_id": "Q9UM07" }, { "function": "Plays a role in the transport of cargos that are too large to fit into COPII-coated vesicles and require specific mechanisms to be incorporated into membrane-bound carriers and exported from the endoplasmic reticulum (PubMed:21525241, PubMed:25202031, PubMed:27138255, PubMed:27170179). Plays a role in the secretion of lipoproteins, pre-chylomicrons and pre-VLDLs, by participating in their export from the endoplasmic reticulum (PubMed:27138255). Thereby, may play a role in cholesterol and triglyceride homeostasis (By similarity). Required for collagen VII (COL7A1) secretion by loading COL7A1 into transport carriers and recruiting PREB/SEC12 at the endoplasmic reticulum exit sites (PubMed:21525241, PubMed:25202031, PubMed:27170179)", "gene_name": "MIA2", "glycan_count": 3, "glycosylation_sites": [ { "position": 59, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 368, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q96PC5", "name": "HAPLN4", "organism": "Homo sapiens", "uniprot_id": "Q96PC5" }, { "function": "Part of the striatin-interacting phosphatase and kinase (STRIPAK) complexes. STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling. Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation", "gene_name": "MOB4", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y3A3", "name": "SUGP1", "organism": "Homo sapiens", "uniprot_id": "Q9Y3A3" }, { "function": "Antigen-presenting protein that binds self and non-self glycolipids and presents them to T-cell receptors on natural killer T-cells", "gene_name": "Cd1d2", "glycan_count": 0, "glycosylation_sites": [ { "position": 25, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 38, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 60, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 128, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 183, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P11610", "name": "CD1", "organism": "Mus musculus", "uniprot_id": "P11610" }, { "function": "Non-inhibitory serpin. Storage protein of egg white", "gene_name": "SERPINB14", "glycan_count": 71, "glycosylation_sites": [ { "position": 293, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01012", "name": "Ovalbumin (egg albumin)", "organism": "Gallus gallus", "uniprot_id": "P01012" }, { "function": "Functions as a ubiquitin ligase protein in vivo, mediating ubiquitination and promoting degradation of MEKK1, suggesting that it may regulate the Notch pathway via some ubiquitin ligase activity (By similarity). Regulator of Notch signaling, a signaling pathway involved in cell-cell communications that regulates a broad spectrum of cell-fate determinations. Mainly acts as a positive regulator of Notch, but it also acts as a negative regulator, depending on the developmental and cell context. Mediates the antineural activity of Notch, possibly by inhibiting the transcriptional activation mediated by MATCH1. Involved in neurogenesis, lymphogenesis and myogenesis, and may also be involved in MZB (Marginal zone B) cell differentiation. Promotes B-cell development at the expense of T-cell development, suggesting that it can antagonize NOTCH1", "gene_name": "DTX1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q86Y01", "name": "BAP-1", "organism": "Homo sapiens", "uniprot_id": "Q86Y01" }, { "function": "Low affinity receptor which can bind to NGF, BDNF, NTF3, and NTF4. Forms a heterodimeric receptor with SORCS2 that binds the precursor forms of NGF, BDNF and NTF3 with high affinity, and has much lower affinity for mature NGF and BDNF (PubMed:24908487). Plays an important role in differentiation and survival of specific neuronal populations during development (By similarity). Can mediate cell survival as well as cell death of neural cells. Plays a role in the inactivation of RHOA (PubMed:26646181). Plays a role in the regulation of the translocation of GLUT4 to the cell surface in adipocytes and skeletal muscle cells in response to insulin, probably by regulating RAB31 activity, and thereby contributes to the regulation of insulin-dependent glucose uptake (By similarity). Necessary for the circadian oscillation of the clock genes BMAL1, PER1, PER2 and NR1D1 in the suprachiasmatic nucleus (SCmgetaN) of the brain and in liver and of the genes involved in glucose and lipid metabolism in the liver (PubMed:23785138). Together with BFAR negatively regulates NF-kappa-B and JNK-related signaling pathways (PubMed:22566094)", "gene_name": "NGFR", "glycan_count": 4, "glycosylation_sites": [ { "position": 60, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08138", "name": "CD271 (NGFR)", "organism": "Homo sapiens", "uniprot_id": "P08138" }, { "function": "Energy-dependent efflux transporter responsible for decreased drug accumulation in multidrug-resistant cells (PubMed:12960149, PubMed:15205344, PubMed:15899824, PubMed:22306008). Specifically present in limbal stem cells, where it plays a key role in corneal development and repair (By similarity)", "gene_name": "ABCB5", "glycan_count": 1, "glycosylation_sites": [ { "position": 17, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 85, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 91, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 371, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 390, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 423, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 789, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 819, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 910, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1188, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q2M3G0", "name": "ABCB5", "organism": "Homo sapiens", "uniprot_id": "Q2M3G0" }, { "function": "Catalyzes preferentially the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the N-acetyl-beta-D-glucosamine (GlcNAc) of an N-acetyllactosamine unit (type 2 chain) of an oligosaccharide, or a glycoprotein- and a glycolipid-linked N-acetyllactosamine unit via an alpha (1,3) linkage and participates in the surface expression of VIM-2, Lewis X/SSEA-1 and sialyl Lewis X antigens (PubMed:14718375, PubMed:1740457, PubMed:17604274, PubMed:29593094, PubMed:7721776, PubMed:9737988, PubMed:9737989). Preferentially transfers fucose to the GlcNAc of an internal N-acetyllactosamine unit of a poly-N-acetyllactosamine chain acceptor substrate (PubMed:17604274, PubMed:7721776). Also catalyzes to a lesser extend the transfer of L-fucose to the GlcNAc of a type 1 (beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl) or H-type 1 (alpha-L-Fuc-(1->2)-beta-D-Gal-(1->3)-D-GlcNAc) chain oligosaccharide via an alpha (1,4) linkage (PubMed:14718375, PubMed:1740457, PubMed:17604274, PubMed:7721776, PubMed:9737988). Preferentially catalyzes sialylated type 2 oligosaccharide acceptors over neutral type 2 or H type 2 (alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-D-GlcNAc) oligosaccharide acceptors (PubMed:1740457, PubMed:9737989). Lactose-based structures are also acceptor substrates (PubMed:1740457, PubMed:7721776)", "gene_name": "FUT5", "glycan_count": 0, "glycosylation_sites": [ { "position": 60, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 105, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 167, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 198, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q11128", "name": "MGAT5", "organism": "Homo sapiens", "uniprot_id": "Q11128" }, { "function": "May function as a growth factor receptor", "gene_name": "Tacstd2", "glycan_count": 0, "glycosylation_sites": [ { "position": 27, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 114, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 162, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 202, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8BGV3", "name": "Trop2", "organism": "Mus musculus", "uniprot_id": "Q8BGV3" }, { "function": "Together with KRT19, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle", "gene_name": "KRT8", "glycan_count": 4, "glycosylation_sites": [], "id": "P05787", "name": "Cytokeratin 8", "organism": "Homo sapiens", "uniprot_id": "P05787" }, { "function": "Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection", "gene_name": "KRT18", "glycan_count": 6, "glycosylation_sites": [ { "position": 30, "type": "O-linked (GlcNAc) serine; alternate" }, { "position": 31, "type": "O-linked (GlcNAc) serine; alternate" }, { "position": 49, "type": "O-linked (GlcNAc) serine; alternate" } ], "id": "P05783", "name": "Cytokeratin 18", "organism": "Homo sapiens", "uniprot_id": "P05783" }, { "function": "Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor", "gene_name": "DBI", "glycan_count": 1, "glycosylation_sites": [], "id": "P07108", "name": "Acyl-CoA Binding Protein (ACBP) / Diazepam-Binding Inhibitor (DBI)", "organism": "Homo sapiens", "uniprot_id": "P07108" }, { "function": "ATP-dependent transporter of the ATP-binding cassette (ABC) family that binds and hydrolyzes ATP to enable active transport of various substrates including many drugs, toxicants and endogenous compound across cell membranes. Transports a wide variety of conjugated organic anions such as sulfate-, glucuronide- and glutathione (GSH)-conjugates of endo- and xenobiotics substrates (PubMed:10220572, PubMed:10421658, PubMed:11500505, PubMed:16332456). Mediates hepatobiliary excretion of mono- and bis-glucuronidated bilirubin molecules and therefore play an important role in bilirubin detoxification (PubMed:10421658). Also mediates hepatobiliary excretion of others glucuronide conjugates such as 17beta-estradiol 17-glucosiduronic acid and leukotriene C4 (PubMed:11500505). Transports sulfated bile salt such as taurolithocholate sulfate (PubMed:16332456). Transports various anticancer drugs, such as anthracycline, vinca alkaloid and methotrexate and HIV-drugs such as protease inhibitors (PubMed:10220572, PubMed:11500505, PubMed:12441801). Confers resistance to several anti-cancer drugs including cisplatin, doxorubicin, epirubicin, methotrexate, etoposide and vincristine (PubMed:10220572, PubMed:11500505)", "gene_name": "ABCC2", "glycan_count": 1, "glycosylation_sites": [ { "position": 7, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 12, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1011, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q92887", "name": "ABCC2 (MRP2)", "organism": "Homo sapiens", "uniprot_id": "Q92887" }, { "function": "ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds, and xenobiotics from cells. Mediates ATP-dependent transport of endogenous metabolites such as cAMP and cGMP, folic acid and N-lactoyl-amino acids (in vitro) (PubMed:10893247, PubMed:12637526, PubMed:12695538, PubMed:15899835, PubMed:17229149, PubMed:25964343). Also acts as a general glutamate conjugate and analog transporter that can limit the brain levels of endogenous metabolites, drugs, and toxins (PubMed:26515061). Confers resistance to the antiviral agent PMEA (PubMed:12695538). Able to transport several anticancer drugs including methotrexate, and nucleotide analogs in vitro, however it does with low affinity, thus the exact role of ABCC5 in mediating resistance still needs to be elucidated (PubMed:10840050, PubMed:12435799, PubMed:12695538, PubMed:15899835). Acts as a heme transporter required for the translocation of cytosolic heme to the secretory pathway (PubMed:24836561). May play a role in energy metabolism by regulating the glucagon-like peptide 1 (GLP-1) secretion from enteroendocrine cells (By similarity)", "gene_name": "ABCC5", "glycan_count": 1, "glycosylation_sites": [ { "position": 494, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 636, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 684, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 890, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 897, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1044, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1329, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1417, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O15440", "name": "ABCC5 (MRP5)", "organism": "Homo sapiens", "uniprot_id": "O15440" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O92782", "name": "HMGCS2", "organism": "Lechiguanas virus", "uniprot_id": "O92782" }, { "function": "E3 ubiquitin-protein ligase that mediates the polyubiquitination of lysine and cysteine residues on target proteins and is thereby implicated in the regulation of various signaling pathways including autophagy, innate immunity or DNA repair (PubMed:20064473, PubMed:31959741, PubMed:33608556). Inhibits TGF-beta signaling by triggering SMAD2 and TGFBR1 ubiquitination and proteasome-dependent degradation (PubMed:15496141). Downregulates autophagy and cell growth by ubiquitinating and reducing cellular ULK1 or ASCT2 levels (PubMed:28820317, PubMed:31959741). Promotes ubiquitination and internalization of various plasma membrane channels such as ENaC, SCN2A/Nav1.2, SCN3A/Nav1.3, SCN5A/Nav1.5, SCN9A/Nav1.7, SCN10A/Nav1.8, KCNA3/Kv1.3, KCNH2, EAAT1, KCNQ2/Kv7.2, KCNQ3/Kv7.3 or CLC5 (PubMed:26363003, PubMed:27445338). Promotes ubiquitination and degradation of SGK1 and TNK2. Ubiquitinates BRAT1 and this ubiquitination is enhanced in the presence of NDFIP1 (PubMed:25631046). Plays a role in dendrite formation by melanocytes (PubMed:23999003). Involved in the regulation of TOR signaling (PubMed:27694961). Ubiquitinates and regulates protein levels of NTRK1 once this one is activated by NGF (PubMed:27445338). Plays a role in antiviral innate immunity by catalyzing 'Lys-29'-linked cysteine ubiquitination of TRAF3, resulting in enhanced 'Lys-48' and 'Lys-63'-linked ubiquitination of TRAF3 (PubMed:33608556). Ubiquitinates TTYH2 and TTYH3 and regulates protein levels of TTYH2 (PubMed:18577513)", "gene_name": "NEDD4L", "glycan_count": 2, "glycosylation_sites": [], "id": "Q96PU5", "name": "NEDD4", "organism": "Homo sapiens", "uniprot_id": "Q96PU5" }, { "function": "Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex. Its ability to bind ubiquitin probably plays a role in endosomal sorting of ubiquitinated cargo proteins by ESCRT complexes. The ESCRT-II complex may also play a role in transcription regulation, possibly via its interaction with ELL. Binds phosphoinosides such as PtdIns(3,4,5)P3", "gene_name": "VPS36", "glycan_count": 0, "glycosylation_sites": [], "id": "Q86VN1", "name": "JAML", "organism": "Homo sapiens", "uniprot_id": "Q86VN1" }, { "function": "RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Preferentially binds to N6-methyladenosine (m6A)-containing mRNAs and increases their stability (PubMed:29476152, PubMed:32245947). Plays a direct role in the transport and translation of transcripts required for axonal regeneration in adult sensory neurons (By similarity). Regulates localized beta-actin/ACTB mRNA translation, a crucial process for cell polarity, cell migration and neurite outgrowth. Co-transcriptionally associates with the ACTB mRNA in the nucleus. This binding involves a conserved 54-nucleotide element in the ACTB mRNA 3'-UTR, known as the 'zipcode'. The RNP thus formed is exported to the cytoplasm, binds to a motor protein and is transported along the cytoskeleton to the cell periphery. During transport, prevents ACTB mRNA from being translated into protein. When the RNP complex reaches its destination near the plasma membrane, IGF2BP1 is phosphorylated. This releases the mRNA, allowing ribosomal 40S and 60S subunits to assemble and initiate ACTB protein synthesis. Monomeric ACTB then assembles into the subcortical actin cytoskeleton (By similarity). During neuronal development, key regulator of neurite outgrowth, growth cone guidance and neuronal cell migration, presumably through the spatiotemporal fine tuning of protein synthesis, such as that of ACTB (By similarity). May regulate mRNA transport to activated synapses (By similarity). Binds to and stabilizes ABCB1/MDR-1 mRNA (By similarity). During interstinal wound repair, interacts with and stabilizes PTGS2 transcript. PTGS2 mRNA stabilization may be crucial for colonic mucosal wound healing (By similarity). Binds to the 3'-UTR of IGF2 mRNA by a mechanism of cooperative and sequential dimerization and regulates IGF2 mRNA subcellular localization and translation. Binds to MYC mRNA, in the coding region instability determinant (CRD) of the open reading frame (ORF), hence preventing MYC cleavage by endonucleases and possibly microRNA targeting to MYC-CRD (PubMed:29476152). Binding to MYC mRNA is enhanced by m6A-modification of the CRD (PubMed:29476152). Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells. Binds to the oncofetal H19 transcript and to the neuron-specific TAU mRNA and regulates their localizations. Binds to and stabilizes BTRC/FBW1A mRNA. Binds to the adenine-rich autoregulatory sequence (ARS) located in PABPC1 mRNA and represses its translation. PABPC1 mRNA-binding is stimulated by PABPC1 protein. Prevents BTRC/FBW1A mRNA degradation by disrupting microRNA-dependent interaction with AGO2. Promotes the directed movement of tumor-derived cells by fine-tuning intracellular signaling networks. Binds to MAPK4 3'-UTR and inhibits its translation. Interacts with PTEN transcript open reading frame (ORF) and prevents mRNA decay. This combined action on MAPK4 (down-regulation) and PTEN (up-regulation) antagonizes HSPB1 phosphorylation, consequently it prevents G-actin sequestration by phosphorylated HSPB1, allowing F-actin polymerization. Hence enhances the velocity of cell migration and stimulates directed cell migration by PTEN-modulated polarization. Interacts with Hepatitis C virus (HCV) 5'-UTR and 3'-UTR and specifically enhances translation at the HCV IRES, but not 5'-cap-dependent translation, possibly by recruiting eIF3. Interacts with HIV-1 GAG protein and blocks the formation of infectious HIV-1 particles. Reduces HIV-1 assembly by inhibiting viral RNA packaging, as well as assembly and processing of GAG protein on cellular membranes. During cellular stress, such as oxidative stress or heat shock, stabilizes target mRNAs that are recruited to stress granules, including CD44, IGF2, MAPK4, MYC, PTEN, RAPGEF2 and RPS6KA5 transcripts", "gene_name": "IGF2BP1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9NZI8", "name": "IGF2BP3", "organism": "Homo sapiens", "uniprot_id": "Q9NZI8" }, { "function": "Plays a role in tyrosine phosphorylation of CBL by linking CBL to the insulin receptor. Required for insulin-stimulated glucose transport. Involved in formation of actin stress fibers and focal adhesions (By similarity)", "gene_name": "SORBS1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9BX66", "name": "SORBS3", "organism": "Homo sapiens", "uniprot_id": "Q9BX66" }, { "function": "Part of the TCR-CD3 complex present on T-lymphocyte cell surface that plays an essential role in adaptive immune response. When antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transmitted across the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3 chains contain immunoreceptor tyrosine-based activation motifs (ITAMs) in their cytoplasmic domain. Upon TCR engagement, these motifs become phosphorylated by Src family protein tyrosine kinases LCK and FYN, resulting in the activation of downstream signaling pathways. In addition of this role of signal transduction in T-cell activation, CD3E plays an essential role in correct T-cell development (PubMed:19956738, PubMed:24899501). Also participates in internalization and cell surface down-regulation of TCR-CD3 complexes via endocytosis sequences present in CD3E cytosolic region. In addition to its role as a TCR coreceptor, it serves as a receptor for ITPRIPL1. Ligand recognition inhibits T-cell activation by promoting interaction with NCK1, which prevents CD3E-ZAP70 interaction and blocks the ERK-NFkB signaling cascade and calcium influx (By similarity)", "gene_name": "Cd3e", "glycan_count": 0, "glycosylation_sites": [], "id": "P22646", "name": "CD3", "organism": "Mus musculus", "uniprot_id": "P22646" }, { "function": "Transcriptional repressor mainly required for germinal center (GC) formation and antibody affinity maturation which has different mechanisms of action specific to the lineage and biological functions. Forms complexes with different corepressors and histone deacetylases to repress the transcriptional expression of different subsets of target genes. Represses its target genes by binding directly to the DNA sequence 5'-TTCCTAGAA-3' (BCL6-binding site) or indirectly by repressing the transcriptional activity of transcription factors. In GC B-cells, represses genes that function in differentiation, inflammation, apoptosis and cell cycle control, also autoregulates its transcriptional expression and up-regulates, indirectly, the expression of some genes important for GC reactions, such as AICDA, through the repression of microRNAs expression, like miR155. An important function is to allow GC B-cells to proliferate very rapidly in response to T-cell dependent antigens and tolerate the physiological DNA breaks required for immunglobulin class switch recombination and somatic hypermutation without inducing a p53/TP53-dependent apoptotic response. In follicular helper CD4(+) T-cells (T(FH) cells), promotes the expression of T(FH)-related genes but inhibits the differentiation of T(H)1, T(H)2 and T(H)17 cells. Also required for the establishment and maintenance of immunological memory for both T- and B-cells. Suppresses macrophage proliferation through competition with STAT5 for STAT-binding motifs binding on certain target genes, such as CCL2 and CCND2. In response to genotoxic stress, controls cell cycle arrest in GC B-cells in both p53/TP53-dependedent and -independent manners. Besides, also controls neurogenesis through the alteration of the composition of NOTCH-dependent transcriptional complexes at selective NOTCH targets, such as HES5, including the recruitment of the deacetylase SIRT1 and resulting in an epigenetic silencing leading to neuronal differentiation", "gene_name": "BCL6", "glycan_count": 0, "glycosylation_sites": [], "id": "P41182", "name": "BCL6", "organism": "Homo sapiens", "uniprot_id": "P41182" }, { "function": "Mediates sodium- and chloride-dependent transport of gamma-aminobutyric acid (GABA) (PubMed:17502375, PubMed:22932902). Mediates transport of beta-alanine (PubMed:17502375). Can also mediate transport of taurine and hypotaurine (By similarity)", "gene_name": "SLC6A13", "glycan_count": 0, "glycosylation_sites": [ { "position": 173, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 269, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NSD5", "name": "CA 19-9", "organism": "Homo sapiens", "uniprot_id": "Q9NSD5" }, { "function": "May play a role in vesicle-mediated protein trafficking to lysosomal compartments and in membrane docking/fusion reactions of late endosomes/lysosomes. Required for proper trafficking and targeting of the collagen-modifying enzyme lysyl hydroxylase 3 (LH3) to intracellular collagen (PubMed:28017832). Mediates phagolysosomal fusion in macrophages (PubMed:18474358). Proposed to be involved in endosomal maturation implicating VIPAS39. In epithelial cells, the VPS33B:VIPAS39 complex may play a role in the apical recycling pathway and in the maintenance of the apical-basolateral polarity (PubMed:20190753). Seems to be involved in the sorting of specific cargos from the trans-Golgi network to alpha-granule-destined multivesicular bodies (MVBs) promoting MVBs maturation in megakaryocytes (By similarity)", "gene_name": "VPS33B", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H267", "name": "VPS33B", "organism": "Homo sapiens", "uniprot_id": "Q9H267" }, { "function": "Catalyzes the transport of triglyceride, cholesteryl ester, and phospholipid between phospholipid surfaces (PubMed:15897609, PubMed:16478722, PubMed:22236406, PubMed:23475612, PubMed:25108285, PubMed:26224785, PubMed:8876250, PubMed:8939939). Required for the assembly and secretion of plasma lipoproteins that contain apolipoprotein B (PubMed:16478722, PubMed:23475612, PubMed:26224785, PubMed:8876250, PubMed:8939939). May be involved in regulating cholesteryl ester biosynthesis in cells that produce lipoproteins (By similarity)", "gene_name": "MTTP", "glycan_count": 1, "glycosylation_sites": [], "id": "P55157", "name": "MTTP", "organism": "Homo sapiens", "uniprot_id": "P55157" }, { "function": "Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6-glucosidase in glycogen degradation", "gene_name": "AGL", "glycan_count": 1, "glycosylation_sites": [], "id": "P35573", "name": "AGL", "organism": "Homo sapiens", "uniprot_id": "P35573" }, { "function": "", "gene_name": "C22orf23", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9BZE7", "name": "FOCAD", "organism": "Homo sapiens", "uniprot_id": "Q9BZE7" }, { "function": "Broad range protease inhibitor", "gene_name": "WFDC2", "glycan_count": 89, "glycosylation_sites": [ { "position": 44, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q14508", "name": "HE4 (WFDC2)", "organism": "Homo sapiens", "uniprot_id": "Q14508" }, { "function": "Gel-forming glycoprotein of gastric and respiratory tract epithelia that protects the mucosa from infection and chemical damage by binding to inhaled microorganisms and particles that are subsequently removed by the mucociliary system (PubMed:14535999, PubMed:14718370). Interacts with H.pylori in the gastric epithelium, Barrett's esophagus as well as in gastric metaplasia of the duodenum (GMD) (PubMed:14535999)", "gene_name": "MUC5AC", "glycan_count": 24, "glycosylation_sites": [ { "position": 205, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 258, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 415, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 524, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1308, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1389, "type": "C-linked (Man) tryptophan" }, { "position": 1584, "type": "C-linked (Man) tryptophan" }, { "position": 1749, "type": "C-linked (Man) tryptophan" }, { "position": 1957, "type": "C-linked (Man) tryptophan" }, { "position": 2122, "type": "C-linked (Man) tryptophan" }, { "position": 2395, "type": "O-linked (GalNAc) threonine" }, { "position": 2405, "type": "O-linked (GalNAc) threonine" }, { "position": 2451, "type": "O-linked (GalNAc) threonine" }, { "position": 2461, "type": "O-linked (GalNAc) threonine" }, { "position": 2531, "type": "O-linked (GalNAc) threonine" }, { "position": 2541, "type": "O-linked (GalNAc) threonine" }, { "position": 2571, "type": "O-linked (GalNAc) threonine" }, { "position": 2581, "type": "O-linked (GalNAc) threonine" }, { "position": 2699, "type": "O-linked (GalNAc) threonine" }, { "position": 2709, "type": "O-linked (GalNAc) threonine" }, { "position": 2883, "type": "O-linked (GalNAc) threonine" }, { "position": 2893, "type": "O-linked (GalNAc) threonine" }, { "position": 2979, "type": "O-linked (GalNAc) threonine" }, { "position": 2989, "type": "O-linked (GalNAc) threonine" }, { "position": 3067, "type": "O-linked (GalNAc) threonine" }, { "position": 3077, "type": "O-linked (GalNAc) threonine" }, { "position": 3228, "type": "C-linked (Man) tryptophan" }, { "position": 3526, "type": "C-linked (Man) tryptophan" }, { "position": 3774, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3959, "type": "C-linked (Man) tryptophan" }, { "position": 4224, "type": "O-linked (GalNAc) threonine" }, { "position": 4234, "type": "O-linked (GalNAc) threonine" }, { "position": 4296, "type": "O-linked (GalNAc) threonine" }, { "position": 4306, "type": "O-linked (GalNAc) threonine" }, { "position": 4320, "type": "O-linked (GalNAc) threonine" }, { "position": 4330, "type": "O-linked (GalNAc) threonine" }, { "position": 4376, "type": "O-linked (GalNAc) threonine" }, { "position": 4386, "type": "O-linked (GalNAc) threonine" }, { "position": 4440, "type": "O-linked (GalNAc) threonine" }, { "position": 4450, "type": "O-linked (GalNAc) threonine" }, { "position": 4480, "type": "O-linked (GalNAc) threonine" }, { "position": 4490, "type": "O-linked (GalNAc) threonine" }, { "position": 4512, "type": "O-linked (GalNAc) threonine" }, { "position": 4522, "type": "O-linked (GalNAc) threonine" }, { "position": 4568, "type": "O-linked (GalNAc) threonine" }, { "position": 4578, "type": "O-linked (GalNAc) threonine" }, { "position": 4633, "type": "C-linked (Man) tryptophan" }, { "position": 4869, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4942, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5057, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5093, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5236, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5347, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5377, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5386, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5455, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5528, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 5591, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P98088", "name": "MUC5AC", "organism": "Homo sapiens", "uniprot_id": "P98088" }, { "function": "Carrier protein. Binds to some hydrophobic molecules and promotes their transfer between the different cellular sites. Binds with high affinity to alpha-tocopherol. Also binds with a weaker affinity to other tocopherols and to tocotrienols. May have a transcriptional activatory activity via its association with alpha-tocopherol. Probably recognizes and binds some squalene structure, suggesting that it may regulate cholesterol biosynthesis by increasing the transfer of squalene to a metabolic active pool in the cell", "gene_name": "SEC14L2", "glycan_count": 1, "glycosylation_sites": [], "id": "O76054", "name": "ATP8B1", "organism": "Homo sapiens", "uniprot_id": "O76054" }, { "function": "Cell surface proteoglycan (PubMed:14610063). Negatively regulates the hedgehog signaling pathway when attached via the GPI-anchor to the cell surface by competing with the hedgehog receptor PTC1 for binding to hedgehog proteins (By similarity). Binding to the hedgehog protein SHH triggers internalization of the complex by endocytosis and its subsequent lysosomal degradation (By similarity). Positively regulates the canonical Wnt signaling pathway by binding to the Wnt receptor Frizzled and stimulating the binding of the Frizzled receptor to Wnt ligands (PubMed:16227623, PubMed:24496449). Positively regulates the non-canonical Wnt signaling pathway (By similarity). Binds to CD81 which decreases the availability of free CD81 for binding to the transcriptional repressor HHEX, resulting in nuclear translocation of HHEX and transcriptional repression (By similarity). Inhibits the dipeptidyl peptidase activity of DPP4 (PubMed:17549790). Plays a role in limb patterning and skeletal development by controlling the cellular response to BMP4 (By similarity). Modulates the effects of growth factors BMP2, BMP7 and FGF7 on renal branching morphogenesis (By similarity). Required for coronary vascular development (By similarity). Plays a role in regulating cell movements during gastrulation (By similarity)", "gene_name": "GPC3", "glycan_count": 12, "glycosylation_sites": [ { "position": 124, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 241, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 418, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 495, "type": "O-linked (Xyl...) (glycosaminoglycan) serine" }, { "position": 509, "type": "O-linked (Xyl...) (glycosaminoglycan) serine" } ], "id": "P51654", "name": "Glypican-3", "organism": "Homo sapiens", "uniprot_id": "P51654" }, { "function": "Transcriptional regulator that acts as a repressor or activator, depending on the context. Binds to NF-E2 DNA binding sites. Plays important roles in coordinating transcription activation and repression by MAFK (By similarity). Together with MAF, represses the transcription of genes under the control of the NFE2L2 oxidative stress pathway (PubMed:24035498)", "gene_name": "BACH1", "glycan_count": 0, "glycosylation_sites": [], "id": "O14867", "name": "BACH1", "organism": "Homo sapiens", "uniprot_id": "O14867" }, { "function": "Receptor for bile acid. Bile acid-binding induces its internalization, activation of extracellular signal-regulated kinase and intracellular cAMP production. May be involved in the suppression of macrophage functions by bile acids", "gene_name": "GPBAR1", "glycan_count": 0, "glycosylation_sites": [ { "position": 4, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 76, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8TDU6", "name": "TGR5 (GPBAR1)", "organism": "Homo sapiens", "uniprot_id": "Q8TDU6" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P26039 (ITGA7)", "name": "\u03b17\u03b21 integrin", "organism": "", "uniprot_id": "" }, { "function": "High molecular weight cytoskeletal protein concentrated at regions of cell-matrix and cell-cell contacts. Involved in connections of major cytoskeletal structures to the plasma membrane. With KANK1 co-organize the assembly of cortical microtubule stabilizing complexes (CMSCs) positioned to control microtubule-actin crosstalk at focal adhesions (FAs) rims", "gene_name": "Tln1", "glycan_count": 1, "glycosylation_sites": [], "id": "P26039", "name": "integrin \u03b17", "organism": "Mus musculus", "uniprot_id": "P26039" }, { "function": "Ghrelin is the ligand for growth hormone secretagogue receptor type 1 (GHSR) (PubMed:10604470). Induces the release of growth hormone from the pituitary (PubMed:10604470). Has an appetite-stimulating effect, induces adiposity and stimulates gastric acid secretion. Involved in growth regulation", "gene_name": "GHRL", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UBU3", "name": "Ghrelin", "organism": "Homo sapiens", "uniprot_id": "Q9UBU3" }, { "function": "Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of non-reducing N-acetylglucosamine (GlcNAc) residues. Preferentially acts on mannose-linked GlcNAc. Also able to catalyze the transfer of sulfate to position 6 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Also acts on core 2 mucin-type oligosaccharide and N-acetyllactosamine oligomer with a lower efficiency. Has weak or no activity toward keratan sulfate and oligosaccharides containing the Galbeta1-4GlcNAc. Catalyzes 6-O-sulfation of beta-benzyl GlcNAc but not alpha- or beta-benzyl GalNAc", "gene_name": "CHST7", "glycan_count": 4, "glycosylation_sites": [ { "position": 88, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 186, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 407, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NS84", "name": "\u03b2-1,3-galactosyltransferase 5 (B3GALT5)", "organism": "Homo sapiens", "uniprot_id": "Q9NS84" }, { "function": "Produced by activated monocytes and neutrophils and expressed at sites of inflammation. Hematoregulatory chemokine, which, in vitro, suppresses hematopoietic progenitor cell proliferation. GRO-beta(5-73) shows a highly enhanced hematopoietic activity", "gene_name": "CXCL2", "glycan_count": 0, "glycosylation_sites": [], "id": "P19875", "name": "CXCL2", "organism": "Homo sapiens", "uniprot_id": "P19875" }, { "function": "Mediates the import of long-chain fatty acids (LCFA) into the cell by facilitating their transport at the plasma membrane (PubMed:12556534, PubMed:20530735, PubMed:21395585, PubMed:28178239). Also functions as an acyl-CoA ligase catalyzing the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates, which prevents fatty acid efflux from cells and might drive more fatty acid uptake. May act directly as a bona fide transporter, or alternatively, in a cytoplasmic or membrane-associated multimeric protein complex to trap and draw fatty acids towards accumulation. Plays a pivotal role in regulating available LCFA substrates from exogenous sources in tissues undergoing high levels of beta-oxidation or triglyceride synthesis. May be involved in regulation of cholesterol metabolism (By similarity). Probably involved in fatty acid transport across the blood barrier (PubMed:21395585)", "gene_name": "SLC27A1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6PCB7", "name": "SLC27A4 (FATP4)", "organism": "Homo sapiens", "uniprot_id": "Q6PCB7" }, { "function": "Nuclear receptor that binds and is activated by variety of endogenous and xenobiotic compounds. Transcription factor that activates the transcription of multiple genes involved in the metabolism and secretion of potentially harmful xenobiotics, drugs and endogenous compounds. Activated by the antibiotic rifampicin and various plant metabolites, such as hyperforin, guggulipid, colupulone, and isoflavones. Response to specific ligands is species-specific. Activated by naturally occurring steroids, such as pregnenolone and progesterone. Binds to a response element in the promoters of the CYP3A4 and ABCB1/MDR1 genes", "gene_name": "NR1I2", "glycan_count": 0, "glycosylation_sites": [], "id": "O75469", "name": "PXR (NR1I2)", "organism": "Homo sapiens", "uniprot_id": "O75469" }, { "function": "Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin (PubMed:26599395). Required for normal proliferation and recruitment of pericytes and vascular smooth muscle cells in the central nervous system, skin, lung, heart and placenta. Required for normal blood vessel development, and for normal development of kidney glomeruli. Plays an important role in wound healing. Signaling is modulated by the formation of heterodimers with PDGFA (By similarity)", "gene_name": "PDGFB", "glycan_count": 6, "glycosylation_sites": [ { "position": 63, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01127", "name": "Platelet-Derived Growth Factor Beta (PDGF-\u03b2)", "organism": "Homo sapiens", "uniprot_id": "P01127" }, { "function": "Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays essential roles in the regulation of multiple cellular processes linked to cytoskeletal proteins, such as cell adhesion, motility, migration and cell cycle, functions in neuron growth and ion channel regulation, and is involved in immune response, cancer cell invasion and regulation of apoptosis. Mediates cell adhesion to the extracellular matrix via integrin-dependent signaling, by mediating angiotensin-2-induced activation of integrin beta-1 (ITGB1) in cardiac fibroblasts. Phosphorylates MARCKS, which phosphorylates and activates PTK2/FAK, leading to the spread of cardiomyocytes. Involved in the control of the directional transport of ITGB1 in mesenchymal cells by phosphorylating vimentin (VIM), an intermediate filament (IF) protein. In epithelial cells, associates with and phosphorylates keratin-8 (KRT8), which induces targeting of desmoplakin at desmosomes and regulates cell-cell contact. Phosphorylates IQGAP1, which binds to CDC42, mediating epithelial cell-cell detachment prior to migration. During cytokinesis, forms a complex with YWHAB, which is crucial for daughter cell separation, and facilitates abscission by a mechanism which may implicate the regulation of RHOA. In cardiac myocytes, regulates myofilament function and excitation coupling at the Z-lines, where it is indirectly associated with F-actin via interaction with COPB1. During endothelin-induced cardiomyocyte hypertrophy, mediates activation of PTK2/FAK, which is critical for cardiomyocyte survival and regulation of sarcomere length. Plays a role in the pathogenesis of dilated cardiomyopathy via persistent phosphorylation of troponin I (TNNI3). Involved in nerve growth factor (NFG)-induced neurite outgrowth and neuron morphological change independently of its kinase activity, by inhibition of RHOA pathway, activation of CDC42 and cytoskeletal rearrangement. May be involved in presynaptic facilitation by mediating phorbol ester-induced synaptic potentiation. Phosphorylates gamma-aminobutyric acid receptor subunit gamma-2 (GABRG2), which reduces the response of GABA receptors to ethanol and benzodiazepines and may mediate acute tolerance to the intoxicating effects of ethanol. Upon PMA treatment, phosphorylates the capsaicin- and heat-activated cation channel TRPV1, which is required for bradykinin-induced sensitization of the heat response in nociceptive neurons. Is able to form a complex with PDLIM5 and N-type calcium channel, and may enhance channel activities and potentiates fast synaptic transmission by phosphorylating the pore-forming alpha subunit CACNA1B (CaV2.2). Downstream of TLR4, plays an important role in the lipopolysaccharide (LPS)-induced immune response by phosphorylating and activating TICAM2/TRAM, which in turn activates the transcription factor IRF3 and subsequent cytokines production. In differentiating erythroid progenitors, is regulated by EPO and controls the protection against the TNFSF10/TRAIL-mediated apoptosis, via BCL2. May be involved in the regulation of the insulin-induced phosphorylation and activation of AKT1. Phosphorylates NLRP5/MATER and may thereby modulate AKT pathway activation in cumulus cells (By similarity). Phosphorylates and activates LRRK1, which phosphorylates RAB proteins involved in intracellular trafficking (By similarity)", "gene_name": "Prkce", "glycan_count": 1, "glycosylation_sites": [], "id": "P16054", "name": "PDGF Receptor Beta (PDGF-R\u03b2)", "organism": "Mus musculus", "uniprot_id": "P16054" }, { "function": "Has an actin-binding and actin-bundling activity. Can induce the formation of F-actin networks in an isoform-specific manner (PubMed:23225103, PubMed:24005909). At the sarcomeric Z lines is proposed to act as adapter protein that links nascent myofibers to the sarcolemma via ZYX and may play a role in early assembly and stabilization of the Z lines. Involved in autophagosome formation. May play a role in chaperone-assisted selective autophagy (CASA) involved in Z lines maintenance in striated muscle under mechanical tension; may link the client-processing CASA chaperone machinery to a membrane-tethering and fusion complex providing autophagosome membranes (By similarity). Involved in regulation of cell migration (PubMed:22915763, PubMed:25883213). May be a tumor suppressor (PubMed:16885336)", "gene_name": "SYNPO2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UMS6", "name": "Synaptopodin", "organism": "Homo sapiens", "uniprot_id": "Q9UMS6" }, { "function": "Enzyme with a broad specificity. Negatively regulates TGF-beta signaling through dephosphorylating SMAD2 and SMAD3, resulting in their dissociation from SMAD4, nuclear export of the SMADs and termination of the TGF-beta-mediated signaling. Dephosphorylates PRKAA1 and PRKAA2. Plays an important role in the termination of TNF-alpha-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB", "gene_name": "PPM1A", "glycan_count": 3, "glycosylation_sites": [], "id": "P35813", "name": "gp210", "organism": "Homo sapiens", "uniprot_id": "P35813" }, { "function": "Electroneutral sodium- and bicarbonate-dependent cotransporter with a Na(+):HCO3(-) 1:1 stoichiometry (PubMed:10347222, PubMed:12403779, PubMed:14578046, PubMed:14736710). Mediates the sodium-dependent bicarbonate transport important for pH recovery after acid load as well as for regulation of steady-state pH in the duodenum and vascular smooth muscle cells (By similarity). Plays a key role in macrophage acidification, mediating bicarbonate import into the cytoplasm which is crucial for net acid extrusion and maintenance of cytoplasmic pH during phagocytosis (PubMed:29779931). Provides cellular bicarbonate for de novo purine and pyrimidine synthesis and is a key mediator of de novo nucleotide synthesis downstream of mTORC1 signaling in proliferating cells (PubMed:35772404)", "gene_name": "SLC4A7", "glycan_count": 11, "glycosylation_sites": [ { "position": 171, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 269, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 398, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 406, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 776, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 786, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 791, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y6M7", "name": "AE2 (SLC4A2)", "organism": "Homo sapiens", "uniprot_id": "Q9Y6M7" }, { "function": "As part of the pyruvate dehydrogenase complex, catalyzes the transfers of an acetyl group to a lipoic acid moiety (Probable). The pyruvate dehydrogenase complex, catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links cytoplasmic glycolysis and the mitochondrial tricarboxylic acid (TCA) cycle (Probable)", "gene_name": "DLAT", "glycan_count": 1, "glycosylation_sites": [], "id": "P10515", "name": "PDC-E2", "organism": "Homo sapiens", "uniprot_id": "P10515" }, { "function": "Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a negative regulator of Wnt signaling pathway and ER-Golgi transport (PubMed:22358839, PubMed:27565346). The BCR(KLHL12) complex is involved in ER-Golgi transport by regulating the size of COPII coats, thereby playing a key role in collagen export, which is required for embryonic stem (ES) cells division: BCR(KLHL12) acts by mediating monoubiquitination of SEC31 (SEC31A or SEC31B) (PubMed:22358839, PubMed:27565346). The BCR(KLHL12) complex is also involved in neural crest specification: in response to cytosolic calcium increase, interacts with the heterodimer formed with PEF1 and PDCD6/ALG-2, leading to bridge together the BCR(KLHL12) complex and SEC31 (SEC31A or SEC31B), promoting monoubiquitination of SEC31 and subsequent collagen export (PubMed:27716508). As part of the BCR(KLHL12) complex, also acts as a negative regulator of the Wnt signaling pathway by mediating ubiquitination and subsequent proteolysis of DVL3 (PubMed:16547521). The BCR(KLHL12) complex also mediates polyubiquitination of DRD4 and PEF1, without leading to degradation of these proteins (PubMed:18303015, PubMed:20100572, PubMed:27716508)", "gene_name": "KLHL12", "glycan_count": 0, "glycosylation_sites": [], "id": "Q53G59", "name": "KLHL12", "organism": "Homo sapiens", "uniprot_id": "Q53G59" }, { "function": "Catalyzes the phosphorylation of various hexoses, such as D-glucose, D-glucosamine, D-fructose, D-mannose and 2-deoxy-D-glucose, to hexose 6-phosphate (D-glucose 6-phosphate, D-glucosamine 6-phosphate, D-fructose 6-phosphate, D-mannose 6-phosphate and 2-deoxy-D-glucose 6-phosphate, respectively) (PubMed:1637300, PubMed:25316723, PubMed:27374331). Does not phosphorylate N-acetyl-D-glucosamine (PubMed:27374331). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate (By similarity). Involved in innate immunity and inflammation by acting as a pattern recognition receptor for bacterial peptidoglycan (PubMed:27374331). When released in the cytosol, N-acetyl-D-glucosamine component of bacterial peptidoglycan inhibits the hexokinase activity of HK1 and causes its dissociation from mitochondrial outer membrane, thereby activating the NLRP3 inflammasome (PubMed:27374331)", "gene_name": "HK1", "glycan_count": 2, "glycosylation_sites": [], "id": "P19367", "name": "Hexokinase 1 (HK-1)", "organism": "Homo sapiens", "uniprot_id": "P19367" }, { "function": "G protein-coupled receptor activated by secretin (SCT), which is involved in different processes such as regulation of the pH of the duodenal content, food intake and water homeostasis (PubMed:25332973, PubMed:32811827, PubMed:33008599, PubMed:7612008). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and activates cAMP-dependent pathway (PubMed:32811827, PubMed:33008599). Upon binding to secretin, regulates the pH of the duodenum by (1) inhibiting the secretion of gastric acid from the parietal cells of the stomach and (2) stimulating the production of bicarbonate (NaHCO(3)) from the ductal cells of the pancreas (By similarity). In addition to regulating the pH of the duodenal content, plays a central role in diet induced thermogenesis: acts as a non-sympathetic brown fat (BAT) activator mediating prandial thermogenesis, which consequentially induces satiation. Mechanistically, secretin released by the gut after a meal binds to secretin receptor (SCTR) in brown adipocytes, activating brown fat thermogenesis by stimulating lipolysis, which is sensed in the brain and promotes satiation. Also able to stimulate lipolysis in white adipocytes. Also plays an important role in cellular osmoregulation by regulating renal water reabsorption. Also plays a role in the central nervous system: required for synaptic plasticity (By similarity)", "gene_name": "SCTR", "glycan_count": 0, "glycosylation_sites": [ { "position": 72, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 100, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 106, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 128, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 291, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P47872", "name": "Secretin receptor", "organism": "Homo sapiens", "uniprot_id": "P47872" }, { "function": "Ligand of the EGF receptor/EGFR. Autocrine growth factor as well as a mitogen for a broad range of target cells including astrocytes, Schwann cells and fibroblasts", "gene_name": "AREG", "glycan_count": 3, "glycosylation_sites": [ { "position": 30, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 113, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 119, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P15514", "name": "Amphiregulin (AREG)", "organism": "Homo sapiens", "uniprot_id": "P15514" }, { "function": "Transmembrane metalloprotease which mediates the ectodomain shedding of a myriad of transmembrane proteins including adhesion proteins, growth factor precursors and cytokines important for inflammation and immunity (PubMed:24226769, PubMed:24227843, PubMed:28060820, PubMed:28923481). Cleaves the membrane-bound precursor of TNF-alpha to its mature soluble form (PubMed:36078095, PubMed:9034191). Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface (PubMed:20592283). Responsible for the proteolytic release of several other cell-surface proteins, including p75 TNF-receptor, interleukin 1 receptor type II, p55 TNF-receptor, transforming growth factor-alpha, L-selectin, growth hormone receptor, MUC1 and the amyloid precursor protein (PubMed:12441351). Acts as an activator of Notch pathway by mediating cleavage of Notch, generating the membrane-associated intermediate fragment called Notch extracellular truncation (NEXT) (PubMed:24226769). Plays a role in the proteolytic processing of ACE2 (PubMed:24227843). Plays a role in hemostasis through shedding of GP1BA, the platelet glycoprotein Ib alpha chain (By similarity). Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3 (By similarity). Mediates the proteolytic cleavage of IL6R, leading to the release of secreted form of IL6R (PubMed:26876177, PubMed:28060820). Mediates the proteolytic cleavage and shedding of FCGR3A upon NK cell stimulation, a mechanism that allows for increased NK cell motility and detachment from opsonized target cells. Cleaves TREM2, resulting in shedding of the TREM2 ectodomain (PubMed:28923481)", "gene_name": "ADAM17", "glycan_count": 58, "glycosylation_sites": [ { "position": 103, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 157, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 174, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 264, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 452, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 498, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 539, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 551, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 594, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P78536", "name": "ADAM17 (TACE)", "organism": "Homo sapiens", "uniprot_id": "P78536" }, { "function": "Stimulates the release of gastrin and other gastrointestinal hormones (By similarity). Contributes to the perception of prurient stimuli and to the transmission of itch signals in the spinal cord that promote scratching behavior (By similarity). Contributes primarily to nonhistaminergic itch sensation (By similarity). In one study, shown to act in the amygdala as part of an inhibitory network which inhibits memory specifically related to learned fear (By similarity). In another study, shown to act on vasoactive intestinal peptide (VIP)-expressing cells in the auditory cortex, most likely via extrasynaptic diffusion from local and long-range sources, to mediate disinhibition of glutamatergic cells via VIP cell-specific GRPR signaling which leads to enhanced auditory fear memories (By similarity). Contributes to the regulation of food intake (By similarity). Inhibits voltage-gated sodium channels but enhances voltage-gated potassium channels in hippocampal neurons (By similarity). Induces sighing by acting directly on the pre-Botzinger complex, a cluster of several thousand neurons in the ventrolateral medulla responsible for inspiration during respiratory activity (By similarity)", "gene_name": "GRP", "glycan_count": 1, "glycosylation_sites": [], "id": "P07492", "name": "Pro-gastrin-releasing peptide", "organism": "Homo sapiens", "uniprot_id": "P07492" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P05023 (ATP1A1)", "name": "Na+/K+ ATPase", "organism": "", "uniprot_id": "" }, { "function": "Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phospholipids, in particular phosphatidylcholines (PC), from the outer to the inner leaflet of the plasma membrane (PubMed:17948906, PubMed:25315773). May participate in the establishment of the canalicular membrane integrity by ensuring asymmetric distribution of phospholipids in the canicular membrane (By similarity). Thus may have a role in the regulation of bile acids transport into the canaliculus, uptake of bile acids from intestinal contents into intestinal mucosa or both and protect hepatocytes from bile salts (By similarity). Involved in the microvillus formation in polarized epithelial cells; the function seems to be independent from its flippase activity (PubMed:20512993). Participates in correct apical membrane localization of CDC42, CFTR and SLC10A2 (PubMed:25239307, PubMed:27301931). Enables CDC42 clustering at the apical membrane during enterocyte polarization through the interaction between CDC42 polybasic region and negatively charged membrane lipids provided by ATP8B1 (By similarity). Together with TMEM30A is involved in uptake of the synthetic drug alkylphospholipid perifosine (PubMed:20510206). Required for the preservation of cochlear hair cells in the inner ear (By similarity). May act as cardiolipin transporter during inflammatory injury (By similarity)", "gene_name": "ATP8B1", "glycan_count": 0, "glycosylation_sites": [], "id": "O43520", "name": "ATP8B1", "organism": "Homo sapiens", "uniprot_id": "O43520" }, { "function": "E3 ligase that plays an essential role in the differentiation and survival of terminal erythroid cells. May directly bind to PTEN and promote its ubiquitination, resulting in its proteasomal degradation and activation of hypertrophic signaling (By similarity). In addition, plays a role in immune response regulation by repressing the phosphorylation of STAT1 and STAT2 in the interferon/JAK/STAT signaling pathway independent of its E3 ligase activity. Mechanistically, interacts with the intracellular domain of IFNAR1 and thereby inhibits the association between TYK2 and IFNAR1 (PubMed:33811647)", "gene_name": "TRIM10", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UDY6", "name": "TJP2", "organism": "Homo sapiens", "uniprot_id": "Q9UDY6" }, { "function": "Ubiquitin-like protein which plays a key role in the innate immune response to viral infection either via its conjugation to a target protein (ISGylation) or via its action as a free or unconjugated protein (PubMed:27564865, PubMed:39465252). ISGylation involves a cascade of enzymatic reactions involving E1, E2, and E3 enzymes which catalyze the conjugation of ISG15 to a lysine residue in the target protein (PubMed:33727702). Its target proteins include IFIT1, MX1/MxA, PPM1B, UBE2L6, UBA7, CHMP5, CHMP2A, CHMP4B and CHMP6. Isgylation of the viral sensor IFIH1/MDA5 promotes IFIH1/MDA5 oligomerization and triggers activation of innate immunity against a range of viruses, including coronaviruses, flaviviruses and picornaviruses (PubMed:33727702). Can also isgylate: EIF2AK2/PKR which results in its activation, RIGI which inhibits its function in antiviral signaling response, EIF4E2 which enhances its cap structure-binding activity and translation-inhibition activity, UBE2N and UBE2E1 which negatively regulates their activity, IRF3 which inhibits its ubiquitination and degradation and FLNB which prevents its ability to interact with the upstream activators of the JNK cascade thereby inhibiting IFNA-induced JNK signaling. Exhibits antiviral activity towards both DNA and RNA viruses, including influenza A, HIV-1 and Ebola virus. Restricts HIV-1 and ebola virus via disruption of viral budding. Inhibits the ubiquitination of HIV-1 Gag and host TSG101 and disrupts their interaction, thereby preventing assembly and release of virions from infected cells. Inhibits Ebola virus budding mediated by the VP40 protein by disrupting ubiquitin ligase activity of NEDD4 and its ability to ubiquitinate VP40. ISGylates influenza A virus NS1 protein which causes a loss of function of the protein and the inhibition of virus replication. The secreted form of ISG15 can: induce natural killer cell proliferation, act as a chemotactic factor for neutrophils and act as a IFN-gamma-inducing cytokine playing an essential role in antimycobacterial immunity. The secreted form acts through the integrin ITGAL/ITGB2 receptor to initiate activation of SRC family tyrosine kinases including LYN, HCK and FGR which leads to secretion of IFNG and IL10; the interaction is mediated by ITGAL (PubMed:29100055)", "gene_name": "ISG15", "glycan_count": 1, "glycosylation_sites": [], "id": "P05161", "name": "ISG15", "organism": "Homo sapiens", "uniprot_id": "P05161" }, { "function": "This protein aggregates to form microtubular structures", "gene_name": "IFI44", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8TCB0", "name": "IFI44L", "organism": "Homo sapiens", "uniprot_id": "Q8TCB0" }, { "function": "Medium-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats (PubMed:1970566, PubMed:21237683, PubMed:2251268, PubMed:8823175). The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA (PubMed:2251268). Electron transfer flavoprotein (ETF) is the electron acceptor that transfers electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase) (PubMed:15159392, PubMed:25416781). Among the different mitochondrial acyl-CoA dehydrogenases, medium-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 6 to 12 carbons long primary chains (PubMed:1970566, PubMed:21237683, PubMed:2251268, PubMed:8823175)", "gene_name": "ACADM", "glycan_count": 1, "glycosylation_sites": [], "id": "P11310", "name": "ACADM", "organism": "Homo sapiens", "uniprot_id": "P11310" }, { "function": "Catalyzes the transfer of the acyl group of long-chain fatty acid-CoA conjugates onto carnitine, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion (PubMed:11350182, PubMed:14517221, PubMed:16651524, PubMed:9691089). Also possesses a lysine succinyltransferase activity that can regulate enzymatic activity of substrate proteins such as ENO1 and metabolism independent of its classical carnitine O-palmitoyltransferase activity (PubMed:29425493). Plays an important role in hepatic triglyceride metabolism (By similarity). Also plays a role in inducible regulatory T-cell (iTreg) differentiation once activated by butyryl-CoA that antagonizes malonyl-CoA-mediated CPT1A repression (By similarity). Sustains the IFN-I response by recruiting ZDHCC4 to palmitoylate MAVS at the mitochondria leading to MAVS stabilization and activation (PubMed:38016475). Promotes ROS-induced oxidative stress in liver injury via modulation of NFE2L2 and NLRP3-mediated signaling pathways (By similarity)", "gene_name": "CPT1A", "glycan_count": 1, "glycosylation_sites": [], "id": "P50416", "name": "CPT1A", "organism": "Homo sapiens", "uniprot_id": "P50416" }, { "function": "Non-heme iron-containing lipoxygenase which is atypical in that it displays a prominent hydroperoxide isomerase activity and a reduced lipoxygenases activity (PubMed:12881489, PubMed:17045234, PubMed:20921226, PubMed:20923767). The hydroperoxide isomerase activity catalyzes the isomerization of hydroperoxides, derived from arachidonic and linoleic acid by ALOX12B, into hepoxilin-type epoxyalcohols and ketones (PubMed:12881489, PubMed:17045234, PubMed:20923767). In presence of oxygen, oxygenates polyunsaturated fatty acids, including arachidonic acid, to produce fatty acid hydroperoxides (PubMed:20921226). In the skin, acts downstream of ALOX12B on the linoleate moiety of esterified omega-hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega-hydroxyceramide to membrane proteins (PubMed:21558561). Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss (PubMed:21558561). In parallel, it may have a signaling function in barrier formation through the production of hepoxilins metabolites (PubMed:21558561). Also plays a role in adipocyte differentiation through hepoxilin A3 and hepoxilin B3 production which in turn activate PPARG (By similarity). Through the production of hepoxilins in the spinal cord, it may regulate inflammatory tactile allodynia (By similarity)", "gene_name": "ALOXE3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9BYJ1", "name": "ACOT12", "organism": "Homo sapiens", "uniprot_id": "Q9BYJ1" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q3M5F7", "name": "ABCA13", "organism": "Trichormus variabilis (strain ATCC 29413 / PCC 7937)", "uniprot_id": "Q3M5F7" }, { "function": "Neuropeptide that competes with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress", "gene_name": "PENK", "glycan_count": 0, "glycosylation_sites": [], "id": "P01210", "name": "Proenkephalin (PENK, proenkephalin 119\u2013159)", "organism": "Homo sapiens", "uniprot_id": "P01210" }, { "function": "Cell surface receptor for PLXNB1 and PLXNB2 that plays an important role in cell-cell signaling (PubMed:20877282). Regulates GABAergic synapse development (By similarity). Promotes the development of inhibitory synapses in a PLXNB1-dependent manner (By similarity). Modulates the complexity and arborization of developing neurites in hippocampal neurons by activating PLXNB1 and interaction with PLXNB1 mediates activation of RHOA (PubMed:19788569). Promotes the migration of cerebellar granule cells (PubMed:16055703). Plays a role in the immune system; induces B-cells to aggregate and improves their viability (in vitro) (PubMed:8876214). Induces endothelial cell migration through the activation of PTK2B/PYK2, SRC, and the phosphatidylinositol 3-kinase-AKT pathway (PubMed:16055703)", "gene_name": "SEMA4D", "glycan_count": 41, "glycosylation_sites": [ { "position": 49, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 77, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 139, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 191, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 329, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 379, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 419, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 613, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 632, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q92854", "name": "SEMA4D", "organism": "Homo sapiens", "uniprot_id": "Q92854" }, { "function": "May play a role in cell motility and cell adhesion", "gene_name": "SEMA3F", "glycan_count": 8, "glycosylation_sites": [ { "position": 53, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 126, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13275", "name": "SEMA3F", "organism": "Homo sapiens", "uniprot_id": "Q13275" }, { "function": "Bifunctional axonal guidance cue regulated by sulfated proteoglycans; attractive effects result from interactions with heparan sulfate proteoglycans (HSPGs), while the inhibitory effects depend on interactions with chondroitin sulfate proteoglycans (CSPGs) (By similarity). Ligand for receptor PLXNB3. In glioma cells, SEMA5A stimulation of PLXNB3 results in the disassembly of F-actin stress fibers, disruption of focal adhesions and cellular collapse as well as inhibition of cell migration and invasion through ARHGDIA-mediated inactivation of RAC1. May promote angiogenesis by increasing endothelial cell proliferation and migration and inhibiting apoptosis", "gene_name": "SEMA5A", "glycan_count": 2, "glycosylation_sites": [ { "position": 142, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 168, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 227, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 277, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 323, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 367, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 437, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 536, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 591, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 717, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 933, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13591", "name": "SEMA5A", "organism": "Homo sapiens", "uniprot_id": "Q13591" }, { "function": "Has N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Also exhibits a dipeptidyl-peptidase IV type activity. Inactivates the peptide neurotransmitter N-acetylaspartylglutamate", "gene_name": "NAALAD2", "glycan_count": 7, "glycosylation_sites": [ { "position": 111, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 143, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 185, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 314, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 449, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 603, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 628, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y3Q0", "name": "MAN1B1", "organism": "Homo sapiens", "uniprot_id": "Q9Y3Q0" }, { "function": "Tyrosine-protein kinase that plays an essential role as cell surface receptor for neuregulins and EGF family members and regulates development of the heart, the central nervous system and the mammary gland, gene transcription, cell proliferation, differentiation, migration and apoptosis. Required for normal cardiac muscle differentiation during embryonic development, and for postnatal cardiomyocyte proliferation. Required for normal development of the embryonic central nervous system, especially for normal neural crest cell migration and normal axon guidance. Required for mammary gland differentiation, induction of milk proteins and lactation. Acts as cell-surface receptor for the neuregulins NRG1, NRG2, NRG3 and NRG4 and the EGF family members BTC, EREG and HBEGF. Ligand binding triggers receptor dimerization and autophosphorylation at specific tyrosine residues that then serve as binding sites for scaffold proteins and effectors. Ligand specificity and signaling is modulated by alternative splicing, proteolytic processing, and by the formation of heterodimers with other ERBB family members, thereby creating multiple combinations of intracellular phosphotyrosines that trigger ligand- and context-specific cellular responses. Mediates phosphorylation of SHC1 and activation of the MAP kinases MAPK1/ERK2 and MAPK3/ERK1. Isoform JM-A CYT-1 and isoform JM-B CYT-1 phosphorylate PIK3R1, leading to the activation of phosphatidylinositol 3-kinase and AKT1 and protect cells against apoptosis. Isoform JM-A CYT-1 and isoform JM-B CYT-1 mediate reorganization of the actin cytoskeleton and promote cell migration in response to NRG1. Isoform JM-A CYT-2 and isoform JM-B CYT-2 lack the phosphotyrosine that mediates interaction with PIK3R1, and hence do not phosphorylate PIK3R1, do not protect cells against apoptosis, and do not promote reorganization of the actin cytoskeleton and cell migration. Proteolytic processing of isoform JM-A CYT-1 and isoform JM-A CYT-2 gives rise to the corresponding soluble intracellular domains (4ICD) that translocate to the nucleus, promote nuclear import of STAT5A, activation of STAT5A, mammary epithelium differentiation, cell proliferation and activation of gene expression. The ERBB4 soluble intracellular domains (4ICD) colocalize with STAT5A at the CSN2 promoter to regulate transcription of milk proteins during lactation. The ERBB4 soluble intracellular domains can also translocate to mitochondria and promote apoptosis", "gene_name": "ERBB4", "glycan_count": 6, "glycosylation_sites": [ { "position": 138, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 174, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 181, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 253, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 358, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 410, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 473, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 495, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 548, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 576, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 620, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q15303", "name": "HER4 (ERBB4)", "organism": "Homo sapiens", "uniprot_id": "Q15303" }, { "function": "Receptor for somatostatin-14 and -28. This receptor is coupled via pertussis toxin sensitive G proteins to inhibition of adenylyl cyclase. In addition it stimulates phosphotyrosine phosphatase and PLC via pertussis toxin insensitive as well as sensitive G proteins. Inhibits calcium entry by suppressing voltage-dependent calcium channels. Acts as the functionally dominant somatostatin receptor in pancreatic alpha- and beta-cells where it mediates the inhibitory effect of somatostatin-14 on hormone secretion. Inhibits cell growth through enhancement of MAPK1 and MAPK2 phosphorylation and subsequent up-regulation of CDKN1B. Stimulates neuronal migration and axon outgrowth and may participate in neuron development and maturation during brain development. Mediates negative regulation of insulin receptor signaling through PTPN6. Inactivates SSTR3 receptor function following heterodimerization", "gene_name": "SSTR2", "glycan_count": 0, "glycosylation_sites": [ { "position": 9, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 22, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 29, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 32, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P30874", "name": "Somatostatin receptor 2 (SSTR2)", "organism": "Homo sapiens", "uniprot_id": "P30874" }, { "function": "Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated", "gene_name": "MGMT", "glycan_count": 4, "glycosylation_sites": [], "id": "P16455", "name": "MGMT (O6-methylguanine\u2013DNA methyltransferase)", "organism": "Homo sapiens", "uniprot_id": "P16455" }, { "function": "Endopeptidase that degrades various components of the extracellular matrix such as collagen (PubMed:8015608). Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development (By similarity). Activates progelatinase A/MMP2, thereby acting as a positive regulator of cell growth and migration (PubMed:22065321, PubMed:8015608). Involved in the formation of the fibrovascular tissues in association with pro-MMP2 (PubMed:12714657, PubMed:22065321). May be involved in actin cytoskeleton reorganization by cleaving PTK7 (PubMed:20837484). Acts as a regulator of Notch signaling by mediating cleavage and inhibition of DLL1 (PubMed:21572390). Cleaves ADGRB1 to release vasculostatin-40 which inhibits angiogenesis (PubMed:22330140). Acts as a negative regulator of the GDF15-GFRAL aversive response by mediating cleavage and inactivation of GFRAL (PubMed:35177851)", "gene_name": "MMP14", "glycan_count": 3, "glycosylation_sites": [], "id": "P50281", "name": "MMP-14 (MT1-MMP)", "organism": "Homo sapiens", "uniprot_id": "P50281" }, { "function": "Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase", "gene_name": "MMP7", "glycan_count": 0, "glycosylation_sites": [], "id": "P09237", "name": "MMP-7", "organism": "Homo sapiens", "uniprot_id": "P09237" }, { "function": "May play an important role in the progression of epithelial malignancies", "gene_name": "MMP11", "glycan_count": 0, "glycosylation_sites": [], "id": "P24347", "name": "MMP-11", "organism": "Homo sapiens", "uniprot_id": "P24347" }, { "function": "Endopeptidase that degrades various components of the extracellular matrix, such as fibrin. May be involved in the activation of membrane-bound precursors of growth factors or inflammatory mediators, such as tumor necrosis factor-alpha. May also be involved in tumoral process. Cleaves pro-TNF-alpha at the '74-Ala-|-Gln-75' site. Not obvious if able to proteolytically activate progelatinase A. Does not hydrolyze collagen types I, II, III, IV and V, gelatin, fibronectin, laminin, decorin nor alpha1-antitrypsin", "gene_name": "MMP17", "glycan_count": 0, "glycosylation_sites": [ { "position": 137, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 318, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9ULZ9", "name": "MMP-16", "organism": "Homo sapiens", "uniprot_id": "Q9ULZ9" }, { "function": "Precursor of the transcription factor form (Processed cyclic AMP-dependent transcription factor ATF-6 alpha), which is embedded in the endoplasmic reticulum membrane (PubMed:10564271, PubMed:11158310, PubMed:11779464). Endoplasmic reticulum stress promotes processing of this form, releasing the transcription factor form that translocates into the nucleus, where it activates transcription of genes involved in the unfolded protein response (UPR) (PubMed:10564271, PubMed:11158310, PubMed:11779464)", "gene_name": "ATF6", "glycan_count": 6, "glycosylation_sites": [ { "position": 472, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 584, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 643, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P18850", "name": "ATF6 (Activating Transcription Factor 6)", "organism": "Homo sapiens", "uniprot_id": "P18850" }, { "function": "Serine/threonine-protein kinase that acts as a mediator of cell growth (PubMed:11641781, PubMed:17360971). Modulates apoptosis (PubMed:11641781, PubMed:17360971). In association with STK24 negatively regulates Golgi reorientation in polarized cell migration upon RHO activation (PubMed:27807006). Phosphorylates ATG4B at 'Ser-383', thereby increasing autophagic flux (PubMed:29232556). Part of the striatin-interacting phosphatase and kinase (STRIPAK) complexes. STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling. Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation (PubMed:18782753)", "gene_name": "STK26", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9P289", "name": "STK26 (MST4)", "organism": "Homo sapiens", "uniprot_id": "Q9P289" }, { "function": "Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase", "gene_name": "PZP", "glycan_count": 8, "glycosylation_sites": [ { "position": 54, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 69, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 246, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 392, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 406, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 753, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 875, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 932, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 997, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1430, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P20742", "name": "Pregnancy Zone Protein (PZP)", "organism": "Homo sapiens", "uniprot_id": "P20742" }, { "function": "Catalyzes the reversible hydration of carbon dioxide (PubMed:10550681, PubMed:16506782, PubMed:16686544, PubMed:16807956, PubMed:17127057, PubMed:17314045, PubMed:17407288, PubMed:18618712, PubMed:19186056, PubMed:19206230). Can hydrate cyanamide to urea (PubMed:10550681)", "gene_name": "CA1", "glycan_count": 1, "glycosylation_sites": [], "id": "P00915", "name": "Carbonic Anhydrase 1 (CA1)", "organism": "Homo sapiens", "uniprot_id": "P00915" }, { "function": "Trypsin-like serine protease that plays an essential role in regulating the immune response by controlling all complement pathways. Inhibits these pathways by cleaving three peptide bonds in the alpha-chain of C3b and two bonds in the alpha-chain of C4b thereby inactivating these proteins (PubMed:17320177, PubMed:7360115). Essential cofactors for these reactions include factor H and C4BP in the fluid phase and membrane cofactor protein/CD46 and CR1 on cell surfaces (PubMed:12055245, PubMed:2141838, PubMed:9605165). The presence of these cofactors on healthy cells allows degradation of deposited C3b by CFI in order to prevent undesired complement activation, while in apoptotic cells or microbes, the absence of such cofactors leads to C3b-mediated complement activation and subsequent opsonization (PubMed:28671664)", "gene_name": "CFI", "glycan_count": 85, "glycosylation_sites": [ { "position": 70, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 103, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 177, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 464, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 494, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 536, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P05156", "name": "Complement Factor I (CFI)", "organism": "Homo sapiens", "uniprot_id": "P05156" }, { "function": "Transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes. Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelyosomal compartment where the low pH mediates the dissociation of the complex", "gene_name": "M6PR", "glycan_count": 82, "glycosylation_sites": [ { "position": 57, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 83, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 94, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 107, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 113, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P20645", "name": "Mannose-6-phosphate receptor (M6PR)", "organism": "Homo sapiens", "uniprot_id": "P20645" }, { "function": "Muscle-specific filamin, which plays a central role in sarcomere assembly and organization (PubMed:34405687). Critical for normal myogenesis, it probably functions as a large actin-cross-linking protein with structural functions at the Z lines in muscle cells. May be involved in reorganizing the actin cytoskeleton in response to signaling events (By similarity)", "gene_name": "FLNC", "glycan_count": 1, "glycosylation_sites": [], "id": "Q14315", "name": "Filamin C (FLNC)", "organism": "Homo sapiens", "uniprot_id": "Q14315" }, { "function": "May function as an adapter in striated muscle to couple protein kinase C-mediated signaling via its LIM domains to the cytoskeleton", "gene_name": "LDB3", "glycan_count": 1, "glycosylation_sites": [], "id": "O75112", "name": "LDB3/ZASP", "organism": "Homo sapiens", "uniprot_id": "O75112" }, { "function": "Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis", "gene_name": "PYGM", "glycan_count": 1, "glycosylation_sites": [], "id": "P11217", "name": "Muscle glycogen phosphorylase (PYGM)", "organism": "Homo sapiens", "uniprot_id": "P11217" }, { "function": "Cytoplasmic adapter protein that plays a critical role in clathrin-mediated endocytosis which is important in processes such as internalization of cell receptors, synaptic transmission or removal of apoptotic cells. Recruits AP-2 and attaches clathrin triskelions to the cytoplasmic side of plasma membrane leading to clathrin-coated vesicles (CCVs) assembly (PubMed:10436022, PubMed:16262731, PubMed:27574975). Furthermore, regulates clathrin-coated vesicle size and maturation by directly sensing and driving membrane curvature (PubMed:25898166). In addition to binding to clathrin, mediates the endocytosis of small R-SNARES (Soluble NSF Attachment Protein REceptors) between plasma membranes and endosomes including VAMP2, VAMP3, VAMP4, VAMP7 or VAMP8 (PubMed:21808019, PubMed:22118466, PubMed:23741335). In turn, PICALM-dependent SNARE endocytosis is required for the formation and maturation of autophagic precursors (PubMed:25241929). Modulates thereby autophagy and the turnover of autophagy substrates such as MAPT/TAU or amyloid precursor protein cleaved C-terminal fragment (APP-CTF) (PubMed:24067654, PubMed:25241929)", "gene_name": "PICALM", "glycan_count": 2, "glycosylation_sites": [], "id": "Q13492", "name": "Phosphatidylinositol-binding clathrin assembly protein (PICALM)", "organism": "Homo sapiens", "uniprot_id": "Q13492" }, { "function": "Involved in microtubule stabilization in many cell types, including neuronal cells (By similarity). Specifically has microtubule cold stabilizing activity (By similarity). Involved in dendrite morphogenesis and maintenance by regulating lysosomal trafficking via its interaction with TMEM106B (PubMed:24357581). Regulates KIF5A-mediated axonal cargo transport (By similarity). Regulates axonal growth during neuron polarization (By similarity)", "gene_name": "MAP6", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96JE9", "name": "MEN1 (Menin)", "organism": "Homo sapiens", "uniprot_id": "Q96JE9" }, { "function": "Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Down-regulates basal and activated transcription. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Inhibits transcriptional activation of PAX3 and ETS1 through direct protein-protein interactions. Modulates PAX5 activity; the function seems to involve CREBBP. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Acts as a histone chaperone that facilitates deposition of histone H3.3. Acts as a targeting component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Does not affect the ATPase activity of ATRX but alleviates its transcription repression activity. Upon neuronal activation associates with regulatory elements of selected immediate early genes where it promotes deposition of histone H3.3 which may be linked to transcriptional induction of these genes. Required for the recruitment of histone H3.3:H4 dimers to PML-nuclear bodies (PML-NBs); the process is independent of ATRX and facilitated by ASF1A; PML-NBs are suggested to function as regulatory sites for the incorporation of newly synthesized histone H3.3 into chromatin. In case of overexpression of centromeric histone variant CENPA (as found in various tumors) is involved in its mislocalization to chromosomes; the ectopic localization involves a heterotypic tetramer containing CENPA, and histones H3.3 and H4 and decreases binding of CTCF to chromatin. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Shows restriction activity towards human cytomegalovirus (HCMV). Plays a role as a positive regulator of the heat shock transcription factor HSF1 activity during the stress protein response (PubMed:15016915)", "gene_name": "DAXX", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UER7", "name": "DAXX", "organism": "Homo sapiens", "uniprot_id": "Q9UER7" }, { "function": "Involved in transcriptional regulation and chromatin remodeling. Facilitates DNA replication in multiple cellular environments and is required for efficient replication of a subset of genomic loci. Binds to DNA tandem repeat sequences in both telomeres and euchromatin and in vitro binds DNA quadruplex structures. May help stabilizing G-rich regions into regular chromatin structures by remodeling G4 DNA and incorporating H3.3-containing nucleosomes. Catalytic component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Its heterochromatin targeting is proposed to involve a combinatorial readout of histone H3 modifications (specifically methylation states of H3K9 and H3K4) and association with CBX5. Involved in maintaining telomere structural integrity in embryonic stem cells which probably implies recruitment of CBX5 to telomeres. Reports on the involvement in transcriptional regulation of telomeric repeat-containing RNA (TERRA) are conflicting; according to a report, it is not sufficient to decrease chromatin condensation at telomeres nor to increase expression of telomeric RNA in fibroblasts (PubMed:24500201). May be involved in telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines. Acts as a negative regulator of chromatin incorporation of transcriptionally repressive histone MACROH2A1, particularily at telomeres and the alpha-globin cluster in erythroleukemic cells. Participates in the allele-specific gene expression at the imprinted IGF2/H19 gene locus. On the maternal allele, required for the chromatin occupancy of SMC1 and CTCTF within the H19 imprinting control region (ICR) and involved in esatblishment of histone tails modifications in the ICR. May be involved in brain development and facial morphogenesis. Binds to zinc-finger coding genes with atypical chromatin signatures and regulates its H3K9me3 levels. Forms a complex with ZNF274, TRIM28 and SETDB1 to facilitate the deposition and maintenance of H3K9me3 at the 3' exons of zinc-finger genes (PubMed:27029610)", "gene_name": "ATRX", "glycan_count": 1, "glycosylation_sites": [], "id": "P46100", "name": "ATRX", "organism": "Homo sapiens", "uniprot_id": "P46100" }, { "function": "Non-catalytic component of the TSC-TBC complex, a multiprotein complex that acts as a negative regulator of the canonical mTORC1 complex, an evolutionarily conserved central nutrient sensor that stimulates anabolic reactions and macromolecule biosynthesis to promote cellular biomass generation and growth (PubMed:12172553, PubMed:12271141, PubMed:12906785, PubMed:15340059, PubMed:24529379, PubMed:28215400). The TSC-TBC complex acts as a GTPase-activating protein (GAP) for the small GTPase RHEB, a direct activator of the protein kinase activity of mTORC1 (PubMed:12906785, PubMed:15340059, PubMed:24529379). In absence of nutrients, the TSC-TBC complex inhibits mTORC1, thereby preventing phosphorylation of ribosomal protein S6 kinase (RPS6KB1 and RPS6KB2) and EIF4EBP1 (4E-BP1) by the mTORC1 signaling (PubMed:12271141, PubMed:24529379, PubMed:28215400, PubMed:33215753). The TSC-TBC complex is inactivated in response to nutrients, relieving inhibition of mTORC1 (PubMed:12172553, PubMed:24529379). Within the TSC-TBC complex, TSC1 stabilizes TSC2 and prevents TSC2 self-aggregation (PubMed:10585443, PubMed:28215400). Acts as a tumor suppressor (PubMed:9242607). Involved in microtubule-mediated protein transport via its ability to regulate mTORC1 signaling (By similarity). Also acts as a co-chaperone for HSP90AA1 facilitating HSP90AA1 chaperoning of protein clients such as kinases, TSC2 and glucocorticoid receptor NR3C1 (PubMed:29127155). Increases ATP binding to HSP90AA1 and inhibits HSP90AA1 ATPase activity (PubMed:29127155). Competes with the activating co-chaperone AHSA1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:29127155). Recruits TSC2 to HSP90AA1 and stabilizes TSC2 by preventing the interaction between TSC2 and ubiquitin ligase HERC1 (PubMed:16464865, PubMed:29127155)", "gene_name": "TSC1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q92574", "name": "TSC1", "organism": "Homo sapiens", "uniprot_id": "Q92574" }, { "function": "Involved in vitamin K metabolism. Catalytic subunit of the vitamin K epoxide reductase (VKOR) complex which reduces inactive vitamin K 2,3-epoxide to active vitamin K. Vitamin K is required for the gamma-carboxylation of various proteins, including clotting factors, and is required for normal blood coagulation, but also for normal bone development", "gene_name": "VKORC1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9BQB6", "name": "Warfarin-sensitive vitamin K epoxide reductase complex (VKORC1)", "organism": "Homo sapiens", "uniprot_id": "Q9BQB6" }, { "function": "Transcription factor that activates the expression of the EIF2S1 (EIF2-alpha) gene. Links the transcriptional modulation of key metabolic genes to cellular growth and development. Implicated in the control of nuclear genes required for respiration, heme biosynthesis, and mitochondrial DNA transcription and replication", "gene_name": "NRF1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q16656", "name": "Nrf-1", "organism": "Homo sapiens", "uniprot_id": "Q16656" }, { "function": "Binds to the mitochondrial light strand promoter and functions in mitochondrial transcription regulation (PubMed:29445193, PubMed:32183942). Component of the mitochondrial transcription initiation complex, composed at least of TFB2M, TFAM and POLRMT that is required for basal transcription of mitochondrial DNA (PubMed:29149603). In this complex, TFAM recruits POLRMT to a specific promoter whereas TFB2M induces structural changes in POLRMT to enable promoter opening and trapping of the DNA non-template strand (PubMed:20410300). Required for accurate and efficient promoter recognition by the mitochondrial RNA polymerase (PubMed:22037172). Promotes transcription initiation from the HSP1 and the light strand promoter by binding immediately upstream of transcriptional start sites (PubMed:22037172). Is able to unwind DNA (PubMed:22037172). Bends the mitochondrial light strand promoter DNA into a U-turn shape via its HMG boxes (PubMed:1737790). Required for maintenance of normal levels of mitochondrial DNA (PubMed:19304746, PubMed:22841477). May play a role in organizing and compacting mitochondrial DNA (PubMed:22037171)", "gene_name": "TFAM", "glycan_count": 1, "glycosylation_sites": [], "id": "Q00059", "name": "Tfam", "organism": "Homo sapiens", "uniprot_id": "Q00059" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P16860 (BNP)", "name": "Natriuretic Peptides (BNP, NT-proBNP, ANP)", "organism": "", "uniprot_id": "" }, { "function": "Receptor for interleukin-33 (IL-33) which plays crucial roles in innate and adaptive immunity, contributing to tissue homeostasis and responses to environmental stresses together with coreceptor IL1RAP (PubMed:35238669). Its stimulation recruits MYD88, IRAK1, IRAK4, and TRAF6, followed by phosphorylation of MAPK3/ERK1 and/or MAPK1/ERK2, MAPK14, and MAPK8. Possibly involved in helper T-cell function (Probable) (PubMed:16286016). Upon tissue injury, induces UCP2-dependent mitochondrial rewiring that attenuates the generation of reactive oxygen species and preserves the integrity of Krebs cycle required for persistent production of itaconate and subsequent GATA3-dependent differentiation of inflammation-resolving alternatively activated macrophages (By similarity)", "gene_name": "IL1RL1", "glycan_count": 11, "glycosylation_sites": [ { "position": 54, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 95, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 101, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 140, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 191, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 232, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 254, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 273, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q01638", "name": "Suppression of Tumorigenicity-2 (sST2)", "organism": "Homo sapiens", "uniprot_id": "Q01638" }, { "function": "Adrenomedullin/ADM and proadrenomedullin N-20 terminal peptide/PAMP are peptide hormones that act as potent hypotensive and vasodilatator agents (PubMed:8387282, PubMed:9620797). Numerous actions have been reported most related to the physiologic control of fluid and electrolyte homeostasis. In the kidney, ADM is diuretic and natriuretic, and both ADM and PAMP inhibit aldosterone secretion by direct adrenal actions. In pituitary gland, both peptides at physiologically relevant doses inhibit basal ACTH secretion. Both peptides appear to act in brain and pituitary gland to facilitate the loss of plasma volume, actions which complement their hypotensive effects in blood vessels", "gene_name": "ADM", "glycan_count": 2, "glycosylation_sites": [], "id": "P35318", "name": "Adrenomedullin (MR-proADM)", "organism": "Homo sapiens", "uniprot_id": "P35318" }, { "function": "Endothelins are endothelium-derived vasoconstrictor peptides (By similarity). Probable ligand for G-protein coupled receptors EDNRA and EDNRB which activates PTK2B, BCAR1, BCAR3 and, GTPases RAP1 and RHOA cascade in glomerular mesangial cells (PubMed:19086031). Also binds the DEAR/FBXW7-AS1 receptor (PubMed:17446437). Promotes mesenteric arterial wall remodeling via activation of ROCK signaling and subsequent colocalization of NFATC3 with F-actin filaments (By similarity). NFATC3 then translocates to the nucleus where it subsequently promotes the transcription of the smooth muscle hypertrophy and differentiation marker ACTA2 (By similarity)", "gene_name": "EDN1", "glycan_count": 1, "glycosylation_sites": [], "id": "P05305", "name": "Endothelin-1 (ET-1)", "organism": "Homo sapiens", "uniprot_id": "P05305" }, { "function": "Beta subunit of the human chorionic gonadotropin (hCG). hCG is a complex glycoprotein composed of two glycosylated subunits alpha and beta which are non-covalently associated. The alpha subunit is identical to those in the pituitary gonadotropin hormones (LH, FSH and TSH). The beta subunits are distinct in each of the hormones and confer receptor and biological specificity. Has an essential role in pregnancy and maternal adaptation. Stimulates the ovaries to synthesize the steroids that are essential for the maintenance of pregnancy", "gene_name": "CGB3", "glycan_count": 43, "glycosylation_sites": [ { "position": 33, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 50, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 141, "type": "O-linked (GalNAc...) serine" }, { "position": 147, "type": "O-linked (GalNAc...) serine" }, { "position": 152, "type": "O-linked (GalNAc...) serine" }, { "position": 158, "type": "O-linked (GalNAc...) serine" } ], "id": "P0DN86", "name": "Human chorionic gonadotropin (hCG)", "organism": "Homo sapiens", "uniprot_id": "P0DN86" }, { "function": "Multifunctional protein that plays a role in silencing host antiviral defenses and promoting viral transcription. Does not seem to be essential for HBV infection. May be directly involved in development of cirrhosis and liver cancer (hepatocellular carcinoma). Most of cytosolic activities involve modulation of cytosolic calcium. The effect on apoptosis is controversial depending on the cell types in which the studies have been conducted. May induce apoptosis by localizing in mitochondria and causing loss of mitochondrial membrane potential. May also modulate apoptosis by binding host CFLAR, a key regulator of the death-inducing signaling complex (DISC). Promotes viral transcription by using the host E3 ubiquitin ligase DDB1 to target the SMC5-SMC6 complex to proteasomal degradation. This host complex would otherwise bind to viral episomal DNA, and prevents its transcription. Moderately stimulates transcription of many different viral and cellular transcription elements. Promoters and enhancers stimulated by HBx contain DNA binding sites for NF-kappa-B, AP-1, AP-2, c-EBP, ATF/CREB, or the calcium-activated factor NF-AT", "gene_name": "X", "glycan_count": 0, "glycosylation_sites": [], "id": "P03165", "name": "HBsAg (Hepatitis B surface antigen)", "organism": "Hepatitis B virus genotype D subtype ayw (isolate France/Tiollais/1979)", "uniprot_id": "P03165" }, { "function": "Multifunctional protein that plays a role in silencing host antiviral defenses and promoting viral transcription. Does not seem to be essential for HBV infection. May be directly involved in development of cirrhosis and liver cancer (hepatocellular carcinoma). Most of cytosolic activities involve modulation of cytosolic calcium. The effect on apoptosis is controversial depending on the cell types in which the studies have been conducted. May induce apoptosis by localizing in mitochondria and causing loss of mitochondrial membrane potential. May also modulate apoptosis by binding host CFLAR, a key regulator of the death-inducing signaling complex (DISC). Promotes viral transcription by using the host E3 ubiquitin ligase DDB1 to target the SMC5-SMC6 complex to proteasomal degradation. This host complex would otherwise bind to viral episomal DNA, and prevents its transcription. Moderately stimulates transcription of many different viral and cellular transcription elements. Promoters and enhancers stimulated by HBx contain DNA binding sites for NF-kappa-B, AP-1, AP-2, c-EBP, ATF/CREB, or the calcium-activated factor NF-AT", "gene_name": "X", "glycan_count": 0, "glycosylation_sites": [], "id": "P03168", "name": "HBeAg (Hepatitis B e antigen)", "organism": "Ground squirrel hepatitis virus (strain 27)", "uniprot_id": "P03168" }, { "function": "Cytokine receptor that binds to B-lymphocyte chemoattractant (BLC). Involved in B-cell migration into B-cell follicles of spleen and Peyer patches but not into those of mesenteric or peripheral lymph nodes. May have a regulatory function in Burkitt lymphoma (BL) lymphomagenesis and/or B-cell differentiation", "gene_name": "CXCR5", "glycan_count": 0, "glycosylation_sites": [ { "position": 28, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 196, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P32302", "name": "CXCR5", "organism": "Homo sapiens", "uniprot_id": "P32302" }, { "function": "Receptor for the C-C type chemokine CCL20 (PubMed:9169459). Binds to CCL20 and subsequently transduces a signal by increasing the intracellular calcium ion levels (PubMed:20068036). Although CCL20 is its major ligand it can also act as a receptor for non-chemokine ligands such as beta-defensins (PubMed:25585877). Binds to defensin DEFB1 leading to increase in intracellular calcium ions and cAMP levels. Its binding to DEFB1 is essential for the function of DEFB1 in regulating sperm motility and bactericidal activity (PubMed:25122636). Binds to defensins DEFB4 and DEFB4A/B and mediates their chemotactic effects (PubMed:20068036). The ligand-receptor pair CCL20-CCR6 is responsible for the chemotaxis of dendritic cells (DC), effector/ memory T-cells and B-cells and plays an important role at skin and mucosal surfaces under homeostatic and inflammatory conditions, as well as in pathology, including cancer and various autoimmune diseases. CCR6-mediated signals are essential for immune responses to microbes in the intestinal mucosa and in the modulation of inflammatory responses initiated by tissue insult and trauma (PubMed:21376174). CCR6 is essential for the recruitment of both the pro-inflammatory IL17 producing helper T-cells (Th17) and the regulatory T-cells (Treg) to sites of inflammation. Required for the normal migration of Th17 cells in Peyers-patches and other related tissue sites of the intestine and plays a role in regulating effector T-cell balance and distribution in inflamed intestine. Plays an important role in the coordination of early thymocyte precursor migration events important for normal subsequent thymocyte precursor development, but is not required for the formation of normal thymic natural regulatory T-cells (nTregs). Required for optimal differentiation of DN2 and DN3 thymocyte precursors. Essential for B-cell localization in the subepithelial dome of Peyers-patches and for efficient B-cell isotype switching to IgA in the Peyers-patches. Essential for appropriate anatomical distribution of memory B-cells in the spleen and for the secondary recall response of memory B-cells (By similarity). Positively regulates sperm motility and chemotaxis via its binding to CCL20 (PubMed:23765988)", "gene_name": "CCR6", "glycan_count": 0, "glycosylation_sites": [ { "position": 7, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 23, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P51684", "name": "CCR6", "organism": "Homo sapiens", "uniprot_id": "P51684" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P1833", "name": "CD62L (L-selectin)", "organism": "", "uniprot_id": "" }, { "function": "Receptor for the C-X-C chemokine CXCL9, CXCL10 and CXCL11 and mediates the proliferation, survival and angiogenic activity of human mesangial cells (HMC) through a heterotrimeric G-protein signaling pathway (PubMed:12782716). Binds to CCL21. Probably promotes cell chemotaxis response. Upon activation by PF4, induces activated T-lymphocytes migration mediated via downstream Ras/extracellular signal-regulated kinase (ERK) signaling", "gene_name": "CXCR3", "glycan_count": 0, "glycosylation_sites": [ { "position": 22, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 32, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P49682", "name": "CXCR3", "organism": "Homo sapiens", "uniprot_id": "P49682" }, { "function": "High affinity receptor for the C-C type chemokines CCL17/TARC, CCL22/MDC and CKLF isoform 1/CKLF1. The activity of this receptor is mediated by G(i) proteins which activate a phosphatidylinositol-calcium second messenger system. Can function as a chemoattractant homing receptor on circulating memory lymphocytes and as a coreceptor for some primary HIV-2 isolates. In the CNS, could mediate hippocampal-neuron survival", "gene_name": "CCR4", "glycan_count": 0, "glycosylation_sites": [ { "position": 183, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 194, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P51679", "name": "CCR4", "organism": "Homo sapiens", "uniprot_id": "P51679" }, { "function": "It is involved in the regulation of the biosynthesis and biological function of glycoprotein oligosaccharides. Catalyzes the addition of N-acetylglucosamine in beta 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-linked sugar chains, called bisecting N-acetylglucosamine (GlcNAc). It is one of the most important enzymes involved in the regulation of the biosynthesis of glycoprotein oligosaccharides. The addition of this bisecting GlcNAc residue alters not only the composition, but also the conformation of the N-glycan. The introduction of the bisecting GlcNAc residue results in the suppression of further processing and elongation of N-glycans, precluding the formation of beta-1,6 GlcNAc branching, catalyzed by MGAT5 since it is unable to use the bisected oligosaccharide as a substrate (PubMed:19403558). Addition of bisecting N-acetylglucosamine to CDH1/E-cadherin modulates CDH1 cell membrane location (PubMed:19403558). Inhibits NeuAc-alpha-2,3-Gal-beta-1,4-GlcNAc- formation which modulates sialylation levels and plays a role in cell migration regulation (PubMed:26801611). In brain, addition of bisecting N-acetylglucosamine to BACE1 blocks its lysosomal targeting in response to oxidative stress and further degradation which increases its location to early endosome and the APP cleavage (By similarity)", "gene_name": "MGAT3", "glycan_count": 3, "glycosylation_sites": [ { "position": 141, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 241, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 259, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 397, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q09327", "name": "\u03b2-1,4-Galactosyltransferase V (\u03b2-1,4-GalT-V)", "organism": "Homo sapiens", "uniprot_id": "Q09327" }, { "function": "Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion", "gene_name": "MMP13", "glycan_count": 1, "glycosylation_sites": [ { "position": 117, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 152, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P45452", "name": "MMP-13", "organism": "Homo sapiens", "uniprot_id": "P45452" }, { "function": "Intracellular carrier for long-chain fatty acids and related active lipids, such as endocannabinoids, that regulate the metabolism and actions of the ligands they bind. In addition to the cytosolic transport, selectively delivers specific fatty acids from the cytosol to the nucleus, wherein they activate nuclear receptors (PubMed:21395585, PubMed:22170058). Delivers retinoic acid to the nuclear receptor peroxisome proliferator-activated receptor delta; which promotes proliferation and survival. May also serve as a synaptic carrier of endocannabinoid at central synapses and thus controls retrograde endocannabinoid signaling. Modulates inflammation by regulating PTGES induction via NF-kappa-B activation, and prostaglandin E2 (PGE2) biosynthesis during inflammation (By similarity). May be involved in keratinocyte differentiation (PubMed:8092987)", "gene_name": "FABP5", "glycan_count": 1, "glycosylation_sites": [], "id": "Q01469", "name": "FABP5", "organism": "Homo sapiens", "uniprot_id": "Q01469" }, { "function": "Initiates blood coagulation by forming a complex with circulating factor VII or VIIa. The [TF:VIIa] complex activates factors IX or X by specific limited proteolysis. TF plays a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade", "gene_name": "F3", "glycan_count": 9, "glycosylation_sites": [ { "position": 156, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 169, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P13726", "name": "tissue factor", "organism": "Homo sapiens", "uniprot_id": "P13726" }, { "function": "V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268)", "gene_name": "IGKV1-5", "glycan_count": 0, "glycosylation_sites": [], "id": "P01602", "name": "Immunoglobulin kappa variable 4-1 (IGKV4-1)", "organism": "Homo sapiens", "uniprot_id": "P01602" }, { "function": "Bifunctional iron sensor that switches between 2 activities depending on iron availability (PubMed:1281544, PubMed:1946430, PubMed:8041788). Iron deprivation, promotes its mRNA binding activity through which it regulates the expression of genes involved in iron uptake, sequestration and utilization (PubMed:1281544, PubMed:1946430, PubMed:23891004, PubMed:8041788). Binds to iron-responsive elements (IRES) in the untranslated region of target mRNAs preventing for instance the translation of ferritin and aminolevulinic acid synthase and stabilizing the transferrin receptor mRNA (PubMed:1281544, PubMed:1946430, PubMed:23891004, PubMed:8041788)", "gene_name": "ACO1", "glycan_count": 2, "glycosylation_sites": [], "id": "P21399", "name": "Selectin-L (SELL)", "organism": "Homo sapiens", "uniprot_id": "P21399" }, { "function": "Hydrolyzes the toxic metabolites of a variety of organophosphorus insecticides. Capable of hydrolyzing a broad spectrum of organophosphate substrates and lactones, and a number of aromatic carboxylic acid esters. Mediates an enzymatic protection of low density lipoproteins against oxidative modification and the consequent series of events leading to atheroma formation", "gene_name": "PON1", "glycan_count": 55, "glycosylation_sites": [ { "position": 253, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 270, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 324, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P27169", "name": "Paraoxonase 1 (PON1)", "organism": "Homo sapiens", "uniprot_id": "P27169" }, { "function": "Kinase that plays a key role in the regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Inhibition of pyruvate dehydrogenase decreases glucose utilization and increases fat metabolism. Mediates cellular responses to insulin. Plays an important role in maintaining normal blood glucose levels and in metabolic adaptation to nutrient availability. Via its regulation of pyruvate dehydrogenase activity, plays an important role in maintaining normal blood pH and in preventing the accumulation of ketone bodies under starvation. Plays a role in the regulation of cell proliferation and in resistance to apoptosis under oxidative stress. Plays a role in p53/TP53-mediated apoptosis", "gene_name": "PDK2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q15119", "name": "PDK3", "organism": "Homo sapiens", "uniprot_id": "Q15119" }, { "function": "Inflammasome sensor, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis of CD4(+) T-cells and macrophages (PubMed:11408476, PubMed:11821383, PubMed:15030775, PubMed:32051255, PubMed:32840892, PubMed:33542150, PubMed:34019797, PubMed:36357533). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation (PubMed:11408476, PubMed:11821383, PubMed:15030775, PubMed:36357533). Acts as a recognition receptor (PRR): recognizes specific pathogens and other damage-associated signals, such as HIV-1 protease activity or Val-boroPro inhibitor, and mediates CARD8 inflammasome activation (PubMed:32840892, PubMed:33542150, PubMed:36357533). In response to pathogen-associated signals, the N-terminal part of CARD8 is degraded by the proteasome, releasing the cleaved C-terminal part of the protein (Caspase recruitment domain-containing protein 8, C-terminus), which polymerizes to initiate the formation of the inflammasome complex: the CARD8 inflammasome directly recruits pro-caspase-1 (proCASP1) independently of PYCARD/ASC and promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), leading to pyroptosis (PubMed:32051255, PubMed:32840892, PubMed:33053349, PubMed:33542150, PubMed:36357533). Ability to sense HIV-1 protease activity leads to the clearance of latent HIV-1 in patient CD4(+) T-cells after viral reactivation; in contrast, HIV-1 can evade CARD8-sensing when its protease remains inactive in infected cells prior to viral budding (PubMed:33542150). Also acts as a negative regulator of the NLRP3 inflammasome (PubMed:24517500). May also act as an inhibitor of NF-kappa-B activation (PubMed:11551959, PubMed:12067710)", "gene_name": "CARD8", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y2G2", "name": "CARD6", "organism": "Homo sapiens", "uniprot_id": "Q9Y2G2" }, { "function": "May play a role in modulation of fibrillin microfibrils in the extracellular matrix (ECM)", "gene_name": "ADAMTSL5", "glycan_count": 2, "glycosylation_sites": [ { "position": 218, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6ZMM2", "name": "TMTC1", "organism": "Homo sapiens", "uniprot_id": "Q6ZMM2" }, { "function": "Transcription factor which acts as both an activator and a repressor (PubMed:34723967). Activates transcription of a number of genes including the heat shock chaperones HSPA1A and HSPA6 and the antioxidant NADPH-dependent reductase DHRS2 which are involved in protection against oxidative stress (PubMed:34723967). Required for normal brain development (By similarity)", "gene_name": "FOXR1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q6PIV2", "name": "Maltase-glucoamylase 2", "organism": "Homo sapiens", "uniprot_id": "Q6PIV2" }, { "function": "Can degrade fibrillar type I, II, and III collagens", "gene_name": "MMP8", "glycan_count": 2, "glycosylation_sites": [ { "position": 54, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 73, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 112, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 204, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 246, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P22894", "name": "MMP8", "organism": "Homo sapiens", "uniprot_id": "P22894" }, { "function": "Stearoyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates (PubMed:15907797, PubMed:18765284). Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA (PubMed:15907797, PubMed:18765284). Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids (PubMed:15610069). Plays an important role in lipid biosynthesis. Plays an important role in regulating the expression of genes that are involved in lipogenesis and in regulating mitochondrial fatty acid oxidation (By similarity). Plays an important role in body energy homeostasis (By similarity). Contributes to the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides (By similarity)", "gene_name": "SCD", "glycan_count": 1, "glycosylation_sites": [], "id": "O00767", "name": "Stearoyl-CoA desaturase", "organism": "Homo sapiens", "uniprot_id": "O00767" }, { "function": "Promotes absorption of the essential vitamin cobalamin (Cbl) in the ileum. After interaction with CUBN, the CBLIF-cobalamin complex is internalized via receptor-mediated endocytosis", "gene_name": "CBLIF", "glycan_count": 1, "glycosylation_sites": [ { "position": 311, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 330, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 334, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 413, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P27352", "name": "Gastric intrinsic factor", "organism": "Homo sapiens", "uniprot_id": "P27352" }, { "function": "Stimulates the release of tumor necrosis factor alpha and IL-1-beta from the monocytic cell line THP-1", "gene_name": "IL17B", "glycan_count": 0, "glycosylation_sites": [ { "position": 75, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UHF5", "name": "Kidney injury molecule-1 (KIM-1)", "organism": "Homo sapiens", "uniprot_id": "Q9UHF5" }, { "function": "Cell surface receptor that plays a role in various physiological processes including inflammation, phagocytosis, and cell adhesion. Plays a role in phagocytosis and enhances the uptake of apoptotic cells and immune complexes by acting as a receptor for defense collagens including surfactant protein A/SFTPA1, C1q, and mannose-binding lectin (MBL2) (PubMed:7977768). Plays a role in the regulation of endothelial cell function and adhesion by activating angiogenesis (PubMed:24809468). Mechanistically, exerts its angiogenic function by associating with beta-dystroglycan, leading to SRC-dependent phosphorylation and subsequent recruitment of CBL. In turn, CBL provides a docking site for downstream signaling components, such as CRKL to enhance cell migration (PubMed:26848865). Participates in angiogenesis also by acting as a receptor for the ECM pan-endothelial glycoprotein multimerin-2/MMRN2 and IGFBP7 ligands (PubMed:28671670, PubMed:36265539, PubMed:38218180). Both ligands play a non-redundant role in CD93-mediated endothelial cell function (PubMed:38218180). Acts as a key regulator of endothelial barrier function through modulating VEGFR2 function (By similarity)", "gene_name": "CD93", "glycan_count": 2, "glycosylation_sites": [ { "position": 325, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NPY3", "name": "LDL Receptor Adaptor Protein (LDLRAP)", "organism": "Homo sapiens", "uniprot_id": "Q9NPY3" }, { "function": "Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth (PubMed:7763314, PubMed:7903306). Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism (PubMed:14766016). It may also have a role in the development of malignancy and the growth progression of some tumors", "gene_name": "IMPDH2", "glycan_count": 1, "glycosylation_sites": [], "id": "P12268", "name": "Mycophenolate mofetil target (IMPDH2)", "organism": "Homo sapiens", "uniprot_id": "P12268" }, { "function": "", "gene_name": "N", "glycan_count": 0, "glycosylation_sites": [], "id": "Q66528", "name": "Hepatitis C virus envelope glycoprotein E2", "organism": "Equine arteritis virus", "uniprot_id": "Q66528" }, { "function": "Mediates sodium- and chloride-dependent transport of norepinephrine (also known as noradrenaline), the primary signaling neurotransmitter in the autonomic sympathetic nervous system (PubMed:2008212, PubMed:8125921, PubMed:38750358). Is responsible for norepinephrine re-uptake and clearance from the synaptic cleft, thus playing a crucial role in norepinephrine inactivation and homeostasis (By similarity). Can also mediate sodium- and chloride-dependent transport of dopamine (PubMed:11093780, PubMed:8125921, PubMed:39395208, PubMed:39048818)", "gene_name": "SLC6A2", "glycan_count": 0, "glycosylation_sites": [ { "position": 184, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 192, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 198, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P23975", "name": "Norepinephrine transporter (SLC6A2)", "organism": "Homo sapiens", "uniprot_id": "P23975" }, { "function": "Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. Beta-3 is involved in the regulation of lipolysis and thermogenesis", "gene_name": "ADRB3", "glycan_count": 0, "glycosylation_sites": [ { "position": 8, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 26, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P13945", "name": "beta-3 adrenergic receptor (\u03b23-AR)", "organism": "Homo sapiens", "uniprot_id": "P13945" }, { "function": "Catalytic subunit of protein phosphatase 2A (PP2A), a serine/threonine phosphatase involved in the regulation of a wide variety of enzymes, signal transduction pathways, and cellular events (PubMed:10801873, PubMed:12473674, PubMed:17245430, PubMed:22613722, PubMed:33243860, PubMed:34004147, PubMed:9920888). PP2A is the major phosphatase for microtubule-associated proteins (MAPs) (PubMed:22613722). PP2A can modulate the activity of phosphorylase B kinase casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase (PubMed:22613722). Cooperates with SGO2 to protect centromeric cohesin from separase-mediated cleavage in oocytes specifically during meiosis I (By similarity). Can dephosphorylate various proteins, such as SV40 large T antigen, AXIN1, p53/TP53, PIM3, WEE1 (PubMed:10801873, PubMed:12473674, PubMed:17245430, PubMed:9920888). Activates RAF1 by dephosphorylating it at 'Ser-259' (PubMed:10801873). Mediates dephosphorylation of WEE1, preventing its ubiquitin-mediated proteolysis, increasing WEE1 protein levels, and promoting the G2/M checkpoint (PubMed:33108758). Mediates dephosphorylation of MYC; promoting its ubiquitin-mediated proteolysis: interaction with AMBRA1 enhances interaction between PPP2CA and MYC (PubMed:25438055). Mediates dephosphorylation of FOXO3; promoting its stabilization: interaction with AMBRA1 enhances interaction between PPP2CA and FOXO3 (PubMed:30513302). Catalyzes dephosphorylation of the pyrin domain of NLRP3, promoting assembly of the NLRP3 inflammasome (By similarity). Together with RACK1 adapter, mediates dephosphorylation of AKT1 at 'Ser-473', preventing AKT1 activation and AKT-mTOR signaling pathway (By similarity). Dephosphorylation of AKT1 is essential for regulatory T-cells (Treg) homeostasis and stability (By similarity). Catalyzes dephosphorylation of PIM3, promotinh PIM3 ubiquitination and proteasomal degradation (PubMed:12473674). Part of the striatin-interacting phosphatase and kinase (STRIPAK) complexes (PubMed:33633399). STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling (PubMed:33633399). Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation (PubMed:33633399). Key mediator of a quality checkpoint during transcription elongation as part of the Integrator-PP2A (INTAC) complex (PubMed:33243860, PubMed:34004147, PubMed:37080207). The INTAC complex drives premature transcription termination of transcripts that are unfavorably configured for transcriptional elongation: within the INTAC complex, PPP2CA catalyzes dephosphorylation of the C-terminal domain (CTD) of Pol II subunit POLR2A/RPB1 and SUPT5H/SPT5, thereby preventing transcriptional elongation (PubMed:33243860, PubMed:34004147, PubMed:37080207)", "gene_name": "PPP2CA", "glycan_count": 1, "glycosylation_sites": [], "id": "P67775", "name": "Protein Phosphatase 2A (PP2A)", "organism": "Homo sapiens", "uniprot_id": "P67775" }, { "function": "Proline-directed serine/threonine-protein kinase essential for neuronal cell cycle arrest and differentiation and may be involved in apoptotic cell death in neuronal diseases by triggering abortive cell cycle re-entry. Interacts with D1 and D3-type G1 cyclins. Phosphorylates SRC, NOS3, VIM/vimentin, p35/CDK5R1, MEF2A, SIPA1L1, SH3GLB1, PXN, PAK1, MCAM/MUC18, SEPT5, SYN1, DNM1, AMPH, SYNJ1, CDK16, RAC1, RHOA, CDC42, TONEBP/NFAT5, MAPT/TAU, MAP1B, histone H1, p53/TP53, HDAC1, APEX1, PTK2/FAK1, huntingtin/HTT, ATM, MAP2, NEFH and NEFM. Regulates several neuronal development and physiological processes including neuronal survival, migration and differentiation, axonal and neurite growth, synaptogenesis, oligodendrocyte differentiation, synaptic plasticity and neurotransmission, by phosphorylating key proteins. Negatively regulates the CACNA1B/CAV2.2 -mediated Ca(2+) release probability at hippocampal neuronal soma and synaptic terminals (By similarity). Activated by interaction with CDK5R1 (p35) and CDK5R2 (p39), especially in postmitotic neurons, and promotes CDK5R1 (p35) expression in an autostimulation loop. Phosphorylates many downstream substrates such as Rho and Ras family small GTPases (e.g. PAK1, RAC1, RHOA, CDC42) or microtubule-binding proteins (e.g. MAPT/TAU, MAP2, MAP1B), and modulates actin dynamics to regulate neurite growth and/or spine morphogenesis. Also phosphorylates exocytosis associated proteins such as MCAM/MUC18, SEPT5, SYN1, and CDK16/PCTAIRE1 as well as endocytosis associated proteins such as DNM1, AMPH and SYNJ1 at synaptic terminals. In the mature central nervous system (CNS), regulates neurotransmitter movements by phosphorylating substrates associated with neurotransmitter release and synapse plasticity; synaptic vesicle exocytosis, vesicles fusion with the presynaptic membrane, and endocytosis. Promotes cell survival by activating anti-apoptotic proteins BCL2 and STAT3, and negatively regulating of JNK3/MAPK10 activity. Phosphorylation of p53/TP53 in response to genotoxic and oxidative stresses enhances its stabilization by preventing ubiquitin ligase-mediated proteasomal degradation, and induces transactivation of p53/TP53 target genes, thus regulating apoptosis. Phosphorylation of p35/CDK5R1 enhances its stabilization by preventing calpain-mediated proteolysis producing p25/CDK5R1 and avoiding ubiquitin ligase-mediated proteasomal degradation. During aberrant cell-cycle activity and DNA damage, p25/CDK5 activity elicits cell-cycle activity and double-strand DNA breaks that precedes neuronal death by deregulating HDAC1. DNA damage triggered phosphorylation of huntingtin/HTT in nuclei of neurons protects neurons against polyglutamine expansion as well as DNA damage mediated toxicity. Phosphorylation of PXN reduces its interaction with PTK2/FAK1 in matrix-cell focal adhesions (MCFA) during oligodendrocytes (OLs) differentiation. Negative regulator of Wnt/beta-catenin signaling pathway. Activator of the GAIT (IFN-gamma-activated inhibitor of translation) pathway, which suppresses expression of a post-transcriptional regulon of proinflammatory genes in myeloid cells; phosphorylates the linker domain of glutamyl-prolyl tRNA synthetase (EPRS) in a IFN-gamma-dependent manner, the initial event in assembly of the GAIT complex. Phosphorylation of SH3GLB1 is required for autophagy induction in starved neurons. Phosphorylation of TONEBP/NFAT5 in response to osmotic stress mediates its rapid nuclear localization. MEF2 is inactivated by phosphorylation in nucleus in response to neurotoxin, thus leading to neuronal apoptosis. APEX1 AP-endodeoxyribonuclease is repressed by phosphorylation, resulting in accumulation of DNA damage and contributing to neuronal death. NOS3 phosphorylation down regulates NOS3-derived nitrite (NO) levels. SRC phosphorylation mediates its ubiquitin-dependent degradation and thus leads to cytoskeletal reorganization. May regulate endothelial cell migration and angiogenesis via the modulation of lamellipodia formation. Involved in dendritic spine morphogenesis by mediating the EFNA1-EPHA4 signaling. The complex p35/CDK5 participates in the regulation of the circadian clock by modulating the function of CLOCK protein: phosphorylates CLOCK at 'Thr-451' and 'Thr-461' and regulates the transcriptional activity of the CLOCK-BMAL1 heterodimer in association with altered stability and subcellular distribution", "gene_name": "CDK5", "glycan_count": 1, "glycosylation_sites": [], "id": "Q00535", "name": "Cyclin-dependent kinase 5 (Cdk5)", "organism": "Homo sapiens", "uniprot_id": "Q00535" }, { "function": "Plays a role in neuronal development and polarity, as well as in axon growth and guidance, neuronal growth cone collapse and cell migration. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. May play a role in endocytosis", "gene_name": "DPYSL2", "glycan_count": 5, "glycosylation_sites": [], "id": "Q16555", "name": "Collapsin response mediator protein 2 (CRMP2)", "organism": "Homo sapiens", "uniprot_id": "Q16555" }, { "function": "S1 region attaches the virion to the cell membrane by interacting with host ACE2, initiating the infection (PubMed:15897467, PubMed:19901337, PubMed:29142129). Binding to the receptor probably induces conformational changes in the S glycoprotein unmasking the fusion peptide and activating membranes fusion. S2 region belongs to the class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes", "gene_name": "S", "glycan_count": 0, "glycosylation_sites": [ { "position": 35, "type": "N-linked (GlcNAc) asparagine; by host" }, { "position": 52, "type": "N-linked (GlcNAc) asparagine; by host" }, { "position": 98, "type": "N-linked (GlcNAc) asparagine; by host" }, { "position": 155, "type": "N-linked (GlcNAc) asparagine; by host" }, { "position": 187, "type": "N-linked (GlcNAc) asparagine; by host" }, { "position": 193, "type": "N-linked (GlcNAc) asparagine; by host" }, { "position": 240, "type": "N-linked (GlcNAc) asparagine; by host" }, { "position": 276, "type": "N-linked (GlcNAc) asparagine; by host" }, { "position": 301, "type": "N-linked (GlcNAc) asparagine; by host" }, { "position": 330, "type": "N-linked (GlcNAc) asparagine; by host" }, { "position": 354, "type": "N-linked (GlcNAc) asparagine; by host" }, { "position": 358, "type": "N-linked (GlcNAc) asparagine; by host" }, { "position": 403, "type": "N-linked (GlcNAc) asparagine; by host" }, { "position": 426, "type": "N-linked (GlcNAc) asparagine; by host" }, { "position": 486, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 506, "type": "N-linked (GlcNAc) asparagine; by host" }, { "position": 512, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 626, "type": "N-linked (GlcNAc) asparagine; by host" }, { "position": 645, "type": "N-linked (GlcNAc) asparagine; by host" }, { "position": 666, "type": "N-linked (GlcNAc) asparagine; by host" }, { "position": 699, "type": "N-linked (GlcNAc) asparagine; by host" }, { "position": 723, "type": "N-linked (GlcNAc) asparagine; by host" }, { "position": 749, "type": "N-linked (GlcNAc) asparagine; by host" }, { "position": 762, "type": "N-linked (GlcNAc) asparagine; by host" }, { "position": 768, "type": "N-linked (GlcNAc) asparagine; by host" }, { "position": 1111, "type": "N-linked (GlcNAc) asparagine; by host" }, { "position": 1196, "type": "N-linked (GlcNAc) asparagine; by host" }, { "position": 1201, "type": "N-linked (GlcNAc) asparagine; by host" }, { "position": 1218, "type": "N-linked (GlcNAc) asparagine; by host" }, { "position": 1242, "type": "N-linked (GlcNAc) asparagine; by host" }, { "position": 1247, "type": "N-linked (GlcNAc) asparagine; by host" }, { "position": 1277, "type": "N-linked (GlcNAc) asparagine; by host" } ], "id": "Q6Q1S2", "name": "Hemagglutinin-Esterase (HE) glycoprotein", "organism": "Human coronavirus NL63", "uniprot_id": "Q6Q1S2" }, { "function": "Plays a central role in virus morphogenesis and assembly. Acts as a viroporin and self-assembles in host membranes forming pentameric protein-lipid pores that allow ion transport. Also plays a role in the induction of apoptosis (By similarity). Regulates the localization of S protein at cis-Golgi, the place of virus budding (PubMed:33229438). May act by slowing down the cell secretory pathway (PubMed:33229438). May interfere with tight-junction stability by interacting with host MPP5. This would result in disruption of epithelial barriers, thereby amplifying inflammatory processes (PubMed:32891874)", "gene_name": "E", "glycan_count": 0, "glycosylation_sites": [], "id": "P0DTC4", "name": "Envelope (E) protein", "organism": "Severe acute respiratory syndrome coronavirus 2", "uniprot_id": "P0DTC4" }, { "function": "Component of the viral envelope that plays a central role in virus morphogenesis and assembly via its interactions with other viral proteins (By similarity). Regulates the localization of S protein at cis-Golgi, the place of virus budding (PubMed:33229438). May act by binding cytoplasmic c-terminus of S (PubMed:33229438)", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [ { "position": 5, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P0DTC5", "name": "Membrane (M) protein", "organism": "Severe acute respiratory syndrome coronavirus 2", "uniprot_id": "P0DTC5" }, { "function": "Relaxin is an ovarian hormone that acts with estrogen to produce dilatation of the birth canal in many mammals. May be involved in remodeling of connective tissues during pregnancy, promoting growth of pubic ligaments and ripening of the cervix", "gene_name": "RLN1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UQJ1", "name": "gp60 glycoprotein (Cryptosporidium parvum)", "organism": "Homo sapiens", "uniprot_id": "P04808" }, { "function": "Relaxin is an ovarian hormone that acts with estrogen to produce dilatation of the birth canal in many mammals. May be involved in remodeling of connective tissues during pregnancy, promoting growth of pubic ligaments and ripening of the cervix", "gene_name": "RLN2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UQJ2", "name": "\u03b2-giardin (Giardia duodenalis)", "organism": "Homo sapiens", "uniprot_id": "P04090" }, { "function": "As a component of the mitochondrial large ribosomal subunit, plays a role in mitochondrial translation (PubMed:23603806). When present in mitochondria as a free protein not associated with the ribosome, associates with mitochondrial RNA polymerase POLRMT to activate transcription (PubMed:22003127). Required for POLRMT stability (PubMed:26586915)", "gene_name": "MRPL12", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UQJ3", "name": "triosephosphate isomerase (Giardia duodenalis)", "organism": "Homo sapiens", "uniprot_id": "P52815" }, { "function": "Regulates clathrin-mediated receptor endocytosis (PubMed:18657069). Plays a role in the process of neurogenesis (By similarity). Required throughout embryonic neurogenesis to maintain neural progenitor cells, also called radial glial cells (RGCs), by allowing their daughter cells to choose progenitor over neuronal cell fate (By similarity). Not required for the proliferation of neural progenitor cells before the onset of neurogenesis. Also involved postnatally in the subventricular zone (SVZ) neurogenesis by regulating SVZ neuroblasts survival and ependymal wall integrity (By similarity). May also mediate local repair of brain ventricular wall damage (By similarity)", "gene_name": "NUMB", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UQJ4", "name": "glutamate dehydrogenase (Giardia duodenalis)", "organism": "Homo sapiens", "uniprot_id": "P49757" }, { "function": "Receptor for the C-X3-C chemokine fractalkine (CX3CL1) present on many early leukocyte cells; CX3CR1-CX3CL1 signaling exerts distinct functions in different tissue compartments, such as immune response, inflammation, cell adhesion and chemotaxis (PubMed:12055230, PubMed:23125415, PubMed:9390561, PubMed:9782118). CX3CR1-CX3CL1 signaling mediates cell migratory functions (By similarity). Responsible for the recruitment of natural killer (NK) cells to inflamed tissues (By similarity). Acts as a regulator of inflammation process leading to atherogenesis by mediating macrophage and monocyte recruitment to inflamed atherosclerotic plaques, promoting cell survival (By similarity). Involved in airway inflammation by promoting interleukin 2-producing T helper (Th2) cell survival in inflamed lung (By similarity). Involved in the migration of circulating monocytes to non-inflamed tissues, where they differentiate into macrophages and dendritic cells (By similarity). Acts as a negative regulator of angiogenesis, probably by promoting macrophage chemotaxis (PubMed:14581400, PubMed:18971423). Plays a key role in brain microglia by regulating inflammatory response in the central nervous system (CNS) and regulating synapse maturation (By similarity). Required to restrain the microglial inflammatory response in the CNS and the resulting parenchymal damage in response to pathological stimuli (By similarity). Involved in brain development by participating in synaptic pruning, a natural process during which brain microglia eliminates extra synapses during postnatal development (By similarity). Synaptic pruning by microglia is required to promote the maturation of circuit connectivity during brain development (By similarity). Acts as an important regulator of the gut microbiota by controlling immunity to intestinal bacteria and fungi (By similarity). Expressed in lamina propria dendritic cells in the small intestine, which form transepithelial dendrites capable of taking up bacteria in order to provide defense against pathogenic bacteria (By similarity). Required to initiate innate and adaptive immune responses against dissemination of commensal fungi (mycobiota) component of the gut: expressed in mononuclear phagocytes (MNPs) and acts by promoting induction of antifungal IgG antibodies response to confer protection against disseminated C.albicans or C.auris infection (PubMed:29326275). Also acts as a receptor for C-C motif chemokine CCL26, inducing cell chemotaxis (PubMed:20974991)", "gene_name": "CX3CR1", "glycan_count": 0, "glycosylation_sites": [], "id": "P49238", "name": "CX3CR1", "organism": "Homo sapiens", "uniprot_id": "P49238" }, { "function": "Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR3 is a nucleotide-sensing TLR which is activated by double-stranded RNA, a sign of viral infection. Acts via the adapter TRIF/TICAM1, leading to NF-kappa-B activation, IRF3 nuclear translocation, cytokine secretion and the inflammatory response", "gene_name": "TLR3", "glycan_count": 35, "glycosylation_sites": [ { "position": 52, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 57, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 70, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 124, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 196, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 247, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 252, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 265, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 275, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 291, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 398, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 413, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 507, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 636, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 662, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O15455", "name": "TLR3", "organism": "Homo sapiens", "uniprot_id": "O15455" }, { "function": "Plays a role in the regulation of innate resistance to pathogens, inflammatory reactions, possibly clearance of self-components and female fertility", "gene_name": "PTX3", "glycan_count": 6, "glycosylation_sites": [ { "position": 220, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P26022", "name": "Pentraxin-3 (PTX3)", "organism": "Homo sapiens", "uniprot_id": "P26022" }, { "function": "Cytosolic calcium-activated calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytosol and thereby plays a key role in triggering cardiac muscle contraction. Aberrant channel activation can lead to cardiac arrhythmia. In cardiac myocytes, calcium release is triggered by increased Ca(2+) cytosolic levels due to activation of the L-type calcium channel CACNA1C. The calcium channel activity is modulated by formation of heterotetramers with RYR3. Required for cellular calcium ion homeostasis. Required for embryonic heart development", "gene_name": "RYR2", "glycan_count": 2, "glycosylation_sites": [], "id": "Q92736", "name": "Ryanodine receptor 2 (RyR2)", "organism": "Homo sapiens", "uniprot_id": "Q92736" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "XP_053541768.1", "name": "IpSTING", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03437 (H3N2)", "name": "Influenza virus hemagglutinin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03468 (H3N2)", "name": "Influenza virus neuraminidase", "organism": "", "uniprot_id": "" }, { "function": "The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Following initial binding to host receptor, membrane fusion is mediated by the fusion machinery composed of gB and the heterodimer gH/gL. May also be involved in the fusion between the virion envelope and the outer nuclear membrane during virion morphogenesis", "gene_name": "gH", "glycan_count": 0, "glycosylation_sites": [ { "position": 73, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 120, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 216, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 332, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 437, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 670, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 784, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P06477", "name": "Herpes simplex virus-1 glycoprotein D (gD)", "organism": "Human herpesvirus 1 (strain 17)", "uniprot_id": "P06477" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Q6P6", "name": "West Nile virus envelope protein", "organism": "Grapevine leafroll-associated virus 1", "uniprot_id": "Q9Q6P6" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P29990 (type 1), Q6YMS4 (type 4)", "name": "Dengue virus envelope protein (types 1 and 4)", "organism": "", "uniprot_id": "" }, { "function": "Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosacharides, bile acids and xenobiotics substrates. Key enzyme in the polyol pathway, catalyzes reduction of glucose to sorbitol during hyperglycemia (PubMed:1936586). Reduces steroids and their derivatives and prostaglandins. Displays low enzymatic activity toward all-trans-retinal, 9-cis-retinal, and 13-cis-retinal (PubMed:12732097, PubMed:19010934, PubMed:8343525). Catalyzes the reduction of diverse phospholipid aldehydes such as 1-palmitoyl-2-(5-oxovaleroyl)-sn -glycero-3-phosphoethanolamin (POVPC) and related phospholipid aldehydes that are generated from the oxydation of phosphotidylcholine and phosphatdyleethanolamides (PubMed:17381426). Plays a role in detoxifying dietary and lipid-derived unsaturated carbonyls, such as crotonaldehyde, 4-hydroxynonenal, trans-2-hexenal, trans-2,4-hexadienal and their glutathione-conjugates carbonyls (GS-carbonyls) (PubMed:21329684)", "gene_name": "AKR1B1", "glycan_count": 1, "glycosylation_sites": [], "id": "P15121", "name": "Aldose reductase (ALR2)", "organism": "Homo sapiens", "uniprot_id": "P15121" }, { "function": "Plays a role in modulating the host immune response (PubMed:31986261, PubMed:35343786, PubMed:36689483). May act as a secreted virokine by mimicking interleukin-17A (IL17A), and thereby binding to the IL17RA receptor, leading to activation of the IL17 pathway and increased secretion of pro-inflammatory factors (PubMed:35343786, PubMed:36689483). Contributes to the cytokine storm during SARS-CoV-2 infection when secreted by unconventional pathway (PubMed:33723527, PubMed:36689483). May act by down-regulating major histocompability complex class I (MHC-I) at cell surface (PubMed:34021074, PubMed:35157849). May inhibit expression of some members of the IFN-stimulated gene (ISG) family including hosts IGF2BP1/ZBP1, MX1 and MX2, and DHX58 (PubMed:34177923)", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [ { "position": 78, "type": "N-linked (GlcNAc...) (complex) asparagine; by host" } ], "id": "P0DTC8", "name": "ORF8 protein", "organism": "Severe acute respiratory syndrome coronavirus 2", "uniprot_id": "P0DTC8" }, { "function": "Plays a role as antagonist of host tetherin (BST2), disrupting its antiviral effect (PubMed:33930332). Acts by binding to BST2 and sequestering it to perinuclear region, thereby preventing its antiviral function at cell membrane (PubMed:33930332). May specifically downregulate MHC-I allele HLA-A*02:01 (HLA-A2) (PubMed:36574644)", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P0DTC7", "name": "ORF7a protein", "organism": "Severe acute respiratory syndrome coronavirus 2", "uniprot_id": "P0DTC7" }, { "function": "Substrate-recognition component of some SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complexes. Involved in endoplasmic reticulum-associated degradation pathway (ERAD) for misfolded lumenal proteins by recognizing and binding sugar chains on unfolded glycoproteins that are retrotranslocated into the cytosol and promoting their ubiquitination and subsequent degradation. Able to recognize and bind denatured glycoproteins, which are modified with not only high-mannose but also complex-type oligosaccharides. Also recognizes sulfated glycans. Also involved in DNA damage response by specifically recognizing activated CHEK1 (phosphorylated on 'Ser-345'), promoting its ubiquitination and degradation. Ubiquitination of CHEK1 is required to ensure that activated CHEK1 does not accumulate as cells progress through S phase, or when replication forks encounter transient impediments during normal DNA replication", "gene_name": "FBXO6", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NRD1", "name": "Ferroportin (FPN)", "organism": "Homo sapiens", "uniprot_id": "Q9NRD1" }, { "function": "Liver-produced hormone that constitutes the main circulating regulator of iron absorption and distribution across tissues. Acts by promoting endocytosis and degradation of ferroportin/SLC40A1, leading to the retention of iron in iron-exporting cells and decreased flow of iron into plasma (PubMed:22682227, PubMed:29237594, PubMed:32814342). Controls the major flows of iron into plasma: absorption of dietary iron in the intestine, recycling of iron by macrophages, which phagocytose old erythrocytes and other cells, and mobilization of stored iron from hepatocytes (PubMed:22306005)", "gene_name": "HAMP", "glycan_count": 0, "glycosylation_sites": [], "id": "P81172", "name": "Hepcidin", "organism": "Homo sapiens", "uniprot_id": "P81172" }, { "function": "Serine protease inhibitor. The major targets of this inhibitor are plasmin and trypsin, but it also inactivates matriptase-3/TMPRSS7 and chymotrypsin", "gene_name": "SERPINF2", "glycan_count": 8, "glycosylation_sites": [ { "position": 126, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 295, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 309, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 316, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08697", "name": "Apolipoprotein C-III (ApoC-III)", "organism": "Homo sapiens", "uniprot_id": "P08697" }, { "function": "Modulates RecA activity", "gene_name": "recX", "glycan_count": 0, "glycosylation_sites": [], "id": "P0DD93", "name": "M protein", "organism": "Streptococcus pyogenes serotype M3 (strain SSI-1)", "uniprot_id": "P0DD93" }, { "function": "Modulates arousal and anxiety. May play an important anorexigenic role (By similarity). Binds to its receptor NPSR1 with nanomolar affinity to increase intracellular calcium concentrations (PubMed:15312648, PubMed:16790440)", "gene_name": "NPS", "glycan_count": 0, "glycosylation_sites": [], "id": "P0C0P6", "name": "Streptococcal pyrogenic exotoxin A (SpeA)", "organism": "Homo sapiens", "uniprot_id": "P0C0P6" }, { "function": "May play an important anorexigenic role. Modulates arousal and anxiety as well as increases locomotor activity. Binds to its receptor NPSR1 with nanomolar affinity to increase intracellular calcium concentrations", "gene_name": "Nps", "glycan_count": 0, "glycosylation_sites": [], "id": "P0C0P8", "name": "Streptococcal pyrogenic exotoxin C (SpeC)", "organism": "Mus musculus", "uniprot_id": "P0C0P8" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9A0W0", "name": "Streptococcal superantigen (SSA)", "organism": "Streptococcus pyogenes serotype M1", "uniprot_id": "Q9A0W0" }, { "function": "Required for CpsD phosphorylation (By similarity). Involved in the regulation of capsular polysaccharide biosynthesis. May be part of a complex that directs the coordinated polymerization and export to the cell surface of the capsular polysaccharide (By similarity)", "gene_name": "cpsC", "glycan_count": 0, "glycosylation_sites": [], "id": "P0C0T8", "name": "Streptolysin O", "organism": "Streptococcus agalactiae", "uniprot_id": "P0C0T8" }, { "function": "", "gene_name": "Amy2a5", "glycan_count": 0, "glycosylation_sites": [], "id": "P00688", "name": "Streptokinase", "organism": "Mus musculus", "uniprot_id": "P00688" }, { "function": "Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding", "gene_name": "groEL", "glycan_count": 0, "glycosylation_sites": [], "id": "P0C0N7", "name": "Hyaluronidase", "organism": "Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200)", "uniprot_id": "P0C0N7" }, { "function": "This toxin kills sensitive strains of yeast", "gene_name": "SMK1", "glycan_count": 0, "glycosylation_sites": [ { "position": 127, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P19972", "name": "Cysteine proteinase SpeB", "organism": "Millerozyma farinosa", "uniprot_id": "P19972" }, { "function": "Collagen-binding adhesin that mediates bacterial adherence to collagenous tissues such as cartilage (PubMed:8218209). Participates in the infectious process by acting as a virulence factor in many different animal models of staphylococcal infections including arthritis, endocarditis and keratitis (PubMed:10816547, PubMed:15181582). Inhibits the activation of the classical complement pathway by interacting with host C1q and interfering with the association between host C1r with C1q (PubMed:23720782)", "gene_name": "cna", "glycan_count": 0, "glycosylation_sites": [], "id": "Q53654", "name": "C5a peptidase", "organism": "Staphylococcus aureus", "uniprot_id": "Q53654" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04578/P04578", "name": "HIV-1 gp120/gp41 (Env)", "organism": "", "uniprot_id": "" }, { "function": "Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis (PubMed:25122912). Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(o) and JIP. Inhibits G(o) alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity). By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapses in axons (PubMed:17062754, PubMed:23011729). Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1", "gene_name": "APP", "glycan_count": 0, "glycosylation_sites": [ { "position": 542, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 571, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 633, "type": "O-linked (GalNAc...) threonine; partial" }, { "position": 651, "type": "O-linked (GalNAc...) threonine; partial" }, { "position": 652, "type": "O-linked (GalNAc...) threonine; partial" }, { "position": 656, "type": "O-linked (Xyl...) (chondroitin sulfate) serine; in L-APP isoforms" }, { "position": 659, "type": "O-linked (HexNAc...) threonine; partial" }, { "position": 663, "type": "O-linked (GalNAc...) threonine; partial" }, { "position": 667, "type": "O-linked (GalNAc...) serine; partial" }, { "position": 681, "type": "O-linked (HexNAc...) tyrosine; partial" } ], "id": "Q8WZ99", "name": "Human metapneumovirus Fusion (F) glycoprotein", "organism": "Homo sapiens", "uniprot_id": "P05067" }, { "function": "Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters", "gene_name": "WNT11", "glycan_count": 0, "glycosylation_sites": [ { "position": 40, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 90, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 160, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 300, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 304, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8WZ98", "name": "Human metapneumovirus Attachment (G) glycoprotein", "organism": "Homo sapiens", "uniprot_id": "O96014" }, { "function": "Encapsidates the genome protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid (NC) and serves as template for transcription and replication. The NC have a helical organization. Seems to participate in the nuclear relocalization of host PABP1, thereby inhibiting host cellular translation", "gene_name": "N", "glycan_count": 0, "glycosylation_sites": [], "id": "P04873", "name": "PIV5 Fusion (F) Glycoprotein", "organism": "Bunyavirus La Crosse", "uniprot_id": "P04873" }, { "function": "Inhibits host transcriptional machinery, by producing modifications to the phosphorylation state of the C-terminal domain (CTD) of RNA polymerase II. Inhibits phosphorylation at serine 2 in the heptapeptide repeat (YSPTSPS) of the CTD of RNA polymerase II, suggesting that the elongation step of transcription and/or 3'-end processing is prevented. Inhibition of host transcription machinery leads to shut off of host cell protein synthesis and inhibition of the host innate immune response. NSs also seems to be involved in the nuclear relocalization of host PABP1 (By similarity)", "gene_name": "N", "glycan_count": 0, "glycosylation_sites": [], "id": "P04874", "name": "PIV5 Hemagglutinin-Neuraminidase (HN) Glycoprotein", "organism": "Bunyavirus La Crosse", "uniprot_id": "P04874" }, { "function": "Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. During viral entry or virus-mediated fusion between infected cells and neighboring susceptible cells, the head domain of the H protein initially binds to its receptor and then the stalk region of the H protein transmits the fusion-triggering signal to the F protein (By similarity). Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis (By similarity)", "gene_name": "F", "glycan_count": 0, "glycosylation_sites": [ { "position": 29, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 61, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 67, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P69353", "name": "Measles Virus Hemagglutinin (H) Glycoprotein", "organism": "Measles virus (strain Edmonston)", "uniprot_id": "P69353" }, { "function": "This protein recognizes C4b and C3b fragments that condense with cell-surface hydroxyl or amino groups when nascent C4b and C3b are locally generated during C4 and c3 activation. Interaction of daf with cell-associated C4b and C3b polypeptides interferes with their ability to catalyze the conversion of C2 and factor B to enzymatically active C2a and Bb and thereby prevents the formation of C4b2a and C3bBb, the amplification convertases of the complement cascade (PubMed:7525274). Inhibits complement activation by destabilizing and preventing the formation of C3 and C5 convertases, which prevents complement damage (PubMed:28657829)", "gene_name": "CD55", "glycan_count": 15, "glycosylation_sites": [ { "position": 95, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08174", "name": "CD55 (Decay-Accelerating Factor)", "organism": "Homo sapiens", "uniprot_id": "P08174" }, { "function": "O-methyltransferase required for two non-consecutive steps during ubiquinone biosynthesis (By similarity) (PubMed:10777520, PubMed:38425362). Catalyzes the 2 O-methylation of 3,4-dihydroxy-5-(all-trans-decaprenyl)benzoic acid into 4-hydroxy-3-methoxy-5-(all-trans-decaprenyl)benzoic acid (By similarity) (PubMed:10777520, PubMed:38425362). Also catalyzes the last step of ubiquinone biosynthesis by mediating methylation of 3-demethylubiquinone into ubiquinone (By similarity) (PubMed:38425362). Also able to mediate the methylation of 3-demethylubiquinol-10 into ubiquinol-10 (By similarity) (PubMed:10777520)", "gene_name": "COQ3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NZJ6", "name": "Alemtuzumab", "organism": "Homo sapiens", "uniprot_id": "Q9NZJ6" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8B9M1 (for PRRSV-2 GP5, representative)", "name": "Glycoprotein 5 (GP5)", "organism": "", "uniprot_id": "" }, { "function": "May have regulatory role in cell division or differentiation in response to extracellular signals", "gene_name": "Skil", "glycan_count": 1, "glycosylation_sites": [], "id": "Q60665", "name": "F4/80", "organism": "Mus musculus", "uniprot_id": "Q60665" }, { "function": "Transcription factor that plays a key role in the response to oxidative stress: binds to antioxidant response (ARE) elements present in the promoter region of many cytoprotective genes, such as phase 2 detoxifying enzymes, and promotes their expression, thereby neutralizing reactive electrophiles (PubMed:12032331, PubMed:14517290, PubMed:14517554, PubMed:31398338, PubMed:9240432, PubMed:9887101). In normal conditions, ubiquitinated and degraded in the cytoplasm by the BCR(KEAP1) complex (PubMed:14517290, PubMed:15282312, PubMed:15367669, PubMed:15581590). In response to oxidative stress, electrophile metabolites inhibit activity of the BCR(KEAP1) complex, promoting nuclear accumulation of NFE2L2/NRF2, heterodimerization with one of the small Maf proteins and binding to ARE elements of cytoprotective target genes (PubMed:12032331). The NFE2L2/NRF2 pathway is also activated in response to selective autophagy: autophagy promotes interaction between KEAP1 and SQSTM1/p62 and subsequent inactivation of the BCR(KEAP1) complex, leading to NFE2L2/NRF2 nuclear accumulation and expression of cytoprotective genes (PubMed:20173742, PubMed:20421418). The NFE2L2/NRF2 pathway is also activated during the unfolded protein response (UPR), contributing to redox homeostasis and cell survival following endoplasmic reticulum stress (PubMed:14517290, PubMed:14978030). May also be involved in the transcriptional activation of genes of the beta-globin cluster by mediating enhancer activity of hypersensitive site 2 of the beta-globin locus control region (By similarity). Also plays an important role in the regulation of the innate immune response. It is a critical regulator of the innate immune response and survival during sepsis by maintaining redox homeostasis and restraint of the dysregulation of pro-inflammatory signaling pathways like MyD88-dependent and -independent and TNF-alpha signaling (PubMed:16585964). Suppresses macrophage inflammatory response by blocking pro-inflammatory cytokine transcription and the induction of IL6 (PubMed:27211851). Binds to the proximity of pro-inflammatory genes in macrophages and inhibits RNA Pol II recruitment. The inhibition is independent of the Nrf2-binding motif and reactive oxygen species level (PubMed:27211851). Represses antiviral cytosolic DNA sensing by suppressing the expression of the adapter protein STING1 and decreasing responsiveness to STING1 agonists while increasing susceptibility to infection with DNA viruses (By similarity)", "gene_name": "Nfe2l2", "glycan_count": 0, "glycosylation_sites": [ { "position": 454, "type": "N-linked (Glc) (glycation) lysine" }, { "position": 464, "type": "N-linked (Glc) (glycation) lysine" }, { "position": 479, "type": "N-linked (Glc) (glycation) lysine" }, { "position": 491, "type": "N-linked (Glc) (glycation) arginine" }, { "position": 561, "type": "N-linked (Glc) (glycation) arginine" }, { "position": 566, "type": "N-linked (Glc) (glycation) lysine" } ], "id": "Q60795", "name": "Nrf2", "organism": "Mus musculus", "uniprot_id": "Q60795" }, { "function": "Acyl-CoA synthetases (ACSL) activates long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation (PubMed:22633490). Required for the incorporation of fatty acids into phosphatidylcholine, the major phospholipid located on the surface of VLDL (very low density lipoproteins) (PubMed:18003621). Has mainly an anabolic role in energy metabolism. Mediates hepatic lipogenesis. Preferentially uses myristate, laurate, arachidonate and eicosapentaenoate as substrates. Both isoforms exhibit the same level of activity (By similarity)", "gene_name": "ACSL3", "glycan_count": 1, "glycosylation_sites": [], "id": "O95573", "name": "ACSL4", "organism": "Homo sapiens", "uniprot_id": "O95573" }, { "function": "Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the host nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals that are responsible for the active RNP import into the nucleus through cellular importin alpha/beta pathway. Later in the infection, nclear export of RNPs are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that nucleoprotein binds directly host exportin-1/XPO1 and plays an active role in RNPs nuclear export. M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmasks nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus", "gene_name": "NP", "glycan_count": 0, "glycosylation_sites": [], "id": "P03466", "name": "NP (Influenza nucleoprotein)", "organism": "Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)", "uniprot_id": "P03466" }, { "function": "Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes (By similarity). Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system (By similarity). Upon stimulation, positively regulates T and B cell proliferation through iron uptake (PubMed:26642240). Acts as a lipid sensor that regulates mitochondrial fusion by regulating activation of the JNK pathway (By similarity). When dietary levels of stearate (C18:0) are low, promotes activation of the JNK pathway, resulting in HUWE1-mediated ubiquitination and subsequent degradation of the mitofusin MFN2 and inhibition of mitochondrial fusion (By similarity). When dietary levels of stearate (C18:0) are high, TFRC stearoylation inhibits activation of the JNK pathway and thus degradation of the mitofusin MFN2 (By similarity). Mediates uptake of NICOL1 into fibroblasts where it may regulate extracellular matrix production (PubMed:38625739)", "gene_name": "Tfrc", "glycan_count": 7, "glycosylation_sites": [ { "position": 104, "type": "O-linked (GalNAc...) threonine" }, { "position": 253, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 319, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 725, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 730, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q62351", "name": "CD71 (Transferrin receptor)", "organism": "Mus musculus", "uniprot_id": "Q62351" }, { "function": "Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moieties on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication", "gene_name": "NA", "glycan_count": 0, "glycosylation_sites": [ { "position": 44, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 58, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 73, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 131, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 220, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P03468", "name": "Neuraminidase (NA)", "organism": "Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)", "uniprot_id": "P03468" }, { "function": "Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin", "gene_name": "TUBB", "glycan_count": 1, "glycosylation_sites": [], "id": "P07437", "name": "Tubulin beta chain", "organism": "Homo sapiens", "uniprot_id": "P07437" }, { "function": "Envelope glycoprotein that plays a role in host cell entry, cell to-cell virus transmission, and fusion of infected cells. May be involved in the initial attachment via binding to heparan sulfate together with the gM/gN complex that binds heparin with higher affinity. Interacts with host integrin ITGB1, PDGFRA and EGFR that likely serve as postattachment entry receptors. Also participates in the fusion of viral and cellular membranes leading to virus entry into the host cell. Membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL", "gene_name": "gB", "glycan_count": 0, "glycosylation_sites": [ { "position": 37, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 68, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 73, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 85, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 208, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 281, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 286, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 302, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 341, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 383, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 405, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 409, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 417, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 447, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 452, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 464, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 465, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 554, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 585, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P06473", "name": "Cytomegalovirus glycoprotein B (gB)", "organism": "Human cytomegalovirus (strain AD169)", "uniprot_id": "P06473" }, { "function": "Plays an important role in transactivating viral early genes as well as activating its own promoter, probably by altering the viral chromatin structure (By similarity). Expression of IE1 and IE2 proteins is critical for the establishment of lytic infection and reactivation from viral latency (PubMed:27466417). Disrupts PML-associated ND10 nuclear bodies by interfering with host PML and SP100 sumoylation thereby altering the regulation of type I and type II interferon-induced gene expression (PubMed:27903803, PubMed:34370791). Promotes efficient viral growth by interacting with and directing host SP100 to degradation, leading to enhanced acetylation level of histones (By similarity). In addition, functions in counteracting the host innate antiviral response. Inhibits the type I interferon pathway by directly interacting with and sequestrating host STAT2 (By similarity). Also targets type II interferon pathway by repressing IL6- and STAT3 target genes (By similarity). Repression of STAT3 genes is due to STAT3 nuclear accumulation and disruption of IL6-induced STAT3 phosphorylation by IE1 (PubMed:23903834). This repression is followed by phosphorylation and activation of STAT1 (By similarity). Inhibits host ISG transcription by sequestering host ISGF3 in a PML- and STAT2- binding dependent manner (By similarity). Alters host cell cycle progression, probably through its interaction with host E2F1 or RB1 that overcomes the RB1-mediated repression of E2F-responsive promoters (By similarity)", "gene_name": "UL123", "glycan_count": 0, "glycosylation_sites": [], "id": "P13202", "name": "Cytomegalovirus Immediate-Early 1 (IE-1)", "organism": "Human cytomegalovirus (strain AD169)", "uniprot_id": "P13202" }, { "function": "Plays a role in the innate immune response. Binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria (PubMed:24120359, PubMed:7517398). Acts as an affinity enhancer for CD14, facilitating its association with LPS. Promotes the release of cytokines in response to bacterial lipopolysaccharide (PubMed:24120359, PubMed:7517398)", "gene_name": "LBP", "glycan_count": 7, "glycosylation_sites": [ { "position": 300, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 355, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 386, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 394, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P18428", "name": "Lipopolysaccharide-binding protein (LBP)", "organism": "Homo sapiens", "uniprot_id": "P18428" }, { "function": "", "gene_name": "N", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9QF67", "name": "CMV UL18", "organism": "Hantavirus HTN/Far East/4211", "uniprot_id": "Q9QF67" }, { "function": "", "gene_name": "N", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9QF65", "name": "CMV US28", "organism": "Hantavirus HTN/Far East/3829", "uniprot_id": "Q9QF65" }, { "function": "Phosphoinositide-3-kinase (PI3K) phosphorylates phosphatidylinositol (PI) and its phosphorylated derivatives at position 3 of the inositol ring to produce 3-phosphoinositides (PubMed:9235916). Uses ATP and PtdIns(4,5)P2 (phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3) (PubMed:15135396). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Mediates immune responses. Plays a role in B-cell development, proliferation, migration, and function. Required for B-cell receptor (BCR) signaling. Mediates B-cell proliferation response to anti-IgM, anti-CD40 and IL4 stimulation. Promotes cytokine production in response to TLR4 and TLR9. Required for antibody class switch mediated by TLR9. Involved in the antigen presentation function of B-cells. Involved in B-cell chemotaxis in response to CXCL13 and sphingosine 1-phosphate (S1P). Required for proliferation, signaling and cytokine production of naive, effector and memory T-cells. Required for T-cell receptor (TCR) signaling. Mediates TCR signaling events at the immune synapse. Activation by TCR leads to antigen-dependent memory T-cell migration and retention to antigenic tissues. Together with PIK3CG participates in T-cell development. Contributes to T-helper cell expansion and differentiation. Required for T-cell migration mediated by homing receptors SELL/CD62L, CCR7 and S1PR1 and antigen dependent recruitment of T-cells. Together with PIK3CG is involved in natural killer (NK) cell development and migration towards the sites of inflammation. Participates in NK cell receptor activation. Plays a role in NK cell maturation and cytokine production. Together with PIK3CG is involved in neutrophil chemotaxis and extravasation. Together with PIK3CG participates in neutrophil respiratory burst. Plays important roles in mast-cell development and mast cell mediated allergic response. Involved in stem cell factor (SCF)-mediated proliferation, adhesion and migration. Required for allergen-IgE-induced degranulation and cytokine release. The lipid kinase activity is required for its biological function. Isoform 2 may be involved in stabilizing total RAS levels, resulting in increased ERK phosphorylation and increased PI3K activity", "gene_name": "PIK3CD", "glycan_count": 1, "glycosylation_sites": [], "id": "O00329", "name": "PIK3CD", "organism": "Homo sapiens", "uniprot_id": "O00329" }, { "function": "Envelope glycoprotein that forms spikes at the surface of virion envelope and binds to the host cell entry receptors MYH9/NMMHC-IIA and MYH10/NMMHC-IIB, promoting the virus entry into host cells. Essential for the initial attachment to heparan sulfate moieties of the host cell surface proteoglycans. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell: following initial binding to its host cell entry receptors, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May be involved in the fusion between the virion envelope and the outer nuclear membrane during virion egress. Also plays a role, together with gK, in virus-induced cell-to-cell fusion (syncytia formation)", "gene_name": "gB", "glycan_count": 0, "glycosylation_sites": [ { "position": 87, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 141, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 398, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 430, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 489, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 674, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P10211", "name": "HSV-1 glycoprotein B (gB)", "organism": "Human herpesvirus 1 (strain 17)", "uniprot_id": "P10211" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04489", "name": "HSV-1 infected cell protein 0 (ICP0)", "organism": "Human adenovirus C serotype 5", "uniprot_id": "P04489" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P10227", "name": "HSV-1 ICP4", "organism": "Human herpesvirus 1 (strain 17)", "uniprot_id": "P10227" }, { "function": "Essential component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase initiates primer synthesis and thereby produces large amount of short RNA primers on the lagging strand that the polymerase elongates using dNTPs", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P10236", "name": "HSV-1 ICP27", "organism": "Human herpesvirus 1 (strain 17)", "uniprot_id": "P10236" }, { "function": "Transcriptional regulator that binds to the GA element of the CLCNKA promoter. Binds to the KCNIP2 promoter and regulates KCNIP2 circadian expression in the heart (By similarity). Is a repressor of CCN2 expression, involved in the control of cardiac fibrosis. It is also involved in the control of cardiac hypertrophy acting through the inhibition of MEF2A and GATA4 (By similarity). Involved in podocyte differentiation (By similarity). Inhibits MYOCD activity. Is a negative regulator of TP53 acetylation. Inhibits NF-kappa-B activation through repression of EP300-dependent RELA acetylation", "gene_name": "KLF15", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UIH9", "name": "KLF15", "organism": "Homo sapiens", "uniprot_id": "Q9UIH9" }, { "function": "Receptor for glucocorticoids (GC) (PubMed:27120390, PubMed:37478846). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors (PubMed:28139699). Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Involved in chromatin remodeling (PubMed:9590696). Plays a role in rapid mRNA degradation by binding to the 5' UTR of target mRNAs and interacting with PNRC2 in a ligand-dependent manner which recruits the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay (PubMed:25775514). Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth (By similarity)", "gene_name": "NR3C1", "glycan_count": 2, "glycosylation_sites": [], "id": "P04150", "name": "Glucocorticoid receptor (GR)", "organism": "Homo sapiens", "uniprot_id": "P04150" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NPZ3", "name": "Organic Anion Transporting Polypeptide 1B3 (OATP1B3)", "organism": "", "uniprot_id": "Q9NPZ3" }, { "function": "Adapter protein which modulates coupling of cell surface receptor kinases with specific signaling pathways. Binds to, and suppresses signals from, the activated insulin receptor (INSR). Potent inhibitor of insulin-stimulated MAPK3 phosphorylation. Plays a critical role regulating PDPK1 membrane translocation in response to insulin stimulation and serves as an adapter protein to recruit PDPK1 to activated insulin receptor, thus promoting PKB/AKT1 phosphorylation and transduction of the insulin signal", "gene_name": "GRB14", "glycan_count": 1, "glycosylation_sites": [], "id": "Q14449", "name": "GLP-1 receptor", "organism": "Homo sapiens", "uniprot_id": "Q14449" }, { "function": "Specifically catalyzes coenzyme A (CoA)-dependent acylation of 1-acyl-sn-glycerol 3-phosphate (2-lysophosphatidic acid/LPA) to generate phosphatidic acid (PA), an important metabolic intermediate and precursor for both triglycerides and glycerophospholipids. Does not esterify other lysophospholipids. Acyl donors are long chain (at least C16) fatty acyl-CoAs: arachidonoyl-CoA, linoleoyl-CoA, oleoyl-CoA and at a lesser extent palmitoyl-CoA (PubMed:22560221). Additionally possesses low triacylglycerol lipase and CoA-independent acylglycerol transacylase activities and thus may play a role in acyl-chain remodeling of triglycerides (PubMed:15364929, PubMed:20034933, PubMed:22560221). In vitro may express hydrolytic activity against glycerolipids triacylglycerol, diacylglycerol and monoacylglycerol, with a strong preference for oleic acid as the acyl moiety (PubMed:21878620). However, the triacylglycerol hydrolase activity is controversial and may be very low (PubMed:22560221). Possesses phospholipase A2 activity (PubMed:15364929)", "gene_name": "PNPLA3", "glycan_count": 1, "glycosylation_sites": [ { "position": 89, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 280, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NST1", "name": "PNPLA3", "organism": "Homo sapiens", "uniprot_id": "Q9NST1" }, { "function": "Plays a role in neurite development, may be through the activation of the GTPase RAC1. Plays a role in the control of eye movement and gaze stability", "gene_name": "FRMD7", "glycan_count": 1, "glycosylation_sites": [], "id": "Q6ZUT3", "name": "TM6SF2", "organism": "Homo sapiens", "uniprot_id": "Q6ZUT3" }, { "function": "Multifunctional glycoprotein that acts as a receptor for a broad range of ligands. Ligands can be of proteinaceous nature like thrombospondin, fibronectin, collagen or amyloid-beta as well as of lipidic nature such as oxidized low-density lipoprotein (oxLDL), anionic phospholipids, long-chain fatty acids and bacterial diacylated lipopeptides. They are generally multivalent and can therefore engage multiple receptors simultaneously, the resulting formation of CD36 clusters initiates signal transduction and internalization of receptor-ligand complexes. The dependency on coreceptor signaling is strongly ligand specific. Cellular responses to these ligands are involved in angiogenesis, inflammatory response, fatty acid metabolism, taste and dietary fat processing in the intestine (Probable). Binds long-chain fatty acids and facilitates their transport into cells, thus participating in muscle lipid utilization, adipose energy storage, and gut fat absorption (By similarity) (PubMed:18353783, PubMed:21610069). Mechanistically, binding of fatty acids activates downstream kinase LYN, which phosphorylates the palmitoyltransferase ZDHHC5 and inactivates it, resulting in the subsequent depalmitoylation of CD36 and caveolar endocytosis (PubMed:32958780). In the small intestine, plays a role in proximal absorption of dietary fatty acid and cholesterol for optimal chylomicron formation, possibly through the activation of MAPK1/3 (ERK1/2) signaling pathway (By similarity) (PubMed:18753675). Involved in oral fat perception and preferences (PubMed:22240721, PubMed:25822988). Detection into the tongue of long-chain fatty acids leads to a rapid and sustained rise in flux and protein content of pancreatobiliary secretions (By similarity). In taste receptor cells, mediates the induction of an increase in intracellular calcium levels by long-chain fatty acids, leading to the activation of the gustatory neurons in the nucleus of the solitary tract (By similarity). Important factor in both ventromedial hypothalamus neuronal sensing of long-chain fatty acid and the regulation of energy and glucose homeostasis (By similarity). Receptor for thrombospondins, THBS1 and THBS2, mediating their antiangiogenic effects (By similarity). Involved in inducing apoptosis in podocytes in response to elevated free fatty acids, acting together with THBS1 (By similarity). As a coreceptor for TLR4:TLR6 heterodimer, promotes inflammation in monocytes/macrophages. Upon ligand binding, such as oxLDL or amyloid-beta 42, interacts with the heterodimer TLR4:TLR6, the complex is internalized and triggers inflammatory response, leading to NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway, as well as IL1B secretion, through the priming and activation of the NLRP3 inflammasome (By similarity) (PubMed:20037584). Selective and nonredundant sensor of microbial diacylated lipopeptide that signal via TLR2:TLR6 heterodimer, this cluster triggers signaling from the cell surface, leading to the NF-kappa-B-dependent production of TNF, via MYD88 signaling pathway and subsequently is targeted to the Golgi in a lipid-raft dependent pathway (By similarity) (PubMed:16880211)", "gene_name": "CD36", "glycan_count": 0, "glycosylation_sites": [ { "position": 79, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 102, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 134, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 163, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 205, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 220, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 235, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 247, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 321, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 417, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "CD36_HUMAN", "name": "CD36", "organism": "Homo sapiens", "uniprot_id": "P16671" }, { "function": "Receptor that mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (oxLDL) by vascular endothelial cells. OxLDL is a marker of atherosclerosis that induces vascular endothelial cell activation and dysfunction, resulting in pro-inflammatory responses, pro-oxidative conditions and apoptosis. Its association with oxLDL induces the activation of NF-kappa-B through an increased production of intracellular reactive oxygen and a variety of pro-atherogenic cellular responses including a reduction of nitric oxide (NO) release, monocyte adhesion and apoptosis. In addition to binding oxLDL, it acts as a receptor for the HSP70 protein involved in antigen cross-presentation to naive T-cells in dendritic cells, thereby participating in cell-mediated antigen cross-presentation. Also involved in inflammatory process, by acting as a leukocyte-adhesion molecule at the vascular interface in endotoxin-induced inflammation. Also acts as a receptor for advanced glycation end (AGE) products, activated platelets, monocytes, apoptotic cells and both Gram-negative and Gram-positive bacteria", "gene_name": "OLR1", "glycan_count": 0, "glycosylation_sites": [ { "position": 73, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 139, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "OLR1_HUMAN", "name": "LOX-1", "organism": "Homo sapiens", "uniprot_id": "P78380" }, { "function": "Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol (PubMed:16154994, PubMed:16647063, PubMed:32433613, PubMed:32433614, PubMed:32944968, PubMed:9020103). Plays a role in lipoprotein assembly and dietary cholesterol absorption (PubMed:16154994, PubMed:9020103). Preferentially utilizes oleoyl-CoA ((9Z)-octadecenoyl-CoA) as a substrate: shows a higher activity towards an acyl-CoA substrate with a double bond at the delta-9 position (9Z) than towards saturated acyl-CoA or an unsaturated acyl-CoA with a double bond at the delta-7 (7Z) or delta-11 (11Z) positions (PubMed:11294643, PubMed:32433614)", "gene_name": "SOAT1", "glycan_count": 1, "glycosylation_sites": [], "id": "P35610", "name": "ACAT1", "organism": "Homo sapiens", "uniprot_id": "P35610" }, { "function": "Plays a role in virion attachment to host receptor (PubMed:38182887). This attachment induces virion internalization predominantly through clathrin-dependent endocytosis (PubMed:19088291) Glycoprotein N probably locks the Gn-Gc complex in a prefusion state (PubMed:34793197)", "gene_name": "GP", "glycan_count": 0, "glycosylation_sites": [ { "position": 25, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 30, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 196, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 200, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 243, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 376, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 426, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 557, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1054, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1563, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "Q8JSZ3", "name": "CCHFV glycoprotein precursor (GPC)", "organism": "Crimean-Congo hemorrhagic fever virus (strain Nigeria/IbAr10200/1970)", "uniprot_id": "Q8JSZ3" }, { "function": "Binds to folate and reduced folic acid derivatives and mediates delivery of 5-methyltetrahydrofolate and folate analogs into the interior of cells (PubMed:19074442, PubMed:23851396, PubMed:23934049, PubMed:2527252, PubMed:8033114, PubMed:8567728). Has high affinity for folate and folic acid analogs at neutral pH (PubMed:23851396, PubMed:23934049, PubMed:2527252, PubMed:8033114, PubMed:8567728). Exposure to slightly acidic pH after receptor endocytosis triggers a conformation change that strongly reduces its affinity for folates and mediates their release (PubMed:8567728). Required for normal embryonic development and normal cell proliferation (By similarity)", "gene_name": "FOLR1", "glycan_count": 68, "glycosylation_sites": [ { "position": 69, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 161, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 201, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P15328", "name": "Folate receptor", "organism": "Homo sapiens", "uniprot_id": "P15328" }, { "function": "Nucleolin is the major nucleolar protein of growing eukaryotic cells. It is found associated with intranucleolar chromatin and pre-ribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly. May play a role in the process of transcriptional elongation. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats", "gene_name": "NCL", "glycan_count": 5, "glycosylation_sites": [], "id": "P19338", "name": "Nucleolin", "organism": "Homo sapiens", "uniprot_id": "P19338" }, { "function": "Flavin-containing quinone reductase that catalyzes two-electron reduction of quinones to hydroquinones using either NADH or NADPH as electron donors. In a ping-pong kinetic mechanism, the electrons are sequentially transferred from NAD(P)H to flavin cofactor and then from reduced flavin to the quinone, bypassing the formation of semiquinone and reactive oxygen species (By similarity) (PubMed:8999809, PubMed:9271353). Regulates cellular redox state primarily through quinone detoxification. Reduces components of plasma membrane redox system such as coenzyme Q and vitamin quinones, producing antioxidant hydroquinone forms. In the process may function as superoxide scavenger to prevent hydroquinone oxidation and facilitate excretion (PubMed:15102952, PubMed:8999809, PubMed:9271353). Alternatively, can activate quinones and their derivatives by generating redox reactive hydroquinones with DNA cross-linking antitumor potential (PubMed:8999809). Acts as a gatekeeper of the core 20S proteasome known to degrade proteins with unstructured regions. Upon oxidative stress, interacts with tumor suppressors TP53 and TP73 in a NADH-dependent way and inhibits their ubiquitin-independent degradation by the 20S proteasome (PubMed:15687255, PubMed:28291250)", "gene_name": "NQO1", "glycan_count": 1, "glycosylation_sites": [], "id": "P15559", "name": "NQO1", "organism": "Homo sapiens", "uniprot_id": "P15559" }, { "function": "A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins (PubMed:10681376, PubMed:11555828, PubMed:12865317, PubMed:14559847, PubMed:15041462, PubMed:15805301, PubMed:18577768, PubMed:19965576, PubMed:20972997). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase) (PubMed:10681376, PubMed:11555828, PubMed:12865317, PubMed:14559847, PubMed:15041462, PubMed:15805301, PubMed:18577768, PubMed:19965576, PubMed:20972997). Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2, as well as D-ring hydroxylated E1 and E2 at the C15-alpha and C16-alpha positions (PubMed:11555828, PubMed:12865317, PubMed:14559847, PubMed:15805301). Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation (PubMed:15041462, PubMed:18577768). Catalyzes the epoxidation of double bonds of certain PUFA (PubMed:15041462, PubMed:19965576, PubMed:20972997). Converts arachidonic acid toward epoxyeicosatrienoic acid (EET) regioisomers, 8,9-, 11,12-, and 14,15-EET, that function as lipid mediators in the vascular system (PubMed:20972997). Displays an absolute stereoselectivity in the epoxidation of eicosapentaenoic acid (EPA) producing the 17(R),18(S) enantiomer (PubMed:15041462). May play an important role in all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid (PubMed:10681376). May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent) (PubMed:21068195)", "gene_name": "CYP1A1", "glycan_count": 1, "glycosylation_sites": [ { "position": 67, "type": "O-linked (GlcNAc) serine" } ], "id": "P04798", "name": "Cytochrome P450 3A1 (CYP3A1)", "organism": "Homo sapiens", "uniprot_id": "P04798" }, { "function": "Binds and transactivates the retinoic acid response elements that control expression of the retinoic acid receptor beta 2 and alcohol dehydrogenase 3 genes. Transactivates both the phenobarbital responsive element module of the human CYP2B6 gene and the CYP3A4 xenobiotic response element", "gene_name": "NR1I3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q14994", "name": "Constitutive androstane receptor (CAR)", "organism": "Homo sapiens", "uniprot_id": "Q14994" }, { "function": "Precursor of the transcription factor form (Processed sterol regulatory element-binding protein 2), which is embedded in the endoplasmic reticulum membrane (PubMed:32322062). Low sterol concentrations promote processing of this form, releasing the transcription factor form that translocates into the nucleus and activates transcription of genes involved in cholesterol biosynthesis (PubMed:32322062)", "gene_name": "SREBF2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q12772", "name": "Sterol regulatory element-binding protein 1c (SREBP-1c)", "organism": "Homo sapiens", "uniprot_id": "Q12772" }, { "function": "A cytochrome P450 monooxygenase involved in the metabolism of fatty acids (PubMed:10553002, PubMed:18577768). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase) (PubMed:10553002, PubMed:18577768). Catalyzes the hydroxylation of carbon-hydrogen bonds. Hydroxylates fatty acids specifically at the omega-1 position displaying the highest catalytic activity for saturated fatty acids (PubMed:10553002, PubMed:18577768). May be involved in the oxidative metabolism of xenobiotics (Probable)", "gene_name": "CYP2E1", "glycan_count": 0, "glycosylation_sites": [], "id": "P05181", "name": "CYP P450 2E1", "organism": "Homo sapiens", "uniprot_id": "P05181" }, { "function": "Receptor tyrosine kinase involved in the development and the maturation of the central and the peripheral nervous systems through regulation of neuron survival, proliferation, migration, differentiation, and synapse formation and plasticity (By similarity). Receptor for BDNF/brain-derived neurotrophic factor and NTF4/neurotrophin-4. Alternatively can also bind NTF3/neurotrophin-3 which is less efficient in activating the receptor but regulates neuron survival through NTRK2 (PubMed:15494731, PubMed:7574684). Upon ligand-binding, undergoes homodimerization, autophosphorylation and activation (PubMed:15494731). Recruits, phosphorylates and/or activates several downstream effectors including SHC1, FRS2, SH2B1, SH2B2 and PLCG1 that regulate distinct overlapping signaling cascades. Through SHC1, FRS2, SH2B1, SH2B2 activates the GRB2-Ras-MAPK cascade that regulates for instance neuronal differentiation including neurite outgrowth. Through the same effectors controls the Ras-PI3 kinase-AKT1 signaling cascade that mainly regulates growth and survival. Through PLCG1 and the downstream protein kinase C-regulated pathways controls synaptic plasticity. Thereby, plays a role in learning and memory by regulating both short term synaptic function and long-term potentiation. PLCG1 also leads to NF-Kappa-B activation and the transcription of genes involved in cell survival. Hence, it is able to suppress anoikis, the apoptosis resulting from loss of cell-matrix interactions. May also play a role in neutrophin-dependent calcium signaling in glial cells and mediate communication between neurons and glia", "gene_name": "NTRK2", "glycan_count": 22, "glycosylation_sites": [ { "position": 67, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 95, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 121, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 178, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 205, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 241, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 254, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 280, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 325, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 338, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 412, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q16620", "name": "TrkB (NTRK2)", "organism": "Homo sapiens", "uniprot_id": "Q16620" }, { "function": "Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc (By similarity). Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (Probable). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (PubMed:22677715). The shared binding site between zinc and calcium at residue Asp-272 suggests a crosstalk between zinc and calcium transport in the blood (Probable). The rank order of affinity is zinc > calcium > magnesium (Probable). Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli (PubMed:6234017). Does not prevent iron uptake by the bacterial siderophore aerobactin (PubMed:6234017)", "gene_name": "ALB", "glycan_count": 1, "glycosylation_sites": [ { "position": 151, "type": "N-linked (Glc) (glycation) lysine; in vitro" } ], "id": "P02769", "name": "Bovine serum albumin (BSA)", "organism": "Bos taurus", "uniprot_id": "P02769" }, { "function": "Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network (By similarity). Inhibits host IKBKE and IRF3, thereby impairing type I IFN signaling (PubMed:33391252)", "gene_name": "NEC2", "glycan_count": 0, "glycosylation_sites": [], "id": "P03185", "name": "gp350", "organism": "Epstein-Barr virus (strain B95-8)", "uniprot_id": "P03185" }, { "function": "Envelope glycoprotein that plays a role in host cell entry, cell to-cell virus transmission, and fusion of infected cells. May be involved in the initial attachment via binding to heparan sulfate together with the gM/gN complex that binds heparin with higher affinity. Interacts with host integrin ITGB1, PDGFRA and EGFR that likely serve as postattachment entry receptors. Also participates in the fusion of viral and cellular membranes leading to virus entry into the host cell. Membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL", "gene_name": "gB", "glycan_count": 0, "glycosylation_sites": [ { "position": 68, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 73, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 85, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 208, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 281, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 286, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 302, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 341, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 383, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 405, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 409, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 417, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 447, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 452, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 456, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 466, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 555, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 586, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P13201", "name": "glycoprotein B", "organism": "Human cytomegalovirus (strain Towne)", "uniprot_id": "P13201" }, { "function": "Acts as a CD40 functional homolog to prevent apoptosis of infected B-lymphocytes and drive their proliferation. Functions as a constitutively active tumor necrosis factor receptor that induces the activation of several signaling pathways, including those of the NF-kappa-B family. LMP1 signaling leads to up-regulation of antiapoptotic proteins and provide growth signals in latently infected cells. Interacts with host UBE2I and subsequently affects the sumoylation state of several cellular proteins. For example, induces the sumoylation of host IRF7 thereby limiting its transcriptional activity and modulating the activation of innate immune responses. Also inhibits host IFN-alpha-stimulated STAT2 nuclear translocation and interferon-stimulated response element transcriptional activity by interacting with and inhibiting host TYK2. Induces SUMO expression during viral latency thereby dysregulating the host sumoylation processes (PubMed:30659232)", "gene_name": "LMP1", "glycan_count": 0, "glycosylation_sites": [], "id": "P03230", "name": "LMP1", "organism": "Epstein-Barr virus (strain B95-8)", "uniprot_id": "P03230" }, { "function": "Transcriptional activator of immediate-early (IE) gene products (alpha genes). Acts as a key activator of lytic infection by initiating the lytic program through the assembly of the transcriptional regulatory VP16-induced complex composed of VP16 and two cellular factors, HCFC1 and POU2F1. VP16-induced complex represents a regulatory switch: when it is on, it promotes IE-gene expression and thus lytic infection, and when it is off, it limits IE-gene transcription favoring latent infection (By similarity)", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P09265", "name": "Glycoprotein H (gH)", "organism": "Varicella-zoster virus (strain Dumas)", "uniprot_id": "P09265" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P09266", "name": "Glycoprotein L (gL)", "organism": "Varicella-zoster virus (strain Dumas)", "uniprot_id": "P09266" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P09262", "name": "Glycoprotein C (gC)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P33461", "name": "E2 glycoprotein", "organism": "", "uniprot_id": "" }, { "function": "Escorts unspliced or incompletely spliced viral pre-mRNAs (late transcripts) out of the nucleus of infected cells. These pre-mRNAs carry a recognition sequence called Rev responsive element (RRE) located in the env gene, that is not present in fully spliced viral mRNAs (early transcripts). This function is essential since most viral proteins are translated from unspliced or partially spliced pre-mRNAs which cannot exit the nucleus by the pathway used by fully processed cellular mRNAs (By similarity)", "gene_name": "rev", "glycan_count": 0, "glycosylation_sites": [], "id": "P33460", "name": "E1 glycoprotein", "organism": "Caprine arthritis encephalitis virus (strain Cork)", "uniprot_id": "P33460" }, { "function": "Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase", "gene_name": "IFNA7", "glycan_count": 0, "glycosylation_sites": [], "id": "P01567", "name": "IFN-\u03b1", "organism": "Homo sapiens", "uniprot_id": "P01567" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8NAC6", "name": "IL-17", "organism": "", "uniprot_id": "Q8NAC6" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P59594 (SARS-CoV)", "name": "Spike protein (SARS-CoV/SARS-CoV-2)", "organism": "", "uniprot_id": "" }, { "function": "Probable pathogen-recognition receptor involved in peripheral immune surveillance in liver. May mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. Is a receptor for ICAM3, probably by binding to mannose-like carbohydrates", "gene_name": "CLEC4M", "glycan_count": 0, "glycosylation_sites": [ { "position": 92, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 361, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9H2X3", "name": "L-SIGN (CD209L)", "organism": "Homo sapiens", "uniprot_id": "Q9H2X3" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P0DTC2 (region)", "name": "Receptor Binding Domain (RBD) of Spike", "organism": "", "uniprot_id": "" }, { "function": "Forms an icosahedral capsid with a T=4 symmetry composed of 240 copies of the capsid protein surrounded by a lipid membrane through which penetrate 80 spikes composed of trimers of E1-E2 heterodimers (By similarity). The capsid protein binds to the viral RNA genome at a site adjacent to a ribosome binding site for viral genome translation following genome release (By similarity). Possesses a protease activity that results in its autocatalytic cleavage from the nascent structural protein (By similarity). Following its self-cleavage, the capsid protein transiently associates with ribosomes, and within several minutes the protein binds to viral RNA and rapidly assembles into icosahedric core particles (By similarity). The resulting nucleocapsid eventually associates with the cytoplasmic domain of the spike glycoprotein E2 at the cell membrane, leading to budding and formation of mature virions (By similarity). In case of infection, new virions attach to target cells and after clathrin-mediated endocytosis their membrane fuses with the host endosomal membrane (By similarity). This leads to the release of the nucleocapsid into the cytoplasm, followed by an uncoating event necessary for the genomic RNA to become accessible (By similarity). The uncoating might be triggered by the interaction of capsid proteins with ribosomes (By similarity). Binding of ribosomes would release the genomic RNA since the same region is genomic RNA-binding and ribosome-binding (By similarity). Specifically inhibits interleukin-1 receptor-associated kinase 1/IRAK1-dependent signaling during viral entry, representing a means by which the alphaviruses may evade innate immune detection and activation prior to viral gene expression (By similarity). Degrades host cyclic GMP-AMP synthase (CGAS) thereby inhibiting the cGAS-STING pathway (PubMed:33057424)", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [ { "position": 273, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 588, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 670, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 950, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1079, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "Q8JUX5", "name": "CHIKV E2", "organism": "Chikungunya virus (strain S27-African prototype)", "uniprot_id": "Q8JUX5" }, { "function": "Endosomal receptor that plays a key role in innate and adaptive immunity (PubMed:25297876, PubMed:32433612). Controls host immune response against pathogens through recognition of RNA degradation products specific to microorganisms that are initially processed by RNASET2 (PubMed:31778653). Recognizes GU-rich single-stranded RNA (GU-rich RNA) derived from SARS-CoV-2, SARS-CoV-1 and HIV-1 viruses (PubMed:33718825). Upon binding to agonists, undergoes dimerization that brings TIR domains from the two molecules into direct contact, leading to the recruitment of TIR-containing downstream adapter MYD88 through homotypic interaction (PubMed:23520111, PubMed:25599397, PubMed:26929371, PubMed:33718825). In turn, the Myddosome signaling complex is formed involving IRAK4, IRAK1, TRAF6, TRAF3 leading to activation of downstream transcription factors NF-kappa-B and IRF7 to induce pro-inflammatory cytokines and interferons, respectively (PubMed:16737960, PubMed:17932028, PubMed:29155428)", "gene_name": "TLR8", "glycan_count": 17, "glycosylation_sites": [ { "position": 29, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 42, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 80, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 88, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 115, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 160, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 247, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 285, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 293, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 358, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 362, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 395, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 416, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 443, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 511, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 546, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 582, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 590, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 640, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 680, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 752, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NR97", "name": "TLR8", "organism": "Homo sapiens", "uniprot_id": "Q9NR97" }, { "function": "IFN-induced antiviral protein which disrupts intracellular cholesterol homeostasis. Inhibits the entry of viruses to the host cell cytoplasm by preventing viral fusion with cholesterol depleted endosomes. May inactivate new enveloped viruses which buds out of the infected cell, by letting them go out with a cholesterol depleted membrane. Active against multiple viruses, including influenza A virus, SARS coronaviruses (SARS-CoV and SARS-CoV-2), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-1), hepatitis C virus (HCV) and vesicular stomatitis virus (VSV) (PubMed:26354436, PubMed:33239446, PubMed:33270927). Can inhibit: influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2-mediated viral entry, SARS-CoV and SARS-CoV-2 S protein-mediated viral entry and VSV G protein-mediated viral entry (PubMed:33270927). Plays a critical role in the structural stability and function of vacuolar ATPase (v-ATPase). Establishes physical contact with the v-ATPase of endosomes which is critical for proper clathrin localization and is also required for the function of the v-ATPase to lower the pH in phagocytic endosomes thus establishing an antiviral state. In hepatocytes, IFITM proteins act in a coordinated manner to restrict HCV infection by targeting the endocytosed HCV virion for lysosomal degradation (PubMed:26354436). IFITM2 and IFITM3 display anti-HCV activity that may complement the anti-HCV activity of IFITM1 by inhibiting the late stages of HCV entry, possibly in a coordinated manner by trapping the virion in the endosomal pathway and targeting it for degradation at the lysosome (PubMed:26354436). Exerts opposing activities on SARS-CoV-2, including amphipathicity-dependent restriction of virus at endosomes and amphipathicity-independent enhancement of infection at the plasma membrane (PubMed:33270927)", "gene_name": "IFITM3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q01628", "name": "IFITM1", "organism": "Homo sapiens", "uniprot_id": "Q01628" }, { "function": "IFN-induced antiviral protein which inhibits the entry of viruses to the host cell cytoplasm, permitting endocytosis, but preventing subsequent viral fusion and release of viral contents into the cytosol (PubMed:26354436, PubMed:33563656). Active against multiple viruses, including influenza A virus, SARS coronaviruses (SARS-CoV and SARS-CoV-2), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-1), hepatitis C virus (HCV) and vesicular stomatitis virus (VSV) (PubMed:26354436, PubMed:33239446, PubMed:33270927, PubMed:33563656). Can inhibit: influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2-mediated viral entry, SARS-CoV and SARS-CoV-2 S protein-mediated viral entry and VSV G protein-mediated viral entry (PubMed:33563656). Induces cell cycle arrest and mediates apoptosis by caspase activation and in p53-independent manner. In hepatocytes, IFITM proteins act in a coordinated manner to restrict HCV infection by targeting the endocytosed HCV virion for lysosomal degradation (PubMed:26354436). IFITM2 and IFITM3 display anti-HCV activity that may complement the anti-HCV activity of IFITM1 by inhibiting the late stages of HCV entry, possibly in a coordinated manner by trapping the virion in the endosomal pathway and targeting it for degradation at the lysosome (PubMed:26354436)", "gene_name": "IFITM2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q01629", "name": "IFITM2", "organism": "Homo sapiens", "uniprot_id": "Q01629" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8JUX3", "name": "CHIKV nsP2", "organism": "", "uniprot_id": "Q8JUX3" }, { "function": "Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin", "gene_name": "ribH", "glycan_count": 0, "glycosylation_sites": [], "id": "O66529", "name": "Lumazine Synthase (LuS)", "organism": "Aquifex aeolicus (strain VF5)", "uniprot_id": "O66529" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P69399 (IBV S1, reference strain)", "name": "Spike (S) glycoprotein S1 subunit", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P69399 (IBV S2, reference strain)", "name": "Spike (S) glycoprotein S2 subunit", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P33527 (human)", "name": "MRP1 (ABCC1)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UNQ0 (human)", "name": "BCRP (ABCG2)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O15392 (human)", "name": "Survivin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P10415 (human)", "name": "BCL-2", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O15519 (human)", "name": "c-FLIP", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y6L6 (human)", "name": "OATP1B1", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NPD5 (human)", "name": "OATP1B3", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O15431 (human)", "name": "CTR1 (SLC31A1)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q28248", "name": "ABCB1 (canine)", "organism": "Canis lupus familiaris", "uniprot_id": "Q28248" }, { "function": "Plasma membrane-anchored serine protease that cleaves at arginine residues (PubMed:32703818, PubMed:35676539, PubMed:37990007, PubMed:38964328). Participates in proteolytic cascades of relevance for the normal physiologic function of the prostate (PubMed:25122198). Androgen-induced TMPRSS2 activates several substrates that include pro-hepatocyte growth factor/HGF, the protease activated receptor-2/F2RL1 or matriptase/ST14 leading to extracellular matrix disruption and metastasis of prostate cancer cells (PubMed:15537383, PubMed:25122198, PubMed:26018085). In addition, activates trigeminal neurons and contribute to both spontaneous pain and mechanical allodynia (By similarity)", "gene_name": "TMPRSS2", "glycan_count": 10, "glycosylation_sites": [ { "position": 213, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 249, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O15393", "name": "TMPRSS2", "organism": "Homo sapiens", "uniprot_id": "O15393" }, { "function": "Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein", "gene_name": "rep", "glycan_count": 0, "glycosylation_sites": [], "id": "P0DTD1", "name": "PLpro (NSP3)", "organism": "Severe acute respiratory syndrome coronavirus 2", "uniprot_id": "P0DTD1" }, { "function": "Guanine nucleotide-exchange factor (GEF) that activates CDC42 and RAC1 by exchanging bound GDP for free GTP. Essential for dendritic spine morphogenesis in Purkinje cells and in hippocampal neurons, via a CDC42-mediated pathway. Sustains B-cell lymphopoiesis in secondary lymphoid tissues and regulates FCER2/CD23 expression", "gene_name": "DOCK10", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96BY6", "name": "DOCK8", "organism": "Homo sapiens", "uniprot_id": "Q96BY6" }, { "function": "Involved in cytoskeletal rearrangements required for lymphocyte migration in response of chemokines. Activates RAC1 and RAC2, but not CDC42, by functioning as a guanine nucleotide exchange factor (GEF), which exchanges bound GDP for free GTP. May also participate in IL2 transcriptional activation via the activation of RAC2", "gene_name": "DOCK2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q92608", "name": "DOCK2", "organism": "Homo sapiens", "uniprot_id": "Q92608" }, { "function": "Plays a role in cytotoxic granule exocytosis in lymphocytes. Required for both granule maturation and granule docking and priming at the immunologic synapse. Regulates assembly of recycling and late endosomal structures, leading to the formation of an endosomal exocytic compartment that fuses with perforin-containing granules at the immunologic synapse and licences them for exocytosis. Regulates Ca(2+)-dependent secretory lysosome exocytosis in mast cells", "gene_name": "UNC13D", "glycan_count": 2, "glycosylation_sites": [], "id": "Q70J99", "name": "UNC13D (Munc13-4)", "organism": "Homo sapiens", "uniprot_id": "Q70J99" }, { "function": "Potential guanine nucleotide exchange factor (GEF). GEF proteins activate some small GTPases by exchanging bound GDP for free GTP. Its interaction with presenilin proteins as well as its ability to stimulate Tau/MAPT phosphorylation suggest that it may be involved in Alzheimer disease. Ectopic expression in nerve cells decreases the secretion of amyloid-beta APBA1 protein and lowers the rate of cell-substratum adhesion, suggesting that it may affect the function of some small GTPase involved in the regulation of actin cytoskeleton or cell adhesion receptors (By similarity)", "gene_name": "DOCK3", "glycan_count": 2, "glycosylation_sites": [], "id": "Q8IZD9", "name": "DOCK11", "organism": "Homo sapiens", "uniprot_id": "Q8IZD9" }, { "function": "Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-BMAL1|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. The preferred binding motif for the CLOCK-BMAL1 heterodimer is 5'-CACGTGA-3', which contains a flanking adenine nucleotide at the 3-prime end of the canonical 6-nucleotide E-box sequence. CLOCK specifically binds to the half-site 5'-CAC-3', while BMAL1 binds to the half-site 5'-GTGA-3'", "gene_name": "BMAL2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8QGQ7", "name": "IHNV glycoprotein (G protein)", "organism": "Gallus gallus", "uniprot_id": "Q8QGQ7" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6TQR6 (SFTSV polyprotein)", "name": "Gn", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01892 (HLA-A), P01889 (HLA-B), P04222 (HLA-C)", "name": "HLA-I (Human Leukocyte Antigen Class I)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01903 (HLA-DR), P04229 (HLA-DQ)", "name": "HLA-II (Human Leukocyte Antigen Class II)", "organism": "", "uniprot_id": "" }, { "function": "Protein disulfide isomerase that catalyzes the formation, isomerization, and reduction or oxidation of disulfide bonds in client proteins and functions as a protein folding chaperone (PubMed:11825568, PubMed:16193070, PubMed:27897272, PubMed:36104323, PubMed:7487104). Core component of the major histocompatibility complex class I (MHC I) peptide loading complex where it functions as an essential folding chaperone for TAPBP. Through TAPBP, assists the dynamic assembly of the MHC I complex with high affinity antigens in the endoplasmic reticulum. Therefore, plays a crucial role in the presentation of antigens to cytotoxic T cells in adaptive immunity (PubMed:35948544, PubMed:36104323)", "gene_name": "PDIA3", "glycan_count": 2, "glycosylation_sites": [], "id": "P30101", "name": "ERp57 (PDIA3)", "organism": "Homo sapiens", "uniprot_id": "P30101" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P0DTC1 (polyprotein, Nsp1 region)", "name": "SARS-CoV-2 Nsp1", "organism": "", "uniprot_id": "" }, { "function": "Plays a role in viral egress via lysosomal trafficking (PubMed:33157038, PubMed:33422265). Forms homotetrameric ion channels (viroporins) localized at endosomes and lysosomes, that may induce deacidification of lysosomes, allowing safe egress of virions via lysosomal trafficking (PubMed:33157038, PubMed:33422265, PubMed:34158638). Also blocks autolysosome formation by binding and sequestering the host component VPS39 for homotypic fusion and protein sorting (HOPS) on late endosomes (PubMed:33422265). This prevents fusion of autophagosomes with lysosomes, disrupting autophagy and facilitating virus egress (PubMed:33422265). Induces host RETREG1/FAM134B-dependent reticulophagy by interacting with host HMGB1 and enhancing the association between HMGB1 and host BECN1 (PubMed:35239449). This induces endoplasmic reticulum stress and inflammatory responses and facilitates viral infection (PubMed:35239449)", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [ { "position": 32, "type": "O-linked (GalNAc...) threonine; by host" }, { "position": 34, "type": "O-linked (GalNAc...) threonine; by host" } ], "id": "P0DTC3", "name": "SARS-CoV-2 ORF3a", "organism": "Severe acute respiratory syndrome coronavirus 2", "uniprot_id": "P0DTC3" }, { "function": "Catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. It could be a defense mechanism against D-cysteine. Can also catalyze the degradation of 3-chloro-D-alanine", "gene_name": "dcyD", "glycan_count": 0, "glycosylation_sites": [], "id": "P76316", "name": "LuxS", "organism": "Escherichia coli (strain K12)", "uniprot_id": "P76316" }, { "function": "Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity)", "gene_name": "ND3", "glycan_count": 0, "glycosylation_sites": [], "id": "P24883", "name": "Interleukin-6 (IL-6)", "organism": "Ascaris suum", "uniprot_id": "P24883" }, { "function": "Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) generated by peroxisomal oxidases to water and oxygen, thereby protecting cells from the toxic effects of hydrogen peroxide (PubMed:10691967). Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells (PubMed:10691967)", "gene_name": "CAT", "glycan_count": 0, "glycosylation_sites": [], "id": "P00432", "name": "Glutathione peroxidase 1 (GPX1)", "organism": "Bos taurus", "uniprot_id": "P00432" }, { "function": "", "gene_name": "Prss1", "glycan_count": 0, "glycosylation_sites": [], "id": "P00762", "name": "Catalase (CAT)", "organism": "Rattus norvegicus", "uniprot_id": "P00762" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03437 (H9N2 AIV HA)", "name": "Hemagglutinin (HA)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03468 (H9N2 AIV NA)", "name": "Neuraminidase (NA)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P06822 (Influenza A M2)", "name": "Matrix protein 2 extracellular domain (M2e)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P69399 (reference IBV S protein)", "name": "Spike (S) glycoprotein", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P69399-1 (reference IBV S1)", "name": "S1 subunit of Spike glycoprotein", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P16860 (precursor BNP)", "name": "N-terminal pro-brain natriuretic peptide (NT-proBNP)", "organism": "", "uniprot_id": "" }, { "function": "With S4 and S5 plays an important role in translational accuracy. Located at the interface of the 30S and 50S subunits (By similarity)", "gene_name": "rps12", "glycan_count": 0, "glycosylation_sites": [], "id": "P19461", "name": "Cardiac troponin I (cTnI)", "organism": "Guillardia theta", "uniprot_id": "P19461" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P06732 (CKM)", "name": "Creatine kinase-myocardial band (CK-MB)", "organism": "", "uniprot_id": "" }, { "function": "Mediates the transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes (PubMed:18817523, PubMed:2963003). Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6-phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelysosomal compartment where the low pH mediates the dissociation of the complex (PubMed:18817523, PubMed:2963003). The receptor is then recycled back to the Golgi for another round of trafficking through its binding to the retromer (PubMed:18817523). This receptor also binds IGF2 (PubMed:18046459). Acts as a positive regulator of T-cell coactivation by binding DPP4 (PubMed:10900005)", "gene_name": "IGF2R", "glycan_count": 112, "glycosylation_sites": [ { "position": 112, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 400, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 435, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 543, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 581, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 626, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 747, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 871, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 951, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 957, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1164, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1246, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1312, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1656, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1757, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1816, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2085, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2136, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P11717", "name": "Mannose 6-phosphate/IGF-II receptor", "organism": "Homo sapiens", "uniprot_id": "P11717" }, { "function": "Major capsid protein that self-associates to form 240 hexon trimers, each in the shape of a hexagon, building most of the pseudo T=25 capsid. Assembled into trimeric units with the help of the chaperone shutoff protein. Transported by pre-protein VI to the nucleus where it associates with other structural proteins to form an empty capsid. Might be involved, through its interaction with host dyneins, in the intracellular microtubule-dependent transport of incoming viral capsid to the nucleus", "gene_name": "L3", "glycan_count": 0, "glycosylation_sites": [], "id": "P04133", "name": "Adenovirus fiber protein", "organism": "Human adenovirus C serotype 5", "uniprot_id": "P04133" }, { "function": "Attaches the virus to host cellular receptor, inducing endocytosis of the virion by using different host proteins including TFRC, GRM2 and ITGB1 (By similarity). In the endosome, the acidic pH induces conformational changes in the glycoprotein trimer, which trigger fusion between virus and cell membrane. There is convincing in vitro evidence that the muscular form of the nicotinic acetylcholine receptor (nAChR), the neuronal cell adhesion molecule (NCAM), and the p75 neurotrophin receptor (p75NTR) bind glycoprotein and thereby facilitate rabies virus entry into cells (By similarity)", "gene_name": "G", "glycan_count": 0, "glycosylation_sites": [ { "position": 56, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 266, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 338, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P03524", "name": "VSV M protein", "organism": "Rabies virus (strain ERA)", "uniprot_id": "P03524" }, { "function": "Protein with pleiotropic attributes mediated in a cell-compartment- and tissue-specific manner, which include the plasma membrane-associated cell signaling functions, mitochondrial chaperone, and transcriptional co-regulator of transcription factors and sex steroid hormones in the nucleus", "gene_name": "PHB2", "glycan_count": 3, "glycosylation_sites": [], "id": "Q99623", "name": "Prohibitin 2 (PHB2)", "organism": "Homo sapiens", "uniprot_id": "Q99623" }, { "function": "Amylin/IAPP is a glucoregulatory peptide hormone that plays an important role in the regulation of energy homeostasis (PubMed:2690069). Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism. IAPP function is mediated by the CALCR-RAMPs (AMYRs) receptor complexes (By similarity). Amylin can also bind CALCR receptor in the absence of RAMPs, although it is more selective for AMYRs (By similarity)", "gene_name": "IAPP", "glycan_count": 0, "glycosylation_sites": [], "id": "P10997", "name": "Human islet amyloid polypeptide (hIAPP)", "organism": "Homo sapiens", "uniprot_id": "P10997" }, { "function": "Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione (PubMed:20454679, PubMed:23122816, PubMed:9705294). Involved in the regulation of TNF-induced transcriptional activity of NF-kappa-B (PubMed:19199007). Required for normal osteoclastogenesis (By similarity)", "gene_name": "GLO1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q04760", "name": "Glyoxalase 1 (GLO1)", "organism": "Homo sapiens", "uniprot_id": "Q04760" }, { "function": "Capable of hydrolyzing lactones and a number of aromatic carboxylic acid esters. Has antioxidant activity. Is not associated with high density lipoprotein. Prevents LDL lipid peroxidation, reverses the oxidation of mildly oxidized LDL, and inhibits the ability of MM-LDL to induce monocyte chemotaxis", "gene_name": "PON2", "glycan_count": 23, "glycosylation_sites": [ { "position": 254, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 269, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 323, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q15165", "name": "PON2 (Paraoxonase 2)", "organism": "Homo sapiens", "uniprot_id": "Q15165" }, { "function": "Non-selective voltage-gated ion channel that mediates the transport of anions and cations through the mitochondrion outer membrane and plasma membrane (PubMed:10661876, PubMed:11845315, PubMed:18755977, PubMed:30061676, PubMed:8420959). The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis (PubMed:10661876, PubMed:11845315, PubMed:18755977, PubMed:8420959). It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV (PubMed:10661876, PubMed:18755977, PubMed:8420959). The open state has a weak anion selectivity whereas the closed state is cation-selective (PubMed:18755977, PubMed:8420959). Binds various signaling molecules, including the sphingolipid ceramide, the phospholipid phosphatidylcholine, and the sterols cholesterol and oxysterol (PubMed:18755977, PubMed:31015432). In depolarized mitochondria, acts downstream of PRKN and PINK1 to promote mitophagy or prevent apoptosis; polyubiquitination by PRKN promotes mitophagy, while monoubiquitination by PRKN decreases mitochondrial calcium influx which ultimately inhibits apoptosis (PubMed:32047033). May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis (PubMed:15033708, PubMed:25296756). May mediate ATP export from cells (PubMed:30061676). Part of a complex composed of HSPA9, ITPR1 and VDAC1 that regulates mitochondrial calcium-dependent apoptosis by facilitating calcium transport from the ER lumen to the mitochondria intermembrane space thus providing calcium for the downstream calcium channel MCU that directly releases it into mitochondria matrix (By similarity). Mediates cytochrome c efflux (PubMed:20230784)", "gene_name": "VDAC1", "glycan_count": 3, "glycosylation_sites": [], "id": "P21796", "name": "VDAC1 (Voltage-dependent anion-selective channel protein 1)", "organism": "Homo sapiens", "uniprot_id": "P21796" }, { "function": "The C-terminal part of the sonic hedgehog protein precursor displays an autoproteolysis and a cholesterol transferase activity (By similarity). Both activities result in the cleavage of the full-length protein into two parts (ShhN and ShhC) followed by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated ShhN (By similarity). Both activities occur in the endoplasmic reticulum (By similarity). Once cleaved, ShhC is degraded in the endoplasmic reticulum (By similarity)", "gene_name": "SHH", "glycan_count": 0, "glycosylation_sites": [ { "position": 278, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q15465", "name": "Sonic hedgehog (SHH)", "organism": "Homo sapiens", "uniprot_id": "Q15465" }, { "function": "Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane", "gene_name": "EXOC2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q96KP1", "name": "EXOC5 (Exocyst complex component 5)", "organism": "Homo sapiens", "uniprot_id": "Q96KP1" }, { "function": "Thought to act as molecular guidance cue in cellular migration, and function appears to be mediated by interaction with roundabout homolog receptors. During neural development involved in axonal navigation at the ventral midline of the neural tube and projection of axons to different regions. SLIT1 and SLIT2 seem to be essential for midline guidance in the forebrain by acting as repulsive signal preventing inappropriate midline crossing by axons projecting from the olfactory bulb. In spinal cord development may play a role in guiding commissural axons once they reached the floor plate by modulating the response to netrin. In vitro, silences the attractive effect of NTN1 but not its growth-stimulatory effect and silencing requires the formation of a ROBO1-DCC complex. May be implicated in spinal cord midline post-crossing axon repulsion. In vitro, only commissural axons that crossed the midline responded to SLIT2. In the developing visual system appears to function as repellent for retinal ganglion axons by providing a repulsion that directs these axons along their appropriate paths prior to, and after passage through, the optic chiasm. In vitro, collapses and repels retinal ganglion cell growth cones. Seems to play a role in branching and arborization of CNS sensory axons, and in neuronal cell migration. In vitro, Slit homolog 2 protein N-product, but not Slit homolog 2 protein C-product, repels olfactory bulb (OB) but not dorsal root ganglia (DRG) axons, induces OB growth cones collapse and induces branching of DRG axons. Seems to be involved in regulating leukocyte migration", "gene_name": "SLIT2", "glycan_count": 13, "glycosylation_sites": [ { "position": 66, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 186, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 564, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 623, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 794, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 799, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1009, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1010, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1019, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1183, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1266, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1300, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O94813", "name": "SLIT2", "organism": "Homo sapiens", "uniprot_id": "O94813" }, { "function": "Thought to act as molecular guidance cue in cellular migration, and function appears to be mediated by interaction with roundabout homolog receptors. During neural development involved in axonal navigation at the ventral midline of the neural tube and projection of axons to different regions (By similarity). SLIT1 and SLIT2 together seem to be essential for midline guidance in the forebrain by acting as repulsive signal preventing inappropriate midline crossing by axons projecting from the olfactory bulb", "gene_name": "SLIT1", "glycan_count": 2, "glycosylation_sites": [ { "position": 72, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 192, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 406, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 571, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 630, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 762, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 801, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 806, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1026, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1079, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1189, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1259, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1306, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O75093", "name": "SLIT3", "organism": "Homo sapiens", "uniprot_id": "O75093" }, { "function": "", "gene_name": "MEST", "glycan_count": 1, "glycosylation_sites": [ { "position": 163, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q5EB52", "name": "MEST (PEG1)", "organism": "Homo sapiens", "uniprot_id": "Q5EB52" }, { "function": "ATP-driven Ca(2+) ion pump involved in the maintenance of basal intracellular Ca(2+) levels in specialized cells of cerebellar circuit and vestibular and cochlear systems (PubMed:15829536, PubMed:17234811). Uses ATP as an energy source to transport cytosolic Ca(2+) ions across the plasma membrane to the extracellular compartment (PubMed:15829536, PubMed:17234811). Has fast activation and Ca(2+) clearance rate suited to control fast neuronal Ca(2+) dynamics. At parallel fiber to Purkinje neuron synapse, mediates presynaptic Ca(2+) efflux in response to climbing fiber-induced Ca(2+) rise. Provides for fast return of Ca(2+) concentrations back to their resting levels, ultimately contributing to long-term depression induction and motor learning (By similarity). Plays an essential role in hearing and balance (PubMed:15829536, PubMed:17234811). In cochlear hair cells, shuttles Ca(2+) ions from stereocilia to the endolymph and dissipates Ca(2+) transients generated by the opening of the mechanoelectrical transduction channels. Regulates Ca(2+) levels in the vestibular system, where it contributes to the formation of otoconia (PubMed:15829536, PubMed:17234811). In non-excitable cells, regulates Ca(2+) signaling through spatial control of Ca(2+) ions extrusion and dissipation of Ca(2+) transients generated by store-operated channels (PubMed:25690014). In lactating mammary gland, allows for the high content of Ca(2+) ions in the milk (By similarity)", "gene_name": "ATP2B2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q01814", "name": "ATP2B2", "organism": "Homo sapiens", "uniprot_id": "Q01814" }, { "function": "RNA-binding protein that inhibits processing of pre-let-7 miRNAs and regulates translation of mRNAs that control developmental timing, pluripotency and metabolism (PubMed:21247876). Seems to recognize a common structural G-quartet (G4) feature in its miRNA and mRNA targets (Probable). 'Translational enhancer' that drives specific mRNAs to polysomes and increases the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in mRNA stabilization. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 expression. Suppressor of microRNA (miRNA) biogenesis, including that of let-7, miR107, miR-143 and miR-200c. Specifically binds the miRNA precursors (pre-miRNAs), recognizing an 5'-GGAG-3' motif found in pre-miRNA terminal loop, and recruits TUT4 and TUT7 uridylyltransferases (PubMed:18951094, PubMed:19703396, PubMed:22118463, PubMed:22898984). This results in the terminal uridylation of target pre-miRNAs (PubMed:18951094, PubMed:19703396, PubMed:22118463, PubMed:22898984). Uridylated pre-miRNAs fail to be processed by Dicer and undergo degradation. The repression of let-7 expression is required for normal development and contributes to maintain the pluripotent state by preventing let-7-mediated differentiation of embryonic stem cells (PubMed:18951094, PubMed:19703396, PubMed:22118463, PubMed:22898984). Localized to the periendoplasmic reticulum area, binds to a large number of spliced mRNAs and inhibits the translation of mRNAs destined for the ER, reducing the synthesis of transmembrane proteins, ER or Golgi lumen proteins, and secretory proteins. Binds to and enhances the translation of mRNAs for several metabolic enzymes, such as PFKP, PDHA1 or SDHA, increasing glycolysis and oxidative phosphorylation. Which, with the let-7 repression may enhance tissue repair in adult tissue (By similarity)", "gene_name": "LIN28A", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9H9Z2", "name": "LIN28A", "organism": "Homo sapiens", "uniprot_id": "Q9H9Z2" }, { "function": "Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. Part of a PALB2-scaffolded HR complex containing RAD51C and which is thought to play a role in DNA repair by HR. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with PALB2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity. In concert with NPM1, regulates centrosome duplication. Interacts with the TREX-2 complex (transcription and export complex 2) subunits PCID2 and SEM1, and is required to prevent R-loop-associated DNA damage and thus transcription-associated genomic instability. Silencing of BRCA2 promotes R-loop accumulation at actively transcribed genes in replicating and non-replicating cells, suggesting that BRCA2 mediates the control of R-loop associated genomic instability, independently of its known role in homologous recombination (PubMed:24896180)", "gene_name": "BRCA2", "glycan_count": 5, "glycosylation_sites": [], "id": "P51587", "name": "BRCA2", "organism": "Homo sapiens", "uniprot_id": "P51587" }, { "function": "Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix", "gene_name": "COX4I1", "glycan_count": 1, "glycosylation_sites": [], "id": "P13073", "name": "COX4", "organism": "Homo sapiens", "uniprot_id": "P13073" }, { "function": "Ligand for members of the frizzled family of seven transmembrane receptors that functions in the canonical Wnt/beta-catenin signaling pathway (By similarity). Plays an important role in embryonic development, including dorsal versus ventral patterning during limb development, skeleton development and urogenital tract development (PubMed:16826533). Required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation (PubMed:30026314). Required for normal, sexually dimorphic development of the Mullerian ducts, and for normal fertility in both sexes (By similarity). Required for normal neural stem cell proliferation in the hippocampus dentate gyrus (By similarity). Required for normal progress through the cell cycle in neural progenitor cells, for self-renewal of neural stem cells, and for normal neuronal differentiation and maturation (By similarity). Promotes formation of synapses via its interaction with FZD5 (By similarity)", "gene_name": "WNT7A", "glycan_count": 1, "glycosylation_sites": [ { "position": 83, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 127, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 295, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O00755", "name": "Wnt7b", "organism": "Homo sapiens", "uniprot_id": "O00755" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02461 (COL3A1)", "name": "N-terminal propeptide of type III procollagen (PIIINP)", "organism": "", "uniprot_id": "" }, { "function": "Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in positive and negative regulation of cell proliferation, apoptosis, differentiation, migration and adhesion, tumorigenesis, cardiac hypertrophy, angiogenesis, platelet function and inflammation, by directly phosphorylating targets such as RAF1, BCL2, CSPG4, TNNT2/CTNT, or activating signaling cascade involving MAPK1/3 (ERK1/2) and RAP1GAP. Involved in cell proliferation and cell growth arrest by positive and negative regulation of the cell cycle. Can promote cell growth by phosphorylating and activating RAF1, which mediates the activation of the MAPK/ERK signaling cascade, and/or by up-regulating CDKN1A, which facilitates active cyclin-dependent kinase (CDK) complex formation in glioma cells. In intestinal cells stimulated by the phorbol ester PMA, can trigger a cell cycle arrest program which is associated with the accumulation of the hyper-phosphorylated growth-suppressive form of RB1 and induction of the CDK inhibitors CDKN1A and CDKN1B. Exhibits anti-apoptotic function in glioma cells and protects them from apoptosis by suppressing the p53/TP53-mediated activation of IGFBP3, and in leukemia cells mediates anti-apoptotic action by phosphorylating BCL2. During macrophage differentiation induced by macrophage colony-stimulating factor (CSF1), is translocated to the nucleus and is associated with macrophage development. After wounding, translocates from focal contacts to lamellipodia and participates in the modulation of desmosomal adhesion. Plays a role in cell motility by phosphorylating CSPG4, which induces association of CSPG4 with extensive lamellipodia at the cell periphery and polarization of the cell accompanied by increases in cell motility. During chemokine-induced CD4(+) T cell migration, phosphorylates CDC42-guanine exchange factor DOCK8 resulting in its dissociation from LRCH1 and the activation of GTPase CDC42 (PubMed:28028151). Is highly expressed in a number of cancer cells where it can act as a tumor promoter and is implicated in malignant phenotypes of several tumors such as gliomas and breast cancers. Negatively regulates myocardial contractility and positively regulates angiogenesis, platelet aggregation and thrombus formation in arteries. Mediates hypertrophic growth of neonatal cardiomyocytes, in part through a MAPK1/3 (ERK1/2)-dependent signaling pathway, and upon PMA treatment, is required to induce cardiomyocyte hypertrophy up to heart failure and death, by increasing protein synthesis, protein-DNA ratio and cell surface area. Regulates cardiomyocyte function by phosphorylating cardiac troponin T (TNNT2/CTNT), which induces significant reduction in actomyosin ATPase activity, myofilament calcium sensitivity and myocardial contractility. In angiogenesis, is required for full endothelial cell migration, adhesion to vitronectin (VTN), and vascular endothelial growth factor A (VEGFA)-dependent regulation of kinase activation and vascular tube formation. Involved in the stabilization of VEGFA mRNA at post-transcriptional level and mediates VEGFA-induced cell proliferation. In the regulation of calcium-induced platelet aggregation, mediates signals from the CD36/GP4 receptor for granule release, and activates the integrin heterodimer ITGA2B-ITGB3 through the RAP1GAP pathway for adhesion. During response to lipopolysaccharides (LPS), may regulate selective LPS-induced macrophage functions involved in host defense and inflammation. But in some inflammatory responses, may negatively regulate NF-kappa-B-induced genes, through IL1A-dependent induction of NF-kappa-B inhibitor alpha (NFKBIA/IKBA). Upon stimulation with 12-O-tetradecanoylphorbol-13-acetate (TPA), phosphorylates EIF4G1, which modulates EIF4G1 binding to MKNK1 and may be involved in the regulation of EIF4E phosphorylation. Phosphorylates KIT, leading to inhibition of KIT activity. Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription. Phosphorylates SOCS2 at 'Ser-52' facilitating its ubiquitination and proteasomal degradation (By similarity). Phosphorylates KLHL3 in response to angiotensin II signaling, decreasing the interaction between KLHL3 and WNK4 (PubMed:25313067). Phosphorylates and activates LRRK1, which phosphorylates RAB proteins involved in intracellular trafficking (PubMed:36040231)", "gene_name": "PRKCA", "glycan_count": 1, "glycosylation_sites": [], "id": "P17252", "name": "PRKCA", "organism": "Homo sapiens", "uniprot_id": "P17252" }, { "function": "Non-receptor protein-tyrosine kinase that plays an essential role in regulating cell migration, adhesion, spreading, reorganization of the actin cytoskeleton, formation and disassembly of focal adhesions and cell protrusions, cell cycle progression, cell proliferation and apoptosis. Required for early embryonic development and placenta development. Required for embryonic angiogenesis, normal cardiomyocyte migration and proliferation, and normal heart development. Regulates axon growth and neuronal cell migration, axon branching and synapse formation; required for normal development of the nervous system. Plays a role in osteogenesis and differentiation of osteoblasts. Functions in integrin signal transduction, but also in signaling downstream of numerous growth factor receptors, G-protein coupled receptors (GPCR), EPHA2, netrin receptors and LDL receptors. Forms multisubunit signaling complexes with SRC and SRC family members upon activation; this leads to the phosphorylation of additional tyrosine residues, creating binding sites for scaffold proteins, effectors and substrates. Regulates numerous signaling pathways. Promotes activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascade. Promotes activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling cascade. Promotes localized and transient activation of guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), and thereby modulates the activity of Rho family GTPases. Signaling via CAS family members mediates activation of RAC1. Phosphorylates NEDD9 following integrin stimulation (PubMed:9360983). Recruits the ubiquitin ligase MDM2 to P53/TP53 in the nucleus, and thereby regulates P53/TP53 activity, P53/TP53 ubiquitination and proteasomal degradation. Phosphorylates SRC; this increases SRC kinase activity. Phosphorylates ACTN1, ARHGEF7, GRB7, RET and WASL. Promotes phosphorylation of PXN and STAT1; most likely PXN and STAT1 are phosphorylated by a SRC family kinase that is recruited to autophosphorylated PTK2/FAK1, rather than by PTK2/FAK1 itself. Promotes phosphorylation of BCAR1; GIT2 and SHC1; this requires both SRC and PTK2/FAK1. Promotes phosphorylation of BMX and PIK3R1. Isoform 6 (FRNK) does not contain a kinase domain and inhibits PTK2/FAK1 phosphorylation and signaling. Its enhanced expression can attenuate the nuclear accumulation of LPXN and limit its ability to enhance serum response factor (SRF)-dependent gene transcription", "gene_name": "PTK2", "glycan_count": 2, "glycosylation_sites": [], "id": "Q05397", "name": "PTK2 (FAK)", "organism": "Homo sapiens", "uniprot_id": "Q05397" }, { "function": "Probable role in the clearance of triglyceride-rich lipoprotein from blood. Binds chylomicrons, LDL and VLDL in presence of free fatty acids and allows their subsequent uptake in the cells (By similarity). Maintains epithelial barrier function by recruiting MARVELD2/tricellulin to tricellular tight junctions (By similarity)", "gene_name": "LSR", "glycan_count": 3, "glycosylation_sites": [], "id": "Q86X29", "name": "NLRP12", "organism": "Homo sapiens", "uniprot_id": "Q86X29" }, { "function": "Neurotrophic protein; induces extensive neuronal differentiation in retinoblastoma cells. Potent inhibitor of angiogenesis. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, it exhibits no serine protease inhibitory activity", "gene_name": "SERPINF1", "glycan_count": 57, "glycosylation_sites": [ { "position": 285, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P36955", "name": "Pigment epithelium-derived factor", "organism": "Homo sapiens", "uniprot_id": "P36955" }, { "function": "Core component of the complement C1 complex, a multiprotein complex that initiates the classical pathway of the complement system, a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system (PubMed:12847249, PubMed:19006321, PubMed:24626930, PubMed:29449492, PubMed:3258649, PubMed:34155115, PubMed:6249812, PubMed:6776418). The classical complement pathway is initiated by the C1Q subcomplex of the C1 complex, which specifically binds IgG or IgM immunoglobulins complexed with antigens, forming antigen-antibody complexes on the surface of pathogens: C1QA, together with C1QB and C1QC, specifically recognizes and binds the Fc regions of IgG or IgM via its C1q domain (PubMed:12847249, PubMed:19006321, PubMed:24626930, PubMed:29449492, PubMed:3258649, PubMed:6776418). Immunoglobulin-binding activates the proenzyme C1R, which cleaves C1S, initiating the proteolytic cascade of the complement system (PubMed:29449492). The C1Q subcomplex is activated by a hexamer of IgG complexed with antigens, while it is activated by a pentameric IgM (PubMed:19706439, PubMed:24626930, PubMed:29449492). The C1Q subcomplex also recognizes and binds phosphatidylserine exposed on the surface of cells undergoing programmed cell death, possibly promoting activation of the complement system (PubMed:18250442)", "gene_name": "C1QB", "glycan_count": 0, "glycosylation_sites": [], "id": "P02746", "name": "Complement C1q subcomponent subunit B", "organism": "Homo sapiens", "uniprot_id": "P02746" }, { "function": "Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with G at the virion surface. Upon G binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis", "gene_name": "F", "glycan_count": 0, "glycosylation_sites": [ { "position": 64, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 67, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 99, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 414, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 464, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "Q9IH63", "name": "Nipah virus glycoprotein G", "organism": "Nipah virus", "uniprot_id": "Q9IH63" }, { "function": "Interacts with host ephrinB2/EFNB2 or ephrin B3/EFNB3 to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin-mediated endocytosis", "gene_name": "G", "glycan_count": 0, "glycosylation_sites": [ { "position": 72, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 159, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 306, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 378, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 417, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 481, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 529, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "Q9IH62", "name": "Nipah virus fusion glycoprotein F", "organism": "Nipah virus", "uniprot_id": "Q9IH62" }, { "function": "", "gene_name": "env", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9IH61", "name": "Nipah virus P protein", "organism": "Human immunodeficiency virus type 1", "uniprot_id": "Q9IH61" }, { "function": "", "gene_name": "env", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9IH60", "name": "Nipah virus L protein", "organism": "Human immunodeficiency virus type 1", "uniprot_id": "Q9IH60" }, { "function": "", "gene_name": "env", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9IH59", "name": "Nipah virus N protein", "organism": "Human immunodeficiency virus type 1", "uniprot_id": "Q9IH59" }, { "function": "", "gene_name": "env", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9IH58", "name": "Nipah virus M protein", "organism": "Human immunodeficiency virus type 1", "uniprot_id": "Q9IH58" }, { "function": "Part of the tectonic-like complex which is required for tissue-specific ciliogenesis and may regulate ciliary membrane composition (By similarity). May be involved in apoptosis regulation. Necessary for signal transduction through the sonic hedgehog (Shh) signaling pathway", "gene_name": "TCTN3", "glycan_count": 11, "glycosylation_sites": [ { "position": 78, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 179, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 347, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6NUS6", "name": "UDP-glucuronosyltransferase (UGT2A1)", "organism": "Homo sapiens", "uniprot_id": "Q6NUS6" }, { "function": "", "gene_name": "CD44", "glycan_count": 0, "glycosylation_sites": [], "id": "P16070-6", "name": "CD44v6", "organism": "Homo sapiens", "uniprot_id": "P16070-6" }, { "function": "", "gene_name": "CD44", "glycan_count": 81, "glycosylation_sites": [], "id": "P16070-1", "name": "CD44s", "organism": "Homo sapiens", "uniprot_id": "P16070-1" }, { "function": "Facilitative glucose transporter (PubMed:26176916, PubMed:32860739, PubMed:9477959). Can also mediate the uptake of various other monosaccharides across the cell membrane (PubMed:26176916, PubMed:9477959). Mediates the uptake of glucose, 2-deoxyglucose, galactose, mannose, xylose and fucose, and probably also dehydroascorbate (PubMed:26176916, PubMed:9477959). Does not mediate fructose transport (PubMed:26176916, PubMed:9477959). Required for mesendoderm differentiation (By similarity)", "gene_name": "SLC2A3", "glycan_count": 1, "glycosylation_sites": [ { "position": 43, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P11169", "name": "GLUT3", "organism": "Homo sapiens", "uniprot_id": "P11169" }, { "function": "Catalyzes the phosphorylation of hexose, such as D-glucose and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D-fructose 6-phosphate, respectively) (PubMed:23185017, PubMed:26985301, PubMed:29298880). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate (PubMed:29298880). Plays a key role in maintaining the integrity of the outer mitochondrial membrane by preventing the release of apoptogenic molecules from the intermembrane space and subsequent apoptosis (PubMed:18350175)", "gene_name": "HK2", "glycan_count": 1, "glycosylation_sites": [], "id": "P52789", "name": "Hexokinase 2 (HK2)", "organism": "Homo sapiens", "uniprot_id": "P52789" }, { "function": "Catalyzes the cleavage of citrate into oxaloacetate and acetyl-CoA, the latter serving as common substrate in multiple biochemical reactions in protein, carbohydrate and lipid metabolism", "gene_name": "ACLY", "glycan_count": 1, "glycosylation_sites": [], "id": "P53396", "name": "ATP-citrate lyase (ACLY)", "organism": "Homo sapiens", "uniprot_id": "P53396" }, { "function": "Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Plays a central role in the regulatory network for splicing, controlling the intranuclear distribution of splicing factors in interphase cells and the reorganization of nuclear speckles during mitosis. Can influence additional steps of mRNA maturation, as well as other cellular activities, such as chromatin reorganization in somatic and sperm cells and cell cycle progression. Isoform 2 phosphorylates SFRS2, ZRSR2, LBR and PRM1. Isoform 2 phosphorylates SRSF1 using a directional (C-terminal to N-terminal) and a dual-track mechanism incorporating both processive phosphorylation (in which the kinase stays attached to the substrate after each round of phosphorylation) and distributive phosphorylation steps (in which the kinase and substrate dissociate after each phosphorylation event). The RS domain of SRSF1 binds first to a docking groove in the large lobe of the kinase domain of SRPK1. This induces certain structural changes in SRPK1 and/or RRM2 domain of SRSF1, allowing RRM2 to bind the kinase and initiate phosphorylation. The cycles continue for several phosphorylation steps in a processive manner (steps 1-8) until the last few phosphorylation steps (approximately steps 9-12). During that time, a mechanical stress induces the unfolding of the beta-4 motif in RRM2, which then docks at the docking groove of SRPK1. This also signals RRM2 to begin to dissociate, which facilitates SRSF1 dissociation after phosphorylation is completed. Isoform 2 can mediate hepatitis B virus (HBV) core protein phosphorylation. It plays a negative role in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein but by reducing the packaging efficiency of the pregenomic RNA (pgRNA) without affecting the formation of the viral core particles. Isoform 1 and isoform 2 can induce splicing of exon 10 in MAPT/TAU. The ratio of isoform 1/isoform 2 plays a decisive role in determining cell fate in K-562 leukaemic cell line: isoform 2 favors proliferation where as isoform 1 favors differentiation", "gene_name": "SRPK1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96SB4", "name": "SRPK2", "organism": "Homo sapiens", "uniprot_id": "Q96SB4" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P49840/P49841", "name": "Glycogen synthase kinase-3 (GSK-3)", "organism": "", "uniprot_id": "" }, { "function": "Functions as a fructose transporter that has only low activity with other monosaccharides (PubMed:16186102, PubMed:17710649, PubMed:28083649, PubMed:29548810, PubMed:8333543). Can mediate the uptake of 2-deoxyglucose, but with low efficiency (PubMed:1695905). Essential for fructose uptake in the small intestine (By similarity). Plays a role in the regulation of salt uptake and blood pressure in response to dietary fructose (By similarity). Required for the development of high blood pressure in response to high dietary fructose intake (By similarity)", "gene_name": "SLC2A5", "glycan_count": 0, "glycosylation_sites": [ { "position": 51, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P22732", "name": "GLUT5", "organism": "Homo sapiens", "uniprot_id": "P22732" }, { "function": "Proton-dependent transporter of monocarboxylates such as L-lactate and pyruvate (PubMed:11101640, PubMed:23935841, PubMed:31719150). Plays a predominant role in L-lactate efflux from highly glycolytic cells (By similarity)", "gene_name": "SLC16A3", "glycan_count": 1, "glycosylation_sites": [], "id": "O15427", "name": "MCT4", "organism": "Homo sapiens", "uniprot_id": "O15427" }, { "function": "Binds gangliosides and stimulates ganglioside GM2 degradation. It stimulates only the breakdown of ganglioside GM2 and glycolipid GA2 by beta-hexosaminidase A. It extracts single GM2 molecules from membranes and presents them in soluble form to beta-hexosaminidase A for cleavage of N-acetyl-D-galactosamine and conversion to GM3. The large binding pocket can accommodate several single chain phospholipids and fatty acids, GM2A also exhibits some calcium-independent phospholipase activity. Has cholesterol transfer activity (By similarity)", "gene_name": "Gm2a", "glycan_count": 0, "glycosylation_sites": [ { "position": 151, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q60648", "name": "Serum amyloid A3 (Saa3)", "organism": "Mus musculus", "uniprot_id": "Q60648" }, { "function": "Major acute phase protein", "gene_name": "Saa1", "glycan_count": 0, "glycosylation_sites": [], "id": "P05366", "name": "Serum amyloid A1 (Saa1)", "organism": "Mus musculus", "uniprot_id": "P05366" }, { "function": "A cytochrome P450 monooxygenase that catalyzes the side-chain hydroxylation and cleavage of cholesterol to pregnenolone, the precursor of most steroid hormones (PubMed:1773895, PubMed:2039527). Catalyzes three sequential oxidation reactions of cholesterol, namely the hydroxylation at C22 followed with the hydroxylation at C20 to yield 20R,22R-hydroxycholesterol that is further cleaved between C20 and C22 to yield the C21-steroid pregnenolone and 4-methylpentanal (PubMed:1773895, PubMed:2039527). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate and reducing the second into a water molecule. Two electrons are provided by NADPH via a two-protein mitochondrial transfer system comprising flavoprotein FDXR (adrenodoxin/ferredoxin reductase) and nonheme iron-sulfur protein FDX1 or FDX2 (adrenodoxin/ferredoxin) (PubMed:1773895, PubMed:2039527)", "gene_name": "CYP11A1", "glycan_count": 0, "glycosylation_sites": [], "id": "P10612", "name": "Cytochrome P450 2b10 (Cyp2b10)", "organism": "Sus scrofa", "uniprot_id": "P10612" }, { "function": "Involved in trafficking and recycling of synaptic vesicles", "gene_name": "Tmem230", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8CIB6", "name": "Carboxylesterase 2a (Ces2a)", "organism": "Mus musculus", "uniprot_id": "Q8CIB6" }, { "function": "Malonate and methylmalonate semialdehyde dehydrogenase involved in the catabolism of valine, thymine, and compounds catabolized by way of beta-alanine, including uracil and cytidine", "gene_name": "Aldh6a1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8CIB4", "name": "Carboxylesterase 2c (Ces2c)", "organism": "Mus musculus", "uniprot_id": "Q9EQ20" }, { "function": "Participates in the surface-dependent activation of blood coagulation. Activates, in a reciprocal reaction, coagulation factor XII/F12 after binding to negatively charged surfaces. Releases bradykinin from HMW kininogen and may also play a role in the renin-angiotensin system by converting prorenin into renin", "gene_name": "KLKB1", "glycan_count": 49, "glycosylation_sites": [ { "position": 127, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 308, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 396, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 453, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 494, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P03952", "name": "Adipsin (Complement factor D)", "organism": "Homo sapiens", "uniprot_id": "P03952" }, { "function": "Metalloproteinase with a rather broad substrate specificity that can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates different molecules including growth factors, plasminogen or other matrix metalloproteinases such as MMP9. Once released into the extracellular matrix (ECM), the inactive pro-enzyme is activated by the plasmin cascade signaling pathway. Also acts intracellularly. For example, in dopaminergic neurons, gets activated by the serine protease HTRA2 upon stress and plays a pivotal role in DA neuronal degeneration by mediating microglial activation and alpha-synuclein/SNCA cleavage (PubMed:17116747). In addition, plays a role in immune response and possesses antiviral activity against various viruses (PubMed:35940311). Mechanistically, translocates from the cytoplasm into the cell nucleus upon virus infection to influence NF-kappa-B activities (PubMed:35940311)", "gene_name": "Mmp3", "glycan_count": 0, "glycosylation_sites": [], "id": "P28862", "name": "Matrix metalloproteinase 3 (Mmp3)", "organism": "Mus musculus", "uniprot_id": "P28862" }, { "function": "Fatty acid synthetase is a multifunctional enzyme that catalyzes the de novo biosynthesis of long-chain saturated fatty acids starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This multifunctional protein contains 7 catalytic activities and a site for the binding of the prosthetic group 4'-phosphopantetheine of the acyl carrier protein ([ACP]) domain", "gene_name": "Fasn", "glycan_count": 3, "glycosylation_sites": [], "id": "P19096", "name": "Fatty acid synthase (Fas)", "organism": "Mus musculus", "uniprot_id": "P19096" }, { "function": "May play a role as endocytotic lectin receptor displaying calcium-dependent lectin activity. Internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. May be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. May contribute to cellular uptake, remodeling and degradation of extracellular collagen matrices. May participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs)", "gene_name": "Mrc2", "glycan_count": 9, "glycosylation_sites": [ { "position": 101, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 139, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 363, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1028, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1348, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q64449", "name": "Cytochrome P450 2b9 (Cyp2b9)", "organism": "Mus musculus", "uniprot_id": "Q64449" }, { "function": "Phosphorylates a large number of substrates in the cytoplasm and the nucleus (PubMed:15642694, PubMed:15905176, PubMed:16387847, PubMed:17333334, PubMed:17565987, PubMed:17693412, PubMed:18836454, PubMed:19949837, PubMed:20356841, PubMed:21085490, PubMed:21514275, PubMed:21812984, PubMed:31112131). Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA, SOX9 and VASP (PubMed:15642694, PubMed:15905176, PubMed:16387847, PubMed:17333334, PubMed:17565987, PubMed:17693412, PubMed:18836454, PubMed:19949837, PubMed:20356841, PubMed:21085490, PubMed:21514275, PubMed:21812984). Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis (PubMed:21423175). RORA is activated by phosphorylation (PubMed:21514275). Required for glucose-mediated adipogenic differentiation increase and osteogenic differentiation inhibition from osteoblasts (PubMed:19949837). Involved in chondrogenesis by mediating phosphorylation of SOX9 (By similarity). Involved in the regulation of platelets in response to thrombin and collagen; maintains circulating platelets in a resting state by phosphorylating proteins in numerous platelet inhibitory pathways when in complex with NF-kappa-B (NFKB1 and NFKB2) and I-kappa-B-alpha (NFKBIA), but thrombin and collagen disrupt these complexes and free active PRKACA stimulates platelets and leads to platelet aggregation by phosphorylating VASP (PubMed:15642694, PubMed:20356841). Prevents the antiproliferative and anti-invasive effects of alpha-difluoromethylornithine in breast cancer cells when activated (PubMed:17333334). RYR2 channel activity is potentiated by phosphorylation in presence of luminal Ca(2+), leading to reduced amplitude and increased frequency of store overload-induced Ca(2+) release (SOICR) characterized by an increased rate of Ca(2+) release and propagation velocity of spontaneous Ca(2+) waves, despite reduced wave amplitude and resting cytosolic Ca(2+) (PubMed:17693412). PSMC5/RPT6 activation by phosphorylation stimulates proteasome (PubMed:17565987). Negatively regulates tight junctions (TJs) in ovarian cancer cells via CLDN3 phosphorylation (PubMed:15905176). NFKB1 phosphorylation promotes NF-kappa-B p50-p50 DNA binding (PubMed:15642694). Required for phosphorylation of GLI transcription factors which inhibits them and prevents transcriptional activation of Hedgehog signaling pathway target genes (By similarity). GLI transcription factor phosphorylation is inhibited by interaction of PRKACA with SMO which sequesters PRKACA at the cell membrane (By similarity). Involved in embryonic development by down-regulating the Hedgehog (Hh) signaling pathway that determines embryo pattern formation and morphogenesis most probably through the regulation of OFD1 in ciliogenesis (PubMed:33934390). Prevents meiosis resumption in prophase-arrested oocytes via CDC25B inactivation by phosphorylation (By similarity). May also regulate rapid eye movement (REM) sleep in the pedunculopontine tegmental (PPT) (By similarity). Phosphorylates APOBEC3G and AICDA (PubMed:16387847, PubMed:18836454). Phosphorylates HSF1; this phosphorylation promotes HSF1 nuclear localization and transcriptional activity upon heat shock (PubMed:21085490). Acts as a negative regulator of mTORC1 by mediating phosphorylation of RPTOR (PubMed:31112131)", "gene_name": "PRKACA", "glycan_count": 1, "glycosylation_sites": [], "id": "P17612", "name": "PRKACA", "organism": "Homo sapiens", "uniprot_id": "P17612" }, { "function": "Potent inhibitor of cell death. Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis", "gene_name": "BCL2L1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q07817", "name": "BCL2L1", "organism": "Homo sapiens", "uniprot_id": "Q07817" }, { "function": "Integrin ITGAL/ITGB2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. Integrin ITGAL/ITGB2 is also a receptor for the secreted form of ubiquitin-like protein ISG15; the interaction is mediated by ITGAL (PubMed:29100055). Integrins ITGAM/ITGB2 and ITGAX/ITGB2 are receptors for the iC3b fragment of the third complement component and for fibrinogen. Integrin ITGAX/ITGB2 recognizes the sequence G-P-R in fibrinogen alpha-chain. Integrin ITGAM/ITGB2 recognizes P1 and P2 peptides of fibrinogen gamma chain. Integrin ITGAM/ITGB2 is also a receptor for factor X. Integrin ITGAD/ITGB2 is a receptor for ICAM3 and VCAM1. Contributes to natural killer cell cytotoxicity (PubMed:15356110). Involved in leukocyte adhesion and transmigration of leukocytes including T-cells and neutrophils (PubMed:11812992, PubMed:28807980). Triggers neutrophil transmigration during lung injury through PTK2B/PYK2-mediated activation (PubMed:18587400). Integrin ITGAL/ITGB2 in association with ICAM3, contributes to apoptotic neutrophil phagocytosis by macrophages (PubMed:23775590). In association with alpha subunit ITGAM/CD11b, required for CD177-PRTN3-mediated activation of TNF primed neutrophils (PubMed:21193407)", "gene_name": "ITGB2", "glycan_count": 51, "glycosylation_sites": [ { "position": 50, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 116, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 212, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 254, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 501, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 642, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P05107", "name": "ITGB2", "organism": "Homo sapiens", "uniprot_id": "P05107" }, { "function": "Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (PubMed:20949621, PubMed:39809765). Plays an important role in the regulation of cell proliferation (PubMed:22711838, PubMed:23698361). Plays a role in promoting oncogenic events by inducing transcriptional silencing of tumor suppressor genes (TSGs) in colorectal cancer (CRC) cells in a ZNF304-dependent manner (PubMed:24623306)", "gene_name": "KRAS", "glycan_count": 0, "glycosylation_sites": [ { "position": 35, "type": "(Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL" } ], "id": "P01116", "name": "HRAS", "organism": "Homo sapiens", "uniprot_id": "P01116" }, { "function": "Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268)", "gene_name": "IGHG2", "glycan_count": 136, "glycosylation_sites": [ { "position": 176, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P01859", "name": "Immunoglobulin heavy constant gamma-2 (IGHG2)", "organism": "Homo sapiens", "uniprot_id": "P01859" }, { "function": "May play a role in cell-cell or cell-ligand interactions during synaptogenesis and other events in the brain", "gene_name": "THY1", "glycan_count": 67, "glycosylation_sites": [ { "position": 42, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 79, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 119, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 139, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P04216", "name": "CD90 (Thy-1)", "organism": "Homo sapiens", "uniprot_id": "P04216" }, { "function": "Broad specificity aminopeptidase which plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. Also involved in the processing of various peptides including peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines. May also be involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis and promote cholesterol crystallization. May have a role in amino acid transport by acting as binding partner of amino acid transporter SLC6A19 and regulating its activity (By similarity)", "gene_name": "ANPEP", "glycan_count": 197, "glycosylation_sites": [ { "position": 128, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 234, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 265, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 319, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 527, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 573, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 625, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 681, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 735, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 818, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P15144", "name": "CD13 (ANPEP)", "organism": "Homo sapiens", "uniprot_id": "P15144" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01892 (HLA-A)", "name": "MHC class I", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O15131 (alpha)", "name": "Sarcoglycans (alpha, beta, gamma)", "organism": "", "uniprot_id": "" }, { "function": "Component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling (PubMed:24662292, PubMed:9354782, PubMed:9632816). The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane (By similarity). PEX12 also regulates PEX5 recycling by activating the E3 ubiquitin-protein ligase activity of PEX10 (PubMed:24662292). When PEX5 recycling is compromised, PEX12 stimulates PEX10-mediated polyubiquitination of PEX5, leading to its subsequent degradation (By similarity)", "gene_name": "PEX12", "glycan_count": 0, "glycosylation_sites": [], "id": "O00623", "name": "Caveolin-3", "organism": "Homo sapiens", "uniprot_id": "O00623" }, { "function": "Cystine/H(+) symporter that mediates export of cystine, the oxidized dimer of cysteine, from lysosomes (PubMed:11689434, PubMed:15128704, PubMed:18337546, PubMed:22232659, PubMed:29467429, PubMed:33208952, PubMed:36113465). Plays an important role in melanin synthesis by catalyzing cystine export from melanosomes, possibly by inhibiting pheomelanin synthesis (PubMed:22649030). In addition to cystine export, also acts as a positive regulator of mTORC1 signaling in kidney proximal tubular cells, via interactions with components of the v-ATPase and Ragulator complexes (PubMed:36113465). Also involved in small GTPase-regulated vesicle trafficking and lysosomal localization of LAMP2A, independently of cystine transporter activity (By similarity)", "gene_name": "CTNS", "glycan_count": 0, "glycosylation_sites": [ { "position": 36, "type": "N-linked (GlcNAc...) (high mannose) asparagine" }, { "position": 41, "type": "N-linked (GlcNAc...) (high mannose) asparagine" }, { "position": 51, "type": "N-linked (GlcNAc...) (high mannose) asparagine" }, { "position": 66, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 84, "type": "N-linked (GlcNAc...) (high mannose) asparagine" }, { "position": 104, "type": "N-linked (GlcNAc...) (high mannose) asparagine" }, { "position": 107, "type": "N-linked (GlcNAc...) (high mannose) asparagine" } ], "id": "O60931", "name": "Cystinosin", "organism": "Homo sapiens", "uniprot_id": "O60931" }, { "function": "Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the N-acetyl glucosamine (GlcNAc) of a distal alpha2,3 sialylated lactosamine unit of a glycoprotein or a glycolipid-linked sialopolylactosamines chain through an alpha-1,3 glycosidic linkage and participates in the final fucosylation step in the biosynthesis of the sialyl Lewis X (sLe(x)), a carbohydrate involved in cell and matrix adhesion during leukocyte trafficking and fertilization (PubMed:11404359, PubMed:15632313, PubMed:15926890, PubMed:18402946, PubMed:18553500, PubMed:29593094, PubMed:8207002, PubMed:8666674, PubMed:8752218, PubMed:9299472, PubMed:9405391, PubMed:9461592, PubMed:9473504, PubMed:9499379). In vitro, also synthesizes sialyl-dimeric-Lex structures, from VIM-2 structures and both di-fucosylated and trifucosylated structures from mono-fucosylated precursors (PubMed:9499379). However does not catalyze alpha 1-3 fucosylation when an internal alpha 1-3 fucosylation is present in polylactosamine chain and the fucosylation rate of the internal GlcNAc residues is reduced once fucose has been added to the distal GlcNAc (PubMed:9473504, PubMed:9499379). Also catalyzes the transfer of a fucose from GDP-beta-fucose to the 6-sulfated a(2,3)sialylated substrate to produce 6-sulfo sLex mediating significant L-selectin-dependent cell adhesion (PubMed:10200296, PubMed:8752218). Through sialyl-Lewis(x) biosynthesis, can control SELE- and SELP-mediated cell adhesion with leukocytes and allows leukocytes tethering and rolling along the endothelial tissue thereby enabling the leukocytes to accumulate at a site of inflammation (PubMed:10386892, PubMed:29138114, PubMed:8666674, PubMed:9473504, PubMed:9834120). May enhance embryo implantation through sialyl Lewis X (sLeX)-mediated adhesion of embryo cells to endometrium (PubMed:18402946, PubMed:18553500). May affect insulin signaling by up-regulating the phosphorylation and expression of some signaling molecules involved in the insulin-signaling pathway through SLe(x) which is present on the glycans of the INSRR alpha subunit (PubMed:17229154)", "gene_name": "FUT7", "glycan_count": 0, "glycosylation_sites": [ { "position": 81, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 291, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q11130", "name": "Mgat5", "organism": "Homo sapiens", "uniprot_id": "Q11130" }, { "function": "Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins", "gene_name": "FUCA1", "glycan_count": 53, "glycosylation_sites": [ { "position": 241, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 268, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 382, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P04066", "name": "FUCA1", "organism": "Homo sapiens", "uniprot_id": "P04066" }, { "function": "Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Essential component of the endosomal pH-sensing machinery (PubMed:16415858). May play a role in maintaining the Golgi functions, such as glycosylation maturation, by controlling the Golgi pH (PubMed:18157129). In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (PubMed:28296633)", "gene_name": "ATP6V0A2", "glycan_count": 7, "glycosylation_sites": [ { "position": 484, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 505, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y487", "name": "ATP6AP1 (Ac45)", "organism": "Homo sapiens", "uniprot_id": "Q9Y487" }, { "function": "Involved in ER-Golgi transport (PubMed:11929878). Also involved in retrograde (Golgi to ER) transport (PubMed:37711075)", "gene_name": "COG3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96JB2", "name": "COG6", "organism": "Homo sapiens", "uniprot_id": "Q96JB2" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8N7C6", "name": "GALNT15", "organism": "", "uniprot_id": "Q8N7C6" }, { "function": "Ferritin receptor that mediates non-transferrin-dependent delivery of iron. Mediates cellular uptake of ferritin-bound iron by stimulating ferritin endocytosis from the cell surface with consequent iron delivery within the cell. Delivery of iron to cells by ferritin is required for the development of specific cell types, suggesting the existence of cell type-specific mechanisms of iron traffic in organogenesis, which alternatively utilize transferrin or non-transferrin iron delivery pathways. Ferritin mediates iron uptake in capsule cells of the developing kidney. Preferentially binds ferritin light chain (FTL) compared to heavy chain (FTH1)", "gene_name": "SCARA5", "glycan_count": 3, "glycosylation_sites": [ { "position": 102, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 134, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 193, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 231, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 254, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 397, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6ZMJ2", "name": "CHST14", "organism": "Homo sapiens", "uniprot_id": "Q6ZMJ2" }, { "function": "Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-67 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase (By similarity). Also acts as a stimulator of insulin secretion by interacting with sulfonylurea receptor (ABCC8), thereby preventing sulfonylurea from binding to its receptor and reducing K(ATP) channel currents", "gene_name": "ENSA", "glycan_count": 2, "glycosylation_sites": [], "id": "O43768", "name": "EXTL1", "organism": "Homo sapiens", "uniprot_id": "O43768" }, { "function": "Postsynaptic scaffolding protein that plays a critical role in synaptogenesis and synaptic plasticity by providing a platform for the postsynaptic clustering of crucial synaptic proteins. Interacts with the cytoplasmic tail of NMDA receptor subunits and shaker-type potassium channels. Required for synaptic plasticity associated with NMDA receptor signaling. Overexpression or depletion of DLG4 changes the ratio of excitatory to inhibitory synapses in hippocampal neurons. May reduce the amplitude of ASIC3 acid-evoked currents by retaining the channel intracellularly. May regulate the intracellular trafficking of ADR1B. Also regulates AMPA-type glutamate receptor (AMPAR) immobilization at postsynaptic density keeping the channels in an activated state in the presence of glutamate and preventing synaptic depression (By similarity). Under basal conditions, cooperates with FYN to stabilize palmitoyltransferase ZDHHC5 at the synaptic membrane through FYN-mediated phosphorylation of ZDHHC5 and its subsequent inhibition of association with endocytic proteins (PubMed:26334723)", "gene_name": "DLG4", "glycan_count": 1, "glycosylation_sites": [], "id": "P78352", "name": "PSD-95 (DLG4)", "organism": "Homo sapiens", "uniprot_id": "P78352" }, { "function": "Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of actin, tubulin and other proteins upon ATP hydrolysis (PubMed:25467444, PubMed:36493755, PubMed:35449234, PubMed:37193829). The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance (PubMed:25467444). As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia (PubMed:20080638)", "gene_name": "CCT4", "glycan_count": 1, "glycosylation_sites": [], "id": "P50991", "name": "Annexin A11", "organism": "Homo sapiens", "uniprot_id": "P50991" }, { "function": "Protein with pleiotropic attributes mediated in a cell-compartment- and tissue-specific manner, which include the plasma membrane-associated cell signaling functions, mitochondrial chaperone, and transcriptional co-regulator of transcription factors in the nucleus (PubMed:11302691, PubMed:20959514, PubMed:28017329, PubMed:31522117). Plays a role in adipose tissue and glucose homeostasis in a sex-specific manner (By similarity). Contributes to pulmonary vascular remodeling by accelerating proliferation of pulmonary arterial smooth muscle cells (By similarity)", "gene_name": "PHB1", "glycan_count": 3, "glycosylation_sites": [], "id": "P35232", "name": "Prohibitin", "organism": "Homo sapiens", "uniprot_id": "P35232" }, { "function": "Postsynaptic scaffolding protein that plays a critical role in synaptogenesis and synaptic plasticity by providing a platform for the postsynaptic clustering of crucial synaptic proteins (PubMed:15358775, PubMed:9853749). Interacts with the cytoplasmic tail of NMDA receptor subunits and shaker-type potassium channels. Required for synaptic plasticity associated with NMDA receptor signaling. Overexpression or depletion of DLG4 changes the ratio of excitatory to inhibitory synapses in hippocampal neurons. May reduce the amplitude of ASIC3 acid-evoked currents by retaining the channel intracellularly. May regulate the intracellular trafficking of ADR1B. Also regulates AMPA-type glutamate receptor (AMPAR) immobilization at postsynaptic density keeping the channels in an activated state in the presence of glutamate and preventing synaptic depression (Probable). Under basal conditions, cooperates with FYN to stabilize palmitoyltransferase ZDHHC5 at the synaptic membrane through FYN-mediated phosphorylation of ZDHHC5 and its subsequent inhibition of association with endocytic proteins (By similarity)", "gene_name": "Dlg4", "glycan_count": 2, "glycosylation_sites": [], "id": "Q62108", "name": "\u03b1-dystroglycan (\u03b1-DAG)", "organism": "Mus musculus", "uniprot_id": "Q62108" }, { "function": "Extracellular matrix serine protease secreted by pioneer neurons that plays a role in layering of neurons in the cerebral cortex and cerebellum by coordinating cell positioning during neurodevelopment (PubMed:10880573, PubMed:11689558, PubMed:7715726, PubMed:8987733). Regulates microtubule function in neurons and neuronal migration (PubMed:10880573, PubMed:7715726, PubMed:8987733). Binding to the extracellular domains of lipoprotein receptors VLDLR and LRP8/APOER2 induces tyrosine phosphorylation of DAB1 and modulation of TAU phosphorylation (PubMed:10571241). Affects migration of sympathetic preganglionic neurons in the spinal cord, where it seems to act as a barrier to neuronal migration (PubMed:11689558, PubMed:7715726, PubMed:8987733). Enzymatic activity is important for the modulation of cell adhesion (PubMed:11689558, PubMed:8987733)", "gene_name": "Reln", "glycan_count": 12, "glycosylation_sites": [ { "position": 141, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 258, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 290, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 306, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 629, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1267, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1447, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1600, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1750, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1921, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2145, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2269, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2317, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2569, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2962, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3016, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3073, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3185, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3412, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3439, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q60841", "name": "Reelin", "organism": "Mus musculus", "uniprot_id": "Q60841" }, { "function": "Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components", "gene_name": "Lama1", "glycan_count": 23, "glycosylation_sites": [ { "position": 370, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 672, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1344, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1659, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1686, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1718, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1725, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1763, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1811, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1935, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2026, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2045, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2066, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2355, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2834, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2923, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P19137", "name": "Laminin subunit beta-1 (LAMB1)", "organism": "Mus musculus", "uniprot_id": "P19137" }, { "function": "DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Forms part of the jaw domain", "gene_name": "rpo1C", "glycan_count": 0, "glycosylation_sites": [], "id": "P14247", "name": "RPSA (Laminin receptor)", "organism": "Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)", "uniprot_id": "P14247" }, { "function": "GDP-dissociation inhibitor preventing the GDP to GTP exchange of most Rab proteins. By keeping these small GTPases in their inactive GDP-bound form regulates intracellular membrane trafficking. Negatively regulates protein transport to the cilium and ciliogenesis through the inhibition of RAB8A", "gene_name": "Gdi2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q61598", "name": "Serpinf1 (PEDF)", "organism": "Mus musculus", "uniprot_id": "Q61598" }, { "function": "Key downstream component of the canonical Wnt signaling pathway (PubMed:15132997). In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes (By similarity). Also acts as a coactivator for other transcription factors, such as NR5A2 (By similarity). Promotes epithelial to mesenchymal transition/mesenchymal to epithelial transition (EMT/MET) via driving transcription of CTNNB1/TCF-target genes (By similarity). Involved in the regulation of cell adhesion, as component of an E-cadherin:catenin adhesion complex (PubMed:16325582, PubMed:18093941). Acts as a negative regulator of centrosome cohesion. Involved in the CDK2/PTPN6/CTNNB1/CEACAM1 pathway of insulin internalization. Blocks anoikis of malignant kidney and intestinal epithelial cells and promotes their anchorage-independent growth by down-regulating DAPK2. Disrupts PML function and PML-NB formation by inhibiting RANBP2-mediated sumoylation of PML (By similarity). Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle (PubMed:21325504). Involved in chondrocyte differentiation via interaction with SOX9: SOX9-binding competes with the binding sites of TCF/LEF within CTNNB1, thereby inhibiting the Wnt signaling (PubMed:15132997). Acts as a positive regulator of odontoblast differentiation during mesenchymal tooth germ formation, via promoting the transcription of differentiation factors such as LEF1, BMP2 and BMP4 (PubMed:29148101). Activity is repressed in a MSX1-mediated manner at the bell stage of mesenchymal tooth germ formation which prevents premature differentiation of odontoblasts (PubMed:29148101)", "gene_name": "Ctnnb1", "glycan_count": 3, "glycosylation_sites": [ { "position": 23, "type": "O-linked (GlcNAc) serine; alternate" } ], "id": "Q02248", "name": "CTNNB1 (\u03b2-catenin)", "organism": "Mus musculus", "uniprot_id": "Q02248" }, { "function": "Probable thiol protease", "gene_name": "RD19D", "glycan_count": 0, "glycosylation_sites": [ { "position": 61, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 254, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8VYS0", "name": "LIN28A", "organism": "Arabidopsis thaliana", "uniprot_id": "Q8VYS0" }, { "function": "Cell surface receptor that plays an important role in the immune system, particularly in intercellular adhesion, lymphocyte signaling, cytotoxicity and lymphokine secretion mediated by cytotoxic T-cells and NK cells (PubMed:19029379, PubMed:24658051, PubMed:26552706). Functions as a costimulatory receptor upon recognition of target cells, such as virus-infected or tumor cells. Upon binding to its ligands PVR/CD155 or NECTIN2/CD112 on target cells, promotes the cytotoxic activity of NK cells and CTLs, enhancing their ability to kill these cells (PubMed:30591568). Mechanistically, phosphorylation by Src kinases such as LYN of FYN, enables binding to adapter GRB2, leading to activation of VAV1, PI3K and PLCG1. Promotes also activation of kinases ERK and AKT, as well as calcium fluxes (By similarity)", "gene_name": "Cd226", "glycan_count": 0, "glycosylation_sites": [ { "position": 44, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 84, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 91, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 98, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 181, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 199, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 233, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8K4F0", "name": "TBR2 (EOMES)", "organism": "Mus musculus", "uniprot_id": "Q8K4F0" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q4QFZ4", "name": "Glycoprotein 63 (GP63)", "organism": "Leishmania major", "uniprot_id": "Q4QFZ4" }, { "function": "Catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, and is considered to be a rate-limiting enzyme in steroid biosynthesis", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q4QFZ2", "name": "Farnesyl diphosphate synthase (FPPS)", "organism": "Leishmania major", "uniprot_id": "Q4QFZ2" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q4QFZ3", "name": "N-myristoyltransferase (NMT)", "organism": "Leishmania major", "uniprot_id": "Q4QFZ3" }, { "function": "Beta-1,3-N-acetylglucosaminyltransferase involved in the synthesis of poly-N-acetyllactosamine. Has activity for type 2 oligosaccharides (PubMed:11042166). Also acts as a core1-1,3-N-acetylglucosaminyltransferase (Core1-beta3GlcNAcT) to form the 6-sulfo sialyl Lewis x on extended core1 O-glycans (PubMed:11439191)", "gene_name": "B3GNT3", "glycan_count": 0, "glycosylation_sites": [ { "position": 64, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 184, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 202, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 362, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 367, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y2A9", "name": "GALGT2 (Beta-1,4-N-acetylgalactosaminyltransferase 2)", "organism": "Homo sapiens", "uniprot_id": "Q9Y2A9" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q13683/Q08648", "name": "Integrin alpha7/beta1", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q14623/Q16787", "name": "Laminin alpha4/alpha5", "organism": "", "uniprot_id": "" }, { "function": "Required for the normal development of the forebrain, eyes and other anterior structures such as the olfactory placodes and pituitary gland. Possible transcriptional repressor. Binds to the palindromic PIII sequence, 5'-AGCTTGAGTCTAATTGAATTAACTGTAC-3'. HESX1 and PROP1 bind as heterodimers on this palindromic site, and, in vitro, HESX1 can antagonize PROP1 activation", "gene_name": "HESX1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UBX0", "name": "Alpha-dystrobrevin", "organism": "Homo sapiens", "uniprot_id": "Q9UBX0" }, { "function": "Inactive precursor of the viral replicase, which is activated by cleavages carried out by the viral protease nsP2", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03317", "name": "E2 glycoprotein", "organism": "Sindbis virus", "uniprot_id": "P03317" }, { "function": "Forms an icosahedral capsid with a T=4 symmetry composed of 240 copies of the capsid protein surrounded by a lipid membrane through which penetrate 80 spikes composed of trimers of E1-E2 heterodimers (PubMed:12388725, PubMed:16407066, PubMed:22001018, PubMed:8415660). The capsid protein binds to the viral RNA genome at a site adjacent to a ribosome binding site for viral genome translation following genome release (By similarity). Possesses a protease activity that results in its autocatalytic cleavage from the nascent structural protein (PubMed:1944569). Following its self-cleavage, the capsid protein transiently associates with ribosomes, and within several minutes the protein binds to viral RNA and rapidly assembles into icosahedric core particles (By similarity). The resulting nucleocapsid eventually associates with the cytoplasmic domain of the spike glycoprotein E2 at the cell membrane, leading to budding and formation of mature virions (PubMed:9143274). In case of infection, new virions attach to target cells and after clathrin-mediated endocytosis their membrane fuses with the host endosomal membrane (PubMed:9707418). This leads to the release of the nucleocapsid into the cytoplasm, followed by an uncoating event necessary for the genomic RNA to become accessible (By similarity). The uncoating might be triggered by the interaction of capsid proteins with ribosomes (PubMed:3656418). Binding of ribosomes would release the genomic RNA since the same region is genomic RNA-binding and ribosome-binding (By similarity). Specifically inhibits interleukin-1 receptor-associated kinase 1/IRAK1-dependent signaling during viral entry, representing a means by which the alphaviruses may evade innate immune detection and activation prior to viral gene expression (PubMed:33673546)", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [ { "position": 278, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 524, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 646, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 945, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1051, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P03316", "name": "E1 glycoprotein", "organism": "Sindbis virus", "uniprot_id": "P03316" }, { "function": "Forms an icosahedral capsid with a T=4 symmetry composed of 240 copies of the capsid protein surrounded by a lipid membrane through which penetrate 80 spikes composed of trimers of E1-E2 heterodimers (PubMed:16407067). The capsid protein binds to the viral RNA genome at a site adjacent to a ribosome binding site for viral genome translation following genome release (By similarity). Possesses a protease activity that results in its autocatalytic cleavage from the nascent structural protein (PubMed:3553612, PubMed:9642067). Following its self-cleavage, the capsid protein transiently associates with ribosomes, and within several minutes the protein binds to viral RNA and rapidly assembles into icosahedric core particles (PubMed:516447). The resulting nucleocapsid eventually associates with the cytoplasmic domain of the spike glycoprotein E2 at the cell membrane, leading to budding and formation of mature virions (By similarity). In case of infection, new virions attach to target cells and after clathrin-mediated endocytosis their membrane fuses with the host endosomal membrane (PubMed:15954801). This leads to the release of the nucleocapsid into the cytoplasm, followed by an uncoating event necessary for the genomic RNA to become accessible (PubMed:1433506). The uncoating might be triggered by the interaction of capsid proteins with ribosomes (PubMed:1433506). Binding of ribosomes would release the genomic RNA since the same region is genomic RNA-binding and ribosome-binding (PubMed:1433506). Specifically inhibits interleukin-1 receptor-associated kinase 1/IRAK1-dependent signaling during viral entry, representing a means by which the alphaviruses may evade innate immune detection and activation prior to viral gene expression (By similarity)", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [ { "position": 280, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 327, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 533, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 595, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 956, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1085, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P03315", "name": "Capsid protein", "organism": "Semliki forest virus", "uniprot_id": "P03315" }, { "function": "Co-receptor of B cell receptor (BCR) that plays both positive and negative roles on B-cell functions. Recognizes the Sm/ribonucleoprotein (RNP) self-antigen ligand, and coligation of CD72 and BCR inhibits BCR signaling. Mechanistically, ligand binding leads to the recruitment of PTPN6/SHP-1 to the BCR complex which is inhibitory to BCR signaling. Also acts as a ligand for CD5 and thereby plays a critical role in maintaining regulatory T and B-cell homeostasis", "gene_name": "CD72", "glycan_count": 3, "glycosylation_sites": [ { "position": 136, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P21854", "name": "CD10", "organism": "Homo sapiens", "uniprot_id": "P21854" }, { "function": "Required in cooperation with CD79B for initiation of the signal transduction cascade activated by binding of antigen to the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Also required for BCR surface expression and for efficient differentiation of pro- and pre-B-cells. Stimulates SYK autophosphorylation and activation. Binds to BLNK, bringing BLNK into proximity with SYK and allowing SYK to phosphorylate BLNK. Also interacts with and increases activity of some Src-family tyrosine kinases. Represses BCR signaling during development of immature B-cells", "gene_name": "CD79A", "glycan_count": 4, "glycosylation_sites": [ { "position": 57, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 63, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 73, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 88, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 97, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 112, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P11912", "name": "CD79a", "organism": "Homo sapiens", "uniprot_id": "P11912" }, { "function": "Actin nucleation and elongation factor required for the assembly of F-actin structures, such as actin cables and stress fibers (By similarity). Binds to the barbed end of the actin filament and slows down actin polymerization and depolymerization (By similarity). Required for cytokinesis, and transcriptional activation of the serum response factor (By similarity). DFR proteins couple Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics (By similarity). Functions as a scaffold protein for MAPRE1 and APC to stabilize microtubules and promote cell migration (By similarity). Has neurite outgrowth promoting activity. Acts in a Rho-dependent manner to recruit PFY1 to the membrane (By similarity). In hear cells, it may play a role in the regulation of actin polymerization in hair cells (PubMed:20937854, PubMed:21834987, PubMed:26912466). The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (PubMed:20937854, PubMed:21834987). It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity (PubMed:20937854, PubMed:21834987). In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization (PubMed:20937854, PubMed:21834987). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape (PubMed:20937854, PubMed:21834987). Plays a role in brain development (PubMed:24781755). Also acts as an actin nucleation and elongation factor in the nucleus by promoting nuclear actin polymerization inside the nucleus to drive serum-dependent SRF-MRTFA activity (By similarity)", "gene_name": "DIAPH1", "glycan_count": 2, "glycosylation_sites": [], "id": "O60610", "name": "CD79b", "organism": "Homo sapiens", "uniprot_id": "O60610" }, { "function": "Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2) (PubMed:9084911). Participates in the formation of novel hepoxilin regioisomers (PubMed:21046276). Negatively regulates CDK5 activity via p25/p35 translocation to prevent neurodegeneration", "gene_name": "GSTP1", "glycan_count": 1, "glycosylation_sites": [], "id": "P09211", "name": "Glutathione S-transferase pi (GST-\u03c0)", "organism": "Homo sapiens", "uniprot_id": "P09211" }, { "function": "Plays a role in the formation of tricellular tight junctions and of epithelial barriers (By similarity). Required for normal hearing via its role in the separation of the endolymphatic and perilymphatic spaces of the organ of Corti in the inner ear, and for normal survival of hair cells in the organ of Corti (PubMed:17186462)", "gene_name": "MARVELD2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8N4S9", "name": "CFAP47", "organism": "Homo sapiens", "uniprot_id": "Q8N4S9" }, { "function": "Mediates selective neuronal growth and axon targeting. Contributes to the guidance of developing axons and remodeling of mature circuits in the limbic system. Essential for normal growth of the hippocampal mossy fiber projection (By similarity)", "gene_name": "LSAMP", "glycan_count": 3, "glycosylation_sites": [ { "position": 40, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 66, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 136, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 148, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 279, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 287, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 300, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 315, "type": "N-linked (GlcNAc...) asparagine; alternate" } ], "id": "Q13449", "name": "EMP1", "organism": "Homo sapiens", "uniprot_id": "Q13449" }, { "function": "Protein kinase which is a key regulator of the actin cytoskeleton and cell polarity (PubMed:10436159, PubMed:10652353, PubMed:11018042, PubMed:11283607, PubMed:17158456, PubMed:18573880, PubMed:19131646, PubMed:8617235, PubMed:9722579). Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of DAPK3, GFAP, LIMK1, LIMK2, MYL9/MLC2, TPPP, PFN1 and PPP1R12A (PubMed:10436159, PubMed:10652353, PubMed:11018042, PubMed:11283607, PubMed:17158456, PubMed:18573880, PubMed:19131646, PubMed:23093407, PubMed:23355470, PubMed:8617235, PubMed:9722579). Phosphorylates FHOD1 and acts synergistically with it to promote SRC-dependent non-apoptotic plasma membrane blebbing (PubMed:18694941). Phosphorylates JIP3 and regulates the recruitment of JNK to JIP3 upon UVB-induced stress (PubMed:19036714). Acts as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability (By similarity). Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation (PubMed:19181962). Required for centrosome positioning and centrosome-dependent exit from mitosis (By similarity). Plays a role in terminal erythroid differentiation (PubMed:21072057). Inhibits podocyte motility via regulation of actin cytoskeletal dynamics and phosphorylation of CFL1 (By similarity). Promotes keratinocyte terminal differentiation (PubMed:19997641). Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization (By similarity). May regulate closure of the eyelids and ventral body wall by inducing the assembly of actomyosin bundles (By similarity)", "gene_name": "ROCK1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q13464", "name": "ROCK1", "organism": "Homo sapiens", "uniprot_id": "Q13464" }, { "function": "ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome. In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon (By similarity)", "gene_name": "tif1", "glycan_count": 0, "glycosylation_sites": [], "id": "P47943", "name": "SOX4", "organism": "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "uniprot_id": "P47943" }, { "function": "Functions as a transcriptional regulator. Functions in cell cycle regulation through CCNA2. Plays an important role in chromosome condensation during the meiotic G2/M transition of spermatocytes. Plays a role in postnatal myogenesis, is involved in satellite cell activation (By similarity). Positively regulates IGF2 expression through PLAG1 and in a PLAG1-independent manner (PubMed:28796236)", "gene_name": "HMGA2", "glycan_count": 1, "glycosylation_sites": [], "id": "P52926", "name": "HMGA2", "organism": "Homo sapiens", "uniprot_id": "P52926" }, { "function": "Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773)", "gene_name": "EIF3J", "glycan_count": 1, "glycosylation_sites": [], "id": "O75822", "name": "EIF2B5", "organism": "Homo sapiens", "uniprot_id": "O75822" }, { "function": "Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (PubMed:31831667). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity (By similarity)", "gene_name": "RPN1", "glycan_count": 23, "glycosylation_sites": [ { "position": 299, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P04843", "name": "RPN2", "organism": "Homo sapiens", "uniprot_id": "P04843" }, { "function": "Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (PubMed:31831667). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity (By similarity). Required for the assembly of both SST3A- and SS3B-containing OST complexes (PubMed:22467853)", "gene_name": "DDOST", "glycan_count": 1, "glycosylation_sites": [], "id": "P39656", "name": "DDOST", "organism": "Homo sapiens", "uniprot_id": "P39656" }, { "function": "May be required for replication-independent chromatin assembly. May serve as a negative regulator of T-cell receptor (TCR) signaling via inhibition of calcineurin. Inhibition of activated calcineurin is dependent on both PKC and calcium signals. Acts as a negative regulator of p53/TP53 by keeping p53 in an inactive state on chromatin at promoters of a subset of it's target genes", "gene_name": "CABIN1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y6J0", "name": "MFNG", "organism": "Homo sapiens", "uniprot_id": "Q9Y6J0" }, { "function": "Plays a role as a transcription factor (PubMed:22132193, PubMed:25355627). Mediates positive transcriptional regulation of several chaperone genes during the heat shock response in a HSF1-dependent manner (PubMed:25355627, PubMed:25816751). Mediates negative transcriptional regulation of CDC25B expression (PubMed:22132193). Plays a role in the dephosphorylation of the heat shock factor HSF1 and ribosomal protein S6 kinase (S6K) by the protein phosphatase PP2A (PubMed:25816751, PubMed:26496226). Involved in the regulation of cell proliferation and resistance to thermal stress (PubMed:22132193, PubMed:25355627, PubMed:26496226). Involved in the cell cycle checkpoint and survival in response to ionizing radiation (PubMed:19238419, PubMed:22132193). Associates with chromatin to the CDC25B promoter (PubMed:22132193)", "gene_name": "IER5", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NY49", "name": "XYLT2", "organism": "Homo sapiens", "uniprot_id": "Q5VY09" }, { "function": "Required for the biosynthesis of the tetrasaccharide linkage region of proteoglycans, especially for small proteoglycans in skin fibroblasts", "gene_name": "B4GALT7", "glycan_count": 1, "glycosylation_sites": [ { "position": 154, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UBV7", "name": "B4GALT2", "organism": "Homo sapiens", "uniprot_id": "Q9UBV7" }, { "function": "Catalyzes the second step of glycosylphosphatidylinositol (GPI) biosynthesis, which is the de-N-acetylation of N-acetylglucosaminyl-phosphatidylinositol", "gene_name": "PIGL", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y2B2", "name": "PIGC", "organism": "Homo sapiens", "uniprot_id": "Q9Y2B2" }, { "function": "Pore-forming (alpha) subunit of a voltage-gated delayed rectifier (PubMed:10455180). Activates at more negative voltages, exhibits fast prepulse-independent activation kinetics and deactivates much more slowly, but shows no inactivation (By similarity)", "gene_name": "KCNH4", "glycan_count": 0, "glycosylation_sites": [ { "position": 326, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 414, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 473, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UQ05", "name": "NfH (Neurofilament heavy polypeptide)", "organism": "Homo sapiens", "uniprot_id": "Q9UQ05" }, { "function": "Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,3- or alpha-2,6-linked sialic acid (By similarity). The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, seems to act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules (PubMed:11284738, PubMed:12163025). Involved in negative regulation of B-cell antigen receptor signaling. The inhibition of B cell activation is dependent on PTPN6/SHP-1 (By similarity). In association with CD24 may be involved in the selective suppression of the immune response to danger-associated molecular patterns (DAMPs) such as HMGB1, HSP70 and HSP90 (By similarity). In association with CD24 may regulate the immune repsonse of natural killer (NK) cells (PubMed:25450598). Plays a role in the control of autoimmunity (By similarity). During initiation of adaptive immune responses by CD8-alpha(+) dendritic cells inhibits cross-presentation by impairing the formation of MHC class I-peptide complexes. The function seems to implicate recruitment of PTPN6/SHP-1, which dephosphorylates NCF1 of the NADPH oxidase complex consequently promoting phagosomal acidification (By similarity)", "gene_name": "SIGLEC10", "glycan_count": 4, "glycosylation_sites": [ { "position": 100, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 355, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 364, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 486, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 504, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q96LC7", "name": "SIGLEC10", "organism": "Homo sapiens", "uniprot_id": "Q96LC7" }, { "function": "Heterophilic receptor of the signaling lymphocytic activation molecule (SLAM) family; its ligand is CD48. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. Acts as activating natural killer (NK) cell receptor (PubMed:10359122, PubMed:11714776, PubMed:8376943). Activating function implicates association with SH2D1A and FYN (PubMed:15713798). Downstreaming signaling involves predominantly VAV1, and, to a lesser degree, INPP5D/SHIP1 and CBL. Signal attenuation in the absence of SH2D1A is proposed to be dependent on INPP5D and to a lesser extent PTPN6/SHP-1 and PTPN11/SHP-2 (PubMed:10934222, PubMed:15713798). Stimulates NK cell cytotoxicity, production of IFN-gamma and granule exocytosis (PubMed:11714776, PubMed:8376943). Optimal expansion and activation of NK cells seems to be dependent on the engagement of CD244 with CD48 expressed on neighboring NK cells (By similarity). Acts as costimulator in NK activation by enhancing signals by other NK receptors such as NCR3 and NCR1 (PubMed:10741393). At early stages of NK cell differentiation may function as an inhibitory receptor possibly ensuring the self-tolerance of developing NK cells (PubMed:11917118). Involved in the regulation of CD8(+) T-cell proliferation; expression on activated T-cells and binding to CD48 provides costimulatory-like function for neighboring T-cells (By similarity). Inhibits inflammatory responses in dendritic cells (DCs) (By similarity)", "gene_name": "CD244", "glycan_count": 0, "glycosylation_sites": [ { "position": 71, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 77, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 89, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 164, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 181, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 192, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 200, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 213, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9BZW8", "name": "CD244", "organism": "Homo sapiens", "uniprot_id": "Q9BZW8" }, { "function": "Antigen-presenting protein that binds self and non-self glycolipids and presents them to T-cell receptors on natural killer T-cells", "gene_name": "CD1D", "glycan_count": 0, "glycosylation_sites": [ { "position": 38, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 60, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 126, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 181, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P15813", "name": "CD1a", "organism": "Homo sapiens", "uniprot_id": "P15813" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q61292 (mouse)", "name": "Laminin \u03b12 (LAMA2)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q61285 (mouse)", "name": "Laminin \u03b11 (LAMA1)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04370 (mouse)", "name": "Myelin basic protein (MBP)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P31001 (mouse)", "name": "Desmin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P11276 (mouse)", "name": "Fibronectin (Fn1)", "organism": "", "uniprot_id": "" }, { "function": "Thiol protease involved in different programmed cell death processes, such as apoptosis, pyroptosis or granzyme-mediated programmed cell death, by proteolytically cleaving target proteins (PubMed:11257230, PubMed:11257231, PubMed:11701129, PubMed:15314233, PubMed:16916640, PubMed:17646170, PubMed:18723680, PubMed:19581639, PubMed:8521391, PubMed:8567622, PubMed:8576161, PubMed:9070923). Has a marked preference for Asp-Glu-Val-Asp (DEVD) consensus sequences, with some plasticity for alternate non-canonical sequences (PubMed:12824163, PubMed:15314233, PubMed:17697120, PubMed:19581639, PubMed:20566630, PubMed:23650375, PubMed:23897474, PubMed:27032039). Its involvement in the different programmed cell death processes is probably determined by upstream proteases that activate CASP7 (By similarity). Acts as an effector caspase involved in the execution phase of apoptosis: following cleavage and activation by initiator caspases (CASP8, CASP9 and/or CASP10), mediates execution of apoptosis by catalyzing cleavage of proteins, such as CLSPN, PARP1, PTGES3 and YY1 (PubMed:10497198, PubMed:16123041, PubMed:16374543, PubMed:16916640, PubMed:18723680, PubMed:20566630, PubMed:21555521, PubMed:22184066, PubMed:22451931, PubMed:27889207, PubMed:28863261, PubMed:31586028, PubMed:34156061, PubMed:35338844, PubMed:35446120). Compared to CASP3, acts as a minor executioner caspase and cleaves a limited set of target proteins (PubMed:18723680). Acts as a key regulator of the inflammatory response in response to bacterial infection by catalyzing cleavage and activation of the sphingomyelin phosphodiesterase SMPD1 in the extracellular milieu, thereby promoting membrane repair (PubMed:21157428). Regulates pyroptosis in intestinal epithelial cells: cleaved and activated by CASP1 in response to S.typhimurium infection, promoting its secretion to the extracellular milieu, where it catalyzes activation of SMPD1, generating ceramides that repair membranes and counteract the action of gasdermin-D (GSDMD) pores (By similarity). Regulates granzyme-mediated programmed cell death in hepatocytes: cleaved and activated by granzyme B (GZMB) in response to bacterial infection, promoting its secretion to the extracellular milieu, where it catalyzes activation of SMPD1, generating ceramides that repair membranes and counteract the action of perforin (PRF1) pores (By similarity). Following cleavage by CASP1 in response to inflammasome activation, catalyzes processing and inactivation of PARP1, alleviating the transcription repressor activity of PARP1 (PubMed:22464733). Acts as an inhibitor of type I interferon production during virus-induced apoptosis by mediating cleavage of antiviral proteins CGAS, IRF3 and MAVS, thereby preventing cytokine overproduction (By similarity). Cleaves and activates sterol regulatory element binding proteins (SREBPs) (PubMed:8643593). Cleaves phospholipid scramblase proteins XKR4, XKR8 and XKR9 (By similarity). In case of infection, catalyzes cleavage of Kaposi sarcoma-associated herpesvirus protein ORF57, thereby preventing expression of viral lytic genes (PubMed:20159985). Cleaves BIRC6 following inhibition of BIRC6-caspase binding by DIABLO/SMAC (PubMed:36758104, PubMed:36758106)", "gene_name": "CASP7", "glycan_count": 9, "glycosylation_sites": [], "id": "P55210", "name": "Caspase 7", "organism": "Homo sapiens", "uniprot_id": "P55210" }, { "function": "Apoptotic adapter molecule that recruits caspases CASP8 or CASP10 to the activated FAS/CD95 or TNFRSF1A/TNFR-1 receptors (PubMed:16762833, PubMed:19118384, PubMed:20935634, PubMed:23955153, PubMed:24025841, PubMed:7538907, PubMed:9184224). The resulting aggregate called the death-inducing signaling complex (DISC) performs CASP8 proteolytic activation (PubMed:16762833, PubMed:19118384, PubMed:20935634, PubMed:7538907, PubMed:9184224). Active CASP8 initiates the subsequent cascade of caspases mediating apoptosis (PubMed:16762833). Involved in interferon-mediated antiviral immune response, playing a role in the positive regulation of interferon signaling (PubMed:21109225, PubMed:24204270)", "gene_name": "FADD", "glycan_count": 2, "glycosylation_sites": [ { "position": 117, "type": "(Microbial infection) N-beta-linked (GlcNAc) arginine" } ], "id": "Q13158", "name": "FADD", "organism": "Homo sapiens", "uniprot_id": "Q13158" }, { "function": "Induces caspases and apoptosis (PubMed:14583606). Counters the protective effect of BCL2 (By similarity)", "gene_name": "BID", "glycan_count": 1, "glycosylation_sites": [], "id": "P55957", "name": "Bid", "organism": "Homo sapiens", "uniprot_id": "P55957" }, { "function": "Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain", "gene_name": "CYCS", "glycan_count": 1, "glycosylation_sites": [], "id": "P99999", "name": "Cytochrome c", "organism": "Homo sapiens", "uniprot_id": "P99999" }, { "function": "Functions as a chaperone necessary for a stable expression of the CYBA and CYBB subunits of the cytochrome b-245 heterodimer (PubMed:30361506). Controls the phagocyte respiratory burst and is essential for innate immunity (By similarity)", "gene_name": "CYBC1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9BQA9", "name": "SELENOK", "organism": "Homo sapiens", "uniprot_id": "Q9BQA9" }, { "function": "Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates and is involved in a variety of cellular processes (PubMed:15489887, PubMed:15603740, PubMed:24705354, PubMed:27911442, PubMed:28757145). Has no stringent fatty acid selectivity and in addition to palmitate can also transfer onto target proteins myristate from tetradecanoyl-CoA and stearate from octadecanoyl-CoA (By similarity). Palmitoyltransferase specific for a subset of neuronal proteins, including SNAP25, DLG4/PSD95, GAD2, SYT1 and HTT (PubMed:15489887, PubMed:15603740, PubMed:19139280, PubMed:28757145). Also palmitoylates neuronal protein GPM6A as well as SPRED1 and SPRED3 (PubMed:24705354). Could also play a role in axonogenesis through the regulation of NTRK1 and the downstream ERK1/ERK2 signaling cascade (By similarity). May be involved in the sorting or targeting of critical proteins involved in the initiating events of endocytosis at the plasma membrane (PubMed:12393793). May play a role in Mg(2+) transport (PubMed:18794299). Could also palmitoylate DNAJC5 and regulate its localization to the Golgi membrane (By similarity). Palmitoylates CASP6, thereby preventing its dimerization and subsequent activation (PubMed:27911442)", "gene_name": "ZDHHC17", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8IUH5", "name": "DHHC6", "organism": "Homo sapiens", "uniprot_id": "Q8IUH5" }, { "function": "Ionotropic glutamate receptor that functions as a ligand-gated cation channel, gated by L-glutamate and glutamatergic agonists such as alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA), quisqualic acid, and kainic acid (By similarity). L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system and plays an important role in fast excitatory synaptic transmission by inducing long-term potentiation (By similarity). Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse upon entry of calcium (PubMed:17989220). The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist (PubMed:17989220). In the presence of CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate (PubMed:21172611)", "gene_name": "GRIA3", "glycan_count": 0, "glycosylation_sites": [ { "position": 63, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 266, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 380, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 415, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 422, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P42263", "name": "GluA3 (GRIA3)", "organism": "Homo sapiens", "uniprot_id": "P42263" }, { "function": "May play a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier. It is able to induce adhesion when expressed in cells lacking tight junctions", "gene_name": "OCLN", "glycan_count": 0, "glycosylation_sites": [], "id": "OCLN_HUMAN", "name": "Occludin", "organism": "Homo sapiens", "uniprot_id": "Q16625" }, { "function": "Seems to play a role in epithelial tight junction formation. Appears early in primordial forms of cell junctions and recruits PARD3 (PubMed:11489913). The association of the PARD6-PARD3 complex may prevent the interaction of PARD3 with JAM1, thereby preventing tight junction assembly (By similarity). Plays a role in regulating monocyte transmigration involved in integrity of epithelial barrier (By similarity). Ligand for integrin alpha-L/beta-2 involved in memory T-cell and neutrophil transmigration (PubMed:11812992). Involved in platelet activation (PubMed:10753840)", "gene_name": "F11R", "glycan_count": 16, "glycosylation_sites": [ { "position": 185, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y624", "name": "Junctional Adhesion Molecule A (JAM-A)", "organism": "Homo sapiens", "uniprot_id": "Q9Y624" }, { "function": "Serine/threonine-protein kinase involved in transcription regulation, p53/TP53-mediated cellular apoptosis and regulation of the cell cycle. Acts as a corepressor of several transcription factors, including SMAD1 and POU4F1/Brn3a and probably NK homeodomain transcription factors. Phosphorylates PDX1, ATF1, PML, p53/TP53, CREB1, CTBP1, CBX4, RUNX1, EP300, CTNNB1, HMGA1, ZBTB4 and DAZAP2. Inhibits cell growth and promotes apoptosis through the activation of p53/TP53 both at the transcription level and at the protein level (by phosphorylation and indirect acetylation). The phosphorylation of p53/TP53 may be mediated by a p53/TP53-HIPK2-AXIN1 complex. Involved in the response to hypoxia by acting as a transcriptional co-suppressor of HIF1A. Mediates transcriptional activation of TP73. In response to TGFB, cooperates with DAXX to activate JNK. Negative regulator through phosphorylation and subsequent proteasomal degradation of CTNNB1 and the antiapoptotic factor CTBP1. In the Wnt/beta-catenin signaling pathway acts as an intermediate kinase between MAP3K7/TAK1 and NLK to promote the proteasomal degradation of MYB. Phosphorylates CBX4 upon DNA damage and promotes its E3 SUMO-protein ligase activity. Activates CREB1 and ATF1 transcription factors by phosphorylation in response to genotoxic stress. In response to DNA damage, stabilizes PML by phosphorylation. PML, HIPK2 and FBXO3 may act synergically to activate p53/TP53-dependent transactivation. Promotes angiogenesis, and is involved in erythroid differentiation, especially during fetal liver erythropoiesis. Phosphorylation of RUNX1 and EP300 stimulates EP300 transcription regulation activity. Triggers ZBTB4 protein degradation in response to DNA damage. In response to DNA damage, phosphorylates DAZAP2 which localizes DAZAP2 to the nucleus, reduces interaction of DAZAP2 with HIPK2 and prevents DAZAP2-dependent ubiquitination of HIPK2 by E3 ubiquitin-protein ligase SIAH1 and subsequent proteasomal degradation (PubMed:33591310). Modulates HMGA1 DNA-binding affinity. In response to high glucose, triggers phosphorylation-mediated subnuclear localization shifting of PDX1. Involved in the regulation of eye size, lens formation and retinal lamination during late embryogenesis", "gene_name": "HIPK2", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9H2X6", "name": "Fibroblast Growth Factor 19 (FGF19)", "organism": "Homo sapiens", "uniprot_id": "Q9H2X6" }, { "function": "", "gene_name": "L2HGDH", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H9P8", "name": "GMPPA (guanosine diphosphate-mannose-pyrophosphorylase-A)", "organism": "Homo sapiens", "uniprot_id": "Q9H9P8" }, { "function": "Required for 60S pre-ribosomal subunits export to the cytoplasm", "gene_name": "SDAD1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H9P6", "name": "GMPPB (guanosine diphosphate-mannose-pyrophosphorylase-B)", "organism": "Homo sapiens", "uniprot_id": "Q9NVU7" }, { "function": "Modulates secretion by lacrimal acinar cells", "gene_name": "LACRT", "glycan_count": 2, "glycosylation_sites": [ { "position": 119, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9GZZ8", "name": "Lacritin", "organism": "Homo sapiens", "uniprot_id": "Q9GZZ8" }, { "function": "Histatins (Hsts) are cationic and histidine-rich secreted peptides mainly synthesized by saliva glands of humans and higher primates (PubMed:3286634, PubMed:3944083). Hsts are considered to be major precursors of the protective proteinaceous structure on tooth surfaces (enamel pellicle). Hsts can be divided into two major groups according to their biological functions: antimicrobial Hsts (e.g. Hst 5/HTN3) and cell-activating Hsts (e.g. Hst 1/HTN1 and Hst 2/HTN1) (PubMed:32225006). Hst 1/HTN1 and Hst 2/HTN1 act in different cell types (epithelium, fibroblasts and endothelium) in oral and non-oral mucosa (PubMed:25903106, PubMed:28542418, PubMed:28751526, PubMed:32225006)", "gene_name": "HTN1", "glycan_count": 0, "glycosylation_sites": [], "id": "P15515", "name": "Proline-rich protein 4 (PROL4)", "organism": "Homo sapiens", "uniprot_id": "P15515" }, { "function": "Plays an important role in the maintenance of intestinal epithelial homeostasis and the promotion of mucosal healing. Promotes VEGF-dependent neovascularization (By similarity). Contributes to phagocytic removal of apoptotic cells in many tissues. Specific ligand for the alpha-v/beta-3 and alpha-v/beta-5 receptors. Also binds to phosphatidylserine-enriched cell surfaces in a receptor-independent manner. Zona pellucida-binding protein which may play a role in gamete interaction", "gene_name": "MFGE8", "glycan_count": 69, "glycosylation_sites": [ { "position": 228, "type": "N-linked (GlcNAc...) asparagine; atypical" }, { "position": 238, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 325, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 329, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 350, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q08431", "name": "Lactadherin", "organism": "Homo sapiens", "uniprot_id": "Q08431" }, { "function": "Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer", "gene_name": "15", "glycan_count": 0, "glycosylation_sites": [], "id": "P11187", "name": "VP7 (Rotavirus structural protein)", "organism": "Bacillus phage phi29", "uniprot_id": "P11187" }, { "function": "Relaxin is an ovarian hormone that acts with estrogen to produce dilatation of the birth canal in many mammals", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P11185", "name": "VP8* (Rotavirus spike protein)", "organism": "Balaenoptera edeni", "uniprot_id": "P11185" }, { "function": "May function in innate immunity through activation of the lectin complement pathway. Calcium-dependent and GlcNAc-binding lectin. Has affinity with GalNAc, GlcNAc, D-fucose, as mono/oligosaccharide and lipopolysaccharides from S.typhimurium and S.minnesota", "gene_name": "FCN3", "glycan_count": 14, "glycosylation_sites": [ { "position": 189, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "O75636", "name": "FCN2 (Ficolin-2)", "organism": "Homo sapiens", "uniprot_id": "O75636" }, { "function": "Adipokine that modulates insulin action by specifically inhibiting its target protease KLK7 in white adipose tissues", "gene_name": "SERPINA12", "glycan_count": 1, "glycosylation_sites": [ { "position": 221, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 233, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 267, "type": "N-linked (GlcNAc...) (high mannose) asparagine" } ], "id": "Q8IW75", "name": "SERPINA12 (Vaspin)", "organism": "Homo sapiens", "uniprot_id": "Q8IW75" }, { "function": "Receptor for the cytotoxic ligand TRAIL. Lacks a cytoplasmic death domain and hence is not capable of inducing apoptosis. May protect cells against TRAIL mediated apoptosis by competing with TRAIL-R1 and R2 for binding to the ligand", "gene_name": "TNFRSF10C", "glycan_count": 1, "glycosylation_sites": [ { "position": 77, "type": "N-linked (GlcNAc...) (high mannose) asparagine" }, { "position": 140, "type": "N-linked (GlcNAc...) (high mannose) asparagine" }, { "position": 156, "type": "N-linked (GlcNAc...) (high mannose) asparagine" } ], "id": "O14798", "name": "TNFRSF10C (TRAIL receptor 3)", "organism": "Homo sapiens", "uniprot_id": "O14798" }, { "function": "Renin is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney", "gene_name": "REN", "glycan_count": 32, "glycosylation_sites": [ { "position": 71, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 141, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P00797", "name": "REN (Renin)", "organism": "Homo sapiens", "uniprot_id": "P00797" }, { "function": "Participates in the innate immune response to Gram-positive bacteria and fungi. Specifically recognizes diacylated and, to a lesser extent, triacylated lipopeptides (PubMed:20037584). In response to diacylated lipopeptides, forms the activation cluster TLR2:TLR6:CD14:CD36, this cluster triggers signaling from the cell surface and subsequently is targeted to the Golgi in a lipid-raft dependent pathway (PubMed:16880211). Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Recognizes mycoplasmal macrophage-activating lipopeptide-2kD (MALP-2), soluble tuberculosis factor (STF), phenol-soluble modulin (PSM) and B.burgdorferi outer surface protein A lipoprotein (OspA-L) cooperatively with TLR2 (PubMed:11441107). In complex with TLR4, promotes sterile inflammation in monocytes/macrophages in response to oxidized low-density lipoprotein (oxLDL) or amyloid-beta 42. In this context, the initial signal is provided by oxLDL- or amyloid-beta 42-binding to CD36. This event induces the formation of a heterodimer of TLR4 and TLR6, which is rapidly internalized and triggers inflammatory response, leading to the NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway, as well as IL1B secretion (PubMed:11441107, PubMed:20037584)", "gene_name": "TLR6", "glycan_count": 2, "glycosylation_sites": [ { "position": 144, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 186, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 214, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 253, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 285, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 359, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 423, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 434, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 583, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y2C9", "name": "Absent in melanoma 2 (AIM2)", "organism": "Homo sapiens", "uniprot_id": "Q9Y2C9" }, { "function": "Key component of inflammasomes that indirectly senses specific proteins from pathogenic bacteria and fungi and responds by assembling an inflammasome complex that promotes caspase-1 activation, cytokine production and macrophage pyroptosis (PubMed:15107016). The NLRC4 inflammasome is activated as part of the innate immune response to a range of intracellular bacteria (By similarity)", "gene_name": "NLRC4", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NPP4", "name": "NLR family CARD domain-containing protein 4 (NLRC4)", "organism": "Homo sapiens", "uniprot_id": "Q9NPP4" }, { "function": "Thiol protease involved in a variety of inflammatory processes by proteolytically cleaving other proteins, such as the precursors of the inflammatory cytokines interleukin-1 beta (IL1B) and interleukin 18 (IL18) as well as the pyroptosis inducer Gasdermin-D (GSDMD), into active mature peptides (PubMed:15326478, PubMed:15498465, PubMed:1574116, PubMed:26375003, PubMed:32051255, PubMed:37993714, PubMed:7876192, PubMed:9334240). Plays a key role in cell immunity as an inflammatory response initiator: once activated through formation of an inflammasome complex, it initiates a pro-inflammatory response through the cleavage of the two inflammatory cytokines IL1B and IL18, releasing the mature cytokines which are involved in a variety of inflammatory processes (PubMed:15326478, PubMed:15498465, PubMed:1574116, PubMed:32051255, PubMed:7876192). Cleaves a tetrapeptide after an Asp residue at position P1 (PubMed:15498465, PubMed:1574116, PubMed:7876192). Also initiates pyroptosis, a programmed lytic cell death pathway, through cleavage of GSDMD (PubMed:26375003). In contrast to cleavage of interleukin IL1B, recognition and cleavage of GSDMD is not strictly dependent on the consensus cleavage site but depends on an exosite interface on CASP1 that recognizes and binds the Gasdermin-D, C-terminal (GSDMD-CT) part (PubMed:32051255, PubMed:32109412, PubMed:32553275). Cleaves and activates CASP7 in response to bacterial infection, promoting plasma membrane repair (PubMed:22464733). Upon inflammasome activation, during DNA virus infection but not RNA virus challenge, controls antiviral immunity through the cleavage of CGAS, rendering it inactive (PubMed:28314590). In apoptotic cells, cleaves SPHK2 which is released from cells and remains enzymatically active extracellularly (PubMed:20197547)", "gene_name": "CASP1", "glycan_count": 0, "glycosylation_sites": [], "id": "P29466", "name": "Pro-caspase-1", "organism": "Homo sapiens", "uniprot_id": "P29466" }, { "function": "Precursor of a pore-forming protein that plays a key role in host defense against pathogen infection and danger signals (PubMed:26375003, PubMed:26375259, PubMed:27281216). This form constitutes the precursor of the pore-forming protein: upon cleavage, the released N-terminal moiety (Gasdermin-D, N-terminal) binds to membranes and forms pores, triggering pyroptosis (PubMed:26375003, PubMed:26375259, PubMed:27281216)", "gene_name": "GSDMD", "glycan_count": 1, "glycosylation_sites": [ { "position": 338, "type": "O-linked (GlcNAc) serine" } ], "id": "P57764", "name": "Gasdermin D (GSDMD)", "organism": "Homo sapiens", "uniprot_id": "P57764" }, { "function": "Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus", "gene_name": "LYZ", "glycan_count": 0, "glycosylation_sites": [], "id": "P00698", "name": "Lysozyme", "organism": "Gallus gallus", "uniprot_id": "P00698" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q03721 (rat)", "name": "Kv3.4", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P22001 (rat)", "name": "Kv1.3", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q63420 (rat)", "name": "Kv1.5", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P11166 (human)", "name": "GLUT1", "organism": "", "uniprot_id": "" }, { "function": "Binds fibroblast growth factor and E-selectin (cell-adhesion lectin on endothelial cells mediating the binding of neutrophils)", "gene_name": "GLG1", "glycan_count": 0, "glycosylation_sites": [ { "position": 146, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 191, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 562, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 658, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 767, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Z1E9", "name": "\u03b2-dystroglycan", "organism": "Cricetulus griseus", "uniprot_id": "Q9Z1E9" }, { "function": "Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions (By similarity). Tyr-679 plays a critical role in TEM and is required for efficient trafficking of PECAM1 to and from the lateral border recycling compartment (LBRC) and is also essential for the LBRC membrane to be targeted around migrating leukocytes (By similarity). Trans-homophilic interaction may play a role in endothelial cell-cell adhesion via cell junctions (By similarity). Heterophilic interaction with CD177 plays a role in transendothelial migration of neutrophils (By similarity). Homophilic ligation of PECAM1 prevents macrophage-mediated phagocytosis of neighboring viable leukocytes by transmitting a detachment signal (By similarity). Promotes macrophage-mediated phagocytosis of apoptotic leukocytes by tethering them to the phagocytic cells; PECAM1-mediated detachment signal appears to be disabled in apoptotic leukocytes (By similarity). Modulates bradykinin receptor BDKRB2 activation (By similarity). Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in endothelial cells (By similarity). Induces susceptibility to atherosclerosis (PubMed:19048083)", "gene_name": "Pecam1", "glycan_count": 7, "glycosylation_sites": [ { "position": 74, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 141, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 309, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 345, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 360, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 424, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 540, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q08481", "name": "PECAM-1", "organism": "Mus musculus", "uniprot_id": "Q08481" }, { "function": "Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoA for both synthesis of cellular lipids, and degradation via beta-oxidation (PubMed:23766516, PubMed:28209804, PubMed:9096315). Preferentially activates arachidonate and eicosapentaenoate as substrates (PubMed:9096315). Preferentially activates 8,9-EET > 14,15-EET > 5,6-EET > 11,12-EET (PubMed:23766516). Modulates glucose-stimulated insulin secretion by regulating the levels of unesterified EETs (PubMed:23766516). Modulates prostaglandin E2 secretion (By similarity)", "gene_name": "Acsl4", "glycan_count": 1, "glycosylation_sites": [], "id": "O35547", "name": "Claudin-5", "organism": "Rattus norvegicus", "uniprot_id": "O35547" }, { "function": "Calcium-independent membrane-associated phospholipase that catalyzes complete diacylation of phospholipids by hydrolyzing both sn-1 and sn-2 fatty acyl chains attached to the glycerol backbone (phospholipase B activity) (By similarity). Has dual phospholipase and lysophospholipase activities toward diacylphospholipids (PubMed:11401559, PubMed:9442064, PubMed:9442065). Preferentially cleaves sn-2 ester bonds over sn-1 bonds (PubMed:9442064). Acts as a lipase toward glycerolipid substrates (PubMed:11401559, PubMed:9442064, PubMed:9442065). Hydrolyzes fatty acyl chains of diacylglycerols with preference for the sn-2 position and of triacylglycerols with not positional selectivity (PubMed:11401559, PubMed:9442064, PubMed:9442065). May also hydrolyze long chain retinyl esters such as retinyl palmitate (By similarity). May contribute to digestion of dietary phospholipids, glycerolipids and retinoids, facilitating lipid absorption at the brush border (Probable)", "gene_name": "Plb1", "glycan_count": 0, "glycosylation_sites": [ { "position": 32, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 45, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 179, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 699, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 787, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 801, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 844, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 880, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 926, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1059, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1226, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1280, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1383, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1387, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O54728", "name": "Aquaporin-4", "organism": "Rattus norvegicus", "uniprot_id": "O54728" }, { "function": "Anchors the extracellular matrix to the cytoskeleton via F-actin. Ligand for dystroglycan. Component of the dystrophin-associated glycoprotein complex which accumulates at the neuromuscular junction (NMJ) and at a variety of synapses in the peripheral and central nervous systems and has a structural function in stabilizing the sarcolemma. Also implicated in signaling events and synaptic transmission", "gene_name": "Dmd", "glycan_count": 4, "glycosylation_sites": [], "id": "P11531", "name": "Dystrophin", "organism": "Mus musculus", "uniprot_id": "P11531" }, { "function": "Mediates the anchoring of the endoplasmic reticulum to microtubules", "gene_name": "CKAP4", "glycan_count": 2, "glycosylation_sites": [], "id": "Q07065", "name": "CD13", "organism": "Homo sapiens", "uniprot_id": "Q07065" }, { "function": "Within the IPP (ILK-PINCH-PARVIN) complex, binds to F-actin, promoting F-actin bundling, a process required to generate force for actin cytoskeleton reorganization and subsequent dynamic cell adhesion events such as cell spreading and migration", "gene_name": "Lims1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q99JW4", "name": "Cadherin-13", "organism": "Mus musculus", "uniprot_id": "Q99JW4" }, { "function": "Lipid-binding protein required for SHH long-range signaling by binding to the dually lipid-modified SHH (ShhNp) and by promoting ShhNp mobilization, solubilization and release from the cell membrane (PubMed:22677548, PubMed:22902404). Acts by enhancing the proteolytic processing (shedding) of the lipid-modified N- and C- terminal of ShhNp at the cell surface (PubMed:24522195). Synergizes with DISP1 to increase SHH secretion (PubMed:22902404). Probable cell surface coreceptor for VEGFR2 involved in VEGFR2-mediated angiogenesis (PubMed:27834687)", "gene_name": "SCUBE2", "glycan_count": 3, "glycosylation_sites": [ { "position": 659, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NQ36", "name": "Soluble Suppression of Tumorigenicity-2 (sST2)", "organism": "Homo sapiens", "uniprot_id": "Q9NQ36" }, { "function": "Mediates selective transcytosis of polymeric IgA and IgM across mucosal epithelial cells. Binds polymeric IgA and IgM at the basolateral surface of epithelial cells. The complex is then transported across the cell to be secreted at the apical surface. During this process, a cleavage occurs that separates the extracellular (known as the secretory component) from the transmembrane segment", "gene_name": "PIGR", "glycan_count": 323, "glycosylation_sites": [ { "position": 83, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 90, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 135, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 186, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 421, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 469, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 499, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01833", "name": "Polymeric Immunoglobulin Receptor (PIGR)", "organism": "Homo sapiens", "uniprot_id": "P01833" }, { "function": "Functions as a carrier for hydrophobic molecules in body fluids (Probable). Essential for the solubility and activity of lipidated Wnt family members, including WNT1, WNT2B, WNT3, WNT3A, WNT5A, WNT7A, WNT7B, WNT8, WNT9A, WNT9B, WNT10A and WNT10B (PubMed:26902720). Binds vitamin E (PubMed:12463752, PubMed:15952736). May transport vitamin E in body fluids under conditions where the lipoprotein system is not sufficient (PubMed:15952736). May be involved in the transport of vitamin E across the blood-brain barrier (PubMed:19046407)", "gene_name": "AFM", "glycan_count": 68, "glycosylation_sites": [ { "position": 33, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 109, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 383, "type": "N-linked (GlcNAc...) (complex) asparagine; atypical" }, { "position": 402, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 488, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P43652", "name": "Afamin (AFM)", "organism": "Homo sapiens", "uniprot_id": "P43652" }, { "function": "Component of the epidermal cornified cell envelopes", "gene_name": "HRNR", "glycan_count": 1, "glycosylation_sites": [], "id": "Q86YZ3", "name": "Hornerin (HRNR)", "organism": "Homo sapiens", "uniprot_id": "Q86YZ3" }, { "function": "Digestive protease that cleaves proteins preferentially after an Arg residue and has proteolytic activity toward Kunitz-type trypsin inhibitors", "gene_name": "PRSS3", "glycan_count": 1, "glycosylation_sites": [], "id": "P35030", "name": "Serine Protease 3 (PRSS3)", "organism": "Homo sapiens", "uniprot_id": "P35030" }, { "function": "Glycosyltransferase that catalyze the transfer of GlcNAc from UDP-GlcNAc to the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans through a beta1-4 linkage and participates in the production of tri- and tetra-antennary N-linked sugar chains (PubMed:17006639). Involved in glucose transport by mediating SLC2A2/GLUT2 glycosylation, thereby controlling cell-surface expression of SLC2A2 in pancreatic beta cells (By similarity)", "gene_name": "MGAT4A", "glycan_count": 0, "glycosylation_sites": [ { "position": 77, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 458, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UM21", "name": "TMEM106B", "organism": "Homo sapiens", "uniprot_id": "Q9UM21" }, { "function": "Inhibitor of lipoprotein binding to the low density lipoprotein (LDL) receptor, LDL receptor-related protein, and very low density lipoprotein (VLDL) receptor. Associates with high density lipoproteins (HDL) and the triacylglycerol-rich lipoproteins in the plasma and makes up about 10% of the protein of the VLDL and 2% of that of HDL. Appears to interfere directly with fatty acid uptake and is also the major plasma inhibitor of cholesteryl ester transfer protein (CETP). Binds free fatty acids and reduces their intracellular esterification. Modulates the interaction of APOE with beta-migrating VLDL and inhibits binding of beta-VLDL to the LDL receptor-related protein", "gene_name": "APOC1", "glycan_count": 0, "glycosylation_sites": [], "id": "P02654", "name": "Apolipoprotein C1 (ApoC1)", "organism": "Homo sapiens", "uniprot_id": "P02654" }, { "function": "GTPase activator for the Rho, Rac and Cdc42 proteins, converting them to the putatively inactive GDP-bound state. Cdc42 seems to be the preferred substrate", "gene_name": "ARHGAP1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q07960", "name": "IQ motif containing GTPase activating protein 1 (IQGAP1)", "organism": "Homo sapiens", "uniprot_id": "Q07960" }, { "function": "Signaling adapter protein that participates in the signal transduction from two prominent receptor tyrosine kinases, insulin receptor/INSR and insulin-like growth factor I receptor/IGF1R (PubMed:25879670). Plays therefore an important role in development, growth, glucose homeostasis as well as lipid metabolism (PubMed:24616100). Upon phosphorylation by the insulin receptor, functions as a signaling scaffold that propagates insulin action through binding to SH2 domain-containing proteins including the p85 regulatory subunit of PI3K, NCK1, NCK2, GRB2 or SHP2 (PubMed:15316008, PubMed:19109239). Recruitment of GRB2 leads to the activation of the guanine nucleotide exchange factor SOS1 which in turn triggers the Ras/Raf/MEK/MAPK signaling cascade (By similarity). Activation of the PI3K/AKT pathway is responsible for most of insulin metabolic effects in the cell, and the Ras/Raf/MEK/MAPK is involved in the regulation of gene expression and in cooperation with the PI3K pathway regulates cell growth and differentiation. Acts a positive regulator of the Wnt/beta-catenin signaling pathway through suppression of DVL2 autophagy-mediated degradation leading to cell proliferation (PubMed:24616100). Plays a role in cell cycle progression by promoting a robust spindle assembly checkpoint (SAC) during M-phase (PubMed:32554797). In macrophages, IL4-induced tyrosine phosphorylation of IRS2 leads to the recruitment and activation of phosphoinositide 3-kinase (PI3K) (PubMed:19109239)", "gene_name": "IRS2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y4H2", "name": "Insulin receptor substrate 2 (IRS2)", "organism": "Homo sapiens", "uniprot_id": "Q9Y4H2" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Various", "name": "Exocyst complex proteins (Sec5, Sec8, Exo70)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "N/A", "name": "Pancreatic \u03b2 cell insulin secretory machinery", "organism": "", "uniprot_id": "" }, { "function": "Modulates apoptotic signal transduction or effector structures within the mitochondrial matrix. Affect cytochrome C release from the mitochondria and caspase 3 activation, but not caspase 8 activation. Isoform 1 increases apoptosis triggered by both TNF and the DNA-damaging agent mytomycin C; in sharp contrast, isoform 2 suppresses apoptosis. Can modulate IFN-gamma-mediated transcriptional activity (By similarity). Isoform 2 may play a role in neuromuscular junction development as an effector of the MUSK signaling pathway", "gene_name": "Dnaja3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q99M87", "name": "ST6GAL1", "organism": "Mus musculus", "uniprot_id": "Q99M87" }, { "function": "Inhibitory receptor on antigen activated T-cells that plays a critical role in induction and maintenance of immune tolerance to self (PubMed:10485649, PubMed:11209085, PubMed:11698646, PubMed:21300912). Delivers inhibitory signals upon binding to ligands, such as CD274/PDCD1L1 and CD273/PDCD1LG2 (PubMed:11015443, PubMed:11224527, PubMed:18287011, PubMed:18641123, PubMed:22641383). Following T-cell receptor (TCR) engagement, PDCD1 associates with CD3-TCR in the immunological synapse and directly inhibits T-cell activation (PubMed:22641383). Suppresses T-cell activation through the recruitment of PTPN11/SHP-2: following ligand-binding, PDCD1 is phosphorylated within the ITSM motif, leading to the recruitment of the protein tyrosine phosphatase PTPN11/SHP-2 that mediates dephosphorylation of key TCR proximal signaling molecules, such as ZAP70, PRKCQ/PKCtheta and CD247/CD3zeta (PubMed:11698646, PubMed:22641383). The PDCD1-mediated inhibitory pathway is exploited by tumors to attenuate anti-tumor immunity and facilitate tumor survival (By similarity)", "gene_name": "Pdcd1", "glycan_count": 0, "glycosylation_sites": [ { "position": 49, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 58, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 74, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 116, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q02242", "name": "PD-1 (Programmed cell death protein 1)", "organism": "Mus musculus", "uniprot_id": "Q02242" }, { "function": "Inhibitory receptor acting as a major negative regulator of T-cell responses. The affinity of CTLA4 for its natural B7 family ligands, CD80 and CD86, is considerably stronger than the affinity of their cognate stimulatory coreceptor CD28", "gene_name": "Ctla4", "glycan_count": 1, "glycosylation_sites": [ { "position": 108, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 113, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 145, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P09793", "name": "CTLA-4", "organism": "Mus musculus", "uniprot_id": "P09793" }, { "function": "Lymphocyte activation gene 3 protein: Inhibitory receptor on antigen activated T-cells (PubMed:12209638, PubMed:12421911, PubMed:12672063, PubMed:15100286, PubMed:15634887, PubMed:30580966). Delivers inhibitory signals upon binding to ligands, such as FGL1 (PubMed:30580966). FGL1 constitutes a major ligand of LAG3 and is responsible for LAG3 T-cell inhibitory function (PubMed:30580966). Following TCR engagement, LAG3 associates with CD3-TCR in the immunological synapse and directly inhibits T-cell activation (PubMed:12209638, PubMed:12421911, PubMed:12672063, PubMed:15100286, PubMed:15634887). May inhibit antigen-specific T-cell activation in synergy with PDCD1/PD-1, possibly by acting as a coreceptor for PDCD1/PD-1 (PubMed:21300912). Negatively regulates the proliferation, activation, effector function and homeostasis of both CD8(+) and CD4(+) T-cells (PubMed:12209638, PubMed:12421911, PubMed:12672063, PubMed:15100286, PubMed:15634887). Also mediates immune tolerance: constitutively expressed on a subset of regulatory T-cells (Tregs) and contributes to their suppressive function (PubMed:15485628). Also acts as a negative regulator of plasmacytoid dendritic cell (pDCs) activation (PubMed:19201841). Binds MHC class II (MHC-II); the precise role of MHC-II-binding is however unclear (PubMed:12209638, PubMed:12421911, PubMed:15634887)", "gene_name": "Lag3", "glycan_count": 0, "glycosylation_sites": [ { "position": 184, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 244, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 309, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 337, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 381, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q61790", "name": "LAG-3", "organism": "Mus musculus", "uniprot_id": "Q61790" }, { "function": "Cell surface receptor implicated in modulating innate and adaptive immune responses. Generally accepted to have an inhibiting function. Reports on stimulating functions suggest that the activity may be influenced by the cellular context and/or the respective ligand (PubMed:18006747). Regulates macrophage activation (PubMed:11823861). Inhibits T-helper type 1 lymphocyte (Th1)-mediated auto- and alloimmune responses and promotes immunological tolerance (PubMed:14556006, PubMed:18006747). In CD8+ cells attenuates TCR-induced signaling, specifically by blocking NF-kappaB and NFAT promoter activities resulting in the loss of IL-2 secretion. The function may implicate its association with LCK proposed to impair phosphorylation of TCR subunits (By similarity). In contrast, shown to activate TCR-induced signaling in T-cells probably implicating ZAP70, LCP2, LCK and FYN (PubMed:21807895). Expressed on Treg cells can inhibit Th17 cell responses (By similarity). Receptor for LGALS9. Binding to LGALS9 is believed to result in suppression of T-cell responses; the resulting apoptosis of antigen-specific cells may implicate HAVCR2 phosphorylation and disruption of its association with BAG6 (PubMed:22863785). Binding to LGALS9 is proposed to be involved in innate immune response to intracellular pathogens. Expressed on Th1 cells interacts with LGALS9 expressed on Mycobacterium tuberculosis-infected macrophages to stimulate antibactericidal activity including IL-1 beta secretion and to restrict intracellular bacterial growth (PubMed:20937702). However, the function as receptor for LGALS9 has been challenged (By similarity). Also reported to enhance CD8+ T-cell responses to an acute infection such as by Listeria monocytogenes (PubMed:24567532). Receptor for phosphatidylserine (PtSer); PtSer-binding is calcium-dependent (PubMed:20083673). May recognize PtSer on apoptotic cells leading to their phagocytosis. Mediates the engulfment of apoptotic cells by dendritic cells (PubMed:19224762). Expressed on T-cells, promotes conjugation but not engulfment of apoptotic cells (PubMed:20083673). Expressed on dendritic cells (DCs) positively regulates innate immune response and in synergy with Toll-like receptors promotes secretion of TNF-alpha (PubMed:18006747). In tumor-imfiltrating DCs suppresses nucleic acid-mediated innate immune repsonse by interaction with HMGB1 and interfering with nucleic acid-sensing and trafficking of nucleid acids to endosomes (PubMed:22842346). Can enhance mast cell production of Th2 cytokines Il-4, IL-6 and IL-13 (PubMed:17620455). Expressed on natural killer (NK) cells acts as a coreceptor to enhance IFN-gamma production in response to LGALS9. In contrast, shown to suppress NK cell-mediated cytotoxicity (By similarity). Negatively regulates NK cell function in LPS-induced endotoxic shock (PubMed:25337993)", "gene_name": "Havcr2", "glycan_count": 1, "glycosylation_sites": [ { "position": 74, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 100, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 146, "type": "O-linked (GalNAc...) threonine" }, { "position": 172, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8VIM0", "name": "TIM-3", "organism": "Mus musculus", "uniprot_id": "Q8VIM0" }, { "function": "Calcium-dependent lectin that mediates cell adhesion by binding to glycoproteins on neighboring cells. Mediates the adherence of lymphocytes to endothelial cells of high endothelial venules in peripheral lymph nodes (PubMed:1693096). Promotes initial tethering and rolling of leukocytes in endothelia (By similarity)", "gene_name": "Sell", "glycan_count": 1, "glycosylation_sites": [ { "position": 60, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 177, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 216, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 226, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 246, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 278, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 288, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 308, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 320, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P18337", "name": "CD62L (L-selectin)", "organism": "Mus musculus", "uniprot_id": "P18337" }, { "function": "Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class I molecule:peptide complex. The antigens presented by class I peptides are derived from cytosolic proteins while class II derived from extracellular proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class I proteins presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of cytotoxic T-lymphocytes (CTLs). This mechanism enables CTLs to recognize and eliminate infected cells and tumor cells. In NK-cells, the presence of CD8A homodimers at the cell surface provides a survival mechanism allowing conjugation and lysis of multiple target cells. CD8A homodimer molecules also promote the survival and differentiation of activated lymphocytes into memory CD8 T-cells", "gene_name": "Cd8a", "glycan_count": 0, "glycosylation_sites": [ { "position": 69, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 97, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 150, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01731", "name": "CD8", "organism": "Mus musculus", "uniprot_id": "P01731" }, { "function": "Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class II molecule:peptide complex. The antigens presented by class II peptides are derived from extracellular proteins while class I peptides are derived from cytosolic proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class II presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. LCK then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of T-helper cells. In other cells such as macrophages or NK cells, plays a role in differentiation/activation, cytokine expression and cell migration in a TCR/LCK-independent pathway. Participates in the development of T-helper cells in the thymus and triggers the differentiation of monocytes into functional mature macrophages", "gene_name": "Cd4", "glycan_count": 0, "glycosylation_sites": [ { "position": 187, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 298, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 323, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 392, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P06332", "name": "CD4", "organism": "Mus musculus", "uniprot_id": "P06332" }, { "function": "May be implicated in B-cell differentiation and lymphomagenesis", "gene_name": "FCRLA", "glycan_count": 1, "glycosylation_sites": [], "id": "Q7L513", "name": "FcRn", "organism": "Homo sapiens", "uniprot_id": "Q7L513" }, { "function": "Receptor for gastrin and cholecystokinin. The CCK-B receptors occur throughout the central nervous system where they modulate anxiety, analgesia, arousal, and neuroleptic activity. This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system", "gene_name": "CCKBR", "glycan_count": 0, "glycosylation_sites": [ { "position": 7, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 30, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 36, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P32239", "name": "Cholecystokinin B receptor", "organism": "Homo sapiens", "uniprot_id": "P32239" }, { "function": "Transports Fe(2+) from the inside of a cell to the outside of the cell, playing a key role for maintaining systemic iron homeostasis (PubMed:15692071, PubMed:22178646, PubMed:22682227, PubMed:24304836, PubMed:29237594, PubMed:29599243, PubMed:30247984). Transports iron from intestinal, splenic, hepatic cells, macrophages and erythrocytes into the blood to provide iron to other tissues (By similarity). Controls therefore dietary iron uptake, iron recycling by macrophages and erythrocytes, and release of iron stores in hepatocytes (By similarity). When iron is in excess in serum, circulating HAMP/hepcidin levels increase resulting in a degradation of SLC40A1, thus limiting the iron efflux to plasma (PubMed:22682227, PubMed:29237594, PubMed:32814342)", "gene_name": "SLC40A1", "glycan_count": 1, "glycosylation_sites": [ { "position": 434, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NP59", "name": "Ferroportin (FPN1)", "organism": "Homo sapiens", "uniprot_id": "Q9NP59" }, { "function": "Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) generated by peroxisomal oxidases to water and oxygen, thereby protecting cells from the toxic effects of hydrogen peroxide (PubMed:7882369). Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells (PubMed:7882369)", "gene_name": "CAT", "glycan_count": 17, "glycosylation_sites": [], "id": "P04040", "name": "Catalase (CAT)", "organism": "Homo sapiens", "uniprot_id": "P04040" }, { "function": "Secreted glycoprotein that is involved in various physiological processes, such as angiogenesis, regulation of the immune response, cell proliferation and differentiation (PubMed:22265692, PubMed:29212066). Plays a role in the development of the central nervous system, skeletal system, lungs, and ureter (By similarity). Promotes endothelial cell survival, migration and differentiation into network structures in an AKT-dependent manner. Also promotes survival of cardiac myocytes (By similarity). Initiates various signaling cascades by activating different receptors on the cell surface such as DIP2A, TLR4 or BMP receptors (PubMed:20054002, PubMed:22265692)", "gene_name": "FSTL1", "glycan_count": 27, "glycosylation_sites": [ { "position": 144, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 175, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 180, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q12841", "name": "FSTL1", "organism": "Homo sapiens", "uniprot_id": "Q12841" }, { "function": "This is one of the three pore-forming subunits of the heterotrimeric epithelial sodium channel (ENaC), a critical regulator of sodium balance and fluid homeostasis (PubMed:30251954, PubMed:32729833, PubMed:8023962, PubMed:8278374, PubMed:9792722). ENaC operates in epithelial tissues, where it mediates the electrodiffusion of sodium ions from extracellular fluid through the apical membrane of cells, with water following osmotically (PubMed:24124190, PubMed:28710092, PubMed:8278374). It plays a key role in maintaining sodium homeostasis through electrogenic sodium reabsorption in the kidneys (PubMed:12107247). Additionally, ENaC is essential for airway surface liquid homeostasis, which is crucial for proper mucus clearance (PubMed:24124190, PubMed:28710092)", "gene_name": "SCNN1A", "glycan_count": 3, "glycosylation_sites": [], "id": "P37088", "name": "\u03b1ENaC (SCNN1A)", "organism": "Homo sapiens", "uniprot_id": "P37088" }, { "function": "Receptor component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity. May act through the stabilization of endothelial cell junctions", "gene_name": "HEG1", "glycan_count": 32, "glycosylation_sites": [ { "position": 67, "type": "O-linked (GalNAc...) threonine" }, { "position": 123, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 159, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 180, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 314, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 462, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 520, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 610, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1137, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9ULI3", "name": "DAAM2", "organism": "Homo sapiens", "uniprot_id": "Q9ULI3" }, { "function": "Key regulator of protein phosphatase 1C (PPP1C). Mediates binding to myosin. As part of the PPP1C complex, involved in dephosphorylation of PLK1. Capable of inhibiting HIF1AN-dependent suppression of HIF1A activity", "gene_name": "PPP1R12A", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9BYH0", "name": "CHL1", "organism": "Homo sapiens", "uniprot_id": "O14974" }, { "function": "Actin-organizing protein that may cause stress fiber formation together with cell elongation (By similarity). Isoform 4 may play a role in actin filament polymerization in cardiomyocytes", "gene_name": "FHOD3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q2V2M9", "name": "FHOD3", "organism": "Homo sapiens", "uniprot_id": "Q2V2M9" }, { "function": "Involved in the splicing process and participates in early heat shock-induced splicing arrest. Due to their great structural variations the different isoforms may possess different functions in the splicing reaction", "gene_name": "HNRNPH3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UFU4", "name": "MYO18A", "organism": "Homo sapiens", "uniprot_id": "P31942" }, { "function": "Subunit of non-clathrin- and clathrin-associated adaptor protein complex 3 (AP-3) that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. AP-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related organelles. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals", "gene_name": "AP3B1", "glycan_count": 1, "glycosylation_sites": [], "id": "O00203", "name": "\u03b2-Sarcoglycan (SGCB)", "organism": "Homo sapiens", "uniprot_id": "O00203" }, { "function": "Transcription factor that plays a key role in cardiovascular development by promoting pharyngeal arch segmentation during embryonic development (By similarity). Also involved in craniofacial muscle development (By similarity). Together with NKX2-5, acts as a regulator of asymmetric cardiac morphogenesis by promoting expression of PITX2 (By similarity). Acts upstream of TBX1 for the formation of the thymus and parathyroid glands from the third pharyngeal pouch (By similarity). Required for hair follicle stem cell self-renewal (By similarity). Binds to the palindromic T site 5'-TTCACACCTAGGTGTGAA-3' DNA sequence (PubMed:11111039, PubMed:22095455)", "gene_name": "TBX1", "glycan_count": 0, "glycosylation_sites": [], "id": "O43435", "name": "\u03b3-Sarcoglycan (SGCG)", "organism": "Homo sapiens", "uniprot_id": "O43435" }, { "function": "Catalytic tRNA acetyltransferase subunit of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine) (PubMed:29415125). In the elongator complex, acts as a tRNA uridine(34) acetyltransferase by mediating formation of carboxymethyluridine in the wobble base at position 34 in tRNAs (By similarity). May also act as a protein lysine acetyltransferase by mediating acetylation of target proteins; such activity is however unclear in vivo and recent evidences suggest that ELP3 primarily acts as a tRNA acetyltransferase (PubMed:29415125). Involved in neurogenesis: regulates the migration and branching of projection neurons in the developing cerebral cortex, through a process depending on alpha-tubulin acetylation (PubMed:19185337). Required for acetylation of GJA1 in the developing cerebral cortex (By similarity)", "gene_name": "ELP3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H9T3", "name": "FKRP", "organism": "Homo sapiens", "uniprot_id": "Q9H9T3" }, { "function": "Tyrosine kinase that functions as a cell surface receptor for fibrillar collagen and regulates cell attachment to the extracellular matrix, remodeling of the extracellular matrix, cell migration, differentiation, survival and cell proliferation. Collagen binding triggers a signaling pathway that involves SRC and leads to the activation of MAP kinases. Regulates remodeling of the extracellular matrix by up-regulation of the matrix metalloproteinases MMP2, MMP7 and MMP9, and thereby facilitates cell migration and wound healing. Required for normal blastocyst implantation during pregnancy, for normal mammary gland differentiation and normal lactation. Required for normal ear morphology and normal hearing (By similarity). Promotes smooth muscle cell migration, and thereby contributes to arterial wound healing. Also plays a role in tumor cell invasion. Phosphorylates PTPN11", "gene_name": "DDR1", "glycan_count": 1, "glycosylation_sites": [ { "position": 211, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 260, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 370, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 394, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q08345", "name": "GMPPB", "organism": "Homo sapiens", "uniprot_id": "Q08345" }, { "function": "Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (PubMed:12411443, PubMed:12475965). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (PubMed:12411443). Acts as a key repressor of the EIF2AK3/PERK and ERN1/IRE1-mediated unfolded protein response (UPR) (PubMed:10854322). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to disrupt the dimerization of ERN1/IRE1, thereby inactivating ERN1/IRE1 (By similarity). Also binds and inactivates EIF2AK3/PERK in unstressed cells (PubMed:10854322). Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP from ERN1/IRE1 and EIF2AK3/PERK, allowing their homodimerization and subsequent activation (PubMed:10854322). Plays an auxiliary role in post-translational transport of small presecretory proteins across endoplasmic reticulum (ER). May function as an allosteric modulator for SEC61 channel-forming translocon complex, likely cooperating with SEC62 to enable the productive insertion of these precursors into SEC61 channel. Appears to specifically regulate translocation of precursors having inhibitory residues in their mature region that weaken channel gating. May also play a role in apoptosis and cell proliferation (By similarity)", "gene_name": "Hspa5", "glycan_count": 1, "glycosylation_sites": [], "id": "P20029", "name": "GRP78 (Glucose-regulated protein 78)", "organism": "Mus musculus", "uniprot_id": "P20029" }, { "function": "Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane", "gene_name": "SPTA1", "glycan_count": 1, "glycosylation_sites": [], "id": "P02549", "name": "Spectrin", "organism": "Homo sapiens", "uniprot_id": "P02549" }, { "function": "Catalyzes the hydrolysis of GTP and utilizes this energy to mediate vesicle scission and participates in many forms of endocytosis, such as clathrin-mediated endocytosis or synaptic vesicle endocytosis as well as rapid endocytosis (RE) (PubMed:15703209, PubMed:20428113, PubMed:29668686, PubMed:8101525, PubMed:8910402, PubMed:9362482). Associates to the membrane, through lipid binding, and self-assembles into rings and stacks of interconnected rings through oligomerization to form a helical polymer around the vesicle membrane leading to constriction of invaginated coated pits around their necks (PubMed:30069048, PubMed:7877694, PubMed:9922133). Self-assembly of the helical polymer induces membrane tubules narrowing until the polymer reaches a length sufficient to trigger GTP hydrolysis (PubMed:19084269). Depending on the curvature imposed on the tubules, membrane detachment from the helical polymer upon GTP hydrolysis can cause spontaneous hemifission followed by complete fission (PubMed:19084269). May play a role in regulating early stages of clathrin-mediated endocytosis in non-neuronal cells through its activation by dephosphorylation via the signaling downstream of EGFR (PubMed:29668686). Controls vesicle size at a step before fission, during formation of membrane pits, at hippocampal synapses (By similarity). Controls plastic adaptation of the synaptic vesicle recycling machinery to high levels of activity (By similarity). Mediates rapid endocytosis (RE), a Ca(2+)-dependent and clathrin- and K(+)-independent process in chromaffin cells (By similarity). Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP (By similarity). Through its interaction with DNAJC6, acts during the early steps of clathrin-coated vesicle (CCV) formation (PubMed:12791276)", "gene_name": "DNM1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q05193", "name": "Dynamin-1", "organism": "Homo sapiens", "uniprot_id": "Q05193" }, { "function": "", "gene_name": "ASXL1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6P1M8", "name": "CD36", "organism": "Homo sapiens", "uniprot_id": "Q6P1M8" }, { "function": "", "gene_name": "MRPS7", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y2R9", "name": "SR-AI/II (SCARA1)", "organism": "Homo sapiens", "uniprot_id": "Q9Y2R9" }, { "function": "", "gene_name": "pol", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9QJY9", "name": "PRV glycoprotein gB", "organism": "Human immunodeficiency virus type 1", "uniprot_id": "Q9QJY9" }, { "function": "", "gene_name": "pol", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9QJY8", "name": "PRV glycoprotein gD", "organism": "Human immunodeficiency virus type 1", "uniprot_id": "Q9QJY8" }, { "function": "Actin cytoskeleton-organizing protein that plays a role in the formation of cell projections (PubMed:20215400). Required for actin polymerization at immunological synapses (IS) and for the recruitment of the chemokine receptor CXCR4 to IS (PubMed:20215400). Plays a role in dendritic spine morphogenesis and organization, including the localization of the dopamine receptor DRD1 to the dendritic spines (By similarity). Involved in memory-related synaptic plasticity in the hippocampus (By similarity)", "gene_name": "DBN1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q16643", "name": "Drebrin", "organism": "Homo sapiens", "uniprot_id": "Q16643" }, { "function": "RNA-binding protein that associates with the RNA exosome complex. Involved in the 3'-processing of the 7S pre-RNA to the mature 5.8S rRNA and play a role in recruiting the RNA exosome complex to pre-rRNA; this function may include C1D", "gene_name": "MPHOSPH6", "glycan_count": 1, "glycosylation_sites": [], "id": "Q99547", "name": "THBS3", "organism": "Homo sapiens", "uniprot_id": "Q99547" }, { "function": "Seems to be involved in cell adhesion through trans-homophilic and -heterophilic interactions, the latter including specifically interactions with NECTIN1. Does not act as receptor for alpha-herpesvirus entry into cells", "gene_name": "NECTIN4", "glycan_count": 7, "glycosylation_sites": [ { "position": 281, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q96NY8", "name": "Nectin-4", "organism": "Homo sapiens", "uniprot_id": "Q96NY8" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P33478 (DENV2)", "name": "NS1 (Non-structural protein 1)", "organism": "", "uniprot_id": "" }, { "function": "Functions as a positive regulator of osteoclastogenesis (By similarity). Cell surface receptor that signals via TYROBP (PubMed:10449773). Regulates inflammatory responses (By similarity)", "gene_name": "CLEC5A", "glycan_count": 0, "glycosylation_sites": [ { "position": 32, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 93, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 144, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 151, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NY25", "name": "CLEC5A", "organism": "Homo sapiens", "uniprot_id": "Q9NY25" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02468 (LAMA1, example)", "name": "Laminin", "organism": "", "uniprot_id": "" }, { "function": "May associate with CD21. May regulate the release of Ca(2+) from intracellular stores", "gene_name": "Anxa6", "glycan_count": 1, "glycosylation_sites": [], "id": "P14824", "name": "Annexin A6 (Anxa6)", "organism": "Mus musculus", "uniprot_id": "P14824" }, { "function": "Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease (By similarity)", "gene_name": "DKK3", "glycan_count": 16, "glycosylation_sites": [ { "position": 26, "type": "O-linked (GalNAc...) threonine" }, { "position": 28, "type": "O-linked (GalNAc...) threonine" }, { "position": 96, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 106, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 121, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 204, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UBP4", "name": "Latent TGF-\u03b2 binding protein 4 (Ltbp4)", "organism": "Homo sapiens", "uniprot_id": "Q9UBP4" }, { "function": "ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds, and xenobiotics from cells. Mediates ATP-dependent transport of glutathione conjugates such as leukotriene-c4 (LTC4) and N-ethylmaleimide S-glutathione (NEM-GS) (in vitro), and an anionic cyclopentapeptide endothelin antagonist, BQ-123 (PubMed:11880368, PubMed:12414644). May contribute to regulate the transport of organic compounds in testes across the blood-testis-barrier (Probable). Does not appear to actively transport drugs outside the cell. Confers low levels of cellular resistance to etoposide, teniposide, anthracyclines and cisplatin (PubMed:12414644)", "gene_name": "ABCC6", "glycan_count": 1, "glycosylation_sites": [ { "position": 15, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O95255", "name": "ABCC6", "organism": "Homo sapiens", "uniprot_id": "O95255" }, { "function": "Probably involved in cell proliferation and cell-cell interactions", "gene_name": "EMP3", "glycan_count": 2, "glycosylation_sites": [ { "position": 47, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 56, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P54852", "name": "EMP3", "organism": "Homo sapiens", "uniprot_id": "P54852" }, { "function": "Pore-forming subunit of Nav1.5, a voltage-gated sodium (Nav) channel that directly mediates the depolarizing phase of action potentials in excitable membranes. Navs, also called VGSCs (voltage-gated sodium channels) or VDSCs (voltage-dependent sodium channels), operate by switching between closed and open conformations depending on the voltage difference across the membrane. In the open conformation they allow Na(+) ions to selectively pass through the pore, along their electrochemical gradient. The influx of Na(+) ions provokes membrane depolarization, initiating the propagation of electrical signals throughout cells and tissues (PubMed:1309946, PubMed:21447824, PubMed:23085483, PubMed:23420830, PubMed:25370050, PubMed:26279430, PubMed:26392562, PubMed:26776555). Nav1.5 is the predominant sodium channel expressed in myocardial cells and it is responsible for the initial upstroke of the action potential in cardiac myocytes, thereby initiating the heartbeat (PubMed:11234013, PubMed:11804990, PubMed:12569159, PubMed:1309946). Required for normal electrical conduction including formation of the infranodal ventricular conduction system and normal action potential configuration, as a result of its interaction with XIRP2 (By similarity)", "gene_name": "SCN5A", "glycan_count": 3, "glycosylation_sites": [ { "position": 214, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 283, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 288, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 291, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 318, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 328, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 740, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 803, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 864, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1365, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1374, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1380, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1388, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1736, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q14524", "name": "SCN5A (Sodium channel protein type 5 subunit alpha)", "organism": "Homo sapiens", "uniprot_id": "Q14524" }, { "function": "Sensor component of the AIM2 inflammasome, which mediates inflammasome activation in response to the presence of double-stranded DNA (dsDNA) in the cytosol, leading to subsequent pyroptosis (PubMed:17726700, PubMed:19158675, PubMed:19158676, PubMed:19158679, PubMed:20566831, PubMed:23530044, PubMed:26197926, PubMed:26583071, PubMed:29440442, PubMed:33980849, PubMed:37364111). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation (PubMed:17726700, PubMed:19158675, PubMed:19158676, PubMed:19158679, PubMed:20566831, PubMed:26197926, PubMed:29440442, PubMed:33980849). Acts as a recognition receptor (PRR): specifically recognizes and binds dsDNA in the cytosol, and mediates the formation of the inflammasome polymeric complex composed of AIM2, CASP1 and PYCARD/ASC (PubMed:17726700, PubMed:19158675, PubMed:19158676, PubMed:19158679, PubMed:20566831, PubMed:26197926, PubMed:29440442, PubMed:33980849). Recruitment of pro-caspase-1 (proCASP1) to the AIM2 inflammasome promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), promoting cytokine secretion (PubMed:17726700, PubMed:19158675, PubMed:19158676, PubMed:19158679, PubMed:20566831). In some cells, CASP1 activation mediates cleavage and activation of GSDMD, triggering pyroptosis without promoting cytokine secretion (PubMed:19158675, PubMed:19158676). Detects cytosolic dsDNA of viral and bacterial origin in a non-sequence-specific manner (PubMed:17726700, PubMed:19158675, PubMed:19158676, PubMed:19158679, PubMed:20566831, PubMed:26197926, PubMed:26583071, PubMed:29440442, PubMed:33980849). Involved in the DNA damage response caused by acute ionizing radiation by mediating pyroptosis of intestinal epithelial cells and bone marrow cells in response to double-strand DNA breaks (By similarity). Mechanistically, AIM2 senses DNA damage in the nucleus to mediate inflammasome assembly and inflammatory cell death (By similarity). Also acts as a regulator of neurodevelopment via its role in the DNA damage response: acts by promoting neural cell death in response to DNA damage in the developing brain, thereby purging genetically compromised cells of the central nervous system (By similarity). Pyroptosis mediated by the AIM2 inflammasome in response to DNA damage is dependent on GSDMD without involving IL1B and IL18 cytokine secretion (By similarity). Also acts as a mediator of pyroptosis, necroptosis and apoptosis (PANoptosis), an integral part of host defense against pathogens, in response to bacterial infection (By similarity). Can also trigger PYCARD/ASC-dependent, caspase-1-independent cell death that involves caspase-8 (CASP8) (By similarity)", "gene_name": "AIM2", "glycan_count": 0, "glycosylation_sites": [], "id": "O14862", "name": "AIM2", "organism": "Homo sapiens", "uniprot_id": "O14862" }, { "function": "Acts as an E3 ubiquitin-protein ligase able to ubiquitinate p53/TP53 which promotes its relocalization to discrete foci associated with PML nuclear bodies. Exhibits preference for UBE2D2 as a E2 enzyme", "gene_name": "RNF38", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H0F5", "name": "ZBP1", "organism": "Homo sapiens", "uniprot_id": "Q9H0F5" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P27958/P27959", "name": "HCV envelope glycoproteins (E1/E2)", "organism": "", "uniprot_id": "" }, { "function": "Endonuclease that mediates miRNA decay of both protein-free and AGO2-loaded miRNAs (PubMed:18453631, PubMed:28546213). As part of its function in miRNA decay, regulates mRNAs involved in G1-to-S phase transition (PubMed:28546213). Functions as a bridging factor between STAT6 and the basal transcription factor (PubMed:12234934). Plays a role in PIM1 regulation of MYB activity (PubMed:9809063). Functions as a transcriptional coactivator for STAT5 (By similarity)", "gene_name": "SND1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q7KZF4", "name": "SND1", "organism": "Homo sapiens", "uniprot_id": "Q7KZF4" }, { "function": "Cell surface glycoprotein that plays a role in cell adhesion and tumor progression (PubMed:10910050, PubMed:11590190, PubMed:1378450, PubMed:16204051, PubMed:2022629, PubMed:2803308, PubMed:8776764). Intercellular adhesion occurs in a calcium- and fibronectin-independent manner (PubMed:16204051, PubMed:2022629). Mediates homophilic and heterophilic cell adhesion with other carcinoembryonic antigen-related cell adhesion molecules, such as CEACAM5 and CEACAM8 (PubMed:11590190, PubMed:16204051, PubMed:2022629, PubMed:2803308, PubMed:8776764). Heterophilic interaction with CEACAM8 occurs in activated neutrophils (PubMed:8776764). Plays a role in neutrophil adhesion to cytokine-activated endothelial cells (PubMed:1378450). Plays a role in cell migration and cell adhesion to endothelial cells (PubMed:16204051)", "gene_name": "CEACAM6", "glycan_count": 10, "glycosylation_sites": [ { "position": 104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 111, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 115, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 152, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 173, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 197, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 224, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 256, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 274, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 288, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 292, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 309, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P40199", "name": "CEACAM6", "organism": "Homo sapiens", "uniprot_id": "P40199" }, { "function": "Component of the small ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797)", "gene_name": "RPS11", "glycan_count": 1, "glycosylation_sites": [], "id": "P62280", "name": "RPS11", "organism": "Homo sapiens", "uniprot_id": "P62280" }, { "function": "May affect the rate of fibrils formation", "gene_name": "DCN", "glycan_count": 197, "glycosylation_sites": [ { "position": 34, "type": "O-linked (Xyl...) (glycosaminoglycan) serine" }, { "position": 211, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 262, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 303, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P07585", "name": "DCN (Decorin)", "organism": "Homo sapiens", "uniprot_id": "P07585" }, { "function": "Receptor involved in the costimulatory signal essential for T-lymphocyte proliferation and interleukin-2 production, by binding CD28 or CTLA-4. May play a critical role in the early events of T-cell activation and costimulation of naive T-cells, such as deciding between immunity and anergy that is made by T-cells within 24 hours after activation. Also involved in the regulation of B cells function, plays a role in regulating the level of IgG(1) produced. Upon CD40 engagement, activates NF-kappa-B signaling pathway via phospholipase C and protein kinase C activation (PubMed:23241883)", "gene_name": "Cd86", "glycan_count": 0, "glycosylation_sites": [ { "position": 33, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 47, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 92, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 135, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 146, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 154, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 175, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 190, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 231, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P42082", "name": "CD86", "organism": "Mus musculus", "uniprot_id": "P42082" }, { "function": "Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle (PubMed:18485873). The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (PubMed:18485873). The APC/C complex catalyzes assembly of branched 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on target proteins (PubMed:29033132)", "gene_name": "ANAPC4", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UJX5", "name": "CD146 (MCAM/MUC18)", "organism": "Homo sapiens", "uniprot_id": "Q9UJX5" }, { "function": "Forms a water-specific channel (PubMed:19800950, PubMed:7509789, PubMed:7528931). Plays an important role in brain water homeostasis and in glymphatic solute transport. Required for a normal rate of water exchange across the blood brain interface. Required for normal levels of cerebrospinal fluid influx into the brain cortex and parenchyma along paravascular spaces that surround penetrating arteries, and for normal drainage of interstitial fluid along paravenous drainage pathways. Thereby, it is required for normal clearance of solutes from the brain interstitial fluid, including soluble beta-amyloid peptides derived from APP. Plays a redundant role in urinary water homeostasis and urinary concentrating ability (By similarity)", "gene_name": "Aqp4", "glycan_count": 0, "glycosylation_sites": [ { "position": 153, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P47863", "name": "Aquaporin-4 (AQP4)", "organism": "Rattus norvegicus", "uniprot_id": "P47863" }, { "function": "Non-selective calcium permeant cation channel involved in osmotic sensitivity and mechanosensitivity (PubMed:16293632, PubMed:18695040, PubMed:18826956, PubMed:22526352, PubMed:23136043, PubMed:29899501). Activation by exposure to hypotonicity within the physiological range exhibits an outward rectification (PubMed:18695040, PubMed:18826956, PubMed:29899501). Also activated by heat, low pH, citrate and phorbol esters (PubMed:16293632, PubMed:18695040, PubMed:18826956, PubMed:20037586, PubMed:21964574, PubMed:25256292). Increase of intracellular Ca(2+) potentiates currents. Channel activity seems to be regulated by a calmodulin-dependent mechanism with a negative feedback mechanism (PubMed:12724311, PubMed:18826956). Promotes cell-cell junction formation in skin keratinocytes and plays an important role in the formation and/or maintenance of functional intercellular barriers (By similarity). Acts as a regulator of intracellular Ca(2+) in synoviocytes (PubMed:19759329). Plays an obligatory role as a molecular component in the nonselective cation channel activation induced by 4-alpha-phorbol 12,13-didecanoate and hypotonic stimulation in synoviocytes and also regulates production of IL-8 (PubMed:19759329). Together with PKD2, forms mechano- and thermosensitive channels in cilium (PubMed:18695040). Negatively regulates expression of PPARGC1A, UCP1, oxidative metabolism and respiration in adipocytes (By similarity). Regulates expression of chemokines and cytokines related to pro-inflammatory pathway in adipocytes (By similarity). Together with AQP5, controls regulatory volume decrease in salivary epithelial cells (By similarity). Required for normal development and maintenance of bone and cartilage (PubMed:26249260). In its inactive state, may sequester DDX3X at the plasma membrane. When activated, the interaction between both proteins is affected and DDX3X relocalizes to the nucleus (PubMed:29899501). In neurons of the central nervous system, could play a role in triggering voluntary water intake in response to increased sodium concentration in body fluid (By similarity)", "gene_name": "TRPV4", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9HBA0", "name": "Transient receptor potential vanilloid 4 (TRPV4)", "organism": "Homo sapiens", "uniprot_id": "Q9HBA0" }, { "function": "Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. Mainly associated with cytoskeleton organization, in active state binds to a variety of effector proteins to regulate cellular responses such as cytoskeletal dynamics, cell migration and cell cycle (PubMed:23871831). Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers (PubMed:31570889, PubMed:8910519, PubMed:9121475). Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis (PubMed:12900402, PubMed:16236794). Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion (PubMed:20974804, PubMed:23940119). Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly (PubMed:19934221). The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization (PubMed:20937854). Regulates KCNA2 potassium channel activity by reducing its location at the cell surface in response to CHRM1 activation; promotes KCNA2 endocytosis (PubMed:19403695, PubMed:9635436). Acts as an allosteric activator of guanine nucleotide exchange factor ECT2 by binding in its activated GTP-bound form to the PH domain of ECT2 which stimulates the release of PH inhibition and promotes the binding of substrate RHOA to the ECT2 catalytic center (PubMed:31888991). May be an activator of PLCE1 (PubMed:16103226). In neurons, involved in the inhibition of the initial spine growth. Upon activation by CaMKII, modulates dendritic spine structural plasticity by relaying CaMKII transient activation to synapse-specific, long-term signaling (By similarity). Acts as a regulator of platelet alpha-granule release during activation and aggregation of platelets (By similarity). When activated by DAAM1 may signal centrosome maturation and chromosomal segregation during cell division. May also be involved in contractile ring formation during cytokinesis", "gene_name": "RHOA", "glycan_count": 1, "glycosylation_sites": [ { "position": 34, "type": "(Microbial infection) O-linked (GlcNAc) tyrosine; by Photorhabdus PAU_02230; alternate" }, { "position": 37, "type": "(Microbial infection) O-alpha-linked (GlcNAc) threonine; by C.novyi toxin TcdA; alternate" }, { "position": 37, "type": "(Microbial infection) O-linked (Glc) threonine; by C.difficile toxins TcdA and TcdB; alternate" } ], "id": "P61586", "name": "Ras homolog family member A (RhoA)", "organism": "Homo sapiens", "uniprot_id": "P61586" }, { "function": "Bifunctional enzyme localized in the lumen of the endoplasmic reticulum that catalyzes the first two steps of the oxidative branch of the pentose phosphate pathway/shunt, an alternative to glycolysis and a major source of reducing power and metabolic intermediates for biosynthetic processes (By similarity). Has a hexose-6-phosphate dehydrogenase activity, with broad substrate specificity compared to glucose-6-phosphate 1-dehydrogenase/G6PD, and catalyzes the first step of the pentose phosphate pathway (PubMed:12858176, PubMed:18628520, PubMed:23132696). In addition, acts as a 6-phosphogluconolactonase and catalyzes the second step of the pentose phosphate pathway (By similarity). May have a dehydrogenase activity for alternative substrates including glucosamine 6-phosphate and glucose 6-sulfate (By similarity). The main function of this enzyme is to provide reducing equivalents such as NADPH to maintain the adequate levels of reductive cofactors in the oxidizing environment of the endoplasmic reticulum (PubMed:12858176, PubMed:18628520, PubMed:23132696). By producing NADPH that is needed by reductases of the lumen of the endoplasmic reticulum like corticosteroid 11-beta-dehydrogenase isozyme 1/HSD11B1, indirectly regulates their activity (PubMed:18628520)", "gene_name": "H6PD", "glycan_count": 20, "glycosylation_sites": [ { "position": 157, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 282, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 683, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O95479", "name": "H6PD", "organism": "Homo sapiens", "uniprot_id": "O95479" }, { "function": "Serine/threonine-protein kinase involved in various processes such as cell proliferation, differentiation, migration, transformation and programmed cell death (PubMed:10376527, PubMed:15805466, PubMed:17525747, PubMed:19675674, PubMed:20595622, PubMed:21364637, PubMed:22441692, PubMed:34048572). Extracellular stimuli such as pro-inflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK9/JNK2 (PubMed:10376527, PubMed:15805466, PubMed:17525747, PubMed:19675674, PubMed:20595622, PubMed:21364637, PubMed:22441692, PubMed:34048572). In turn, MAPK9/JNK2 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional activity (PubMed:10376527). In response to oxidative or ribotoxic stresses, inhibits rRNA synthesis by phosphorylating and inactivating the RNA polymerase 1-specific transcription initiation factor RRN3 (PubMed:15805466). Promotes stressed cell apoptosis by phosphorylating key regulatory factors including TP53 and YAP1 (PubMed:17525747, PubMed:21364637). In T-cells, MAPK8 and MAPK9 are required for polarized differentiation of T-helper cells into Th1 cells (PubMed:19290929). Upon T-cell receptor (TCR) stimulation, is activated by CARMA1, BCL10, MAP2K7 and MAP3K7/TAK1 to regulate JUN protein levels (PubMed:19290929). Plays an important role in the osmotic stress-induced epithelial tight-junctions disruption (PubMed:20595622). When activated, promotes beta-catenin/CTNNB1 degradation and inhibits the canonical Wnt signaling pathway (PubMed:19675674). Also participates in neurite growth in spiral ganglion neurons (By similarity). Phosphorylates the CLOCK-BMAL1 heterodimer and plays a role in the regulation of the circadian clock (PubMed:22441692). Phosphorylates POU5F1, which results in the inhibition of POU5F1's transcriptional activity and enhances its proteasomal degradation (By similarity). Phosphorylates ALKBH5 in response to reactive oxygen species (ROS), promoting ALKBH5 sumoylation and inactivation (PubMed:34048572)", "gene_name": "MAPK9", "glycan_count": 2, "glycosylation_sites": [], "id": "P45984", "name": "c-Jun N-terminal kinase 2 (JNK2)", "organism": "Homo sapiens", "uniprot_id": "P45984" }, { "function": "E3 ubiquitin-protein ligase that regulates activation of NF-kappa-B and JNK and plays a central role in the regulation of cell survival and apoptosis (PubMed:10346818, PubMed:11784851, PubMed:12917689, PubMed:15383523, PubMed:18981220, PubMed:19150425, PubMed:19810754, PubMed:19918265, PubMed:19937093, PubMed:20047764, PubMed:20064526, PubMed:20385093, PubMed:20577214, PubMed:22212761). Catalyzes 'Lys-63'-linked ubiquitination of target proteins, such as BIRC3, IKBKE, MLST8, RIPK1 and TICAM1 (PubMed:23453969, PubMed:28489822). Is an essential constituent of several E3 ubiquitin-protein ligase complexes, where it promotes the ubiquitination of target proteins by bringing them into contact with other E3 ubiquitin ligases (PubMed:15383523, PubMed:18981220). Regulates BIRC2 and BIRC3 protein levels by inhibiting their autoubiquitination and subsequent degradation; this does not depend on the TRAF2 RING-type zinc finger domain (PubMed:11907583, PubMed:19506082). Plays a role in mediating activation of NF-kappa-B by EIF2AK2/PKR (PubMed:15121867). In complex with BIRC2 or BIRC3, promotes ubiquitination of IKBKE (PubMed:23453969). Acts as a regulator of mTORC1 and mTORC2 assembly by mediating 'Lys-63'-linked ubiquitination of MLST8, thereby inhibiting formation of the mTORC2 complex, while facilitating assembly of the mTORC1 complex (PubMed:28489822). Required for normal antibody isotype switching from IgM to IgG (By similarity)", "gene_name": "TRAF2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q12933", "name": "TRAF2", "organism": "Homo sapiens", "uniprot_id": "Q12933" }, { "function": "Adapter protein and signal transducer that links members of the tumor necrosis factor receptor family to different signaling pathways by association with the receptor cytoplasmic domain and kinases. Mediates activation of NF-kappa-B and probably JNK. Seems to be involved in apoptosis. Plays a role in mediating activation of NF-kappa-B by EIF2AK2/PKR", "gene_name": "TRAF5", "glycan_count": 0, "glycosylation_sites": [], "id": "O00463", "name": "TRAF5", "organism": "Homo sapiens", "uniprot_id": "O00463" }, { "function": "Adapter required to activate the JNK and NF-kappa-B signaling pathways through the specific recognition of 'Lys-63'-linked polyubiquitin chains by its RanBP2-type zinc finger (NZF) (PubMed:10882101, PubMed:11460167, PubMed:15327770, PubMed:22158122, PubMed:27746020, PubMed:33184450, PubMed:36681779). Acts as an adapter linking MAP3K7/TAK1 and TRAF6 to 'Lys-63'-linked polyubiquitin chains (PubMed:10882101, PubMed:11460167, PubMed:15327770, PubMed:22158122, PubMed:27746020). The RanBP2-type zinc finger (NZF) specifically recognizes Lys-63'-linked polyubiquitin chains unanchored or anchored to the substrate proteins such as RIPK1/RIP1 and RIPK2: this acts as a scaffold to organize a large signaling complex to promote autophosphorylation of MAP3K7/TAK1, and subsequent activation of I-kappa-B-kinase (IKK) core complex by MAP3K7/TAK1 (PubMed:15327770, PubMed:18079694, PubMed:22158122). Also recognizes and binds Lys-63'-linked polyubiquitin chains of heterotypic 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains (PubMed:27746020). Regulates the IL1-mediated translocation of NCOR1 out of the nucleus (By similarity). Involved in heart development (PubMed:20493459)", "gene_name": "TAB2", "glycan_count": 3, "glycosylation_sites": [], "id": "Q9NYJ8", "name": "TAB2", "organism": "Homo sapiens", "uniprot_id": "Q9NYJ8" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02452 (COL1A1)", "name": "Type I Collagen", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P62736 (ACTA2)", "name": "\u03b1-Smooth Muscle Actin (\u03b1-SMA)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q92187 (mouse)", "name": "ST3GAL1", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q80Z19 (mouse)", "name": "NRXN2 (Neurexin 2)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8C0C4 (mouse)", "name": "DNER", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q62009 (mouse)", "name": "OMGP", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9QYF7 (mouse)", "name": "CSPG5", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q5S007 (mouse)", "name": "LRRK2", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q60805 (mouse)", "name": "MERTK", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9D1A2 (mouse)", "name": "MPDU1", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8C0Q9 (mouse)", "name": "BCAS3", "organism": "", "uniprot_id": "" }, { "function": "Uniporter that mediates the uptake of cationic L-amino acids such as L-arginine, L-lysine and L-ornithine (PubMed:11591158). The transport is sodium ions- and pH-independent, moderately trans-stimulated and is mediated by passive diffusion (PubMed:11591158)", "gene_name": "SLC7A3", "glycan_count": 0, "glycosylation_sites": [ { "position": 232, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q96SZ7", "name": "Siglec-11", "organism": "Homo sapiens", "uniprot_id": "Q8WY07" }, { "function": "Endoribonuclease that specifically cleaves inosine-containing RNAs: cleaves RNA at the second phosphodiester bond 3' to inosine (PubMed:23912683, PubMed:23912718, PubMed:25195743, PubMed:27573237, PubMed:31703097). Active against both single-stranded and double-stranded RNAs (PubMed:25195743, PubMed:31703097). Has strong preference for single-stranded RNAs (ssRNAs) toward double-stranded RNAs (dsRNAs) (PubMed:23912718). Cleaves mRNAs and tRNAs containing inosine (PubMed:23912683, PubMed:31703097). Also able to cleave structure-specific dsRNA substrates containing the specific sites 5'-IIUI-3' and 5'-UIUU-3' (PubMed:23912718, PubMed:27573237). Inosine is present in a number of RNAs following editing; the function of inosine-specific endoribonuclease is still unclear: it could either play a regulatory role in edited RNAs, or be involved in antiviral response by removing the hyperedited long viral dsRNA genome that has undergone A-to-I editing (Probable). Binds branched DNA structures (PubMed:23139746)", "gene_name": "ENDOV", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8N8Q3", "name": "FNDC3B", "organism": "Homo sapiens", "uniprot_id": "Q8N8Q3" }, { "function": "Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules and MHC class II antigen presentation (PubMed:30612035). The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L", "gene_name": "CTSS", "glycan_count": 0, "glycosylation_sites": [ { "position": 104, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P25774", "name": "CTSS (Cathepsin S)", "organism": "Homo sapiens", "uniprot_id": "P25774" }, { "function": "Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper eye, face, body wall, limb and neural tube development. They also suppress a number of genes including MCAM/MUC18, C/EBP alpha and MYC. AP-2-alpha is the only AP-2 protein required for early morphogenesis of the lens vesicle. Together with the CITED2 coactivator, stimulates the PITX2 P1 promoter transcription activation. Associates with chromatin to the PITX2 P1 promoter region", "gene_name": "TFAP2A", "glycan_count": 1, "glycosylation_sites": [], "id": "P05549", "name": "TFAP2A", "organism": "Homo sapiens", "uniprot_id": "P05549" }, { "function": "Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus", "gene_name": "KPNA6", "glycan_count": 1, "glycosylation_sites": [], "id": "O60684", "name": "KPNA2", "organism": "Homo sapiens", "uniprot_id": "O60684" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P35439 (GRIN1 subunit)", "name": "N-methyl-D-aspartate receptor", "organism": "", "uniprot_id": "" }, { "function": "Involved in osteopontin/bone sialoprotein dephosphorylation. Its expression seems to increase in certain pathological states such as Gaucher and Hodgkin diseases, the hairy cell, the B-cell, and the T-cell leukemias", "gene_name": "ACP5", "glycan_count": 0, "glycosylation_sites": [ { "position": 116, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 147, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P13686", "name": "Tartrate-resistant acid phosphatase 5 (TRAP5/ACP5)", "organism": "Homo sapiens", "uniprot_id": "P13686" }, { "function": "Cytokine that plays a major role in the development of inflammatory and protective immune responses to microbial invaders and parasites by modulating immune cells of both the innate and adaptive immune systems (PubMed:15123770). Stimulates the proliferation of natural killer cells, T-cells and B-cells and promotes the secretion of several cytokines (PubMed:8178155, PubMed:9326248). In monocytes, induces the production of IL8 and monocyte chemotactic protein 1/CCL2, two chemokines that attract neutrophils and monocytes respectively to sites of infection (PubMed:9326248). Unlike most cytokines, which are secreted in soluble form, IL15 is expressed in association with its high affinity IL15RA on the surface of IL15-producing cells and delivers signals to target cells that express IL2RB and IL2RG receptor subunits (PubMed:10233906, PubMed:23104097, PubMed:8026467). Binding to its receptor triggers the phosphorylation of JAK1 and JAK3 and the recruitment and subsequent phosphorylation of signal transducer and activator of transcription-3/STAT3 and STAT5 (PubMed:7568001). In mast cells, induces the rapid tyrosine phosphorylation of STAT6 and thereby controls mast cell survival and release of cytokines such as IL4 (By similarity)", "gene_name": "IL15", "glycan_count": 0, "glycosylation_sites": [ { "position": 127, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P40933", "name": "IL-13", "organism": "Homo sapiens", "uniprot_id": "P40933" }, { "function": "Cell surface receptor that plays a role in various physiological processes including inflammation, phagocytosis, and cell adhesion. Plays a role in phagocytosis and enhances the uptake of apoptotic cells and immune complexes by acting as a receptor for defense collagens including surfactant protein A/SFTPA1, C1q, and mannose-binding lectin (MBL2) (PubMed:7977768). Plays a role in the regulation of endothelial cell function and adhesion by activating angiogenesis (PubMed:24809468). Mechanistically, exerts its angiogenic function by associating with beta-dystroglycan, leading to SRC-dependent phosphorylation and subsequent recruitment of CBL. In turn, CBL provides a docking site for downstream signaling components, such as CRKL to enhance cell migration (PubMed:26848865). Participates in angiogenesis also by acting as a receptor for the ECM pan-endothelial glycoprotein multimerin-2/MMRN2 and IGFBP7 ligands (PubMed:28671670, PubMed:36265539, PubMed:38218180). Both ligands play a non-redundant role in CD93-mediated endothelial cell function (PubMed:38218180). Acts as a key regulator of endothelial barrier function through modulating VEGFR2 function (By similarity)", "gene_name": "CD93", "glycan_count": 0, "glycosylation_sites": [ { "position": 325, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O00274", "name": "Eotaxin (CCL11)", "organism": "Homo sapiens", "uniprot_id": "Q9NPY3" }, { "function": "Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen", "gene_name": "Col4a1", "glycan_count": 0, "glycosylation_sites": [ { "position": 126, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P02463", "name": "Collagen I", "organism": "Mus musculus", "uniprot_id": "P02463" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q15796/Q13485", "name": "Smad2/3", "organism": "", "uniprot_id": "" }, { "function": "Recognizes and binds the palindromic sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication", "gene_name": "NFIX", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y6R8", "name": "ATP-citrate lyase (ACLY)", "organism": "Homo sapiens", "uniprot_id": "Q14938" }, { "function": "May have regulatory role in cell division or differentiation in response to extracellular signals", "gene_name": "SKIL", "glycan_count": 0, "glycosylation_sites": [], "id": "O00464", "name": "Pax7", "organism": "Homo sapiens", "uniprot_id": "P12757" }, { "function": "Nuclear corepressor for KRAB domain-containing zinc finger proteins (KRAB-ZFPs) (PubMed:20164836, PubMed:22110054, PubMed:25247314, PubMed:27658112). Mediates gene silencing by recruiting CHD3, a subunit of the nucleosome remodeling and deacetylation (NuRD) complex, and SETDB1 (which specifically methylates histone H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target genes. Enhances transcriptional repression by coordinating the increase in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14' acetylation (H3K9ac and H3K14ac, respectively) and the disposition of HP1 proteins to silence gene expression. Recruitment of SETDB1 induces heterochromatinization. May play a role as a coactivator for CEBPB and NR3C1 in the transcriptional activation of ORM1. Also a corepressor for ERBB4. Inhibits E2F1 activity by stimulating E2F1-HDAC1 complex formation and inhibiting E2F1 acetylation. May serve as a partial backup to prevent E2F1-mediated apoptosis in the absence of RB1. Important regulator of CDKN1A/p21(CIP1). Has E3 SUMO-protein ligase activity toward itself via its PHD-type zinc finger. Specifically sumoylates IRF7, thereby inhibiting its transactivation activity. Ubiquitinates p53/TP53 leading to its proteasomal degradation; the function is enhanced by MAGEC2 and MAGEA2, and possibly MAGEA3 and MAGEA6. Mediates the nuclear localization of KOX1, ZNF268 and ZNF300 transcription factors. Probably forms a corepressor complex required for activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) or other tumor-related genes in colorectal cancer (CRC) cells. Required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs) (PubMed:20164836). In ESCs, in collaboration with SETDB1, is also required for H3K9me3 and silencing of endogenous and introduced retroviruses in a DNA-methylation independent-pathway (PubMed:20164836). Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing. The SETDB1-TRIM28-ZNF274 complex may play a role in recruiting ATRX to the 3'-exons of zinc-finger coding genes with atypical chromatin signatures to establish or maintain/protect H3K9me3 at these transcriptionally active regions (By similarity). Acts as a corepressor for ZFP568 (PubMed:22110054, PubMed:27658112)", "gene_name": "Trim28", "glycan_count": 2, "glycosylation_sites": [], "id": "Q62318", "name": "TRP1", "organism": "Mus musculus", "uniprot_id": "Q62318" }, { "function": "Mediates electroneutral potassium-chloride cotransport in mature neurons and is required for neuronal Cl(-) homeostasis (By similarity). As major extruder of intracellular chloride, it establishes the low neuronal Cl(-) levels required for chloride influx after binding of GABA-A and glycine to their receptors, with subsequent hyperpolarization and neuronal inhibition (By similarity). Involved in the regulation of dendritic spine formation and maturation (By similarity)", "gene_name": "Slc12a5", "glycan_count": 0, "glycosylation_sites": [ { "position": 314, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 333, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 351, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 362, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Z0M7", "name": "Fc\u03b3RIII", "organism": "Mus musculus", "uniprot_id": "Q91V14" }, { "function": "Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) with up to 10 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP). Cleaves cap analog structures like tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with very poor efficiency. Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules longer than 25 nucleotides. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) to m7GMP. May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by DCPS to m7GMP. Binds to m7GpppG and strongly to m7GDP. Plays a role in first intron splicing of pre-mRNAs. Inhibits activation-induced cell death", "gene_name": "Dcps", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8K4F7", "name": "Fc\u03b3RIV", "organism": "Rattus norvegicus", "uniprot_id": "Q8K4F7" }, { "function": "Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues", "gene_name": "GH1", "glycan_count": 0, "glycosylation_sites": [], "id": "P01241", "name": "Growth Hormone (GH)", "organism": "Homo sapiens", "uniprot_id": "P01241" }, { "function": "Signal transducer and transcription activator that mediates cellular responses to interleukins, KITLG/SCF, LEP and other growth factors (PubMed:23917203, PubMed:26026268). Once activated, recruits coactivators, such as NCOA1 or MED1, to the promoter region of the target gene (By similarity). May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4 (By similarity). Upon activation of IL6ST/gp130 signaling by interleukin-6 (IL6), binds to the IL6-responsive elements identified in the promoters of various acute-phase protein genes (By similarity). Activated by IL31 through IL31RA (By similarity). Acts as a regulator of inflammatory response by regulating differentiation of naive CD4(+) T-cells into T-helper Th17 or regulatory T-cells (Treg): acetylation promotes its transcription activity and cell differentiation while deacetylation and oxidation of lysine residues by LOXL3 inhibits differentiation (By similarity). Involved in cell cycle regulation by inducing the expression of key genes for the progression from G1 to S phase, such as CCND1 (By similarity). Mediates the effects of LEP on melanocortin production, body energy homeostasis and lactation (PubMed:12594516). May play an apoptotic role by transctivating BIRC5 expression under LEP activation (PubMed:16825198). Cytoplasmic STAT3 represses macroautophagy by inhibiting EIF2AK2/PKR activity (By similarity). Plays a crucial role in basal beta cell functions, such as regulation of insulin secretion (PubMed:20215569). Following JAK/STAT signaling activation and as part of a complex with NFATC3 and NFATC4, binds to the alpha-beta E4 promoter region of CRYAB and activates transcription in cardiomyocytes (PubMed:19538478). Plays an important role in host defense in methicillin-resistant S.aureus lung infection by regulating the expression of the antimicrobial lectin REG3G (PubMed:23401489)", "gene_name": "Stat3", "glycan_count": 2, "glycosylation_sites": [], "id": "P42227", "name": "STAT3", "organism": "Mus musculus", "uniprot_id": "P42227" }, { "function": "Thrombin inhibitor activated by the glycosaminoglycans, heparin or dermatan sulfate. In the presence of the latter, HC-II becomes the predominant thrombin inhibitor in place of antithrombin III (AT-III). Also inhibits chymotrypsin, but in a glycosaminoglycan-independent manner", "gene_name": "SERPIND1", "glycan_count": 66, "glycosylation_sites": [ { "position": 49, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 188, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 387, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P05546", "name": "VTN (Vitronectin)", "organism": "Homo sapiens", "uniprot_id": "P05546" }, { "function": "Major structural protein of tissues such as aorta and nuchal ligament, which must expand rapidly and recover completely. Molecular determinant of the late arterial morphogenesis, stabilizing arterial structure by regulating proliferation and organization of vascular smooth muscle (By similarity)", "gene_name": "ELN", "glycan_count": 1, "glycosylation_sites": [], "id": "P15502", "name": "Elastin", "organism": "Homo sapiens", "uniprot_id": "P15502" }, { "function": "Might be responsible for some of the extracellular antioxidant defense properties of selenium or might be involved in the transport of selenium. May supply selenium to tissues such as brain and testis", "gene_name": "SELENOP", "glycan_count": 53, "glycosylation_sites": [ { "position": 46, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 83, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 119, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 128, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 174, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 338, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P49908", "name": "Selenoprotein P", "organism": "Homo sapiens", "uniprot_id": "P49908" }, { "function": "Potent mitogen for mature parenchymal hepatocyte cells, seems to be a hepatotrophic factor, and acts as a growth factor for a broad spectrum of tissues and cell types (PubMed:20624990). Activating ligand for the receptor tyrosine kinase MET by binding to it and promoting its dimerization (PubMed:15167892, PubMed:20977675). Activates MAPK signaling following TMPRSS13 cleavage and activation (PubMed:20977675)", "gene_name": "HGF", "glycan_count": 31, "glycosylation_sites": [ { "position": 294, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 402, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 476, "type": "O-linked (GalNAc...) threonine" }, { "position": 566, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 653, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P14210", "name": "HGF", "organism": "Homo sapiens", "uniprot_id": "P14210" }, { "function": "Has a neutrophil chemotactic activity. Also a positive regulator of chondrocyte proliferation (PubMed:9524238). Does not show metalloendopeptidase activity (PubMed:27334921)", "gene_name": "LECT2", "glycan_count": 0, "glycosylation_sites": [], "id": "O14960", "name": "LECT2", "organism": "Homo sapiens", "uniprot_id": "O14960" }, { "function": "Receptor for the heterotrimeric lymphotoxin containing LTA and LTB, and for TNFS14/LIGHT (PubMed:24248355). Activates NF-kappa-B signaling pathway upon stimulation with lymphotoxin (LTA(1)-LTB(2)) (PubMed:24248355). Promotes apoptosis via TRAF3 and TRAF5. May play a role in the development of lymphoid organs", "gene_name": "LTBR", "glycan_count": 3, "glycosylation_sites": [ { "position": 40, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 177, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P36941", "name": "Lymphotoxin \u03b2 receptor (LTBR)", "organism": "Homo sapiens", "uniprot_id": "P36941" }, { "function": "Stimulates guanylyl cyclase 1 (GC1) and GC2 when free calcium ions concentration is low and inhibits guanylyl cyclases when free calcium ions concentration is elevated. This Ca(2+)-sensitive regulation of guanylyl cyclase (GC) is a key event in recovery of the dark state of rod photoreceptors following light exposure", "gene_name": "GUCA1C", "glycan_count": 0, "glycosylation_sites": [], "id": "O95843", "name": "CLCA1", "organism": "Homo sapiens", "uniprot_id": "O95843" }, { "function": "Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues (PubMed:15062093, PubMed:1860873). Fibrillin-1-containing microfibrils provide long-term force bearing structural support (PubMed:27026396). In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin (PubMed:27026396). In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus where they provide tensile strength and have anchoring roles (PubMed:27026396). Fibrillin-1 also plays a key role in tissue homeostasis through specific interactions with growth factors, such as the bone morphogenetic proteins (BMPs), growth and differentiation factors (GDFs) and latent transforming growth factor-beta-binding proteins (LTBPs), cell-surface integrins and other extracellular matrix protein and proteoglycan components (PubMed:27026396). Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively (By similarity). Negatively regulates osteoclastogenesis by binding and sequestering an osteoclast differentiation and activation factor TNFSF11 (PubMed:24039232). This leads to disruption of TNFSF11-induced Ca(2+) signaling and impairment of TNFSF11-mediated nuclear translocation and activation of transcription factor NFATC1 which regulates genes important for osteoclast differentiation and function (PubMed:24039232). Mediates cell adhesion via its binding to cell surface receptors integrins ITGAV:ITGB3 and ITGA5:ITGB1 (PubMed:12807887, PubMed:17158881). Binds heparin and this interaction has an important role in the assembly of microfibrils (PubMed:11461921)", "gene_name": "FBN1", "glycan_count": 111, "glycosylation_sites": [ { "position": 268, "type": "O-linked (Glc) serine" }, { "position": 448, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 471, "type": "O-linked (Glc) serine" }, { "position": 510, "type": "O-linked (Glc) serine" }, { "position": 552, "type": "O-linked (Glc) serine" }, { "position": 593, "type": "O-linked (Glc) serine" }, { "position": 634, "type": "O-linked (Glc) serine" }, { "position": 787, "type": "O-linked (Glc) serine" }, { "position": 827, "type": "O-linked (Glc) serine" }, { "position": 1050, "type": "O-linked (Glc) serine" }, { "position": 1067, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1135, "type": "O-linked (Glc) serine" }, { "position": 1149, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1218, "type": "O-linked (Glc) serine" }, { "position": 1302, "type": "O-linked (Glc) serine" }, { "position": 1345, "type": "O-linked (Glc) serine" }, { "position": 1369, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1386, "type": "O-linked (Glc) serine" }, { "position": 1484, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1508, "type": "O-linked (Glc) serine" }, { "position": 1581, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1628, "type": "O-linked (Glc) serine" }, { "position": 1669, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1703, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1713, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1830, "type": "O-linked (Glc) serine" }, { "position": 1871, "type": "O-linked (Glc) serine" }, { "position": 1902, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1911, "type": "O-linked (Glc) serine" }, { "position": 1953, "type": "O-linked (Glc) serine" }, { "position": 2035, "type": "O-linked (Glc) serine" }, { "position": 2077, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2148, "type": "O-linked (Glc) serine" }, { "position": 2178, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2227, "type": "O-linked (Glc) serine" }, { "position": 2313, "type": "O-linked (Glc) serine" }, { "position": 2465, "type": "O-linked (Glc) serine" }, { "position": 2547, "type": "O-linked (Glc) serine" }, { "position": 2628, "type": "O-linked (Glc) serine" }, { "position": 2734, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2750, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2767, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P35555", "name": "FBN1", "organism": "Homo sapiens", "uniprot_id": "P35555" }, { "function": "Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the antibacterial immune response via both innate and T-cell mediated pathways", "gene_name": "FGB", "glycan_count": 124, "glycosylation_sites": [ { "position": 394, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P02675", "name": "FGB", "organism": "Homo sapiens", "uniprot_id": "P02675" }, { "function": "Protective protein appears to be essential for both the activity of beta-galactosidase and neuraminidase, it associates with these enzymes and exerts a protective function necessary for their stability and activity. This protein is also a carboxypeptidase and can deamidate tachykinins", "gene_name": "CTSA", "glycan_count": 58, "glycosylation_sites": [ { "position": 145, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 333, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P10619", "name": "CTSA", "organism": "Homo sapiens", "uniprot_id": "P10619" }, { "function": "Lysosomal serine protease with tripeptidyl-peptidase I activity (PubMed:11054422, PubMed:19038966, PubMed:19038967). May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases (PubMed:11054422, PubMed:19038966, PubMed:19038967). Requires substrates with an unsubstituted N-terminus (PubMed:19038966)", "gene_name": "TPP1", "glycan_count": 25, "glycosylation_sites": [ { "position": 210, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 222, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 286, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 313, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 443, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O14773", "name": "TPP1", "organism": "Homo sapiens", "uniprot_id": "O14773" }, { "function": "Coreceptor for GDNF, a neurotrophic factor that enhances survival and morphological differentiation of dopaminergic neurons and increases their high-affinity dopamine uptake (PubMed:10829012, PubMed:31535977). GDNF-binding leads to autophosphorylation and activation of the RET receptor (PubMed:31535977)", "gene_name": "GFRA1", "glycan_count": 14, "glycosylation_sites": [ { "position": 59, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 347, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 406, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P56159", "name": "ITGA1", "organism": "Homo sapiens", "uniprot_id": "P56159" }, { "function": "Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. In the lumen of the endoplasmic reticulum, adds the first dolichyl beta-D-mannosyl phosphate derived mannose in an alpha-1,3 linkage to Man(5)GlcNAc(2)-PP-dolichol to produce Man(6)GlcNAc(2)-PP-dolichol (PubMed:10581255). Man(6)GlcNAc(2)-PP-dolichol is a substrate for ALG9, the following enzyme in the biosynthetic pathway (PubMed:10581255)", "gene_name": "ALG3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q92685", "name": "Alpha-1,3-mannosyltransferase (ALG3)", "organism": "Homo sapiens", "uniprot_id": "Q92685" }, { "function": "Serine protease which preferentially hydrolyzes peptides with Arg at the P1 position", "gene_name": "TMPRSS7", "glycan_count": 0, "glycosylation_sites": [], "id": "Q7RTY8", "name": "Butyrophilin subfamily 2 member A1 (BTN2A1)", "organism": "Homo sapiens", "uniprot_id": "Q7RTY8" }, { "function": "", "gene_name": "PRSS41", "glycan_count": 2, "glycosylation_sites": [ { "position": 211, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 284, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q7RTY9", "name": "Butyrophilin subfamily 3 member A2 (BTN3A2)", "organism": "Homo sapiens", "uniprot_id": "Q7RTY9" }, { "function": "Non-classical major histocompatibility class Ib molecule involved in immune self-nonself discrimination. In complex with B2M/beta-2-microglobulin binds nonamer self-peptides derived from the signal sequence of classical MHC class Ia molecules (VL9 peptides - VMAPRT[V/L][L/V/I/F]L) (PubMed:18083576, PubMed:18339401, PubMed:35705051, PubMed:37264229, PubMed:9754572). Peptide-bound HLA-E-B2M heterotrimeric complex primarily functions as a ligand for natural killer (NK) cell inhibitory receptor KLRD1-KLRC1, enabling NK cells to monitor the expression of other MHC class I molecules in healthy cells and to tolerate self (PubMed:17179229, PubMed:18083576, PubMed:37264229, PubMed:9486650, PubMed:9754572). Upon cellular stress, preferentially binds signal sequence-derived peptides from stress-induced chaperones and is no longer recognized by NK cell inhibitory receptor KLRD1-KLRC1, resulting in impaired protection from NK cells (PubMed:12461076). Binds signal sequence-derived peptides from non-classical MHC class Ib HLA-G molecules and acts as a ligand for NK cell activating receptor KLRD1-KLRC2, likely playing a role in the generation and effector functions of adaptive NK cells and in maternal-fetal tolerance during pregnancy (PubMed:30134159, PubMed:37264229, PubMed:9754572). Besides self-peptides, can also bind and present pathogen-derived peptides conformationally similar to VL9 peptides to alpha-beta T cell receptor (TCR) on unconventional CD8-positive cytotoxic T cells, ultimately triggering antimicrobial immune response (PubMed:16474394, PubMed:20195504, PubMed:30087334, PubMed:34228645). Presents HIV gag peptides (immunodominant KAFSPEVIPMF and subdominant KALGPAATL epitopes) predominantly to CD8-positive T cell clones expressing a TRAV17-containing TCR, triggering HLA-E-restricted T cell responses (PubMed:34228645). Presents mycobacterial peptides to HLA-E-restricted CD8-positive T cells eliciting both cytotoxic and immunoregulatory functions (PubMed:20195504, PubMed:35705051)", "gene_name": "HLA-E", "glycan_count": 9, "glycosylation_sites": [ { "position": 107, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P13747", "name": "Human leukocyte antigen E (HLA-E)", "organism": "Homo sapiens", "uniprot_id": "P13747" }, { "function": "Receptor for pituitary gland growth hormone (GH1) involved in regulating postnatal body growth (PubMed:1549776, PubMed:2825030, PubMed:8943276). On ligand binding, couples to the JAK2/STAT5 pathway (PubMed:1549776, PubMed:15690087, PubMed:2825030, PubMed:8943276)", "gene_name": "GHR", "glycan_count": 2, "glycosylation_sites": [ { "position": 46, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 115, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 156, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 161, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 200, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P10912", "name": "Growth hormone receptor", "organism": "Homo sapiens", "uniprot_id": "P10912" }, { "function": "Mediates the proteolytic cleavage of HP/haptoglobin in the endoplasmic reticulum", "gene_name": "C1RL", "glycan_count": 34, "glycosylation_sites": [ { "position": 147, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 166, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 242, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 296, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 363, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NZP8", "name": "Complement C1r-like protein (C1RL)", "organism": "Homo sapiens", "uniprot_id": "Q9NZP8" }, { "function": "Receptor tyrosine kinase which binds membrane-bound ephrin family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Highly promiscuous, it has the unique property among Eph receptors to bind and to be physiologically activated by both GPI-anchored ephrin-A and transmembrane ephrin-B ligands including EFNA1 and EFNB3. Upon activation by ephrin ligands, modulates cell morphology and integrin-dependent cell adhesion through regulation of the Rac, Rap and Rho GTPases activity. Plays an important role in the development of the nervous system controlling different steps of axonal guidance including the establishment of the corticospinal projections. May also control the segregation of motor and sensory axons during neuromuscular circuit development. In addition to its role in axonal guidance plays a role in synaptic plasticity. Activated by EFNA1 phosphorylates CDK5 at 'Tyr-15' which in turn phosphorylates NGEF regulating RHOA and dendritic spine morphogenesis. In the nervous system, also plays a role in repair after injury preventing axonal regeneration and in angiogenesis playing a role in central nervous system vascular formation. Additionally, its promiscuity makes it available to participate in a variety of cell-cell signaling regulating for instance the development of the thymic epithelium. During development of the cochlear organ of Corti, regulates pillar cell separation by forming a ternary complex with ADAM10 and CADH1 which facilitates the cleavage of CADH1 by ADAM10 and disruption of adherens junctions (By similarity). Phosphorylates CAPRIN1, promoting CAPRIN1-dependent formation of a membraneless compartment (By similarity)", "gene_name": "EPHA4", "glycan_count": 2, "glycosylation_sites": [ { "position": 235, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 340, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 408, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 545, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P54764", "name": "Ephrin type-A receptor 4 (EPHA4)", "organism": "Homo sapiens", "uniprot_id": "P54764" }, { "function": "Calcium-dependent lectin that acts as a pattern recognition receptor (PRR) of the innate immune system: recognizes damage-associated molecular patterns (DAMPs) of abnormal self and pathogen-associated molecular patterns (PAMPs) of bacteria and fungi (PubMed:18490740, PubMed:18509109, PubMed:18776906, PubMed:19171887, PubMed:20008526, PubMed:23602766). The PAMPs notably include mycobacterial trehalose 6,6'-dimycolate (TDM), a cell wall glycolipid with potent adjuvant immunomodulatory functions (PubMed:20008526, PubMed:23602766). Interacts with signaling adapter Fc receptor gamma chain/FCER1G to form a functional complex in myeloid cells (PubMed:18776906, PubMed:23602766). Binding of mycobacterial trehalose 6,6'-dimycolate (TDM) to this receptor complex leads to phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) of FCER1G, triggering activation of SYK, CARD9 and NF-kappa-B, consequently driving maturation of antigen-presenting cells and shaping antigen-specific priming of T-cells toward effector T-helper 1 (Th1) and T-helper 17 (Th17) cell subtypes (PubMed:23602766). Also recognizes alpha-mannose residues on pathogenic fungi of the genus Malassezia and mediates macrophage activation (PubMed:19171887). Through recognition of DAMPs released upon nonhomeostatic cell death, enables immune sensing of damaged self and promotes inflammatory cell infiltration into the damaged tissue (PubMed:18776906)", "gene_name": "Clec4e", "glycan_count": 0, "glycosylation_sites": [ { "position": 107, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9R0Q8", "name": "\u03b1-Syntrophin", "organism": "Mus musculus", "uniprot_id": "Q9R0Q8" }, { "function": "Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1. Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation. Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle. Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation", "gene_name": "Hspa1b", "glycan_count": 2, "glycosylation_sites": [], "id": "P17879", "name": "Hspa1a (Heat shock protein 70)", "organism": "Mus musculus", "uniprot_id": "P17879" }, { "function": "Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. Positive regulator of PRKN translocation to damaged mitochondria", "gene_name": "Hspa1l", "glycan_count": 3, "glycosylation_sites": [], "id": "P16627", "name": "Hspa1b (Heat shock protein 70)", "organism": "Mus musculus", "uniprot_id": "P16627" }, { "function": "Pattern recognition receptor (PRR) that detects bacterial peptidoglycan fragments and other danger signals and plays an important role in gastrointestinal immunity (PubMed:15692051, PubMed:15692052, PubMed:19805227, PubMed:21715553). Specifically activated by muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan found in every bacterial peptidoglycan type (PubMed:15692051, PubMed:15692052, PubMed:25429073). NOD2 specifically recognizes and binds 6-O-phospho-MDP, the phosphorylated form of MDP, which is generated by NAGK (PubMed:36002575). 6-O-phospho-MDP-binding triggers oligomerization that facilitates the binding and subsequent activation of the proximal adapter receptor-interacting RIPK2 (PubMed:15692051, PubMed:15692052, PubMed:22607974). Following recruitment, RIPK2 undergoes 'Met-1'- (linear) and 'Lys-63'-linked polyubiquitination by E3 ubiquitin-protein ligases XIAP, BIRC2, BIRC3 and the LUBAC complex, becoming a scaffolding protein for downstream effectors, triggering activation of the NF-kappa-B and MAP kinases signaling (PubMed:15692051, PubMed:15692052, PubMed:22607974). This in turn leads to the transcriptional activation of hundreds of genes involved in immune response (PubMed:22607974). Its ability to detect bacterial MDP plays a central role in maintaining the equilibrium between intestinal microbiota and host immune responses to control inflammation (PubMed:19805227, PubMed:21421666, PubMed:23281400, PubMed:24062413, PubMed:24882705, PubMed:25088769, PubMed:25666722, PubMed:28127403). An imbalance in this relationship results in dysbiosis, whereby pathogenic bacteria prevail on commensals, causing damage in the intestinal epithelial barrier as well as allowing bacterial invasion and inflammation (PubMed:23281400, PubMed:25088769). Acts as a regulator of appetite by sensing MDP in a subset of brain neurons: microbiota-derived MDP reach the brain, where they bind and activate NOD2 in inhibitory hypothalamic neurons, decreasing neuronal activity, thereby regulating satiety and body temperature (PubMed:35420957). NOD2-dependent MDP-sensing of bacterial cell walls in the intestinal epithelial compartment contributes to sustained postnatal growth upon undernutrition (PubMed:36821686). Also plays a role in antiviral response by acting as a sensor of single-stranded RNA (ssRNA) from viruses: upon ssRNA-binding, interacts with MAVS, leading to activation of interferon regulatory factor-3/IRF3 and expression of type I interferon (By similarity). Also acts as a regulator of autophagy in dendritic cells via its interaction with ATG16L1, possibly by recruiting ATG16L1 at the site of bacterial entry (PubMed:19898471, PubMed:19966812, PubMed:27230380). NOD2 activation in the small intestine crypt also contributes to intestinal stem cells survival and function: acts by promoting mitophagy via its association with ATG16L1 (PubMed:31919280). In addition to its main role in innate immunity, also regulates the adaptive immune system by acting as regulator of helper T-cell and regulatory T-cells (Tregs) (PubMed:21856952, PubMed:27230380). Besides recognizing pathogens, also involved in the endoplasmic reticulum stress response: acts by sensing and binding to the cytosolic metabolite sphingosine-1-phosphate generated in response to endoplasmic reticulum stress, initiating an inflammation process that leads to activation of the NF-kappa-B and MAP kinases signaling (PubMed:27007849). May also be involved in NLRP1 activation following activation by MDP, leading to CASP1 activation and IL1B release in macrophages (PubMed:18511561)", "gene_name": "Nod2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8K3Z0", "name": "Grem2 (Gremlin 2)", "organism": "Mus musculus", "uniprot_id": "Q8K3Z0" }, { "function": "Hormone that plays a key role in mediating cardio-renal homeostasis, and is involved in vascular remodeling and regulating energy metabolism (PubMed:15741263, PubMed:16875975, PubMed:18835931, PubMed:21672517, PubMed:22307324, PubMed:2532366, PubMed:2825692, PubMed:7595132, PubMed:7720651, PubMed:8087923, PubMed:8653797). Acts by specifically binding and stimulating NPR1 to produce cGMP, which in turn activates effector proteins, such as PRKG1, that drive various biological responses (PubMed:1660465, PubMed:1672777, PubMed:21098034, PubMed:2162527, PubMed:22307324, PubMed:25401746, PubMed:2825692, PubMed:7720651, PubMed:8384600, PubMed:9893117). Regulates vasodilation, natriuresis, diuresis and aldosterone synthesis and is therefore essential for regulating blood pressure, controlling the extracellular fluid volume and maintaining the fluid-electrolyte balance (PubMed:2532366, PubMed:2825692, PubMed:7595132, PubMed:7720651, PubMed:8087923, PubMed:8653797). Also involved in inhibiting cardiac remodeling and cardiac hypertrophy by inducing cardiomyocyte apoptosis and attenuating the growth of cardiomyocytes and fibroblasts (PubMed:16875975). Plays a role in female pregnancy by promoting trophoblast invasion and spiral artery remodeling in uterus, and thus prevents pregnancy-induced hypertension (By similarity). In adipose tissue, acts in various cGMP- and PKG-dependent pathways to regulate lipid metabolism and energy homeostasis (PubMed:15741263, PubMed:18835931, PubMed:21672517, PubMed:22307324). This includes up-regulating lipid metabolism and mitochondrial oxygen utilization by activating the AMP-activated protein kinase (AMPK), and increasing energy expenditure by acting via MAPK11 to promote the UCP1-dependent thermogenesis of brown adipose tissue (PubMed:15741263, PubMed:18835931, PubMed:21672517, PubMed:22307324). Binds the clearance receptor NPR3 which removes the hormone from circulation (PubMed:1672777)", "gene_name": "NPPA", "glycan_count": 1, "glycosylation_sites": [], "id": "P01160", "name": "Nppa (Atrial natriuretic peptide precursor A)", "organism": "Homo sapiens", "uniprot_id": "P01160" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P63104 (YWHAZ)", "name": "14-3-3\u03b6/\u03b4", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P62258 (YWHAE)", "name": "14-3-3\u03b5", "organism": "", "uniprot_id": "" }, { "function": "Functions as a molecular adapter coordinating multiple protein-protein interactions at the focal adhesion complex and in the nucleus. Links various intracellular signaling modules to plasma membrane receptors and regulates the Wnt and TGFB signaling pathways. May also regulate SLC6A3 and SLC6A4 targeting to the plasma membrane hence regulating their activity. In the nucleus, functions as a nuclear receptor coactivator regulating glucocorticoid, androgen, mineralocorticoid and progesterone receptor transcriptional activity. May play a role in the processes of cell growth, proliferation, migration, differentiation and senescence. May have a zinc-dependent DNA-binding activity", "gene_name": "TGFB1I1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y2V5", "name": "NPTX2", "organism": "Homo sapiens", "uniprot_id": "O43294" }, { "function": "Positively regulates a late step in exocytosis of various cytoplasmic vesicles, such as synaptic vesicles and other secretory vesicles (PubMed:21785414). Organizes the SNAREs into a cross-linked zigzag topology that, when interposed between the vesicle and plasma membranes, is incompatible with fusion, thereby preventing SNAREs from releasing neurotransmitters until an action potential arrives at the synapse (PubMed:21785414). Also involved in glucose-induced secretion of insulin by pancreatic beta-cells. Essential for motor behavior", "gene_name": "CPLX1", "glycan_count": 0, "glycosylation_sites": [], "id": "O14810", "name": "Complexin-2", "organism": "Homo sapiens", "uniprot_id": "O14810" }, { "function": "Required for normal Golgi function", "gene_name": "COG6", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y2V7", "name": "NPTXR", "organism": "Homo sapiens", "uniprot_id": "Q9Y2V7" }, { "function": "Folate-dependent enzyme, that displays both transferase and deaminase activity. Serves to channel one-carbon units from formiminoglutamate to the folate pool", "gene_name": "FTCD", "glycan_count": 0, "glycosylation_sites": [], "id": "O95954", "name": "CD153", "organism": "Homo sapiens", "uniprot_id": "O95954" }, { "function": "Predominantly catalyzes the biosynthesis of ganglioside GD1alpha from GM1b in the brain, by transferring the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc to the GalNAc residue on the NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc sequence of GM1b (PubMed:12668675). GD1alpha is a critical molecule in the communication and interaction between neuronal cells and their supportive cells, particularly in brain tissues, and functions as an adhesion molecule in the process of metastasis (By similarity). Also shows activity towards sialyl Lc4Cer (N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-N-acyl-sphing-4-enine) generating disialyl Lc4Cer, which can lead to the synthesis of disialyl Lewis a (Le(a)), suggested to be a cancer-associated antigen (PubMed:12668675)", "gene_name": "ST6GALNAC5", "glycan_count": 0, "glycosylation_sites": [ { "position": 137, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 161, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9BVH7", "name": "ST6GalNAc5", "organism": "Homo sapiens", "uniprot_id": "Q9BVH7" }, { "function": "Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc onto glycoproteins and glycolipids, forming an alpha-2,6-linkage. Produces branched type disialyl structures by transfer of a sialyl group onto the GalNAc or GlcNAc residue inside backbone core chains having a terminal sialic acid with an alpha-2,3-linkage on Gal. ST6GalNAcVI prefers glycolipids to glycoproteins, predominantly catalyzing the biosynthesis of ganglioside GD1alpha from GM1b (PubMed:12668675, PubMed:17123352). Besides GMb1, MSGG and other glycolipids, it shows activity towards sialyl Lc4Cer generating disialyl Lc4Cer, which can lead to the synthesis of disialyl Lewis a (Le(a)), suggested to be a cancer-associated antigen (PubMed:12668675). Also has activity toward GD1a and GT1b, and can generate DSGG (disialylgalactosylgloboside) from MSGG (monosialylgalactosylgloboside) (By similarity)", "gene_name": "ST6GALNAC6", "glycan_count": 1, "glycosylation_sites": [ { "position": 98, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q969X2", "name": "ST6GalNAc6", "organism": "Homo sapiens", "uniprot_id": "Q969X2" }, { "function": "Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen", "gene_name": "COL4A2", "glycan_count": 6, "glycosylation_sites": [ { "position": 138, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08572", "name": "COL4A2", "organism": "Homo sapiens", "uniprot_id": "P08572" }, { "function": "Heme transporter that regulates intracellular heme availability through the endosomal or lysosomal compartment (PubMed:18418376). In macrophages of the reticuloendothelial system, is the heme transporter for heme-iron recycling. Essential for macrophage iron homeostasis, transports heme from the phagolysosome to the cytoplasm during erythrophagocytosis (EP) (PubMed:23395172)", "gene_name": "SLC48A1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6P1K1", "name": "FLVCR2", "organism": "Homo sapiens", "uniprot_id": "Q6P1K1" }, { "function": "Plays a role in mitotic exit and cytokinesis (PubMed:16198290, PubMed:17853893). Recruits PDCD6IP and TSG101 to midbody during cytokinesis. Required for successful completion of cytokinesis (PubMed:17853893). Not required for microtubule nucleation (PubMed:16198290). Plays a role in the development of the brain and kidney (PubMed:28264986)", "gene_name": "CEP55", "glycan_count": 1, "glycosylation_sites": [], "id": "Q53EZ4", "name": "CEP55", "organism": "Homo sapiens", "uniprot_id": "Q53EZ4" }, { "function": "Junctional adhesion protein that mediates heterotypic cell-cell interactions with its cognate receptor JAM2 to regulate different cellular processes (PubMed:11590146, PubMed:11823489). Plays a role in homing and mobilization of hematopoietic stem and progenitor cells within the bone marrow. At the surface of bone marrow stromal cells, it contributes to the retention of the hematopoietic stem and progenitor cells expressing JAM3 (PubMed:11590146, PubMed:24357068). Plays a central role in leukocytes extravasation by facilitating transmigration through the endothelium (By similarity). Plays a role in spermatogenesis where JAM2 and JAM3, which are respectively expressed by Sertoli and germ cells, mediate an interaction between both cell types and play an essential role in the anchorage of germ cells onto Sertoli cells and the assembly of cell polarity complexes during spermatid differentiation (By similarity). Also functions as a counter-receptor for ITGAM, mediating leukocyte-platelet interactions and is involved in the regulation of transepithelial migration of polymorphonuclear neutrophils (PMN) (PubMed:12208882, PubMed:15194813). Plays a role in angiogenesis (PubMed:23255084). Plays a role in the regulation of cell migration (Probable). During myogenesis, it is involved in myocyte fusion (By similarity)", "gene_name": "JAM3", "glycan_count": 7, "glycosylation_sites": [ { "position": 104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 192, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9BX67", "name": "JAM3", "organism": "Homo sapiens", "uniprot_id": "Q9BX67" }, { "function": "E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3 (PubMed:15236971, PubMed:21532592, PubMed:23707686, PubMed:24076655, PubMed:27565346). Acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-RING ubiquitin ligase (CRL) complexes and initiating ubiquitination of CRL substrates: associates with CRL complexes and specifically mediates addition of the first ubiquitin on CRLs targets (PubMed:27565346). The initial ubiquitin is then elongated by CDC34/UBE2R1 and UBE2R2 (PubMed:27565346). E3 ubiquitin-protein ligase activity is activated upon binding to neddylated cullin-RING ubiquitin ligase complexes (PubMed:24076655, PubMed:27565346). Plays a role in protein translation in response to DNA damage by mediating ubiquitination of EIF4E2, the consequences of EIF4E2 ubiquitination are however unclear (PubMed:25624349). According to a report, EIF4E2 ubiquitination leads to promote EIF4E2 cap-binding and protein translation arrest (PubMed:25624349). According to another report EIF4E2 ubiquitination leads to its subsequent degradation (PubMed:14623119). Acts as the ligase involved in ISGylation of EIF4E2 (PubMed:17289916). In vitro, controls the degradation of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex member SUN2 and may therefore have a role in the formation and localization of the LINC complex, and as a consequence, nuclear subcellular localization and nuclear morphology (PubMed:29689197)", "gene_name": "ARIH1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y4X5", "name": "USP18", "organism": "Homo sapiens", "uniprot_id": "Q9Y4X5" }, { "function": "Protein disulfide isomerase (By similarity). Promotes the localization of acetylcholine receptors (AChRs) to the plasma membrane (By similarity)", "gene_name": "CRELD1", "glycan_count": 8, "glycosylation_sites": [ { "position": 79, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 205, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q96HD1", "name": "RNASET2", "organism": "Homo sapiens", "uniprot_id": "Q96HD1" }, { "function": "NADPH-dependent oxidoreductase which catalyzes the reduction of a variety of compounds bearing carbonyl groups including ketosteroids, alpha-dicarbonyl compounds, aldehydes, aromatic ketones and quinones (PubMed:18571493, PubMed:19056333). Reduces 3-ketosteroids and benzil into 3beta-hydroxysteroids and R-benzoin, respectively, in contrast to the stereoselectivity of non-primate DHRS4s which produce 3alpha-hydroxysteroids and S-benzoin (PubMed:19056333). Diplays low activity toward all-trans-retinal and no activity toward 9-cis-retinal as compared to non-primate mammals (PubMed:18571493, PubMed:19056333). In the reverse reaction, catalyze the NAD-dependent oxidation of 3beta-hydroxysteroids and alcohol, but with much lower efficiency (PubMed:18571493, PubMed:19056333). Involved in the metabolism of 3beta-hydroxysteroids, isatin and xenobiotic carbonyl compounds (PubMed:18571493, PubMed:19056333)", "gene_name": "DHRS4", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9BTZ2", "name": "DHRS7", "organism": "Homo sapiens", "uniprot_id": "Q9BTZ2" }, { "function": "Actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also plays an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration (By similarity)", "gene_name": "CALD1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q05682", "name": "CALD1", "organism": "Homo sapiens", "uniprot_id": "Q05682" }, { "function": "Transports retinoic acid to the nucleus. Regulates the access of retinoic acid to the nuclear retinoic acid receptors", "gene_name": "CRABP2", "glycan_count": 0, "glycosylation_sites": [], "id": "P29373", "name": "CRABP2", "organism": "Homo sapiens", "uniprot_id": "P29373" }, { "function": "Rab effector involved in exocytosis (By similarity). May act as scaffold protein that regulates neurotransmitter release at the active zone. Essential for maintaining normal probability of neurotransmitter release and for regulating release during short-term synaptic plasticity (By similarity). Plays a role in dendrite formation by melanocytes (PubMed:23999003)", "gene_name": "RIMS1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q86UR5", "name": "RIMS1", "organism": "Homo sapiens", "uniprot_id": "Q86UR5" }, { "function": "S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C(5) position of cytosine 4447 in 28S rRNA (PubMed:26196125). Required for efficient rRNA processing and 60S ribosomal subunit biogenesis (PubMed:24120868, PubMed:36161484). Regulates pre-rRNA processing through non-catalytic complex formation with box C/D snoRNAs and facilitates the recruitment of U3 and U8 snoRNAs to pre-90S ribosomal particles and their stable assembly into snoRNP complexes (PubMed:36161484). May play a role in the regulation of the cell cycle and the increased nucleolar activity that is associated with the cell proliferation (PubMed:24120868)", "gene_name": "NOP2", "glycan_count": 2, "glycosylation_sites": [], "id": "P46087", "name": "NOP2", "organism": "Homo sapiens", "uniprot_id": "P46087" }, { "function": "Beta-1,4 N-acetylgalactosaminyltransferase involved in the biosynthesis of Sd(a) histo-blood group antigen. Catalyzes the transfer of N-acetylgalactosamine (GalNAc) group in a beta-1,4-linkage from UDP-GalNAc to the galactose residue of NeuAcalpha2->3Gal-R to form Sd(a) glycan epitope GalNAcbeta1->4(NeuAcalpha2->3)Gal-R. The Sd(a) epitope is carried in O- and N-linked glycoproteins and glycolipids, including O-linked core 1 structures on GYPA/glycophorin, SLC4A1 and SLC29A1 in erythrocytes, N-linked glycans attached to the Tamm-Horsfall glycoprotein UMOD/uromodulin in renal fluids, O-linked core 3 glycans on mucins in colon and neolactosides in gastric mucosa (PubMed:12678917, PubMed:14688233, PubMed:16024623, PubMed:35409292). Confers protection against influenza A virus strains that attach to NeuAcalpha2->3-carrying host receptors. Modifies N-glycan chains on host receptors and prevents virus entry into cells (PubMed:28813663)", "gene_name": "B4GALNT2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8NHY0", "name": "GALNT10", "organism": "Homo sapiens", "uniprot_id": "Q8NHY0" }, { "function": "Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins (PubMed:29858230). Plays an important role in ER stress-induced, CHOP-dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1. Involved in the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thereby playing a role in retrotranslocation of the toxin", "gene_name": "ERO1A", "glycan_count": 25, "glycosylation_sites": [ { "position": 280, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 384, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q96HE7", "name": "COSMC", "organism": "Homo sapiens", "uniprot_id": "Q96HE7" }, { "function": "Plays an important role in homologous strand exchange, a key step in DNA repair through homologous recombination (HR) (PubMed:12205100, PubMed:18417535, PubMed:20231364, PubMed:20348101, PubMed:22325354, PubMed:23509288, PubMed:23754376, PubMed:26681308, PubMed:28575658, PubMed:32640219). Binds to single-stranded DNA in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange (PubMed:12205100, PubMed:18417535, PubMed:20231364, PubMed:20348101, PubMed:23509288, PubMed:23754376, PubMed:26681308, PubMed:28575658). Catalyzes the recognition of homology and strand exchange between homologous DNA partners to form a joint molecule between a processed DNA break and the repair template (PubMed:12205100, PubMed:18417535, PubMed:20231364, PubMed:20348101, PubMed:23509288, PubMed:23754376, PubMed:26681308, PubMed:28575658, PubMed:38459011). Recruited to resolve stalled replication forks during replication stress (PubMed:27797818, PubMed:31844045). Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR (PubMed:12442171, PubMed:24141787). Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51C and XRCC3 (PubMed:20413593). Also involved in interstrand cross-link repair (PubMed:26253028)", "gene_name": "RAD51", "glycan_count": 0, "glycosylation_sites": [], "id": "Q06609", "name": "Rad51", "organism": "Homo sapiens", "uniprot_id": "Q06609" }, { "function": "Transcription factor specifically required for the formation of motile cilia (PubMed:31630787). Acts by activating transcription of genes that mediate assembly of motile cilia, such as CFAP157. Binds the DNA consensus sequences 5'-HWDTGTTTGTTTA-3' or 5'-KTTTGTTGTTKTW-3' (where H is not G, W is A or T, D is not C, and K is G or T). Activates the transcription of a variety of ciliary proteins in the developing brain and lung", "gene_name": "FOXJ1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q92949", "name": "GMDS (GDP-mannose 4,6-dehydratase)", "organism": "Homo sapiens", "uniprot_id": "Q92949" }, { "function": "Catalyzes the transfer of a sialic acid from a CMP-linked sialic acid donor onto a terminal alpha-2,3-, alpha-2,6-, or alpha-2,8-linked sialic acid of an N-linked glycan acceptor through alpha-2,8-linkages (Probable) (PubMed:10766765, PubMed:11744634, PubMed:9054414, PubMed:9774483). Therefore, participates in polysialic acid synthesis on various sialylated N-acetyllactosaminyl oligosaccharides (alpha-2,3-, alpha-2,6-, or alpha-2,8-linked sialic acid), including NCAM1, NCAM1 N-glycans, FETUB N-glycans, and to a lesser extent sialylparagloboside (SPG) and AHSG, which does not require the initial addition of an alpha 2,8-sialic acid (Probable) (PubMed:7559389). However, does not exhibit sialic acid-polymerase activity (By similarity). Catalyzes polysialic acid synthesis in the hippocampal on NCAM1 and supports neurite outgrowth (PubMed:9054414). ST8SIA2-mediated polysialylation influences on oligodendrocyte differentiation and may promote the integrity of myelin and axons (By similarity)", "gene_name": "ST8SIA2", "glycan_count": 1, "glycosylation_sites": [ { "position": 60, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 72, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 89, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 134, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 219, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 234, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q92186", "name": "ST8SIA1 (GD3 synthase)", "organism": "Homo sapiens", "uniprot_id": "Q92186" }, { "function": "Sodium-coupled antiporter of neutral amino acids. In a tri-substrate transport cycle, exchanges neutral amino acids between the extracellular and intracellular compartments, coupled to the inward cotransport of at least one sodium ion (PubMed:17094966, PubMed:23756778, PubMed:26492990, PubMed:29872227, PubMed:34741534, PubMed:8702519). The preferred substrate is the essential amino acid L-glutamine, a precursor for biosynthesis of proteins, nucleotides and amine sugars as well as an alternative fuel for mitochondrial oxidative phosphorylation. Exchanges L-glutamine with other neutral amino acids such as L-serine, L-threonine and L-asparagine in a bidirectional way. Provides L-glutamine to proliferating stem and activated cells driving the metabolic switch toward cell differentiation (PubMed:23756778, PubMed:24953180). The transport cycle is usually pH-independent, with the exception of L-glutamate. Transports extracellular L-glutamate coupled to the cotransport of one proton and one sodium ion in exchange for intracellular L-glutamine counter-ion. May provide for L-glutamate uptake in glial cells regulating glutamine/glutamate cycle in the nervous system (PubMed:32733894). Can transport D-amino acids. Mediates D-serine release from the retinal glia potentially affecting NMDA receptor function in retinal neurons (PubMed:17094966). Displays sodium- and amino acid-dependent but uncoupled channel-like anion conductance with a preference SCN(-) >> NO3(-) > I(-) > Cl(-) (By similarity). Through binding of the fusogenic protein syncytin-1/ERVW-1 may mediate trophoblasts syncytialization, the spontaneous fusion of their plasma membranes, an essential process in placental development (PubMed:10708449, PubMed:23492904)", "gene_name": "SLC1A5", "glycan_count": 11, "glycosylation_sites": [ { "position": 163, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 212, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q15758", "name": "SLC1A5 (ASCT2)", "organism": "Homo sapiens", "uniprot_id": "Q15758" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P16860 (precursor)", "name": "N-terminal pro-BNP (NT-proBNP)", "organism": "", "uniprot_id": "" }, { "function": "E3 ubiquitin ligase involved in different processes such as development and immune response (PubMed:22588174, PubMed:30231667). Serves as a negative regulator for innate immune signaling pathways by suppressing RLR-induced activation of IRF3/7 and NF-kappa-B via interaction with adapter ECSIT (PubMed:22588174). Regulates autophagy through modulating both the transcription and the ubiquitination of BECN1 (PubMed:30231667). On the one hand, regulates the transcription of BECN1 through negatively modulating the NF-kappa-B pathway. On the other hand, regulates TRAF6-mediated 'Lys-63'-linked ubiquitination of BECN1, thus affecting the formation of the BECN1-PIK3C3 complex. In addition, mediates 'Lys-48'-linked ubiquitination of TRAF6 and thereby promotes TRAF6 proteasomal degradation (PubMed:30231667). Also acts as a critical regulator for early embryo development from blastocyst stage to gastrula through modulating F-actin assembly and WASH1 'Lys-63'-linked ubiquitination (By similarity)", "gene_name": "TRIM59", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8IWR1", "name": "TRIM59", "organism": "Homo sapiens", "uniprot_id": "Q8IWR1" }, { "function": "Receptor that may have an important role in cell/cell signaling during nervous system formation", "gene_name": "CELSR1", "glycan_count": 46, "glycosylation_sites": [ { "position": 403, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 546, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 634, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 778, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1114, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1139, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1213, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1249, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1259, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1287, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1576, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1623, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1640, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1979, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2103, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2122, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2257, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2415, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2437, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2523, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NYQ6", "name": "CLDN18", "organism": "Homo sapiens", "uniprot_id": "Q9NYQ6" }, { "function": "Translation elongation factor that catalyzes the GTP-dependent binding of aminoacyl-tRNA (aa-tRNA) to the A-site of ribosomes during the elongation phase of protein synthesis (PubMed:26593721, PubMed:26651998, PubMed:36123449, PubMed:36264623, PubMed:36638793). Base pairing between the mRNA codon and the aa-tRNA anticodon promotes GTP hydrolysis, releasing the aa-tRNA from EEF1A1 and allowing its accommodation into the ribosome (PubMed:26593721, PubMed:26651998, PubMed:36123449, PubMed:36264623, PubMed:36638793). The growing protein chain is subsequently transferred from the P-site peptidyl tRNA to the A-site aa-tRNA, extending it by one amino acid through ribosome-catalyzed peptide bond formation (PubMed:26593721, PubMed:26651998, PubMed:36123449, PubMed:36264623). Also plays a role in the positive regulation of IFNG transcription in T-helper 1 cells as part of an IFNG promoter-binding complex with TXK and PARP1 (PubMed:17177976). Also plays a role in cytoskeleton organization by promoting actin bundling (By similarity)", "gene_name": "EEF1A1", "glycan_count": 7, "glycosylation_sites": [], "id": "P68104", "name": "EEF1A1", "organism": "Homo sapiens", "uniprot_id": "P68104" }, { "function": "Might be involved in growth regulation, and in myelinization in the peripheral nervous system", "gene_name": "PMP22", "glycan_count": 0, "glycosylation_sites": [ { "position": 41, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q01453", "name": "PMP22", "organism": "Homo sapiens", "uniprot_id": "Q01453" }, { "function": "Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates such as CTNND2, CD36, GSDMD, NLRP3, NOD1, NOD2, STAT3 and S1PR1 thus plays a role in various biological processes including cell adhesion, inflammation, fatty acid uptake, bacterial sensing or cardiac functions (PubMed:21820437, PubMed:29185452, PubMed:31402609, PubMed:31649195, PubMed:34293401, PubMed:38092000, PubMed:38530158, PubMed:38599239). Plays an important role in the regulation of synapse efficacy by mediating palmitoylation of delta-catenin/CTNND2, thereby increasing synaptic delivery and surface stabilization of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors (AMPARs) (PubMed:26334723). Under basal conditions, remains at the synaptic membrane through FYN-mediated phosphorylation that prevents association with endocytic proteins (PubMed:26334723). Neuronal activity enhances the internalization and trafficking of DHHC5 from spines to dendritic shafts where it palmitoylates delta-catenin/CTNND2 (PubMed:26334723). Regulates cell adhesion at the plasma membrane by palmitoylating GOLGA7B and DSG2 (PubMed:31402609). Plays a role in innate immune response by mediating the palmitoylation of NOD1 and NOD2 and their proper recruitment to the bacterial entry site and phagosomes (PubMed:31649195, PubMed:34293401). Also participates in fatty acid uptake by palmitoylating CD36 and thereby targeting it to the plasma membrane (PubMed:32958780). Upon binding of fatty acids to CD36, gets phosphorylated by LYN leading to inactivation and subsequent CD36 caveolar endocytosis (PubMed:32958780). Controls oligodendrocyte development by catalyzing STAT3 palmitoylation (By similarity). Acts as a regulator of inflammatory response by mediating palmitoylation of NLRP3 and GSDMD (PubMed:38092000, PubMed:38530158, PubMed:38599239). Palmitoylates NLRP3 to promote inflammasome assembly and activation (PubMed:38092000). Activates pyroptosis by catalyzing palmitoylation of gasdermin-D (GSDMD), thereby promoting membrane translocation and pore formation of GSDMD (PubMed:38530158, PubMed:38599239)", "gene_name": "ZDHHC5", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9C0B5", "name": "TRAPPC11", "organism": "Homo sapiens", "uniprot_id": "Q9C0B5" }, { "function": "Structural component of hyaline cartilage and vitreous of the eye", "gene_name": "COL9A2", "glycan_count": 1, "glycosylation_sites": [ { "position": 169, "type": "O-linked (Xyl...) (glycosaminoglycan) serine" }, { "position": 183, "type": "O-linked (Gal...) hydroxylysine" } ], "id": "Q14055", "name": "COL6A3", "organism": "Homo sapiens", "uniprot_id": "Q14055" }, { "function": "May play a role in the molecular organization of synapses and neuronal cell signaling. Could be an adapter protein linking ion channel to the subsynaptic cytoskeleton. May induce enrichment of PSD-95/SAP90 at the plasma membrane", "gene_name": "DLGAP4", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9Y2H0", "name": "HS3ST3A1", "organism": "Homo sapiens", "uniprot_id": "Q9Y2H0" }, { "function": "Mitochondrial adenylate kinase with a specific GTP:AMP phosphotransferase activity (PubMed:11485571, PubMed:32822537). Could also use ITP as phosphate donor (PubMed:11485571). Its physiological function is to recycle GTP into GDP which is necessary for the TCA cycle in the mitochondrial matrix (Probable)", "gene_name": "AK3", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9UIJ7", "name": "CDH12", "organism": "Homo sapiens", "uniprot_id": "Q9UIJ7" }, { "function": "Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2) (PubMed:9084911). Participates in the formation of novel hepoxilin regioisomers (PubMed:21046276)", "gene_name": "GSTM1", "glycan_count": 0, "glycosylation_sites": [], "id": "P09488", "name": "GSTM1", "organism": "Homo sapiens", "uniprot_id": "P09488" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01857 (IgG1), P01859 (IgG2), P01860 (IgG3), P01861 (IgG4)", "name": "Immunoglobulin G (IgG)", "organism": "", "uniprot_id": "" }, { "function": "Transporter for the divalent cation Zn(2+) (PubMed:10681536, PubMed:29791142, PubMed:30914478). Mediates the influx of Zn(2+) into cells from extracellular space. The Zn(2+) uniporter activity is independent of H(+)-driving force, but is modulated by extracellular pH and membrane potential. Also transports other divalent cations Zn(2+), Cd2(+), Cu2(+), Co2(+) in the order of decreasing affinity, respectively (PubMed:29791142, PubMed:30914478). In the skin, aids in the differentiation of keratinocytes in the epidermis (By similarity)", "gene_name": "SLC39A2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NP94", "name": "ZIP8 (SLC39A8)", "organism": "Homo sapiens", "uniprot_id": "Q9NP94" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q80YX1 (mouse)", "name": "Muc2", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01861 (IgG4 heavy chain)", "name": "IgG4", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q02413/Q14574", "name": "Desmoglein 1/3", "organism": "", "uniprot_id": "" }, { "function": "Constant region of immunoglobulin heavy chains. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268). IgD is the major antigen receptor isotype on the surface of most peripheral B-cells, where it is coexpressed with IgM. The membrane-bound IgD (mIgD) induces the phosphorylation of CD79A and CD79B by the Src family of protein tyrosine kinases. Soluble IgD (sIgD) concentration in serum below those of IgG, IgA, and IgM but much higher than that of IgE. IgM and IgD molecules present on B cells have identical V regions and antigen-binding sites. After the antigen binds to the B-cell receptor, the secreted form sIgD is shut off. IgD is a potent inducer of TNF, IL1B, and IL1RN. IgD also induces release of IL6, IL10, and LIF from peripheral blood mononuclear cells. Monocytes seem to be the main producers of cytokines in vitro in the presence of IgD (PubMed:10702483, PubMed:11282392, PubMed:8774350)", "gene_name": "IGHD", "glycan_count": 57, "glycosylation_sites": [ { "position": 109, "type": "O-linked (GalNAc...) serine" }, { "position": 110, "type": "O-linked (GalNAc...) serine" }, { "position": 113, "type": "O-linked (GalNAc...) threonine" }, { "position": 126, "type": "O-linked (GalNAc...) threonine" }, { "position": 127, "type": "O-linked (GalNAc...) threonine" }, { "position": 131, "type": "O-linked (GalNAc...) threonine" }, { "position": 132, "type": "O-linked (GalNAc...) threonine" }, { "position": 225, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 316, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 367, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01880", "name": "Immunoglobulin D (IgD)", "organism": "Homo sapiens", "uniprot_id": "P01880" }, { "function": "Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein (PubMed:10926824, PubMed:14734552, PubMed:1538405, PubMed:16227998, PubMed:20151848, PubMed:24121512, PubMed:28387307, PubMed:35835865). Component of the ankyrin-1 complex of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the interactions of its cytoplasmic domain with cytoskeletal proteins, glycolytic enzymes, and hemoglobin (PubMed:1538405, PubMed:20151848, PubMed:35835865). Functions as a transporter that mediates the 1:1 exchange of inorganic anions across the erythrocyte membrane. Mediates chloride-bicarbonate exchange in the kidney, and is required for normal acidification of the urine (PubMed:10926824, PubMed:14734552, PubMed:16227998, PubMed:24121512, PubMed:28387307)", "gene_name": "SLC4A1", "glycan_count": 50, "glycosylation_sites": [ { "position": 642, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P02730", "name": "Band 3 protein", "organism": "Homo sapiens", "uniprot_id": "P02730" }, { "function": "", "gene_name": "Zfp759", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8C0P2", "name": "Myomaker", "organism": "Mus musculus", "uniprot_id": "Q8C0P2" }, { "function": "Acts as an adapter for the myotubularin-related phosphatases (PubMed:23818870). Regulates phosphatase MTM1 protein stability and possibly its intracellular location (PubMed:23818870). By stabilizing MTM1 protein levels, required for skeletal muscle maintenance but not for myogenesis (PubMed:23818870)", "gene_name": "Mtmr12", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8C0P1", "name": "Myomerger", "organism": "Mus musculus", "uniprot_id": "Q80TA6" }, { "function": "The alpha-2/delta subunit of voltage-dependent calcium channels regulates calcium current density and activation/inactivation kinetics of the calcium channel. Acts as a regulatory subunit for P/Q-type calcium channel (CACNA1A), N-type (CACNA1B), L-type (CACNA1C OR CACNA1D) and possibly T-type (CACNA1G) (PubMed:15111129, PubMed:23339110). Overexpression induces apoptosis", "gene_name": "CACNA2D2", "glycan_count": 6, "glycosylation_sites": [ { "position": 386, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 418, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 507, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 540, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 624, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 861, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NY47", "name": "CACNA2D1", "organism": "Homo sapiens", "uniprot_id": "Q9NY47" }, { "function": "Alpha subunit of the heteropentameric ligand-gated chloride channel gated by gamma-aminobutyric acid (GABA), a major inhibitory neurotransmitter in the brain (PubMed:16412217, PubMed:29053855). GABA-gated chloride channels, also named GABA(A) receptors (GABAAR), consist of five subunits arranged around a central pore and contain GABA active binding site(s) located at the alpha and beta subunit interface(s) (By similarity). When activated by GABA, GABAARs selectively allow the flow of chloride anions across the cell membrane down their electrochemical gradient (PubMed:16412217, PubMed:29053855). Chloride influx into the postsynaptic neuron following GABAAR opening decreases the neuron ability to generate a new action potential, thereby reducing nerve transmission (PubMed:16412217, PubMed:29053855)", "gene_name": "GABRA3", "glycan_count": 3, "glycosylation_sites": [ { "position": 63, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 163, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 176, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 228, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P34903", "name": "GABRA3", "organism": "Homo sapiens", "uniprot_id": "P34903" }, { "function": "Multiligand endocytic receptor (By similarity). Acts together with CUBN to mediate endocytosis of high-density lipoproteins (By similarity). Mediates receptor-mediated uptake of polybasic drugs such as aprotinin, aminoglycosides and polymyxin B (By similarity). In the kidney, mediates the tubular uptake and clearance of leptin (By similarity). Also mediates transport of leptin across the blood-brain barrier through endocytosis at the choroid plexus epithelium (By similarity). Endocytosis of leptin in neuronal cells is required for hypothalamic leptin signaling and leptin-mediated regulation of feeding and body weight (By similarity). Mediates endocytosis and subsequent lysosomal degradation of CST3 in kidney proximal tubule cells (By similarity). Mediates renal uptake of 25-hydroxyvitamin D3 in complex with the vitamin D3 transporter GC/DBP (By similarity). Mediates renal uptake of metallothionein-bound heavy metals (PubMed:15126248). Together with CUBN, mediates renal reabsorption of myoglobin (By similarity). Mediates renal uptake and subsequent lysosomal degradation of APOM (By similarity). Plays a role in kidney selenium homeostasis by mediating renal endocytosis of selenoprotein SEPP1 (By similarity). Mediates renal uptake of the antiapoptotic protein BIRC5/survivin which may be important for functional integrity of the kidney (PubMed:23825075). Mediates renal uptake of matrix metalloproteinase MMP2 in complex with metalloproteinase inhibitor TIMP1 (By similarity). Mediates endocytosis of Sonic hedgehog protein N-product (ShhN), the active product of SHH (By similarity). Also mediates ShhN transcytosis (By similarity). In the embryonic neuroepithelium, mediates endocytic uptake and degradation of BMP4, is required for correct SHH localization in the ventral neural tube and plays a role in patterning of the ventral telencephalon (By similarity). Required at the onset of neurulation to sequester SHH on the apical surface of neuroepithelial cells of the rostral diencephalon ventral midline and to control PTCH1-dependent uptake and intracellular trafficking of SHH (By similarity). During neurulation, required in neuroepithelial cells for uptake of folate bound to the folate receptor FOLR1 which is necessary for neural tube closure (By similarity). In the adult brain, negatively regulates BMP signaling in the subependymal zone which enables neurogenesis to proceed (By similarity). In astrocytes, mediates endocytosis of ALB which is required for the synthesis of the neurotrophic factor oleic acid (By similarity). Involved in neurite branching (By similarity). During optic nerve development, required for SHH-mediated migration and proliferation of oligodendrocyte precursor cells (By similarity). Mediates endocytic uptake and clearance of SHH in the retinal margin which protects retinal progenitor cells from mitogenic stimuli and keeps them quiescent (By similarity). Plays a role in reproductive organ development by mediating uptake in reproductive tissues of androgen and estrogen bound to the sex hormone binding protein SHBG (By similarity). Mediates endocytosis of angiotensin-2 (By similarity). Also mediates endocytosis of angiotensis 1-7 (By similarity). Binds to the complex composed of beta-amyloid protein 40 and CLU/APOJ and mediates its endocytosis and lysosomal degradation (By similarity). Required for embryonic heart development (By similarity). Required for normal hearing, possibly through interaction with estrogen in the inner ear (By similarity)", "gene_name": "LRP2", "glycan_count": 192, "glycosylation_sites": [ { "position": 159, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 178, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 299, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 300, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 341, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 388, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 463, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 866, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1064, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1144, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1186, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1327, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1340, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1383, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1464, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1496, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1550, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1675, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1810, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2055, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2177, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2224, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2499, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2547, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2781, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2809, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2810, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2947, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2987, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3125, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3211, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3257, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3315, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3355, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3446, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3564, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3680, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3978, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4068, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4327, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P98164", "name": "LRP2", "organism": "Homo sapiens", "uniprot_id": "P98164" }, { "function": "May play a role in postsynaptic function. The C-terminal gamma-secretase processed fragment, ALID1, activates transcription activation through APBB1 (Fe65) binding (By similarity). Couples to JIP signal transduction through C-terminal binding. May interact with cellular G-protein signaling pathways. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I", "gene_name": "APLP1", "glycan_count": 3, "glycosylation_sites": [ { "position": 215, "type": "O-linked (GalNAc...) threonine" }, { "position": 227, "type": "O-linked (GalNAc...) serine" }, { "position": 228, "type": "O-linked (GalNAc...) threonine" }, { "position": 337, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 461, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 551, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P51693", "name": "APLP1", "organism": "Homo sapiens", "uniprot_id": "P51693" }, { "function": "Choline-specific phosphodiesterase that hydrolyzes sphingomyelin releasing the ceramide and phosphocholine and therefore is involved in sphingomyelin digestion, ceramide formation, and fatty acid (FA) absorption in the gastrointestinal tract (PubMed:12671034, PubMed:12885774, PubMed:15205117, PubMed:16255717, PubMed:28292932). Also has phospholipase C activity and can also cleave phosphocholine from palmitoyl lyso-phosphatidylcholine and platelet-activating factor (PAF) leading to its inactivation (PubMed:12885774, PubMed:16255717). Does not have nucleotide pyrophosphatase activity (PubMed:12885774). May promote cholesterol absorption by affecting the levels of sphingomyelin derived from either diet or endogenous sources, in the intestinal lumen (By similarity)", "gene_name": "ENPP7", "glycan_count": 14, "glycosylation_sites": [ { "position": 100, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 121, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 146, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 168, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 267, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6UWV6", "name": "ENPP6", "organism": "Homo sapiens", "uniprot_id": "Q6UWV6" }, { "function": "Heterotrimeric G protein-coupled receptor for endocannabinoid 2-arachidonoylglycerol mediating inhibition of adenylate cyclase. May function in inflammatory response, nociceptive transmission and bone homeostasis", "gene_name": "CNR2", "glycan_count": 0, "glycosylation_sites": [ { "position": 11, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P34972", "name": "Cannabinoid receptor 2 (CB2)", "organism": "Homo sapiens", "uniprot_id": "P34972" }, { "function": "In conjunction with another transmembrane protein, CNTNAP2, contributes to the organization of axonal domains at nodes of Ranvier by maintaining voltage-gated potassium channels at the juxtaparanodal region. May be involved in cell adhesion", "gene_name": "CNTN2", "glycan_count": 6, "glycosylation_sites": [ { "position": 76, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 198, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 204, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 461, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 477, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 498, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 525, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 830, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 904, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 918, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 940, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q02246", "name": "Contactin-2 (CNTN2)", "organism": "Homo sapiens", "uniprot_id": "Q02246" }, { "function": "Involved in the maintenance and repair of the intestinal mucosa. Promotes the mobility of epithelial cells in healing processes (motogen)", "gene_name": "TFF3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q07654", "name": "Trefoil factor 3 (TFF3)", "organism": "Homo sapiens", "uniprot_id": "Q07654" }, { "function": "Receptor for TNFSF4/OX40L/GP34. Is a costimulatory molecule implicated in long-term T-cell immunity", "gene_name": "TNFRSF4", "glycan_count": 1, "glycosylation_sites": [ { "position": 146, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 160, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P43489", "name": "OX40", "organism": "Homo sapiens", "uniprot_id": "P43489" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "CXCL9: Q07325, CXCL10: P02778, CXCL11: O14625", "name": "CXCL9/10/11", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "A0A2V1YN43 (P. agglomerans), D4I0C9 (E. amylovora)", "name": "OmpA", "organism": "", "uniprot_id": "" }, { "function": "Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella", "gene_name": "fliC", "glycan_count": 0, "glycosylation_sites": [], "id": "Q5XPM8_ERWAM", "name": "Flagellin (FliC)", "organism": "Erwinia amylovora", "uniprot_id": "Q5XPM8" }, { "function": "Aminoacyl-tRNA synthetase that catalyzes the specific attachment of leucine to its cognate tRNA (tRNA(Leu)) (PubMed:25051973, PubMed:32232361). It performs tRNA aminoacylation in a two-step reaction: Leu is initially activated by ATP to form a leucyl-adenylate (Leu-AMP) intermediate; then the leucyl moiety is transferred to the acceptor 3' end of the tRNA to yield leucyl-tRNA (PubMed:25051973). To improve the fidelity of catalytic reactions, it is also able to hydrolyze misactivated aminoacyl-adenylate intermediates (pre-transfer editing) and mischarged aminoacyl-tRNAs (post-transfer editing) (PubMed:25051973)", "gene_name": "LARS1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9P2J5", "name": "Cysteinyl-tRNA synthetase 1 (CARS1)", "organism": "Homo sapiens", "uniprot_id": "Q9P2J5" }, { "function": "Tyrosine--tRNA ligase that catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr) (Probable) (PubMed:25533949). Also acts as a positive regulator of poly-ADP-ribosylation in the nucleus, independently of its tyrosine--tRNA ligase activity (PubMed:25533949). Activity is switched upon resveratrol-binding: resveratrol strongly inhibits the tyrosine--tRNA ligase activity and promotes relocalization to the nucleus, where YARS1 specifically stimulates the poly-ADP-ribosyltransferase activity of PARP1 (PubMed:25533949)", "gene_name": "YARS1", "glycan_count": 1, "glycosylation_sites": [], "id": "P54577", "name": "Tyrosyl-tRNA synthetase (YARS1)", "organism": "Homo sapiens", "uniprot_id": "P54577" }, { "function": "Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (By similarity). Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen (PubMed:12782676). Has also been implicated in tumor invasion and metastasis (By similarity)", "gene_name": "Ctsb", "glycan_count": 7, "glycosylation_sites": [ { "position": 192, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P10605", "name": "Cathepsin B (CTSB)", "organism": "Mus musculus", "uniprot_id": "P10605" }, { "function": "Acid protease active in intracellular protein breakdown. Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation", "gene_name": "Ctsd", "glycan_count": 12, "glycosylation_sites": [ { "position": 134, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 261, "type": "N-linked (GlcNAc...) (high mannose) asparagine" } ], "id": "P18242", "name": "Cathepsin D (CTSD)", "organism": "Mus musculus", "uniprot_id": "P18242" }, { "function": "Transcription factor that acts as a master regulator of lysosomal biogenesis, autophagy, lysosomal exocytosis, lipid catabolism, energy metabolism and immune response (PubMed:21617040, PubMed:22343943, PubMed:22576015, PubMed:22692423, PubMed:25720963, PubMed:30120233, PubMed:31672913, PubMed:32612235, PubMed:32753672, PubMed:35662396, PubMed:36697823, PubMed:36749723, PubMed:37079666). Specifically recognizes and binds E-box sequences (5'-CANNTG-3'); efficient DNA-binding requires dimerization with itself or with another MiT/TFE family member such as TFE3 or MITF (PubMed:1748288, PubMed:19556463, PubMed:29146937). Involved in the cellular response to amino acid availability by acting downstream of MTOR: in the presence of nutrients, TFEB phosphorylation by MTOR promotes its cytosolic retention and subsequent inactivation (PubMed:21617040, PubMed:22343943, PubMed:22576015, PubMed:22692423, PubMed:25720963, PubMed:32612235, PubMed:32753672, PubMed:35662396, PubMed:36697823). Upon starvation or lysosomal stress, inhibition of MTOR induces TFEB dephosphorylation, resulting in nuclear localization and transcription factor activity (PubMed:22343943, PubMed:22576015, PubMed:22692423, PubMed:25720963, PubMed:32612235, PubMed:32753672, PubMed:35662396, PubMed:36697823). Specifically recognizes and binds the CLEAR-box sequence (5'-GTCACGTGAC-3') present in the regulatory region of many lysosomal genes, leading to activate their expression, thereby playing a central role in expression of lysosomal genes (PubMed:19556463, PubMed:22692423). Regulates lysosomal positioning in response to nutrient deprivation by promoting the expression of PIP4P1 (PubMed:29146937). Acts as a positive regulator of autophagy by promoting expression of genes involved in autophagy (PubMed:21617040, PubMed:22576015, PubMed:23434374, PubMed:27278822). In association with TFE3, activates the expression of CD40L in T-cells, thereby playing a role in T-cell-dependent antibody responses in activated CD4(+) T-cells and thymus-dependent humoral immunity (By similarity). Specifically recognizes the gamma-E3 box, a subset of E-boxes, present in the heavy-chain immunoglobulin enhancer (PubMed:2115126). Plays a role in the signal transduction processes required for normal vascularization of the placenta (By similarity). Involved in the immune response to infection by the bacteria S.aureus, S.typhimurium or S.enterica: infection promotes itaconate production, leading to alkylation, resulting in nuclear localization and transcription factor activity (PubMed:35662396). Itaconate-mediated alkylation activates TFEB-dependent lysosomal biogenesis, facilitating the bacteria clearance during the antibacterial innate immune response (PubMed:35662396). In association with ACSS2, promotes the expression of genes involved in lysosome biogenesis and both autophagy upon glucose deprivation (PubMed:28552616)", "gene_name": "TFEB", "glycan_count": 2, "glycosylation_sites": [], "id": "P19484", "name": "TFEB", "organism": "Homo sapiens", "uniprot_id": "P19484" }, { "function": "Multifunctional protein involved in endocytosis, multivesicular body biogenesis, membrane repair, cytokinesis, apoptosis and maintenance of tight junction integrity. Class E VPS protein involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome. Binds to the phospholipid lysobisphosphatidic acid (LBPA) which is abundant in MVBs internal membranes. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complexes (PubMed:14739459). The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis (PubMed:17556548, PubMed:17853893). Adapter for a subset of ESCRT-III proteins, such as CHMP4, to function at distinct membranes. Required for completion of cytokinesis (PubMed:17556548, PubMed:17853893, PubMed:18641129). May play a role in the regulation of both apoptosis and cell proliferation. Regulates exosome biogenesis in concert with SDC1/4 and SDCBP (PubMed:22660413). By interacting with F-actin, PARD3 and TJP1 secures the proper assembly and positioning of actomyosin-tight junction complex at the apical sides of adjacent epithelial cells that defines a spatial membrane domain essential for the maintenance of epithelial cell polarity and barrier (By similarity)", "gene_name": "PDCD6IP", "glycan_count": 2, "glycosylation_sites": [], "id": "Q8WUM4", "name": "ALIX (PDCD6IP)", "organism": "Homo sapiens", "uniprot_id": "Q8WUM4" }, { "function": "Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released (PubMed:12860994, PubMed:18209100). The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis (PubMed:21310966). Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase (PubMed:26040712). Plays a role in the endosomal sorting pathway. ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. When overexpressed, membrane-assembled circular arrays of CHMP4B filaments can promote or stabilize negative curvature and outward budding. CHMP4A/B/C are required for the exosomal release of SDCBP, CD63 and syndecan (PubMed:22660413). Majority of the protein exists in a folded closed conformation (PubMed:33349255)", "gene_name": "CHMP4B", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H444", "name": "CHMP4B", "organism": "Homo sapiens", "uniprot_id": "Q9H444" }, { "function": "Hormone receptor primarily expressed in adrenal cortex that plays a key role in regulating adrenocortical function (PubMed:36588120). Upon corticotropin (ACTH) binding, facilitates the release of adrenal glucocorticoids, including cortisol and corticosterone. In addition, MC2R is required for fetal and neonatal adrenal gland development (By similarity). Mechanistically, activates adenylate cyclase (cAMP), the MAPK cascade as well as the cAMP-dependent protein kinase A pathway leading to steroidogenic factor 1/NR5A1-mediated transcriptional activation (By similarity)", "gene_name": "MC2R", "glycan_count": 0, "glycosylation_sites": [ { "position": 12, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 17, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q01718", "name": "Adrenocorticotropic hormone receptor (MC2R)", "organism": "Homo sapiens", "uniprot_id": "Q01718" }, { "function": "Catalyzes the production of GABA", "gene_name": "GAD2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q05329", "name": "Glutamic Acid Decarboxylase 65 (GAD65)", "organism": "Homo sapiens", "uniprot_id": "Q05329" }, { "function": "Proton-coupled zinc ion antiporter mediating the entry of zinc into the lumen of pancreatic beta cell secretory granules, thereby regulating insulin secretion", "gene_name": "SLC30A8", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8IWU4", "name": "Zinc Transporter 8 (ZnT8)", "organism": "Homo sapiens", "uniprot_id": "Q8IWU4" }, { "function": "Receptor for arginine vasopressin. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Involved in renal water reabsorption", "gene_name": "AVPR2", "glycan_count": 1, "glycosylation_sites": [ { "position": 22, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P30518", "name": "Vasopressin receptor", "organism": "Homo sapiens", "uniprot_id": "P30518" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P06756 (ITGAV), P05106 (ITGB3)", "name": "Integrin \u03b1V\u03b23", "organism": "", "uniprot_id": "" }, { "function": "Binds to DNA, at nuclear matrix- or scaffold-associated regions. Thought to recognize the sugar-phosphate structure of double-stranded DNA. Transcription factor controlling nuclear gene expression, by binding to matrix attachment regions (MARs) of DNA and inducing a local chromatin-loop remodeling. Acts as a docking site for several chromatin remodeling enzymes and also by recruiting corepressors (HDACs) or coactivators (HATs) directly to promoters and enhancers. Required for the initiation of the upper-layer neurons (UL1) specific genetic program and for the inactivation of deep-layer neurons (DL) and UL2 specific genes, probably by modulating BCL11B expression. Repressor of Ctip2 and regulatory determinant of corticocortical connections in the developing cerebral cortex. May play an important role in palate formation. Acts as a molecular node in a transcriptional network regulating skeletal development and osteoblast differentiation", "gene_name": "SATB2", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9UPW6", "name": "SATB2", "organism": "Homo sapiens", "uniprot_id": "Q9UPW6" }, { "function": "The insulin-like growth factors possess growth-promoting activity (By similarity). Major fetal growth hormone in mammals. Plays a key role in regulating fetoplacental development. IGF2 is influenced by placental lactogen. Also involved in tissue differentiation. In adults, involved in glucose metabolism in adipose tissue, skeletal muscle and liver (Probable). Acts as a ligand for integrin which is required for IGF2 signaling (PubMed:28873464). Positively regulates myogenic transcription factor MYOD1 function by facilitating the recruitment of transcriptional coactivators, thereby controlling muscle terminal differentiation (By similarity). Inhibits myoblast differentiation and modulates metabolism via increasing the mitochondrial respiration rate (By similarity)", "gene_name": "IGF2", "glycan_count": 11, "glycosylation_sites": [ { "position": 96, "type": "O-linked (GalNAc...) threonine" }, { "position": 99, "type": "O-linked (GalNAc...) threonine" }, { "position": 163, "type": "O-linked (GalNAc...) threonine" } ], "id": "P01344", "name": "Insulin-like growth factor II (IGF-II)", "organism": "Homo sapiens", "uniprot_id": "P01344" }, { "function": "Necessary for the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis. Involved in the formation of the transitional endoplasmic reticulum (tER). The transfer of membranes from the endoplasmic reticulum to the Golgi apparatus occurs via 50-70 nm transition vesicles which derive from part-rough, part-smooth transitional elements of the endoplasmic reticulum (tER). Vesicle budding from the tER is an ATP-dependent process. The ternary complex containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope. Regulates E3 ubiquitin-protein ligase activity of RNF19A. Component of the VCP/p97-AMFR/gp78 complex that participates in the final step of the sterol-mediated ubiquitination and endoplasmic reticulum-associated degradation (ERAD) of HMGCR. Mediates the endoplasmic reticulum-associated degradation of CHRNA3 in cortical neurons as part of the STUB1-VCP-UBXN2A complex (PubMed:26265139). Involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation (PubMed:26565908). Involved in clearance process by mediating G3BP1 extraction from stress granules (PubMed:29804830, PubMed:34739333). Also involved in DNA damage response: recruited to double-strand breaks (DSBs) sites in a RNF8- and RNF168-dependent manner and promotes the recruitment of TP53BP1 at DNA damage sites (PubMed:22020440, PubMed:22120668). Recruited to stalled replication forks by SPRTN: may act by mediating extraction of DNA polymerase eta (POLH) to prevent excessive translesion DNA synthesis and limit the incidence of mutations induced by DNA damage (PubMed:23042605, PubMed:23042607). Together with SPRTN metalloprotease, involved in the repair of covalent DNA-protein cross-links (DPCs) during DNA synthesis (PubMed:32152270). Involved in interstrand cross-link repair in response to replication stress by mediating unloading of the ubiquitinated CMG helicase complex (By similarity). Mediates extraction of PARP1 trapped to chromatin: recognizes and binds ubiquitinated PARP1 and promotes its removal (PubMed:35013556). Required for cytoplasmic retrotranslocation of stressed/damaged mitochondrial outer-membrane proteins and their subsequent proteasomal degradation (PubMed:16186510, PubMed:21118995). Essential for the maturation of ubiquitin-containing autophagosomes and the clearance of ubiquitinated protein by autophagy (PubMed:20104022, PubMed:27753622). Acts as a negative regulator of type I interferon production by interacting with RIGI: interaction takes place when RIGI is ubiquitinated via 'Lys-63'-linked ubiquitin on its CARD domains, leading to recruit RNF125 and promote ubiquitination and degradation of RIGI (PubMed:26471729). May play a role in the ubiquitin-dependent sorting of membrane proteins to lysosomes where they undergo degradation (PubMed:21822278). May more particularly play a role in caveolins sorting in cells (PubMed:21822278, PubMed:23335559). By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway (PubMed:26692333)", "gene_name": "VCP", "glycan_count": 1, "glycosylation_sites": [], "id": "P55072", "name": "Valosin-containing protein (VCP/p97)", "organism": "Homo sapiens", "uniprot_id": "P55072" }, { "function": "Regulates COPI-mediated retrograde protein traffic at the interface between the Golgi apparatus and the endoplasmic reticulum (PubMed:18556652). Involved in the maintenance of the Golgi apparatus morphology (PubMed:26581903)", "gene_name": "SCYL1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96KG9", "name": "SCYL1", "organism": "Homo sapiens", "uniprot_id": "Q96KG9" }, { "function": "Guanine nucleotide exchange factor (GEF) which may activate RAB8A and RAB8B (PubMed:12221131, PubMed:26824392). Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form (PubMed:12221131, PubMed:26824392). Mediates the release of GDP from RAB8A and RAB8B but not from RAB3A or RAB5 (PubMed:20937701, PubMed:26824392). Modulates actin organization and promotes polarized transport of RAB8A-specific vesicles to the cell surface (PubMed:12221131). Together with RAB11A, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis (PubMed:20890297). Part of the ciliary targeting complex containing Rab11, ASAP1, RAB3IP and RAB11FIP3 and ARF4 that promotes RAB3IP preciliary vesicle trafficking to mother centriole and ciliogenesis initiation (PubMed:25673879, PubMed:31204173)", "gene_name": "RAB3IP", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96QF0", "name": "NBAS", "organism": "Homo sapiens", "uniprot_id": "Q96QF0" }, { "function": "Involved in regulation of membrane traffic between the Golgi and the endoplasmic reticulum (ER); the function is proposed to depend on its association in the NRZ complex which is believed to play a role in SNARE assembly at the ER. May play a role in cell cycle checkpoint control (PubMed:11096100). Essential for telomere length control (PubMed:16600870)", "gene_name": "RINT1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q6NUQ1", "name": "RINT1", "organism": "Homo sapiens", "uniprot_id": "Q6NUQ1" }, { "function": "", "gene_name": "SORCS1", "glycan_count": 3, "glycosylation_sites": [ { "position": 68, "type": "O-linked (GalNAc...) threonine" }, { "position": 184, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 352, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 433, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 765, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 776, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 816, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 847, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 908, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 929, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8WY21", "name": "SORCS2", "organism": "Homo sapiens", "uniprot_id": "Q8WY21" }, { "function": "Plays an essential role in centriole growth by stabilizing a procentriolar seed composed of at least, SASS6 and CPAP (PubMed:19052644). Required for anchoring microtubules to the centrosomes and for the integrity of the microtubule network (PubMed:16314388, PubMed:17878239, PubMed:28659385). Recruits PPARA to discrete subcellular compartments and thereby modulates PPARA activity (PubMed:15615782). Required for ciliation (PubMed:28659385)", "gene_name": "CEP350", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8WY20", "name": "SORCS3", "organism": "Homo sapiens", "uniprot_id": "Q5VT06" }, { "function": "Transcriptional repressor (PubMed:18347093, PubMed:26647308). Can act with CTBP1 to synergistically repress transcription but CTPBP1 is not essential (By similarity). Plays an important role in the specification and differentiation of lung epithelium. Acts cooperatively with FOXP4 to regulate lung secretory epithelial cell fate and regeneration by restricting the goblet cell lineage program; the function may involve regulation of AGR2. Essential transcriptional regulator of B-cell development. Involved in regulation of cardiac muscle cell proliferation. Involved in the columnar organization of spinal motor neurons. Promotes the formation of the lateral motor neuron column (LMC) and the preganglionic motor column (PGC) and is required for respective appropriate motor axon projections. The segment-appropriate generation of spinal cord motor columns requires cooperation with other Hox proteins. Can regulate PITX3 promoter activity; may promote midbrain identity in embryonic stem cell-derived dopamine neurons by regulating PITX3. Negatively regulates the differentiation of T follicular helper cells T(FH)s. Involved in maintenance of hair follicle stem cell quiescence; the function probably involves regulation of FGF18 (By similarity). Represses transcription of various pro-apoptotic genes and cooperates with NF-kappa B-signaling in promoting B-cell expansion by inhibition of caspase-dependent apoptosis (PubMed:25267198). Binds to CSF1R promoter elements and is involved in regulation of monocyte differentiation and macrophage functions; repression of CSF1R in monocytes seems to involve NCOR2 as corepressor (PubMed:15286807, PubMed:18347093, PubMed:18799727). Involved in endothelial cell proliferation, tube formation and migration indicative for a role in angiogenesis; the role in neovascularization seems to implicate suppression of SEMA5B (PubMed:24023716). Can negatively regulate androgen receptor signaling (PubMed:18640093). Acts as a transcriptional activator of the FBXL7 promoter; this activity is regulated by AURKA (PubMed:28218735)", "gene_name": "FOXP1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9H334", "name": "FOXP2", "organism": "Homo sapiens", "uniprot_id": "Q9H334" }, { "function": "Serine/threonine-protein kinase involved in various processes such as cell adhesion, regulation of cell ploidy and senescence, cell proliferation and tumor progression. Phosphorylates ATM, CASP6, LATS1, PPP1R12A and p53/TP53. Acts as a regulator of cellular senescence and cellular ploidy by mediating phosphorylation of 'Ser-464' of LATS1, thereby controlling its stability. Controls cell adhesion by regulating activity of the myosin protein phosphatase 1 (PP1) complex. Acts by mediating phosphorylation of PPP1R12A subunit of myosin PP1: phosphorylated PPP1R12A then interacts with 14-3-3, leading to reduced dephosphorylation of myosin MLC2 by myosin PP1. May be involved in DNA damage response: phosphorylates p53/TP53 at 'Ser-15' and 'Ser-392' and is recruited to the CDKN1A/WAF1 promoter to participate in transcription activation by p53/TP53. May also act as a tumor malignancy-associated factor by promoting tumor invasion and metastasis under regulation and phosphorylation by AKT1. Suppresses Fas-induced apoptosis by mediating phosphorylation of CASP6, thereby suppressing the activation of the caspase and the subsequent cleavage of CFLAR. Regulates UV radiation-induced DNA damage response mediated by CDKN1A. In association with STK11, phosphorylates CDKN1A in response to UV radiation and contributes to its degradation which is necessary for optimal DNA repair (PubMed:25329316)", "gene_name": "NUAK1", "glycan_count": 0, "glycosylation_sites": [], "id": "O60285", "name": "NUAK1", "organism": "Homo sapiens", "uniprot_id": "O60285" }, { "function": "Acts as a transcription regulator that binds target promoter DNA and bends the DNA. Binds to the sequences 5'-AACAAT-'3 or 5'-AACAAAG-3'. Modulates transcriptional regulation via WNT3A. Inhibits Wnt signaling. Promotes degradation of activated CTNNB1. Plays a key role in the regulation of embryonic development. Required for normal development of the definitive gut endoderm. Required for normal looping of the embryonic heart tube. Plays an important role in embryonic and postnatal vascular development, including development of arteries. Plays an important role in postnatal angiogenesis, where it is functionally redundant with SOX18. Required for the generation and maintenance of fetal hematopoietic stem cells, and for fetal hematopoiesis. Probable transcriptional activator in the premeiotic germ cells", "gene_name": "SOX17", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H6I2", "name": "Isthmin-1 (ISM1)", "organism": "Homo sapiens", "uniprot_id": "Q9H6I2" }, { "function": "Lysine-specific demethylase that specifically demethylates methylated lysine residues of proteins", "gene_name": "RSBN1L", "glycan_count": 1, "glycosylation_sites": [], "id": "Q6PCB5", "name": "Lysine-specific demethylase RSBN1L", "organism": "Homo sapiens", "uniprot_id": "Q6PCB5" }, { "function": "Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping. Required for cortical actin clearance prior to oocyte exocytosis (By similarity). Promotes cell motility in conjunction with S100A4 (PubMed:16707441). During cell spreading, plays an important role in cytoskeleton reorganization, focal contact formation (in the margins but not the central part of spreading cells), and lamellipodial retraction; this function is mechanically antagonized by MYH10 (PubMed:20052411)", "gene_name": "MYH9", "glycan_count": 3, "glycosylation_sites": [], "id": "P35579", "name": "Myosin-9", "organism": "Homo sapiens", "uniprot_id": "P35579" }, { "function": "Muscle contraction", "gene_name": "MYH11", "glycan_count": 2, "glycosylation_sites": [], "id": "P35749", "name": "Myosin-11", "organism": "Homo sapiens", "uniprot_id": "P35749" }, { "function": "Transcriptional regulator required for outer hair cells (OHC) maturation and, consequently, for hearing", "gene_name": "IKZF2", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9UKS7", "name": "RNA polymerase II elongation factor ELL", "organism": "Homo sapiens", "uniprot_id": "Q9UKS7" }, { "function": "Lysophosphatidylserine (LPS) lipase that mediates the hydrolysis of lysophosphatidylserine, a class of signaling lipids that regulates immunological and neurological processes (PubMed:25290914, PubMed:30237167, PubMed:30420694, PubMed:30643283, PubMed:30720278). Represents a major lysophosphatidylserine lipase in the brain, thereby playing a key role in the central nervous system (By similarity). Also able to hydrolyze oxidized phosphatidylserine; oxidized phosphatidylserine is produced in response to severe inflammatory stress and constitutes a proapoptotic 'eat me' signal (PubMed:30643283). Also has monoacylglycerol (MAG) lipase activity: hydrolyzes 2-arachidonoylglycerol (2-AG), thereby acting as a regulator of endocannabinoid signaling pathways (PubMed:22969151, PubMed:24027063). Has a strong preference for very-long-chain lipid substrates; substrate specificity is likely due to improved catalysis and not improved substrate binding (PubMed:30237167)", "gene_name": "ABHD12", "glycan_count": 5, "glycosylation_sites": [ { "position": 123, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8N2K0", "name": "Alpha/beta hydrolase domain-containing protein 14B", "organism": "Homo sapiens", "uniprot_id": "Q8N2K0" }, { "function": "Multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain the subcellular spatial organization. As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. May be involved in nucleus-centrosome attachment and nuclear migration in neural progenitors implicating LINC complex association with SUN1/2 and probably association with cytoplasmic dynein-dynactin motor complexes; SYNE1 and SYNE2 may act redundantly. Required for centrosome migration to the apical cell surface during early ciliogenesis. May be involved in nuclear remodeling during sperm head formation in spermatogenesis; a probable SUN3:SYNE1/KASH1 LINC complex may tether spermatid nuclei to posterior cytoskeletal structures such as the manchette", "gene_name": "SYNE1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q8NF91", "name": "Nesprin-1", "organism": "Homo sapiens", "uniprot_id": "Q8NF91" }, { "function": "Multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain the subcellular spatial organization. As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning (PubMed:34818527). Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. May be involved in nucleus-centrosome attachment. During interkinetic nuclear migration (INM) at G2 phase and nuclear migration in neural progenitors its LINC complex association with SUN1/2 and probable association with cytoplasmic dynein-dynactin motor complexes functions to pull the nucleus toward the centrosome; SYNE1 and SYNE2 may act redundantly. During INM at G1 phase mediates respective LINC complex association with kinesin to push the nucleus away from the centrosome. Involved in nuclear migration in retinal photoreceptor progenitors. Required for centrosome migration to the apical cell surface during early ciliogenesis. Facilitates the relaxation of mechanical stress imposed by compressive actin fibers at the rupture site through its nteraction with SYN2 (PubMed:34818527)", "gene_name": "SYNE2", "glycan_count": 5, "glycosylation_sites": [], "id": "Q8WXH0", "name": "Nesprin-2", "organism": "Homo sapiens", "uniprot_id": "Q8WXH0" }, { "function": "May have an important role in maintaining nuclear envelope structure by organizing protein complexes at the inner nuclear membrane. Required for retaining emerin at the inner nuclear membrane (By similarity). Plays a role in the modulation of innate immune signaling through the cGAS-STING pathway by interacting with RNF26 (PubMed:32614325). In addition, functions as a critical signaling component in mediating NF-kappa-B activation by acting downstream of EGFR and upstream of CARD10 (PubMed:27991920). Contributes to passive conductance current in cochlear glia-like supporting cells, mediated by gap junctions and necessary for hearing and speech discrimination (PubMed:34050020)", "gene_name": "TMEM43", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9BTV4", "name": "Transmembrane protein 43 (TMEM43)", "organism": "Homo sapiens", "uniprot_id": "Q9BTV4" }, { "function": "As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Specifically, SYNE2 and SUN2 assemble in arrays of transmembrane actin-associated nuclear (TAN) lines which are bound to F-actin cables and couple the nucleus to retrograde actin flow during actin-dependent nuclear movement. Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome-nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration. Required for nuclear migration in retinal photoreceptor progenitors implicating association with cytoplasmic dynein-dynactin and kinesin motor complexes, and probably B-type lamins; SUN1 and SUN2 seem to act redundantly. The SUN1/2:KASH5 LINC complex couples telomeres to microtubules during meiosis; SUN1 and SUN2 seem to act at least partial redundantly. Anchors chromosome movement in the prophase of meiosis and is involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis. Required for telomere attachment to nuclear envelope and gametogenesis. May also function on endocytic vesicles as a receptor for RAB5-GDP and participate in the activation of RAB5", "gene_name": "SUN2", "glycan_count": 15, "glycosylation_sites": [ { "position": 636, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UH99", "name": "SUN domain-containing protein 1", "organism": "Homo sapiens", "uniprot_id": "Q9UH99" }, { "function": "As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton (PubMed:18039933, PubMed:18396275). The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning (By similarity). Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome-nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration (By similarity). Involved in telomere attachment to nuclear envelope in the prophase of meiosis implicating a SUN1/2:KASH5 LINC complex in which SUN1 and SUN2 seem to act at least partial redundantly (By similarity). Required for gametogenesis and involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis (By similarity). Helps to define the distribution of nuclear pore complexes (NPCs) (By similarity). Required for efficient localization of SYNE4 in the nuclear envelope (By similarity). May be involved in nuclear remodeling during sperm head formation in spermatogenesis (By similarity). May play a role in DNA repair by suppressing non-homologous end joining repair to facilitate the repair of DNA cross-links (PubMed:24375709)", "gene_name": "SUN1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UH98", "name": "SUN domain-containing protein 2", "organism": "Homo sapiens", "uniprot_id": "O94901" }, { "function": "Serves as a receptor for various ligands including complement component CD3d, HNRNPU OR IFNA1 (PubMed:1849076, PubMed:21527715, PubMed:7753047). When C3d is bound to antigens, attaches to C3d on B-cell surface and thereby facilitates the recognition and uptake of antigens by B-cells (PubMed:21527715). This interaction enhances B-cell activation and subsequent immune responses. Forms a complex with several partners on the surface of B-cells including CD19, FCRL5 and CD81, to form the B-cell coreceptor complex that plays a crucial role in B-cell activation and signaling (PubMed:1383329, PubMed:30107486). Also induces specific intracellular signaling separately from the BCR and CD19 by activating the tyrosine kinase SRC, which then phosphorylates nucleolin/NCL and triggers AKT and GSK3 kinase activities in a SYK/CD19-independent manner (PubMed:12938232). Acts as a ligand for CD23 (FcepsilonRII), a low-affinity receptor for IgE, which is expressed on B-cells and other immune cells, and thus participates in the regulation of IgE production (PubMed:1386409)", "gene_name": "CR2", "glycan_count": 5, "glycosylation_sites": [ { "position": 121, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 127, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 294, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 372, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 492, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 623, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 682, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 800, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 823, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 861, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 911, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P20023", "name": "CR2 (Complement receptor 2)", "organism": "Homo sapiens", "uniprot_id": "P20023" }, { "function": "Regulates activation and degradation of trypsinogens and procarboxypeptidases by targeting specific cleavage sites within their zymogen precursors. Has chymotrypsin-type protease activity and hypocalcemic activity", "gene_name": "CTRC", "glycan_count": 0, "glycosylation_sites": [ { "position": 25, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 52, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 226, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q99895", "name": "Hyaluronan Binding Protein 4 (HABP4)", "organism": "Homo sapiens", "uniprot_id": "Q99895" }, { "function": "Binds and deliver cytosolic copper to the copper ATPase proteins. May be important in cellular antioxidant defense", "gene_name": "ATOX1", "glycan_count": 1, "glycosylation_sites": [], "id": "O00244", "name": "Antioxidant 1 Copper Chaperone (ATOX1)", "organism": "Homo sapiens", "uniprot_id": "O00244" }, { "function": "Reversible hydration of carbon dioxide", "gene_name": "Ca3", "glycan_count": 1, "glycosylation_sites": [], "id": "P16015", "name": "Carbonic Anhydrase 3", "organism": "Mus musculus", "uniprot_id": "P16015" }, { "function": "", "gene_name": "PRSS35", "glycan_count": 2, "glycosylation_sites": [ { "position": 90, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8N3Z0", "name": "TSPAN33", "organism": "Homo sapiens", "uniprot_id": "Q8N3Z0" }, { "function": "Acts as a transcriptional repressor. Inhibits interleukin-2 (IL-2) gene expression. Enhances or represses the promoter activity of the ATP1A1 gene depending on the quantity of cDNA and on the cell type. Represses E-cadherin promoter and induces an epithelial-mesenchymal transition (EMT) by recruiting SMARCA4/BRG1. Represses BCL6 transcription in the presence of the corepressor CTBP1. Positively regulates neuronal differentiation. Represses RCOR1 transcription activation during neurogenesis. Represses transcription by binding to the E box (5'-CANNTG-3'). In the absence of TGFB1, acts as a repressor of COL1A2 transcription via binding to the E-box in the upstream enhancer region (By similarity)", "gene_name": "ZEB1", "glycan_count": 1, "glycosylation_sites": [], "id": "P37275", "name": "ZEB1", "organism": "Homo sapiens", "uniprot_id": "P37275" }, { "function": "Mannosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. In the lumen of the endoplasmic reticulum, catalyzes the addition of the seventh and ninth alpha-1,2-linked mannose residues to Man(6)GlcNAc(2)-PP-dolichol and Man(8)GlcNAc(2)-PP-dolichol respectively", "gene_name": "ALG9", "glycan_count": 2, "glycosylation_sites": [ { "position": 77, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 593, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9H6U8", "name": "ALG11", "organism": "Homo sapiens", "uniprot_id": "Q9H6U8" }, { "function": "ATPase required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum (PubMed:17382883). Recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol. This complex then targets to the endoplasmic reticulum by membrane-bound receptors GET1/WRB and CAMLG/GET2, where the tail-anchored protein is released for insertion. This process is regulated by ATP binding and hydrolysis. ATP binding drives the homodimer towards the closed dimer state, facilitating recognition of newly synthesized TA membrane proteins. ATP hydrolysis is required for insertion. Subsequently, the homodimer reverts towards the open dimer state, lowering its affinity for the GET1-CAMLG receptor, and returning it to the cytosol to initiate a new round of targeting. May be involved in insulin signaling", "gene_name": "GET3", "glycan_count": 1, "glycosylation_sites": [], "id": "O43681", "name": "DPM2", "organism": "Homo sapiens", "uniprot_id": "O43681" }, { "function": "Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (PubMed:10748112, PubMed:10922473, PubMed:10926844, PubMed:14701748, PubMed:28497810). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (PubMed:10748112, PubMed:10922473, PubMed:10926844, PubMed:14701748). Histone deacetylases act via the formation of large multiprotein complexes (PubMed:10748112, PubMed:10922473, PubMed:10926844, PubMed:14701748). Also involved in the deacetylation of cohesin complex protein SMC3 regulating release of cohesin complexes from chromatin (PubMed:22885700). May play a role in smooth muscle cell contractility (PubMed:15772115). In addition to protein deacetylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase by mediating decrotonylation ((2E)-butenoyl) of histones (PubMed:28497810)", "gene_name": "HDAC8", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9BY41", "name": "HDAC8", "organism": "Homo sapiens", "uniprot_id": "Q9BY41" }, { "function": "ATPase involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner (PubMed:15075294, PubMed:29374058, PubMed:30339381, PubMed:32459350). Component of the CREST-BRG1 complex, a multiprotein complex that regulates promoter activation by orchestrating the calcium-dependent release of a repressor complex and the recruitment of an activator complex. In resting neurons, transcription of the c-FOS promoter is inhibited by SMARCA4-dependent recruitment of a phospho-RB1-HDAC repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex. At the same time, there is increased recruitment of CREBBP to the promoter by a CREST-dependent mechanism, which leads to transcriptional activation. The CREST-BRG1 complex also binds to the NR2B promoter, and activity-dependent induction of NR2B expression involves the release of HDAC1 and recruitment of CREBBP (By similarity). Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development, a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. SMARCA4/BAF190A may promote neural stem cell self-renewal/proliferation by enhancing Notch-dependent proliferative signals, while concurrently making the neural stem cell insensitive to SHH-dependent differentiating cues (By similarity). Acts as a corepressor of ZEB1 to regulate E-cadherin transcription and is required for induction of epithelial-mesenchymal transition (EMT) by ZEB1 (PubMed:20418909). Binds via DLX1 to enhancers located in the intergenic region between DLX5 and DLX6 and this binding is stabilized by the long non-coding RNA (lncRNA) Evf2 (By similarity). Binds to RNA in a promiscuous manner (By similarity). In brown adipose tissue, involved in the regulation of thermogenic genes expression (By similarity)", "gene_name": "SMARCA4", "glycan_count": 1, "glycosylation_sites": [], "id": "P51532", "name": "SMARCA4", "organism": "Homo sapiens", "uniprot_id": "P51532" }, { "function": "Necessary for abscisic acid (ABA) binding on the cell membrane and activation of the ABA signaling pathway in granulocytes", "gene_name": "LANCL2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NS86", "name": "Core1 \u03b23-galactosyltransferase (T synthase)", "organism": "Homo sapiens", "uniprot_id": "Q9NS86" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O75112 (FNDC5)", "name": "Irisin (cleaved from FNDC5)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "moaD", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9ZL43", "name": "BabA (Blood group binding adhesin)", "organism": "Helicobacter pylori (strain J99 / ATCC 700824)", "uniprot_id": "Q9ZL43" }, { "function": "Required for correct functioning of cytochrome bd-I oxidase. This protein and AppX may have some functional overlap", "gene_name": "cydX", "glycan_count": 0, "glycosylation_sites": [], "id": "P56100", "name": "FlaA", "organism": "Escherichia coli (strain K12)", "uniprot_id": "P56100" }, { "function": "May have an important role in presynaptic function. May be involved in calcium-dependent neurotransmitter release at nerve endings", "gene_name": "dnajc5", "glycan_count": 0, "glycosylation_sites": [], "id": "P56101", "name": "FlaB", "organism": "Tetronarce californica", "uniprot_id": "P56101" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9PMU3", "name": "CmeA (C. jejuni efflux pump)", "organism": "", "uniprot_id": "Q9PMU3" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q0P9D6", "name": "Cj0843 (C. jejuni exolytic lytic transglycosylase)", "organism": "", "uniprot_id": "Q0P9D6" }, { "function": "Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes", "gene_name": "lpdA", "glycan_count": 0, "glycosylation_sites": [], "id": "P0A9P0", "name": "MurA", "organism": "Escherichia coli (strain K12)", "uniprot_id": "P0A9P0" }, { "function": "Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme a of subunit 1 to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer", "gene_name": "ctaD", "glycan_count": 0, "glycosylation_sites": [], "id": "P98059", "name": "MUC2", "organism": "Rhodobacter capsulatus", "uniprot_id": "P98059" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04490/P04491", "name": "Herpes Simplex Virus gE/gI Complex", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P12318/P08637/P31994", "name": "Fc\u03b3 Receptors (Fc\u03b3RIIa, Fc\u03b3RIIIa, Fc\u03b3RIIb)", "organism": "", "uniprot_id": "" }, { "function": "Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway", "gene_name": "pol", "glycan_count": 0, "glycosylation_sites": [ { "position": 183, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 347, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 433, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 903, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 980, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1132, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1188, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 2300, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 2304, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 2456, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "Q6YMS4", "name": "Dengue Virus Envelope Glycoprotein", "organism": "Dengue virus type 3 (strain Sri Lanka/1266/2000)", "uniprot_id": "Q6YMS4" }, { "function": "Sialomucin that may play a key role in hematopoiesis by facilitating the adhesion of CD34(+) cells to the stroma and by negatively regulating CD34(+)CD38(lo/-) cell proliferation. Modulates the migration of umbilical cord blood CD133+ cells and this is mediated through the CXCL12/CXCR4 axis. May play an important role in prostate cancer metastasis and the infiltration of bone marrow by cancer cells. Promotes myogenesis by enhancing CXCR4-dependent cell motility. Positively regulates myoblast migration and promotes myoblast fusion into myotubes (By similarity)", "gene_name": "CD164", "glycan_count": 36, "glycosylation_sites": [ { "position": 26, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 32, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 41, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 72, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 77, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 94, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 121, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 142, "type": "O-linked (Xyl...) (glycosaminoglycan) serine" }, { "position": 146, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q04900", "name": "CD164", "organism": "Homo sapiens", "uniprot_id": "Q04900" }, { "function": "This protein is a minor sialoglycoprotein in human erythrocyte membranes. The blood group Gerbich antigens and receptors for Plasmodium falciparum merozoites are most likely located within the extracellular domain. Glycophorin-C plays an important role in regulating the stability of red cells", "gene_name": "GYPC", "glycan_count": 13, "glycosylation_sites": [ { "position": 3, "type": "O-linked (GalNAc...) serine" }, { "position": 4, "type": "O-linked (GalNAc...) threonine" }, { "position": 6, "type": "O-linked (GalNAc...) serine" }, { "position": 8, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 9, "type": "O-linked (GalNAc...) serine" }, { "position": 10, "type": "O-linked (GalNAc...) threonine" }, { "position": 15, "type": "O-linked (GalNAc...) serine" }, { "position": 24, "type": "O-linked (GalNAc...) serine" }, { "position": 26, "type": "O-linked (GalNAc...) serine" }, { "position": 27, "type": "O-linked (GalNAc...) threonine" }, { "position": 28, "type": "O-linked (GalNAc...) threonine" }, { "position": 31, "type": "O-linked (GalNAc...) threonine" }, { "position": 32, "type": "O-linked (GalNAc...) threonine" }, { "position": 33, "type": "O-linked (GalNAc...) threonine" }, { "position": 42, "type": "O-linked (GalNAc...) serine" } ], "id": "P04921", "name": "GYPC", "organism": "Homo sapiens", "uniprot_id": "P04921" }, { "function": "Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Binds with a low affinity EFNA3 and EFNA4 and with a high affinity to EFNA1 which most probably constitutes its cognate/functional ligand. Upon activation by EFNA1 induces cell attachment to the extracellular matrix inhibiting cell spreading and motility through regulation of ILK and downstream RHOA and RAC. Also plays a role in angiogenesis and regulates cell proliferation. May play a role in apoptosis", "gene_name": "EPHA1", "glycan_count": 0, "glycosylation_sites": [ { "position": 414, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P21709", "name": "EPHB1", "organism": "Homo sapiens", "uniprot_id": "P21709" }, { "function": "Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Adhesin responsible for the binding to D-mannose. It is laterally positioned at intervals in the structure of the type 1 fimbriae. In order to integrate FimH in the fimbriae FimF and FimG are needed", "gene_name": "fimH", "glycan_count": 0, "glycosylation_sites": [], "id": "P08191", "name": "FimH", "organism": "Escherichia coli (strain K12)", "uniprot_id": "P08191" }, { "function": "Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA)", "gene_name": "dapA", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9I4W3", "name": "LecB", "organism": "Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)", "uniprot_id": "Q9I4W3" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q1B6N3", "name": "BC2L-A", "organism": "", "uniprot_id": "Q1B6N3" }, { "function": "", "gene_name": "adh112", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9U7F6", "name": "Gal/GalNAc adherence lectin", "organism": "Entamoeba histolytica", "uniprot_id": "Q9U7F6" }, { "function": "B-FABP could be involved in the transport of a so far unknown hydrophobic ligand with potential morphogenic activity during CNS development. It is required for the establishment of the radial glial fiber system in developing brain, a system that is necessary for the migration of immature neurons to establish cortical layers (By similarity)", "gene_name": "FABP7", "glycan_count": 0, "glycosylation_sites": [], "id": "O15540", "name": "Fatty Acid Binding Protein 7 (FABP7)", "organism": "Homo sapiens", "uniprot_id": "O15540" }, { "function": "Involved in tethering the chromosomes to the spindle pole and in chromosome movement. Binds to the tail domain of the KIF3A/KIF3B heterodimer to form a heterotrimeric KIF3 complex and may regulate the membrane binding of this complex (By similarity)", "gene_name": "KIFAP3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q92845", "name": "SorLA (SORL1)", "organism": "Homo sapiens", "uniprot_id": "Q92845" }, { "function": "Involved in tumorigenesis and may function by stabilizing p53/TP53", "gene_name": "BRI3BP", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8WY22", "name": "SorCS3", "organism": "Homo sapiens", "uniprot_id": "Q8WY22" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03423 (RSV-A)", "name": "G protein (attachment glycoprotein)", "organism": "", "uniprot_id": "" }, { "function": "Involved in the activation cascade of caspases responsible for apoptosis execution. Binding of caspase-9 to Apaf-1 leads to activation of the protease which then cleaves and activates effector caspases caspase-3 (CASP3) or caspase-7 (CASP7). Promotes DNA damage-induced apoptosis in a ABL1/c-Abl-dependent manner. Proteolytically cleaves poly(ADP-ribose) polymerase (PARP). Cleaves BIRC6 following inhibition of BIRC6-caspase binding by DIABLO/SMAC (PubMed:36758105, PubMed:36758106)", "gene_name": "CASP9", "glycan_count": 1, "glycosylation_sites": [], "id": "P55211", "name": "Caspase-9", "organism": "Homo sapiens", "uniprot_id": "P55211" }, { "function": "Mediates the endocytosis of glycoproteins by macrophages. Binds both sulfated and non-sulfated polysaccharide chains", "gene_name": "MRC1", "glycan_count": 47, "glycosylation_sites": [ { "position": 104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 344, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 529, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 926, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 930, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1160, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1205, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P22897", "name": "Mannose receptor (CD206/MRC1)", "organism": "Homo sapiens", "uniprot_id": "P22897" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02671/P02675/P02679", "name": "Fibrinogen", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03437 (H7 subtype)", "name": "Hemagglutinin (HA)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03469 (N9 subtype)", "name": "Neuraminidase (NA)", "organism": "", "uniprot_id": "" }, { "function": "A beta chain of antigen-presenting major histocompatibility complex class II (MHCII) molecule. In complex with the alpha chain HLA-DRA, displays antigenic peptides on professional antigen presenting cells (APCs) for recognition by alpha-beta T cell receptor (TCR) on HLA-DRB1-restricted CD4-positive T cells. This guides antigen-specific T-helper effector functions, both antibody-mediated immune response and macrophage activation, to ultimately eliminate the infectious agents and transformed cells (PubMed:15265931, PubMed:16148104, PubMed:22327072, PubMed:27591323, PubMed:29884618, PubMed:31495665, PubMed:8642306). Typically presents extracellular peptide antigens of 10 to 30 amino acids that arise from proteolysis of endocytosed antigens in lysosomes (PubMed:8145819). In the tumor microenvironment, presents antigenic peptides that are primarily generated in tumor-resident APCs likely via phagocytosis of apoptotic tumor cells or macropinocytosis of secreted tumor proteins (PubMed:31495665). Presents peptides derived from intracellular proteins that are trapped in autolysosomes after macroautophagy, a mechanism especially relevant for T cell selection in the thymus and central immune tolerance (PubMed:17182262, PubMed:23783831). The selection of the immunodominant epitopes follows two processing modes: 'bind first, cut/trim later' for pathogen-derived antigenic peptides and 'cut first, bind later' for autoantigens/self-peptides (PubMed:25413013). The anchor residue at position 1 of the peptide N-terminus, usually a large hydrophobic residue, is essential for high affinity interaction with MHCII molecules (PubMed:8145819)", "gene_name": "HLA-DRB1", "glycan_count": 0, "glycosylation_sites": [ { "position": 48, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P20039", "name": "PB2", "organism": "Homo sapiens", "uniprot_id": "P01911" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P20038", "name": "PB1", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [ { "position": 46, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P20040", "name": "PA", "organism": "Mus musculus", "uniprot_id": "P20040" }, { "function": "Plays critical roles in virus replication, from virus entry and uncoating to assembly and budding of the virus particle. M1 binding to ribonucleocapsids (RNPs) in nucleus seems to inhibit viral transcription. Interaction of viral NEP with M1-RNP is thought to promote nuclear export of the complex, which is targeted to the virion assembly site at the apical plasma membrane in polarized epithelial cells. Interactions with NA and HA may bring M1, a non-raft-associated protein, into lipid rafts. Forms a continuous shell on the inner side of the lipid bilayer in virion, where it binds the RNP. During virus entry into cell, the M2 ion channel acidifies the internal virion core, inducing M1 dissociation from the RNP. M1-free RNPs are transported to the nucleus, where viral transcription and replication can take place", "gene_name": "M", "glycan_count": 0, "glycosylation_sites": [], "id": "P03485", "name": "M1", "organism": "Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)", "uniprot_id": "P03485" }, { "function": "Inhibits post-transcriptional processing of cellular pre-mRNA, by binding and inhibiting two cellular proteins that are required for the 3'-end processing of cellular pre-mRNAs: the 30 kDa cleavage and polyadenylation specificity factor/CPSF4 and the poly(A)-binding protein 2/PABPN1. In turn, unprocessed 3' end pre-mRNAs accumulate in the host nucleus and are no longer exported to the cytoplasm. Cellular protein synthesis is thereby shut off very early after virus infection. Viral protein synthesis is not affected by the inhibition of the cellular 3' end processing machinery because the poly(A) tails of viral mRNAs are produced by the viral polymerase through a stuttering mechanism. Prevents the establishment of the cellular antiviral state by inhibiting TRIM25-mediated RIGI ubiquitination, which normally triggers the antiviral transduction signal that leads to the activation of type I IFN genes by transcription factors IRF3 and IRF7. Also binds poly(A) and U6 snRNA. Inhibits the integrated stress response (ISR) in the infected cell by blocking dsRNA binding by EIF2AK2/PKR and further phosphorylation of EIF2S1/EIF-2ALPHA (PubMed:33766561). Stress granule formation is thus inhibited, which allows protein synthesis and viral replication (PubMed:33766561)", "gene_name": "NS", "glycan_count": 0, "glycosylation_sites": [], "id": "P03496", "name": "NS1", "organism": "Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)", "uniprot_id": "P03496" }, { "function": "Effector serine/threonine-protein kinase component of the WNK-SPAK/OSR1 kinase cascade, which is involved in various processes, such as ion transport, response to hypertonic stress and blood pressure (PubMed:16382158, PubMed:17488636, PubMed:19633012, PubMed:21486947). Specifically recognizes and binds proteins with a RFXV motif (PubMed:14563843). Acts downstream of WNK kinases (WNK1, WNK2, WNK3 or WNK4): following activation by WNK kinases, catalyzes phosphorylation of ion cotransporters, such as SLC12A1/NKCC2, SLC12A2/NKCC1, SLC12A3/NCC, SLC12A5/KCC2 or SLC12A6/KCC3, regulating their activity (PubMed:14563843, PubMed:16382158, PubMed:17488636, PubMed:19633012, PubMed:21486947). Mediates regulatory volume increase in response to hyperosmotic stress by catalyzing phosphorylation of ion cotransporters SLC12A1/NKCC2, SLC12A2/NKCC1 and SLC12A6/KCC3 downstream of WNK1 and WNK3 kinases (By similarity). Phosphorylation of Na-K-Cl cotransporters SLC12A2/NKCC1 and SLC12A2/NKCC1 promote their activation and ion influx; simultaneously, phosphorylation of K-Cl cotransporters SLC12A5/KCC2 and SLC12A6/KCC3 inhibit their activity, blocking ion efflux (By similarity). Acts as a regulator of NaCl reabsorption in the distal nephron by mediating phosphorylation and activation of the thiazide-sensitive Na-Cl cotransporter SLC12A3/NCC in distal convoluted tubule cells of kidney downstream of WNK4 (PubMed:17488636, PubMed:19633012, PubMed:21486947). Mediates the inhibition of SLC4A4, SLC26A6 as well as CFTR activities (PubMed:21317537, PubMed:23542070). Phosphorylates RELT (PubMed:16530727)", "gene_name": "Stk39", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Z1W9", "name": "CHI3L1 (YKL-40)", "organism": "Mus musculus", "uniprot_id": "Q9Z1W9" }, { "function": "Kininogens are plasma glycoproteins with a number of functions: (1) as precursor of the active peptide bradykinin they effect smooth muscle contraction, induction of hypotension and increase of vascular permeability. (2) They play a role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII. (3) They are inhibitor of thiol proteases", "gene_name": "Map1", "glycan_count": 11, "glycosylation_sites": [ { "position": 82, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 168, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 204, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 326, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01048", "name": "KNG1 (Kininogen 1)", "organism": "Rattus norvegicus", "uniprot_id": "P01048" }, { "function": "Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc (By similarity). Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (By similarity). The shared binding site between zinc and calcium at residue Asp-273 suggests a crosstalk between zinc and calcium transport in the blood (By similarity). The rank order of affinity is zinc > calcium > magnesium (By similarity). Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli (By similarity). Does not prevent iron uptake by the bacterial siderophore aerobactin (By similarity)", "gene_name": "Alb", "glycan_count": 1, "glycosylation_sites": [], "id": "P07724", "name": "SERPINA3", "organism": "Mus musculus", "uniprot_id": "P07724" }, { "function": "Plays a role in the organization of endoplasmic reticulum exit sites. Specifically binds to phosphatidylinositol 3-phosphate (PI(3)P), phosphatidylinositol 4-phosphate (PI(4)P) and phosphatidylinositol 5-phosphate (PI(5)P)", "gene_name": "SEC23IP", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9Y6Y8", "name": "CD301 (MGL)", "organism": "Homo sapiens", "uniprot_id": "Q9Y6Y8" }, { "function": "Transforming growth factor beta-3 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-3 (TGF-beta-3) chains, which constitute the regulatory and active subunit of TGF-beta-3, respectively", "gene_name": "TGFB3", "glycan_count": 10, "glycosylation_sites": [ { "position": 74, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 135, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 142, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P10600", "name": "TGF-\u03b23", "organism": "Homo sapiens", "uniprot_id": "P10600" }, { "function": "Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP1 mainly forms the vertices of the capsid (By similarity). Capsid protein VP1 interacts with host cell receptor PVR to provide virion attachment to target host cells (By similarity). This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis in Hela cells and through caveolin-mediated endocytosis in brain microvascular endothelial cells (By similarity). Tyrosine kinases are probably involved in the entry process (By similarity). Virus binding to PVR induces increased junctional permeability and rearrangement of junctional proteins (By similarity). Modulation of endothelial tight junctions, as well as cytolytic infection of endothelial cells themselves, may result in loss of endothelial integrity which may help the virus to reach the CNS (By similarity). After binding to its receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized (By similarity). Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm (By similarity)", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03301", "name": "Hepatitis A Virus (HAV) Capsid Proteins", "organism": "Poliovirus type 1 (strain Sabin)", "uniprot_id": "P03301" }, { "function": "Inhibits angiogenesis in the vitreous humor of the eye, and therefore represses neovascularization (By similarity). Binds collagen fibrils (By similarity). May be involved in collagen fiber organization via regulation of other members of the small leucine-rich repeat proteoglycan superfamily (By similarity)", "gene_name": "OPTC", "glycan_count": 0, "glycosylation_sites": [ { "position": 312, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UBM4", "name": "Glycoprotein non-metastatic melanoma protein B (gpNMB)", "organism": "Homo sapiens", "uniprot_id": "Q9UBM4" }, { "function": "", "gene_name": "HBB", "glycan_count": 0, "glycosylation_sites": [], "id": "O95408", "name": "DcR1 (Decoy Receptor 1)", "organism": "Homo sapiens", "uniprot_id": "O95408" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P11532 (mouse)", "name": "Dystrophin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P23927 (mouse)", "name": "\u03b1B-crystallin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P14602 (mouse)", "name": "HSP27", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Z1Z2 (mouse)", "name": "BAG3", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P07356 (mouse)", "name": "Calpain-1", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P10923 (mouse)", "name": "Osteopontin (SPP1)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9QZQ6 (mouse)", "name": "LTBP4", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q08043 (mouse)", "name": "\u03b1-Actinin-3", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P20152 (mouse)", "name": "Vimentin", "organism": "", "uniprot_id": "" }, { "function": "The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity)", "gene_name": "Copg2", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9QXK3", "name": "MUC2", "organism": "Mus musculus", "uniprot_id": "Q9QXK3" }, { "function": "Translocates drugs and phospholipids across the membrane. Catalyzes the flop of phospholipids from the cytoplasmic to the exoplasmic leaflet of the apical membrane. Participates mainly to the flop of phosphatidylcholine, phosphatidylethanolamine, beta-D-glucosylceramides and sphingomyelins (PubMed:8898203). Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells (By similarity)", "gene_name": "Abcb1a", "glycan_count": 4, "glycosylation_sites": [ { "position": 83, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 87, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 90, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P21447", "name": "P-glycoprotein", "organism": "Mus musculus", "uniprot_id": "P21447" }, { "function": "Receptor for the C-X-C chemokine CXCL12/SDF-1 that transduces a signal by increasing intracellular calcium ion levels and enhancing MAPK1/MAPK3 activation. Involved in the AKT signaling cascade (By similarity). Plays a role in regulation of cell migration, e.g. during wound healing. Acts as a receptor for extracellular ubiquitin; leading to enhanced intracellular calcium ions and reduced cellular cAMP levels. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes (By similarity). Involved in hematopoiesis and in cardiac ventricular septum formation. Also plays an essential role in vascularization of the gastrointestinal tract, probably by regulating vascular branching and/or remodeling processes in endothelial cells. Involved in cerebellar development. In the CNS, could mediate hippocampal-neuron survival (By similarity)", "gene_name": "CXCR4", "glycan_count": 0, "glycosylation_sites": [ { "position": 11, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 18, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" } ], "id": "P79394", "name": "CYP3A4", "organism": "Macaca mulatta", "uniprot_id": "P79394" }, { "function": "Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Does not catalyze the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate and the reversible oxidation of (S)-malate to oxaloacetate", "gene_name": "Phgdh", "glycan_count": 1, "glycosylation_sites": [], "id": "Q61753", "name": "ZO-1", "organism": "Mus musculus", "uniprot_id": "Q61753" }, { "function": "Acts as an E3 ubiquitin-protein ligase (By similarity). May have a role during the programmed cell death of hematopoietic cells", "gene_name": "Rnf130", "glycan_count": 0, "glycosylation_sites": [ { "position": 29, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 40, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 112, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 135, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 172, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 189, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9QZQ6", "name": "ZO-2", "organism": "Mus musculus", "uniprot_id": "Q8VEM1" }, { "function": "", "gene_name": "titin", "glycan_count": 0, "glycosylation_sites": [], "id": "O97791", "name": "Claudin-1", "organism": "Oryctolagus cuniculus", "uniprot_id": "O97791" }, { "function": "Peroxisomal 2-OH acyl-CoA lyase involved in the cleavage (C1 removal) reaction in the fatty acid alpha-oxydation in a thiamine pyrophosphate (TPP)-dependent manner (By similarity). Involved in the degradation of 3-methyl-branched fatty acids like phytanic acid and the shortening of 2-hydroxy long-chain fatty acids (By similarity). Plays a significant role in the biosynthesis of heptadecanal in the liver (PubMed:29027957)", "gene_name": "Hacl1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9QXE0", "name": "Occludin", "organism": "Mus musculus", "uniprot_id": "Q9QXE0" }, { "function": "Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types", "gene_name": "Cdh3", "glycan_count": 1, "glycosylation_sites": [ { "position": 192, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 558, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P10287", "name": "E-cadherin", "organism": "Mus musculus", "uniprot_id": "P10287" }, { "function": "Multifunctional transcription factor that induces cell cycle arrest, DNA repair or apoptosis upon binding to its target DNA sequence. Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Negatively regulates cell division by controlling expression of a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. Its pro-apoptotic activity is activated via its interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 (By similarity). However, this activity is inhibited when the interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 is displaced by PPP1R13L/iASPP (By similarity). In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seems to have an effect on cell-cycle regulation. Regulates the circadian clock by repressing CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER2", "gene_name": "TP53", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9TUB2", "name": "\u03b2-catenin", "organism": "Sus scrofa", "uniprot_id": "Q9TUB2" }, { "function": "Important in genetic recombination, DNA repair, and replication. Possesses pairing and strand-transfer activity. Interacts with dda and gene 32 proteins", "gene_name": "UVSX", "glycan_count": 0, "glycosylation_sites": [], "id": "Q06727", "name": "FABP4", "organism": "Enterobacteria phage T2", "uniprot_id": "Q06727" }, { "function": "Secreted protein that acts as a key regulator of lipid synthesis: mainly expressed by macrophages in lymphoid and inflamed tissues and regulates mechanisms in inflammatory responses, such as infection or atherosclerosis (PubMed:26048980). Able to inhibit lipid droplet size in adipocytes (PubMed:20519120, PubMed:22579686). Following incorporation into mature adipocytes via CD36-mediated endocytosis, associates with cytosolic FASN, inhibiting fatty acid synthase activity and leading to lipolysis, the degradation of triacylglycerols into glycerol and free fatty acids (FFA) (PubMed:20519120). CD5L-induced lipolysis occurs with progression of obesity: participates in obesity-associated inflammation following recruitment of inflammatory macrophages into adipose tissues, a cause of insulin resistance and obesity-related metabolic disease (PubMed:21730133). Regulation of intracellular lipids mediated by CD5L has a direct effect on transcription regulation mediated by nuclear receptors ROR-gamma (RORC) (PubMed:22579686, PubMed:26607793). Acts as a key regulator of metabolic switch in T-helper Th17 cells (PubMed:26607793, PubMed:26607794). Regulates the expression of pro-inflammatory genes in Th17 cells by altering the lipid content and limiting synthesis of cholesterol ligand of RORC, the master transcription factor of Th17-cell differentiation (PubMed:26607793). CD5L is mainly present in non-pathogenic Th17 cells, where it decreases the content of polyunsaturated fatty acyls (PUFA), affecting two metabolic proteins MSMO1 and CYP51A1, which synthesize ligands of RORC, limiting RORC activity and expression of pro-inflammatory genes (PubMed:26607793). Participates in obesity-associated autoimmunity via its association with IgM, interfering with the binding of IgM to Fcalpha/mu receptor and enhancing the development of long-lived plasma cells that produce high-affinity IgG autoantibodies (PubMed:23562157). Also acts as an inhibitor of apoptosis in macrophages: promotes macrophage survival from the apoptotic effects of oxidized lipids in case of atherosclerosis (PubMed:16054063, PubMed:9892623). Involved in early response to microbial infection against various pathogens by acting as a pattern recognition receptor and by promoting autophagy (By similarity)", "gene_name": "Cd5l", "glycan_count": 0, "glycosylation_sites": [ { "position": 99, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 229, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9QWK4", "name": "AIM/CD5L", "organism": "Mus musculus", "uniprot_id": "Q9QWK4" }, { "function": "Cold-inducible mRNA binding protein that plays a protective role in the genotoxic stress response by stabilizing transcripts of genes involved in cell survival. Promotes assembly of stress granules (SGs), when overexpressed. Seems to play an essential role in cold-induced suppression of cell proliferation. Acts as a translational repressor. Acts as a translational activator. Binds specifically to the 3'-untranslated regions (3'-UTRs) of stress-responsive transcripts RPA2 and TXN", "gene_name": "Cirbp", "glycan_count": 1, "glycosylation_sites": [], "id": "P60824", "name": "Extracellular CIRP (eCIRP)", "organism": "Mus musculus", "uniprot_id": "P60824" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "A1KVQ6 (N. meningitidis homolog)", "name": "MafA 2/3", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q03278", "name": "PPAR\u03b1", "organism": "Nasonia vitripennis", "uniprot_id": "Q03278" }, { "function": "Receptor for retinoic acid that acts as a transcription factor (PubMed:10874028, PubMed:11162439, PubMed:11915042, PubMed:37478846). Forms homo- or heterodimers with retinoic acid receptors (RARs) and binds to target response elements in response to their ligands, all-trans or 9-cis retinoic acid, to regulate gene expression in various biological processes (PubMed:10195690, PubMed:11162439, PubMed:11915042, PubMed:16107141, PubMed:17761950, PubMed:18800767, PubMed:19167885, PubMed:28167758, PubMed:37478846). The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 to regulate transcription (PubMed:10195690, PubMed:11162439, PubMed:11915042, PubMed:17761950, PubMed:28167758). The high affinity ligand for retinoid X receptors (RXRs) is 9-cis retinoic acid (PubMed:1310260). In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone deacetylation, chromatin condensation and transcriptional suppression (PubMed:20215566). On ligand binding, the corepressors dissociate from the receptors and coactivators are recruited leading to transcriptional activation (PubMed:20215566, PubMed:37478846, PubMed:9267036). Serves as a common heterodimeric partner for a number of nuclear receptors, such as RARA, RARB and PPARA (PubMed:10195690, PubMed:11915042, PubMed:28167758, PubMed:29021580). The RXRA/RARB heterodimer can act as a transcriptional repressor or transcriptional activator, depending on the RARE DNA element context (PubMed:29021580). The RXRA/PPARA heterodimer is required for PPARA transcriptional activity on fatty acid oxidation genes such as ACOX1 and the P450 system genes (PubMed:10195690). Together with RARA, positively regulates microRNA-10a expression, thereby inhibiting the GATA6/VCAM1 signaling response to pulsatile shear stress in vascular endothelial cells (PubMed:28167758). Acts as an enhancer of RARA binding to RARE DNA element (PubMed:28167758). May facilitate the nuclear import of heterodimerization partners such as VDR and NR4A1 (PubMed:12145331, PubMed:15509776). Promotes myelin debris phagocytosis and remyelination by macrophages (PubMed:26463675). Plays a role in the attenuation of the innate immune system in response to viral infections, possibly by negatively regulating the transcription of antiviral genes such as type I IFN genes (PubMed:25417649). Involved in the regulation of calcium signaling by repressing ITPR2 gene expression, thereby controlling cellular senescence (PubMed:30216632)", "gene_name": "RXRA", "glycan_count": 1, "glycosylation_sites": [], "id": "P19793", "name": "RXR\u03b1", "organism": "Homo sapiens", "uniprot_id": "P19793" }, { "function": "Hydrolyzes glucose-6-phosphate to glucose in the endoplasmic reticulum. Forms with the glucose-6-phosphate transporter (SLC37A4/G6PT) the complex responsible for glucose production in the terminal step of glycogenolysis and gluconeogenesis. Hence, it is the key enzyme in homeostatic regulation of blood glucose levels", "gene_name": "G6PC1", "glycan_count": 1, "glycosylation_sites": [ { "position": 96, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P35575", "name": "G6PC", "organism": "Homo sapiens", "uniprot_id": "P35575" }, { "function": "Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis", "gene_name": "PYGL", "glycan_count": 3, "glycosylation_sites": [], "id": "P06737", "name": "PYGL", "organism": "Homo sapiens", "uniprot_id": "P06737" }, { "function": "Catalyzes the oxidation of cysteine to cysteine sulfinic acid with addition of molecular dioxygen", "gene_name": "CDO1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q16878", "name": "PHKA2", "organism": "Homo sapiens", "uniprot_id": "Q16878" }, { "function": "Acts as a transcriptional regulator. Inhibits myogenesis by sequestrating E proteins, inhibiting trans-activation by MEF2, and inhibiting DNA-binding by MYOD1 through physical interaction. This interaction probably involves the basic domains of both proteins. Also represses expression of pro-inflammatory cytokines such as TNFA and IL1B. Regulates cranial suture patterning and fusion. Activates transcription as a heterodimer with E proteins. Regulates gene expression differentially, depending on dimer composition. Homodimers induce expression of FGFR2 and POSTN while heterodimers repress FGFR2 and POSTN expression and induce THBS1 expression. Heterodimerization is also required for osteoblast differentiation. Represses the activity of the circadian transcriptional activator: NPAS2-BMAL1 heterodimer (By similarity)", "gene_name": "TWIST1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q15672", "name": "Twist", "organism": "Homo sapiens", "uniprot_id": "Q15672" }, { "function": "Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A", "gene_name": "Rabggtb", "glycan_count": 0, "glycosylation_sites": [], "id": "Q08603", "name": "GPV", "organism": "Rattus norvegicus", "uniprot_id": "Q08603" }, { "function": "Calcium-dependent lectin that mediates cell adhesion by binding to glycoproteins on neighboring cells (PubMed:12403782, PubMed:28011641, PubMed:28489325). Mediates the adherence of lymphocytes to endothelial cells of high endothelial venules in peripheral lymph nodes. Promotes initial tethering and rolling of leukocytes in endothelia (PubMed:12403782, PubMed:28011641)", "gene_name": "SELL", "glycan_count": 52, "glycosylation_sites": [ { "position": 60, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 177, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 232, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 246, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 271, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P14151", "name": "L-selectin", "organism": "Homo sapiens", "uniprot_id": "P14151" }, { "function": "D-galactose specific lectin", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02872", "name": "Peanut Agglutinin (PNA)", "organism": "Arachis hypogaea", "uniprot_id": "P02872" }, { "function": "Probable chromatin remodeling factor", "gene_name": "CLSY3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9ZVY9", "name": "Sambucus nigra Agglutinin (SNA)", "organism": "Arabidopsis thaliana", "uniprot_id": "F4I8S3" }, { "function": "Chemokine that acts as a ligand for both CX3CR1 and integrins ITGAV:ITGB3 and ITGA4:ITGB1 (PubMed:12055230, PubMed:21829356, PubMed:23125415, PubMed:9782118, PubMed:9931005). The CX3CR1-CX3CL1 signaling exerts distinct functions in different tissue compartments, such as immune response, inflammation, cell adhesion and chemotaxis (PubMed:12055230, PubMed:9024663, PubMed:9177350, PubMed:9782118). Regulates leukocyte adhesion and migration processes at the endothelium (PubMed:9024663, PubMed:9177350). Can activate integrins in both a CX3CR1-dependent and CX3CR1-independent manner (PubMed:23125415, PubMed:24789099). In the presence of CX3CR1, activates integrins by binding to the classical ligand-binding site (site 1) in integrins (PubMed:23125415, PubMed:24789099). In the absence of CX3CR1, binds to a second site (site 2) in integrins which is distinct from site 1 and enhances the binding of other integrin ligands to site 1 (PubMed:23125415, PubMed:24789099)", "gene_name": "CX3CL1", "glycan_count": 12, "glycosylation_sites": [ { "position": 33, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 183, "type": "O-linked (GalNAc...) threonine" }, { "position": 253, "type": "O-linked (GalNAc...) serine" }, { "position": 329, "type": "O-linked (GalNAc...) threonine" } ], "id": "P78423", "name": "Fractalkine (CX3CL1)", "organism": "Homo sapiens", "uniprot_id": "P78423" }, { "function": "Plasma glycoprotein that binds a number of ligands such as heme, heparin, heparan sulfate, thrombospondin, plasminogen, and divalent metal ions. Binds heparin and heparin/glycosaminoglycans in a zinc-dependent manner. Binds heparan sulfate on the surface of liver, lung, kidney and heart endothelial cells. Binds to N-sulfated polysaccharide chains on the surface of liver endothelial cells. Inhibits rosette formation. Acts as an adapter protein and is implicated in regulating many processes such as immune complex and pathogen clearance, cell chemotaxis, cell adhesion, angiogenesis, coagulation and fibrinolysis. Mediates clearance of necrotic cells through enhancing the phagocytosis of necrotic cells in a heparan sulfate-dependent pathway. This process can be regulated by the presence of certain HRG ligands such as heparin and zinc ions. Binds to IgG subclasses of immunoglobins containing kappa and lambda light chains with different affinities regulating their clearance and inhibiting the formation of insoluble immune complexes. Tethers plasminogen to the cell surface. Binds T-cells and alters the cell morphology. Modulates angiogenesis by blocking the CD6-mediated antiangiongenic effect of thrombospondins, THBS1 and THBS2. Acts as a regulator of the vascular endothelial growth factor (VEGF) signaling pathway; inhibits endothelial cell motility by reducing VEGF-induced complex formation between PXN/paxillin and ILK/integrin-linked protein kinase and by promoting inhibition of VEGF-induced tyrosine phosphorylation of focal adhesion kinases and alpha-actinins in endothelial cells. Also plays a role in the regulation of tumor angiogenesis and tumor immune surveillance. Normalizes tumor vessels and promotes antitumor immunity by polarizing tumor-associated macrophages, leading to decreased tumor growth and metastasis", "gene_name": "HRG", "glycan_count": 105, "glycosylation_sites": [ { "position": 63, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 125, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 344, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 345, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P04196", "name": "Histidine-rich glycoprotein (HRG)", "organism": "Homo sapiens", "uniprot_id": "P04196" }, { "function": "Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. Activation by Wnt5A stimulates PKC activity via a G-protein-dependent mechanism. Involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Plays a role in controlling early axon growth and guidance processes necessary for the formation of a subset of central and peripheral major fiber tracts. Required for the development of major fiber tracts in the central nervous system, including: the anterior commissure, the corpus callosum, the thalamocortical, corticothalamic and nigrostriatal tracts, the corticospinal tract, the fasciculus retroflexus, the mammillothalamic tract, the medial lemniscus, and ascending fiber tracts from the spinal cord to the brain. In the peripheral nervous system, controls axon growth in distinct populations of cranial and spinal motor neurons, including the facial branchimotor nerve, the hypoglossal nerve, the phrenic nerve, and motor nerves innervating dorsal limbs. Involved in the migration of cranial neural crest cells. May also be implicated in the transmission of sensory information from the trunk and limbs to the brain. Controls commissural sensory axons guidance after midline crossing along the anterior-posterior axis in the developing spinal cord in a Wnt-dependent signaling pathway. Together with FZD6, is involved in the neural tube closure and plays a role in the regulation of the establishment of planar cell polarity (PCP), particularly in the orientation of asymmetric bundles of stereocilia on the apical faces of a subset of auditory and vestibular sensory cells located in the inner ear. Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle in a beta-catenin-dependent manner (By similarity)", "gene_name": "FZD3", "glycan_count": 2, "glycosylation_sites": [ { "position": 42, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 265, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 356, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NPG1", "name": "FZD-7", "organism": "Homo sapiens", "uniprot_id": "Q9NPG1" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P08514/P16070", "name": "CD41/CD61 (Integrin \u03b1IIb\u03b23)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q08722/P78324", "name": "CD47/SIRP\u03b1", "organism": "", "uniprot_id": "" }, { "function": "Proposed to be involved in endosomal maturation implicating in part VPS33B. In epithelial cells, the VPS33B:VIPAS39 complex may play a role in the apical RAB11A-dependent recycling pathway and in the maintenance of the apical-basolateral polarity (PubMed:20190753). May play a role in lysosomal trafficking, probably via association with the core HOPS complex in a discrete population of endosomes; the functions seems to be independent of VPS33B (PubMed:19109425). May play a role in vesicular trafficking during spermatogenesis (By similarity). May be involved in direct or indirect transcriptional regulation of E-cadherin (By similarity)", "gene_name": "VIPAS39", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H9C1", "name": "FKRP", "organism": "Homo sapiens", "uniprot_id": "Q9H9C1" }, { "function": "Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components", "gene_name": "LAMB2", "glycan_count": 61, "glycosylation_sites": [ { "position": 248, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 368, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1085, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1249, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1308, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1348, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1499, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P55268", "name": "LAMB2 (laminin beta-2)", "organism": "Homo sapiens", "uniprot_id": "P55268" }, { "function": "Plays an essential role in transcription initiation and cap-stealing mechanism, in which cellular capped pre-mRNAs are used to generate primers for viral transcription. Recognizes and binds the 7-methylguanosine-containing cap of the target pre-RNA which is subsequently cleaved after 10-13 nucleotides by the viral protein PA. Plays a role in the initiation of the viral genome replication and modulates the activity of the ribonucleoprotein (RNP) complex. In addition, participates in the inhibition of type I interferon induction through interaction with and inhibition of the host mitochondrial antiviral signaling protein MAVS", "gene_name": "PB2", "glycan_count": 0, "glycosylation_sites": [], "id": "P03428", "name": "L protein", "organism": "Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)", "uniprot_id": "P03428" }, { "function": "Plays an essential role in transcription initiation and cap-stealing mechanism, in which cellular capped pre-mRNAs are used to generate primers for viral transcription. Recognizes and binds the 7-methylguanosine-containing cap of the target pre-RNA which is subsequently cleaved after 10-13 nucleotides by the viral protein PA. Plays a role in the initiation of the viral genome replication and modulates the activity of the ribonucleoprotein (RNP) complex. In addition, participates in the inhibition of type I interferon induction through interaction with and inhibition of the host mitochondrial antiviral signaling protein MAVS", "gene_name": "PB2", "glycan_count": 0, "glycosylation_sites": [], "id": "P03427", "name": "N protein", "organism": "Influenza A virus (strain A/Wilson-Smith/1933 H1N1)", "uniprot_id": "P03427" }, { "function": "Acts as a negative regulator for transcription and replication by sticking to the nucleocapsid. This effect might be regulated by the cytoplasmic interaction with tubulin that dissociates the M protein from the nucleocapsid (By similarity). Plays a crucial role in virion assembly and budding. Forms a shell at the inner face of the plasma membrane and concentrates the HN and F glycoproteins", "gene_name": "M", "glycan_count": 0, "glycosylation_sites": [], "id": "P03426", "name": "M protein", "organism": "Sendai virus (strain Harris)", "uniprot_id": "P03426" }, { "function": "Apoptosis-inducing protein that can overcome BCL2 suppression. May play a role in repartitioning calcium between the two major intracellular calcium stores in association with BCL2. Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates in mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix. Plays an important role in the calprotectin (S100A8/A9)-induced cell death pathway", "gene_name": "BNIP3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q12983", "name": "BNIP3", "organism": "Homo sapiens", "uniprot_id": "Q12983" }, { "function": "Serine/threonine-protein kinase involved in autophagy in response to starvation (PubMed:18936157, PubMed:21460634, PubMed:21795849, PubMed:23524951, PubMed:25040165, PubMed:29487085, PubMed:31123703). Acts upstream of phosphatidylinositol 3-kinase PIK3C3 to regulate the formation of autophagophores, the precursors of autophagosomes (PubMed:18936157, PubMed:21460634, PubMed:21795849, PubMed:25040165). Part of regulatory feedback loops in autophagy: acts both as a downstream effector and negative regulator of mammalian target of rapamycin complex 1 (mTORC1) via interaction with RPTOR (PubMed:21795849). Activated via phosphorylation by AMPK and also acts as a regulator of AMPK by mediating phosphorylation of AMPK subunits PRKAA1, PRKAB2 and PRKAG1, leading to negatively regulate AMPK activity (PubMed:21460634). May phosphorylate ATG13/KIAA0652 and RPTOR; however such data need additional evidences (PubMed:18936157). Plays a role early in neuronal differentiation and is required for granule cell axon formation (PubMed:11146101). Also phosphorylates SESN2 and SQSTM1 to regulate autophagy (PubMed:25040165, PubMed:37306101). Phosphorylates FLCN, promoting autophagy (PubMed:25126726). Phosphorylates AMBRA1 in response to autophagy induction, releasing AMBRA1 from the cytoskeletal docking site to induce autophagosome nucleation (PubMed:20921139). Phosphorylates ATG4B, leading to inhibit autophagy by decreasing both proteolytic activation and delipidation activities of ATG4B (PubMed:28821708)", "gene_name": "ULK1", "glycan_count": 1, "glycosylation_sites": [], "id": "O75385", "name": "Unc-51 like autophagy activating kinase 1 (ULK1)", "organism": "Homo sapiens", "uniprot_id": "O75385" }, { "function": "Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner. Rate-limiting enzyme in the synthesis of all inositol-containing compounds (By similarity)", "gene_name": "Isyna1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9JHU9", "name": "MUC2", "organism": "Mus musculus", "uniprot_id": "Q9JHU9" }, { "function": "By degrading DNA that enters the cell, plays a role in the competence of cells to be transformed. Degrades both double-stranded, linear and covalently closed circular DNA", "gene_name": "nucA", "glycan_count": 0, "glycosylation_sites": [], "id": "P12667", "name": "F glycoprotein", "organism": "Bacillus subtilis (strain 168)", "uniprot_id": "P12667" }, { "function": "By degrading DNA that enters the cell, plays a role in the competence of cells to be transformed. Degrades both double-stranded, linear and covalently closed circular DNA", "gene_name": "nucA", "glycan_count": 0, "glycosylation_sites": [], "id": "P12668", "name": "HN glycoprotein", "organism": "Bacillus subtilis (strain 168)", "uniprot_id": "P12667" }, { "function": "TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins", "gene_name": "SSR4", "glycan_count": 1, "glycosylation_sites": [], "id": "P51571", "name": "Signal Sequence Receptor Protein 4 (SSR4)", "organism": "Homo sapiens", "uniprot_id": "P51571" }, { "function": "The alpha-V (ITGAV) integrins are receptors for vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin and vWF. They recognize the sequence R-G-D in a wide array of ligands. ITGAV:ITGB3 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling (PubMed:23125415). ITGAV:ITGB3 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling (PubMed:20682778). ITGAV:ITGB3 binds to FGF1 and this binding is essential for FGF1 signaling (PubMed:18441324). ITGAV:ITGB3 binds to FGF2 and this binding is essential for FGF2 signaling (PubMed:28302677). ITGAV:ITGB3 binds to IGF1 and this binding is essential for IGF1 signaling (PubMed:19578119). ITGAV:ITGB3 binds to IGF2 and this binding is essential for IGF2 signaling (PubMed:28873464). ITGAV:ITGB3 binds to IL1B and this binding is essential for IL1B signaling (PubMed:29030430). ITGAV:ITGB3 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1 (PubMed:18635536, PubMed:25398877). ITGAV:ITGB3 and ITGAV:ITGB6 act as receptors for fibrillin-1 (FBN1) and mediate R-G-D-dependent cell adhesion to FBN1 (PubMed:12807887, PubMed:17158881). Integrin alpha-V/beta-6 or alpha-V/beta-8 (ITGAV:ITGB6 or ITGAV:ITGB8) mediates R-G-D-dependent release of transforming growth factor beta-1 (TGF-beta-1) from regulatory Latency-associated peptide (LAP), thereby playing a key role in TGF-beta-1 activation (PubMed:15184403, PubMed:22278742, PubMed:28117447). ITGAV:ITGB3 acts as a receptor for CD40LG (PubMed:31331973). ITGAV:ITGB3 acts as a receptor for IBSP and promotes cell adhesion and migration to IBSP (PubMed:10640428)", "gene_name": "ITGAV", "glycan_count": 114, "glycosylation_sites": [ { "position": 74, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 290, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 296, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 488, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 554, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 615, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 704, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 835, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 851, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 874, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 945, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 973, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 980, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P06756", "name": "ITGAV (Integrin alpha-V)", "organism": "Homo sapiens", "uniprot_id": "P06756" }, { "function": "High affinity receptor for semaphorins 3C, 3F, VEGF-165 and VEGF-145 isoforms of VEGF, and the PLGF-2 isoform of PGF", "gene_name": "NRP2", "glycan_count": 3, "glycosylation_sites": [ { "position": 152, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 157, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 629, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 839, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O60462", "name": "NRP2 (Neuropilin-2)", "organism": "Homo sapiens", "uniprot_id": "O60462" }, { "function": "Acts as a ligand for FGFR1, FGFR2, FGFR3 and FGFR4 (PubMed:8663044). Also acts as an integrin ligand which is required for FGF2 signaling (PubMed:28302677). Binds to integrin ITGAV:ITGB3 (PubMed:28302677). Plays an important role in the regulation of cell survival, cell division, cell differentiation and cell migration (PubMed:28302677, PubMed:8663044). Functions as a potent mitogen in vitro (PubMed:1721615, PubMed:3732516, PubMed:3964259). Can induce angiogenesis (PubMed:23469107, PubMed:28302677). Mediates phosphorylation of ERK1/2 and thereby promotes retinal lens fiber differentiation (PubMed:29501879)", "gene_name": "FGF2", "glycan_count": 1, "glycosylation_sites": [], "id": "P09038", "name": "FGF2 (Fibroblast growth factor 2)", "organism": "Homo sapiens", "uniprot_id": "P09038" }, { "function": "Member of the Wnt ligand gene family that encodes for secreted proteins, which activate the Wnt signaling cascade. Specifically activates canonical Wnt/beta-catenin signaling and thus triggers beta-catenin/LEF/TCF-mediated transcriptional programs. Involved in signaling networks controlling stemness, pluripotency and cell fate decisions. Acts in the immune system, mammary gland, adipose tissue, bone and skin", "gene_name": "WNT10B", "glycan_count": 1, "glycosylation_sites": [ { "position": 93, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 335, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O00744", "name": "WNT10B", "organism": "Homo sapiens", "uniprot_id": "O00744" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P19429/P19430/P19431", "name": "Troponin", "organism": "", "uniprot_id": "" }, { "function": "RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. Within the nucleus, promotes circRNAs processing by stabilizing the regulatory elements residing in the flanking introns of the circularized exons. Plays thereby a role in the back-splicing of a subset of circRNAs (PubMed:28625552). As a consequence, participates in a wide range of transcriptional and post-transcriptional processes. Binds to poly-U elements and AU-rich elements (AREs) in the 3'-UTR of target mRNAs (PubMed:14731398). Upon viral infection, ILF3 accumulates in the cytoplasm and participates in the innate antiviral response (PubMed:21123651, PubMed:34110282). Mechanistically, ILF3 becomes phosphorylated and activated by the double-stranded RNA-activated protein kinase/PKR which releases ILF3 from cellular mature circRNAs. In turn, unbound ILF3 molecules are able to interact with and thus inhibit viral mRNAs (PubMed:21123651, PubMed:28625552)", "gene_name": "ILF3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q12906", "name": "ILF3 (Interleukin enhancer-binding factor 3)", "organism": "Homo sapiens", "uniprot_id": "Q12906" }, { "function": "", "gene_name": "MRPL4", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9BYD3", "name": "MTUS1", "organism": "Homo sapiens", "uniprot_id": "Q9BYD3" }, { "function": "Transcriptional repressor. Down-regulates transcription activation by NF-kappa-B by promoting the deacetylation of RELA at 'Lys-310'. Promotes HDAC1 binding to promoter regions. Down-regulates expression of anti-apoptotic genes that are controlled by NF-kappa-B. Promotes apoptosis in cells that have inadequate adherence to a substrate, a process called anoikis, and may thereby inhibit metastasis. May be a mediator of metastasis suppression in breast carcinoma", "gene_name": "BRMS1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9HCU9", "name": "BRMS1", "organism": "Homo sapiens", "uniprot_id": "Q9HCU9" }, { "function": "Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. May promote the assembly of presynaptic RAD51 nucleoprotein filaments. Binds single-stranded DNA and double-stranded DNA and has DNA-dependent ATPase activity. Part of the RAD51 paralog protein complex BCDX2 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of RAD51 recruitment. BCDX2 binds predominantly to the intersection of the four duplex arms of the Holliday junction and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA. The BCDX2 subcomplex RAD51B:RAD51C exhibits single-stranded DNA-dependent ATPase activity suggesting an involvement in early stages of the HR pathway", "gene_name": "RAD51B", "glycan_count": 1, "glycosylation_sites": [], "id": "O15315", "name": "SHOX2", "organism": "Homo sapiens", "uniprot_id": "O15315" }, { "function": "Mediates a variety of processes including matrix regulation and turnover, inflammation, and angiogenesis, through reversible inhibition of zinc protease superfamily enzymes, primarily matrix metalloproteinases (MMPs). Regulates extracellular matrix (ECM) remodeling through inhibition of matrix metalloproteinases (MMP) including MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, MMP-13, MMP-14 and MMP-15. Additionally, modulates the processing of amyloid precursor protein (APP) and apolipoprotein E receptor ApoER2 by inhibiting two alpha-secretases ADAM10 and ADAM17 (PubMed:17913923). Functions as a tumor suppressor and a potent inhibitor of angiogenesis. Exerts its anti-angiogenic effect by directly interacting with vascular endothelial growth factor (VEGF) receptor-2/KDR, preventing its binding to the VEGFA ligand (PubMed:12652295). Selectively induces apoptosis in angiogenic endothelial cells through a caspase-independent cell death pathway (PubMed:25558000). Mechanistically, inhibits matrix-induced focal adhesion kinase PTK2 tyrosine phosphorylation and association with paxillin/PXN and disrupts the incorporation of ITGB3, PTK2 and PXN into focal adhesion contacts on the matrix (PubMed:25558000)", "gene_name": "TIMP3", "glycan_count": 12, "glycosylation_sites": [], "id": "P35625", "name": "TIMP-3", "organism": "Homo sapiens", "uniprot_id": "P35625" }, { "function": "Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to various stress, such as unfolded protein response (UPR) (PubMed:10026192, PubMed:10677345, PubMed:11907036, PubMed:12086964, PubMed:25925385, PubMed:31023583). Key effector of the integrated stress response (ISR) to unfolded proteins: EIF2AK3/PERK specifically recognizes and binds misfolded proteins, leading to its activation and EIF2S1/eIF-2-alpha phosphorylation (PubMed:10677345, PubMed:27917829, PubMed:31023583). EIF2S1/eIF-2-alpha phosphorylation in response to stress converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, leading to a global attenuation of cap-dependent translation, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activators ATF4 and QRICH1, and hence allowing ATF4- and QRICH1-mediated reprogramming (PubMed:10026192, PubMed:10677345, PubMed:31023583, PubMed:33384352). The EIF2AK3/PERK-mediated unfolded protein response increases mitochondrial oxidative phosphorylation by promoting ATF4-mediated expression of COX7A2L/SCAF1, thereby increasing formation of respiratory chain supercomplexes (PubMed:31023583). In contrast to most subcellular compartments, mitochondria are protected from the EIF2AK3/PERK-mediated unfolded protein response due to EIF2AK3/PERK inhibition by ATAD3A at mitochondria-endoplasmic reticulum contact sites (PubMed:39116259). In addition to EIF2S1/eIF-2-alpha, also phosphorylates NFE2L2/NRF2 in response to stress, promoting release of NFE2L2/NRF2 from the BCR(KEAP1) complex, leading to nuclear accumulation and activation of NFE2L2/NRF2 (By similarity). Serves as a critical effector of unfolded protein response (UPR)-induced G1 growth arrest due to the loss of cyclin-D1 (CCND1) (By similarity). Involved in control of mitochondrial morphology and function (By similarity)", "gene_name": "EIF2AK3", "glycan_count": 3, "glycosylation_sites": [ { "position": 258, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NZJ5", "name": "EIF2AK3", "organism": "Homo sapiens", "uniprot_id": "Q9NZJ5" }, { "function": "Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2, CBX4 or ZNF451 (PubMed:26524494). This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins (PubMed:18408734, PubMed:18538659, PubMed:21965678, PubMed:9556629). Plays a role in the regulation of sumoylation status of SETX (PubMed:24105744)", "gene_name": "SUMO2", "glycan_count": 1, "glycosylation_sites": [], "id": "P61956", "name": "SUMO2", "organism": "Homo sapiens", "uniprot_id": "P61956" }, { "function": "Odorant receptor", "gene_name": "OR4A15", "glycan_count": 0, "glycosylation_sites": [ { "position": 36, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 290, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8NGL6", "name": "P2RY13", "organism": "Homo sapiens", "uniprot_id": "Q8NGL6" }, { "function": "Broad specificity cytosolic 5'-nucleotidase that catalyzes the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates (PubMed:10092873, PubMed:12907246, PubMed:1659319, PubMed:9371705). In addition, possesses a phosphotransferase activity by which it can transfer a phosphate from a donor nucleoside monophosphate to an acceptor nucleoside, preferably inosine, deoxyinosine and guanosine (PubMed:1659319, PubMed:9371705). Has the highest activities for IMP and GMP followed by dIMP, dGMP and XMP (PubMed:10092873, PubMed:12907246, PubMed:1659319, PubMed:9371705). Could also catalyze the transfer of phosphates from pyrimidine monophosphates but with lower efficiency (PubMed:1659319, PubMed:9371705). Through these activities regulates the purine nucleoside/nucleotide pools within the cell (PubMed:10092873, PubMed:12907246, PubMed:1659319, PubMed:9371705)", "gene_name": "NT5C2", "glycan_count": 1, "glycosylation_sites": [], "id": "P49902", "name": "NT5C", "organism": "Homo sapiens", "uniprot_id": "P49902" }, { "function": "May play a role in physiologic lymphocyte functions at mucosal sites", "gene_name": "FGL2", "glycan_count": 125, "glycosylation_sites": [ { "position": 25, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 179, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 235, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 263, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 336, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q14314", "name": "FGL2", "organism": "Homo sapiens", "uniprot_id": "Q14314" }, { "function": "Involved in control of cellular proliferation. Onconcogenic modifier contributing to the tumor suppressor function of DNMT3B", "gene_name": "MENT", "glycan_count": 4, "glycosylation_sites": [], "id": "Q9BUN1", "name": "CLEC3A", "organism": "Homo sapiens", "uniprot_id": "Q9BUN1" }, { "function": "Could be involved in cell-cell and/or cell-matrix interactions necessary for normal growth control. Pro-apoptotic protein that functions intracellularly upstream of JNK activation and cytochrome c release", "gene_name": "LGALS7", "glycan_count": 1, "glycosylation_sites": [], "id": "P47929", "name": "Galectin-7", "organism": "Homo sapiens", "uniprot_id": "P47929" }, { "function": "Serine protease that initiates the alternative pathway of the complement system, a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system (PubMed:21205667, PubMed:22362762, PubMed:6769474, PubMed:874324, PubMed:9748277). In contrast to other complement pathways (classical, lectin and GZMK) that are directly activated by pathogens or antigen-antibody complexes, the alternative complement pathway is initiated by the spontaneous hydrolysis of complement C3 (PubMed:21205667, PubMed:22362762, PubMed:6769474, PubMed:874324). The alternative complement pathway acts as an amplification loop that enhances complement activation by mediating the formation of C3 and C5 convertases (PubMed:21205667, PubMed:22362762, PubMed:6769474, PubMed:874324). Activated CFD cleaves factor B (CFB) when the latter is complexed with complement C3b, activating the C3 convertase of the alternative pathway (PubMed:21205667, PubMed:6769474, PubMed:874324, PubMed:9748277)", "gene_name": "CFD", "glycan_count": 0, "glycosylation_sites": [], "id": "P00746", "name": "Complement factor D", "organism": "Homo sapiens", "uniprot_id": "P00746" }, { "function": "Channel-forming protein essential for import of protein precursors into mitochondria (PubMed:15644312, PubMed:31206022). Plays a role in the assembly of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) by forming a complex with BCAP31 and mediating the translocation of Complex I components from the cytosol to the mitochondria (PubMed:31206022)", "gene_name": "TOMM40", "glycan_count": 1, "glycosylation_sites": [], "id": "O96008", "name": "Translocase of outer mitochondrial membrane 40 homolog (TOMM40)", "organism": "Homo sapiens", "uniprot_id": "O96008" }, { "function": "Acts as a glycogen-targeting subunit for PP1 and regulates its activity. Activates glycogen synthase, reduces glycogen phosphorylase activity and limits glycogen breakdown. Dramatically increases basal and insulin-stimulated glycogen synthesis upon overexpression in a variety of cell types", "gene_name": "PPP1R3C", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UQK1", "name": "CD39 (ENTPD1)", "organism": "Homo sapiens", "uniprot_id": "Q9UQK1" }, { "function": "Receptor for interleukin-7. Also acts as a receptor for thymic stromal lymphopoietin (TSLP)", "gene_name": "IL7R", "glycan_count": 1, "glycosylation_sites": [ { "position": 49, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 65, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 151, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 182, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 232, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 233, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P16871", "name": "CD127 (IL7R)", "organism": "Homo sapiens", "uniprot_id": "P16871" }, { "function": "Catalyzes the deimination of arginine residues of proteins", "gene_name": "PADI1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9ULC6", "name": "Peptidyl arginine deiminase (PADI)", "organism": "Homo sapiens", "uniprot_id": "Q9ULC6" }, { "function": "Central component of the receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with TOM22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the TOM40 translocation pore (By similarity). Required for the translocation across the mitochondrial outer membrane of cytochrome P450 monooxygenases", "gene_name": "TOMM20", "glycan_count": 0, "glycosylation_sites": [], "id": "Q15388", "name": "TOM20", "organism": "Homo sapiens", "uniprot_id": "Q15388" }, { "function": "Kinase that plays a key role in glycerol metabolism, catalyzing its phosphorylation to produce sn-glycerol 3-phosphate. Sn-glycerol 3-phosphate is a crucial intermediate in various metabolic pathways, such as the synthesis of glycerolipids and triglycerides, glycogenesis, glycolysis and gluconeogenesis", "gene_name": "GK", "glycan_count": 1, "glycosylation_sites": [], "id": "P32189", "name": "Glycerol kinase", "organism": "Homo sapiens", "uniprot_id": "P32189" }, { "function": "Receptor for WNT2 that is coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes (By similarity). Plays a role in neuromuscular junction (NMJ) assembly by negatively regulating the clustering of acetylcholine receptors (AChR) through the beta-catenin canonical signaling pathway (By similarity). May play a role in neural progenitor cells (NPCs) viability through the beta-catenin canonical signaling pathway by negatively regulating cell cycle arrest leading to inhibition of neuron apoptotic process (PubMed:27509850). During hippocampal development, regulates neuroblast proliferation and apoptotic cell death. Controls bone formation through non canonical Wnt signaling mediated via ISG15. Positively regulates bone regeneration through non canonical Wnt signaling (By similarity)", "gene_name": "FZD9", "glycan_count": 4, "glycosylation_sites": [ { "position": 53, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 158, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O00144", "name": "NR0B1 (DAX1)", "organism": "Homo sapiens", "uniprot_id": "O00144" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9BYF1 (human)", "name": "ACE2", "organism": "", "uniprot_id": "" }, { "function": "Nuclear receptor coregulator that can have both coactivator and corepressor functions. Interacts with nuclear receptors for steroids (ESR1 and ESR2) independently of the steroid binding domain (AF-2) of the ESR receptors, and with the orphan nuclear receptor NR1D2. Involved in the coactivation of nuclear steroid receptors (ER) as well as the corepression of MYC in response to 17-beta-estradiol (E2)", "gene_name": "NCOA5", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H4Y9", "name": "Betaine\u2013homocysteine S-methyltransferase 2 (BHMT2)", "organism": "Homo sapiens", "uniprot_id": "Q9HCD5" }, { "function": "Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor (PubMed:16638743, PubMed:31932717, PubMed:8663203, PubMed:9295285). Has activity toward HIV envelope glycoprotein gp120, EA2, MUC2, MUC1A and MUC5AC (PubMed:8663203, PubMed:9295285). Probably glycosylates fibronectin in vivo (PubMed:9295285). Glycosylates FGF23 (PubMed:16638743, PubMed:31932717)", "gene_name": "GALNT3", "glycan_count": 7, "glycosylation_sites": [ { "position": 132, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 297, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 484, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q14435", "name": "GALNT3", "organism": "Homo sapiens", "uniprot_id": "Q14435" }, { "function": "Component of a protein kinase signal transduction cascade. Activates the CSBP2, P38 and JNK MAPK pathways, but not the ERK pathway. Specifically phosphorylates and activates MAP2K4 and MAP2K6", "gene_name": "MAP3K4", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y6R4", "name": "MEKK2 fragment", "organism": "Homo sapiens", "uniprot_id": "Q9Y6R4" }, { "function": "Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro (PubMed:20385563, PubMed:8806703). Catalyzes the conversion of leukotriene C4 to leukotriene F4 via the hydrolysis of an amide bond (By similarity)", "gene_name": "CPA1", "glycan_count": 0, "glycosylation_sites": [], "id": "P15085", "name": "Carboxypeptidase A", "organism": "Homo sapiens", "uniprot_id": "P15085" }, { "function": "Catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin-proteasome system (PubMed:1447181, PubMed:1606621, PubMed:33108101). Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP (PubMed:1447181). Essential for the formation of radiation-induced foci, timely DNA repair and for response to replication stress. Promotes the recruitment of TP53BP1 and BRCA1 at DNA damage sites (PubMed:22456334)", "gene_name": "UBA1", "glycan_count": 3, "glycosylation_sites": [], "id": "P22314", "name": "UBA1 (Ubiquitin-like modifier activating enzyme 1)", "organism": "Homo sapiens", "uniprot_id": "P22314" }, { "function": "Transcriptional regulator that plays a role in various cellular processes including embryonic development, cell differentiation, angiogenesis and tissue homeostasis (PubMed:12064918, PubMed:16516194). Upon BMP ligand binding to their receptors at the cell surface, is phosphorylated by activated type I BMP receptors (BMPRIs) and associates with SMAD4 to form a heteromeric complex which translocates into the nucleus acting as transcription factor (PubMed:9442019). In turn, the hetero-trimeric complex recognizes cis-regulatory elements containing Smad Binding Elements (SBEs) to modulate the outcome of the signaling network (PubMed:33510867). Non-phosphorylated SMAD5 has a cytoplasmic role in energy metabolism regulation by promoting mitochondrial respiration and glycolysis in response to cytoplasmic pH changes (PubMed:28675158). Mechanistically, interacts with hexokinase 1/HK1 and thereby accelerates glycolysis (PubMed:28675158)", "gene_name": "SMAD5", "glycan_count": 1, "glycosylation_sites": [], "id": "Q99717", "name": "Smad3", "organism": "Homo sapiens", "uniprot_id": "Q99717" }, { "function": "Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (PubMed:16478993, PubMed:19696785). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:26991466, PubMed:27295069). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. They first alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery (PubMed:18239673). Main chaperone involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription (PubMed:20353823). Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059)", "gene_name": "HSP90AB1", "glycan_count": 6, "glycosylation_sites": [ { "position": 434, "type": "O-linked (GlcNAc) serine" }, { "position": 452, "type": "O-linked (GlcNAc) serine" } ], "id": "P08238", "name": "HSP90", "organism": "Homo sapiens", "uniprot_id": "P08238" }, { "function": "Functions as an intestinal M-cell transcytotic receptor specific for type-I-piliated bacteria that participates in the mucosal immune response toward these bacteria. At the apical membrane of M-cells it binds fimH, a protein of the bacteria type I pilus tip. Internalizes bound bacteria, like E.coli and S.typhimurium, from the lumen of the intestine and delivers them, through M-cells, to the underlying organized lymphoid follicles where they are captured by antigen-presenting dendritic cells to elicit a mucosal immune response", "gene_name": "GP2", "glycan_count": 8, "glycosylation_sites": [ { "position": 65, "type": "N-linked (GlcNAc...) (high mannose) asparagine" }, { "position": 88, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 122, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 134, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 204, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 216, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 260, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 291, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 342, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 362, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P55259", "name": "Glycoprotein 2 (GP2)", "organism": "Homo sapiens", "uniprot_id": "P55259" }, { "function": "Activates insulin, somatostatin, glucokinase, islet amyloid polypeptide and glucose transporter type 2 gene transcription. Particularly involved in glucose-dependent regulation of insulin gene transcription. As part of a PDX1:PBX1b:MEIS2b complex in pancreatic acinar cells is involved in the transcriptional activation of the ELA1 enhancer; the complex binds to the enhancer B element and cooperates with the transcription factor 1 complex (PTF1) bound to the enhancer A element. Binds preferentially the DNA motif 5'-[CT]TAAT[TG]-3'. During development, specifies the early pancreatic epithelium, permitting its proliferation, branching and subsequent differentiation. At adult stage, required for maintaining the hormone-producing phenotype of the beta-cell", "gene_name": "PDX1", "glycan_count": 0, "glycosylation_sites": [], "id": "P52945", "name": "PDX1", "organism": "Homo sapiens", "uniprot_id": "P52945" }, { "function": "Histone demethylase that demethylates 'Lys-4' and 'Lys-36' of histone H3, thereby playing a central role in histone code (PubMed:16362057, PubMed:17994099, PubMed:26237645). Preferentially demethylates trimethylated H3 'Lys-4' and dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36' (PubMed:16362057, PubMed:17994099, PubMed:26237645). Preferentially binds the transcribed region of ribosomal RNA and represses the transcription of ribosomal RNA genes which inhibits cell growth and proliferation (PubMed:16362057, PubMed:17994099). May also serve as a substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex (Probable)", "gene_name": "KDM2B", "glycan_count": 2, "glycosylation_sites": [], "id": "Q8NHM5", "name": "MAFA", "organism": "Homo sapiens", "uniprot_id": "Q8NHM5" }, { "function": "Promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. Interaction with FLNB may allow neuroblast migration from the ventricular zone into the cortical plate. Tethers cell surface-localized furin, modulates its rate of internalization and directs its intracellular trafficking (By similarity). Involved in ciliogenesis. Plays a role in cell-cell contacts and adherens junctions during the development of blood vessels, heart and brain organs. Plays a role in platelets morphology through interaction with SYK that regulates ITAM- and ITAM-like-containing receptor signaling, resulting in by platelet cytoskeleton organization maintenance (By similarity). During the axon guidance process, required for growth cone collapse induced by SEMA3A-mediated stimulation of neurons (PubMed:25358863)", "gene_name": "FLNA", "glycan_count": 12, "glycosylation_sites": [], "id": "P21333", "name": "FLNA (Filamin A)", "organism": "Homo sapiens", "uniprot_id": "P21333" }, { "function": "Non-enzymatic adapter protein that plays a pivotal role in precisely regulated signaling cascades from cell surface receptors to cellular responses, including signaling transduction and gene expression (PubMed:11726515, PubMed:37626338). Thus, participates in many biological processes including regulation of innate and adaptive immunity, autophagy, DNA repair or necroptosis (PubMed:35831301, PubMed:37626338, PubMed:38182563). Controls signaling complexes at the T-cell antigen receptor to facilitate the activation, differentiation, and function of T-cells (PubMed:36864087, PubMed:9489702). Mechanistically, engagement of the TCR leads to phosphorylation of the adapter protein LAT, which serves as docking site for GRB2 (PubMed:9489702). In turn, GRB2 establishes a a connection with SOS1 that acts as a guanine nucleotide exchange factor and serves as a critical regulator of KRAS/RAF1 leading to MAPKs translocation to the nucleus and activation (PubMed:12171928, PubMed:25870599). Functions also a role in B-cell activation by amplifying Ca(2+) mobilization and activation of the ERK MAP kinase pathway upon recruitment to the phosphorylated B-cell antigen receptor (BCR) (PubMed:25413232, PubMed:29523808). Plays a role in switching between autophagy and programmed necrosis upstream of EGFR by interacting with components of necrosomes including RIPK1 and with autophagy regulators SQSTM1 and BECN1 (PubMed:35831301, PubMed:38182563). Regulates miRNA biogenesis by forming a functional ternary complex with AGO2 and DICER1 (PubMed:37328606). Functions in the replication stress response by protecting DNA at stalled replication forks from MRE11-mediated degradation. Mechanistically, inhibits RAD51 ATPase activity to stabilize RAD51 on stalled replication forks (PubMed:38459011). Additionally, directly recruits and later releases MRE11 at DNA damage sites during the homology-directed repair (HDR) process (PubMed:34348893)", "gene_name": "GRB2", "glycan_count": 1, "glycosylation_sites": [], "id": "P62993", "name": "GRB2 (Growth factor receptor-bound protein 2)", "organism": "Homo sapiens", "uniprot_id": "P62993" }, { "function": "Binds to the Fc region of immunoglobulins gamma. Low affinity receptor. By binding to IgG it initiates cellular responses against pathogens and soluble antigens. Promotes phagocytosis of opsonized antigens", "gene_name": "FCGR2A", "glycan_count": 39, "glycosylation_sites": [ { "position": 97, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 178, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P12318", "name": "FCGR2A (Fc gamma receptor IIa)", "organism": "Homo sapiens", "uniprot_id": "P12318" }, { "function": "Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. Plays a role in cell directional movement, orientation, cell sheet organization and Golgi complex polarization at the cell migration front (By similarity). Protects SCRIB from proteasomal degradation and facilitates its localization to intermediate filaments in a cell contact-mediated manner (By similarity)", "gene_name": "Vim", "glycan_count": 2, "glycosylation_sites": [ { "position": 7, "type": "O-linked (GlcNAc) serine; alternate" }, { "position": 33, "type": "O-linked (GlcNAc) threonine" }, { "position": 34, "type": "O-linked (GlcNAc) serine; alternate" } ], "id": "P20152", "name": "Vimentin", "organism": "Mus musculus", "uniprot_id": "P20152" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q16531, Q99958", "name": "Sarcoglycans (\u03b1, \u03b3)", "organism": "", "uniprot_id": "" }, { "function": "High molecular weight cytoskeletal protein concentrated at regions of cell-matrix and cell-cell contacts. Involved in connections of major cytoskeletal structures to the plasma membrane. With KANK1 co-organize the assembly of cortical microtubule stabilizing complexes (CMSCs) positioned to control microtubule-actin crosstalk at focal adhesions (FAs) rims", "gene_name": "TLN1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y490", "name": "Talin", "organism": "Homo sapiens", "uniprot_id": "Q9Y490" }, { "function": "Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion", "gene_name": "VCL", "glycan_count": 3, "glycosylation_sites": [], "id": "P18206", "name": "Vinculin", "organism": "Homo sapiens", "uniprot_id": "P18206" }, { "function": "Degrades chitin and chitotriose. May participate in the defense against nematodes, fungi and other pathogens. Plays a role in T-helper cell type 2 (Th2) immune response. Contributes to the response to IL-13 and inflammation in response to IL-13. Stimulates chemokine production by pulmonary epithelial cells. Protects lung epithelial cells against apoptosis and promotes phosphorylation of AKT1. Its function in the inflammatory response and in protecting cells against apoptosis is inhibited by allosamidin, suggesting that the function of this protein depends on carbohydrate binding", "gene_name": "CHIA", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9BZP6", "name": "YKL-39 (CHI3L2)", "organism": "Homo sapiens", "uniprot_id": "Q9BZP6" }, { "function": "Probably plays a major role in determining the retinal structure as well as in the closure of the neural tube", "gene_name": "COL18A1", "glycan_count": 21, "glycosylation_sites": [ { "position": 68, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 129, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 164, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 889, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 926, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1567, "type": "O-linked (GalNAc...) threonine" } ], "id": "P39060", "name": "Collagen Type XVIII Alpha 1 Chain (COL18A1)", "organism": "Homo sapiens", "uniprot_id": "P39060" }, { "function": "Involved in elastic and collagen fibers formation. It is required for EFEMP2 deposition into the extracellular matrix, and collagen network assembly and cross-linking via protein-lysine 6-oxidase/LOX activity (PubMed:36351433). May be responsible for anchoring smooth muscle cells to elastic fibers, and may be involved in the processes that regulate vessel assembly. Has cell adhesive capacity", "gene_name": "EMILIN1", "glycan_count": 60, "glycosylation_sites": [ { "position": 154, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 415, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 455, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 561, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 658, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 766, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 794, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y6C2", "name": "Emilin-1", "organism": "Homo sapiens", "uniprot_id": "Q9Y6C2" }, { "function": "Cell adhesion glycoprotein which is widely distributed in basement membranes. Binds to collagens I and IV, to perlecan and to laminin 1. Does not bind fibulins. It probably has a role in cell-extracellular matrix interactions", "gene_name": "NID2", "glycan_count": 114, "glycosylation_sites": [ { "position": 358, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 359, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 417, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 452, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 658, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 693, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 703, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1124, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q14112", "name": "Nidogen-2", "organism": "Homo sapiens", "uniprot_id": "Q14112" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q59XU7", "name": "Als3p", "organism": "", "uniprot_id": "Q59XU7" }, { "function": "", "gene_name": "ENO1", "glycan_count": 0, "glycosylation_sites": [], "id": "P00924", "name": "Enolase", "organism": "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "uniprot_id": "P00924" }, { "function": "Bifunctional enzyme catalyzing the last two steps of de novo pyrimidine biosynthesis, orotate phosphoribosyltransferase (OPRT), which converts orotate to orotidine-5'-monophosphate (OMP), and orotidine-5'-monophosphate decarboxylase (ODC), the terminal enzymatic reaction that decarboxylates OMP to uridine monophosphate (UMP)", "gene_name": "UMPS", "glycan_count": 1, "glycosylation_sites": [], "id": "P11172", "name": "HSP60", "organism": "Homo sapiens", "uniprot_id": "P11172" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02735", "name": "Serum Amyloid A (SAA)", "organism": "", "uniprot_id": "P02735" }, { "function": "Catalyzes the interconversion between carbon dioxide and water and the dissociated ions of carbonic acid (i.e. bicarbonate and hydrogen ions)", "gene_name": "CA9", "glycan_count": 5, "glycosylation_sites": [ { "position": 115, "type": "O-linked (GlcNAc...) threonine" }, { "position": 346, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q16790", "name": "Carbonic anhydrase IX (CA IX)", "organism": "Homo sapiens", "uniprot_id": "Q16790" }, { "function": "", "gene_name": "amy1", "glycan_count": 0, "glycosylation_sites": [ { "position": 218, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P0C1B3", "name": "Pneumolysin", "organism": "Aspergillus oryzae (strain ATCC 42149 / RIB 40)", "uniprot_id": "P0C1B3" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8NY49", "name": "PspC", "organism": "", "uniprot_id": "Q8NY49" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9S1T2", "name": "PsaA", "organism": "Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)", "uniprot_id": "Q9S1T2" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8NY50", "name": "BgaA (\u03b2-galactosidase)", "organism": "", "uniprot_id": "Q8NY50" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8NY51", "name": "NanA (neuraminidase)", "organism": "", "uniprot_id": "Q8NY51" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8NY52", "name": "StrH (N-acetylglucosaminidase)", "organism": "", "uniprot_id": "Q8NY52" }, { "function": "E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2)", "gene_name": "sucB", "glycan_count": 0, "glycosylation_sites": [], "id": "Q50993", "name": "PilQ", "organism": "Neisseria gonorrhoeae", "uniprot_id": "Q50993" }, { "function": "", "gene_name": "lpd", "glycan_count": 0, "glycosylation_sites": [], "id": "Q50994", "name": "PilC", "organism": "Neisseria gonorrhoeae", "uniprot_id": "Q50994" }, { "function": "Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs", "gene_name": "rplP", "glycan_count": 0, "glycosylation_sites": [], "id": "Q5F5T4", "name": "VacJ (MlaA)", "organism": "Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)", "uniprot_id": "Q5F5T4" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q5F7C7", "name": "MetQ", "organism": "Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)", "uniprot_id": "Q5F7C7" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q50995", "name": "PilE", "organism": "Neisseria gonorrhoeae", "uniprot_id": "Q50995" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q5F6C2", "name": "NGO1225 (MIP)", "organism": "", "uniprot_id": "Q5F6C2" }, { "function": "Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP", "gene_name": "plsY", "glycan_count": 0, "glycosylation_sites": [], "id": "Q5F8C7", "name": "OmpU (NGO1688)", "organism": "Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)", "uniprot_id": "Q5F8C7" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q50996", "name": "FetA", "organism": "Neisseria gonorrhoeae", "uniprot_id": "Q50996" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q50997", "name": "BamA", "organism": "Neisseria gonorrhoeae", "uniprot_id": "Q50997" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q50998", "name": "PorB", "organism": "Neisseria gonorrhoeae", "uniprot_id": "Q50998" }, { "function": "Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins; catalytic subunit of the dolichol-phosphate mannose (DPM) synthase complex", "gene_name": "DPM1", "glycan_count": 1, "glycosylation_sites": [], "id": "O60762", "name": "DPM1", "organism": "Homo sapiens", "uniprot_id": "O60762" }, { "function": "General vesicular transport factor required for intercisternal transport in the Golgi stack; it is required for transcytotic fusion and/or subsequent binding of the vesicles to the target membrane. May well act as a vesicular anchor by interacting with the target membrane and holding the vesicular and target membranes in proximity", "gene_name": "USO1", "glycan_count": 1, "glycosylation_sites": [], "id": "O60763", "name": "DPAGT1", "organism": "Homo sapiens", "uniprot_id": "O60763" }, { "function": "Lysosomal ceramidase that hydrolyzes sphingolipid ceramides into sphingosine and free fatty acids at acidic pH (PubMed:10610716, PubMed:11451951, PubMed:15655246, PubMed:26898341, PubMed:36752535, PubMed:7744740, PubMed:7852294). Ceramides, sphingosine, and its phosphorylated form sphingosine-1-phosphate are bioactive lipids that mediate cellular signaling pathways regulating several biological processes including cell proliferation, apoptosis and differentiation (PubMed:10610716). Has a higher catalytic efficiency towards C12-ceramides versus other ceramides (PubMed:15655246, PubMed:7744740). Also catalyzes the reverse reaction allowing the synthesis of ceramides from fatty acids and sphingosine (PubMed:12764132, PubMed:12815059). For the reverse synthetic reaction, the natural sphingosine D-erythro isomer is more efficiently utilized as a substrate compared to D-erythro-dihydrosphingosine and D-erythro-phytosphingosine, while the fatty acids with chain lengths of 12 or 14 carbons are the most efficiently used (PubMed:12764132). Also has an N-acylethanolamine hydrolase activity (PubMed:15655246). By regulating the levels of ceramides, sphingosine and sphingosine-1-phosphate in the epidermis, mediates the calcium-induced differentiation of epidermal keratinocytes (PubMed:17713573). Also indirectly regulates tumor necrosis factor/TNF-induced apoptosis (By similarity). By regulating the intracellular balance between ceramides and sphingosine, in adrenocortical cells, probably also acts as a regulator of steroidogenesis (PubMed:22261821)", "gene_name": "ASAH1", "glycan_count": 121, "glycosylation_sites": [ { "position": 173, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 195, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 259, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 286, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 342, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 348, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13510", "name": "ASAH1", "organism": "Homo sapiens", "uniprot_id": "Q13510" }, { "function": "Accessory subunit of the proton-transporting vacuolar (V)-ATPase protein pump, which is required for luminal acidification of secretory vesicles (PubMed:33065002). Guides the V-type ATPase into specialized subcellular compartments, such as neuroendocrine regulated secretory vesicles or the ruffled border of the osteoclast, thereby regulating its activity (PubMed:27231034). Involved in membrane trafficking and Ca(2+)-dependent membrane fusion (PubMed:27231034). May play a role in the assembly of the V-type ATPase complex (Probable). In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (PubMed:28296633). In islets of Langerhans cells, may regulate the acidification of dense-core secretory granules (By similarity)", "gene_name": "ATP6AP1", "glycan_count": 53, "glycosylation_sites": [ { "position": 170, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 261, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 273, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 296, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 303, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 350, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 357, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q15904", "name": "ATP6AP1", "organism": "Homo sapiens", "uniprot_id": "Q15904" }, { "function": "Hydrolyzes the non-reducing end N-acetyl-D-hexosamine and/or sulfated N-acetyl-D-hexosamine of glycoconjugates, such as the oligosaccharide moieties from proteins and neutral glycolipids, or from certain mucopolysaccharides (PubMed:11707436, PubMed:8123671, PubMed:8672428, PubMed:9694901). The isozyme S is as active as the isozyme A on the anionic bis-sulfated glycans, the chondroitin-6-sulfate trisaccharide (C6S-3), and the dermatan sulfate pentasaccharide, and the sulfated glycosphingolipid SM2 (PubMed:11707436). The isozyme B does not hydrolyze each of these substrates, however hydrolyzes efficiently neutral oligosaccharide (PubMed:11707436). Only the isozyme A is responsible for the degradation of GM2 gangliosides in the presence of GM2A (PubMed:8123671, PubMed:8672428, PubMed:9694901)", "gene_name": "HEXA", "glycan_count": 26, "glycosylation_sites": [ { "position": 115, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 157, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 295, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P06865", "name": "HEXA", "organism": "Homo sapiens", "uniprot_id": "P06865" }, { "function": "G-protein coupled receptor for 5-hydroxytryptamine (serotonin), a biogenic hormone that functions as a neurotransmitter, a hormone and a mitogen (PubMed:35714614, PubMed:36989299, PubMed:37327704, PubMed:8522988). Also has a high affinity for tricyclic psychotropic drugs (By similarity). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors (PubMed:35714614). HTR6 is coupled to G(s) G alpha proteins and mediates activation of adenylate cyclase activity (PubMed:35714614, PubMed:37327704). Controls pyramidal neurons migration during corticogenesis, through the regulation of CDK5 activity (By similarity). Is an activator of mTOR signaling (PubMed:23027611)", "gene_name": "HTR6", "glycan_count": 0, "glycosylation_sites": [], "id": "Q13640", "name": "VLDLR", "organism": "Homo sapiens", "uniprot_id": "P50406" }, { "function": "Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (DXXLL) motif (PubMed:11301005, PubMed:15886016). Mediates export of the GPCR receptor ADRA2B to the cell surface (PubMed:27901063). Required for targeting PKD1:PKD2 complex from the trans-Golgi network to the cilium membrane (By similarity). Regulates retrograde transport of proteins such as phosphorylated form of BACE1 from endosomes to the trans-Golgi network (PubMed:15615712, PubMed:15886016)", "gene_name": "GGA1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UJY5", "name": "Desmoglein-3", "organism": "Homo sapiens", "uniprot_id": "Q9UJY5" }, { "function": "Minor apolipoprotein that associates with LDL. Inhibits cholesteryl ester transfer protein (CETP) activity and appears to be an important regulator of cholesterol transport. Also associates to a lesser degree with VLDL, Apo-AI and Apo-AII", "gene_name": "APOF", "glycan_count": 33, "glycosylation_sites": [ { "position": 118, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 274, "type": "O-linked (GalNAc...) threonine" } ], "id": "Q13790", "name": "Apolipoprotein F (APOF)", "organism": "Homo sapiens", "uniprot_id": "Q13790" }, { "function": "Regulator of the tubulin polyglutamylase complex (TPGC) that controls cytoskeletal organization, nuclear shape, and cilium disassembly by balancing microtubule and actin assembly (PubMed:34782749). Regulates the assembly and stability of the TPGC and thereby modulates polyglutamylation of the microtubule, which antagonizes MAP4 binding (PubMed:34782749)", "gene_name": "CSTPP1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H6J7", "name": "Mina53", "organism": "Homo sapiens", "uniprot_id": "Q9H6J7" }, { "function": "Functions in inorganic phosphate uptake, although probably not the main uptake protein under phosphate starvation (PubMed:15731097, PubMed:20933472). Binds phosphate; probably able to bind both H(2)PO(4)(-) and HPO(4)(2-) (PubMed:12842040, PubMed:8294447). Part of the ABC transporter complex PstSACB involved in phosphate import (Probable)", "gene_name": "pstS1", "glycan_count": 0, "glycosylation_sites": [], "id": "P9WGU1", "name": "MPT64", "organism": "Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)", "uniprot_id": "P9WGU1" }, { "function": "FABPs are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. FABP2 is probably involved in triglyceride-rich lipoprotein synthesis. Binds saturated long-chain fatty acids with a high affinity, but binds with a lower affinity to unsaturated long-chain fatty acids. FABP2 may also help maintain energy homeostasis by functioning as a lipid sensor", "gene_name": "FABP2", "glycan_count": 0, "glycosylation_sites": [], "id": "P12104", "name": "Intestinal fatty acid binding protein (IFABP)", "organism": "Homo sapiens", "uniprot_id": "P12104" }, { "function": "Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). Gag-Pol polyprotein may regulate its own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, the polyprotein would promote translation, whereas at high concentration, the polyprotein would encapsidate genomic RNA and then shut off translation", "gene_name": "gag-pol", "glycan_count": 0, "glycosylation_sites": [], "id": "P12497", "name": "HIV p24 Antigen", "organism": "Human immunodeficiency virus type 1 group M subtype B (isolate NY5)", "uniprot_id": "P12497" }, { "function": "Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). Gag-Pol polyprotein may regulate its own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, the polyprotein would promote translation, whereas at high concentration, the polyprotein would encapsidate genomic RNA and then shut off translation", "gene_name": "gag-pol", "glycan_count": 0, "glycosylation_sites": [], "id": "P04585", "name": "HIV Reverse Transcriptase", "organism": "Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)", "uniprot_id": "P04585" }, { "function": "Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi). Gag-Pol polyprotein may regulate its own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, the polyprotein would promote translation, whereas at high concentration, the polyprotein would encapsidate genomic RNA and then shut off translation", "gene_name": "gag-pol", "glycan_count": 0, "glycosylation_sites": [], "id": "P03366", "name": "HIV Protease", "organism": "Human immunodeficiency virus type 1 group M subtype B (isolate BH10)", "uniprot_id": "P03366" }, { "function": "The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. Required for JNK activation in response to excitotoxic stress. Cytoplasmic MAPK8IP1 causes inhibition of JNK-regulated activity by retaining JNK in the cytoplasm and inhibiting JNK phosphorylation of c-Jun. May also participate in ApoER2-specific reelin signaling. Directly, or indirectly, regulates GLUT2 gene expression and beta-cell function. Appears to have a role in cell signaling in mature and developing nerve terminals. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins. Functions as an anti-apoptotic protein and whose level seems to influence the beta-cell death or survival response. Acts as a scaffold protein that coordinates with SH3RF1 in organizing different components of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a functional multiprotein complex to ensure the effective activation of the JNK signaling pathway. Regulates the activation of MAPK8/JNK1 and differentiation of CD8(+) T-cells", "gene_name": "MAPK8IP1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UQF2", "name": "HIV Integrase", "organism": "Homo sapiens", "uniprot_id": "Q9UQF2" }, { "function": "Reversibly inhibits the activity of ATP2A2/SERCA2 in cardiac sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+) (PubMed:28890335). Binds preferentially to the ATP-bound E1 conformational form of ATP2A2 which predominates at low Ca(2+) concentrations during the diastolic phase of the cardiac cycle (By similarity). Inhibits ATP2A2 Ca(2+) affinity by disrupting its allosteric activation by ATP (By similarity). Modulates the contractility of the heart muscle in response to physiological stimuli via its effects on ATP2A2. Modulates calcium re-uptake during muscle relaxation and plays an important role in calcium homeostasis in the heart muscle. The degree of ATP2A2 inhibition depends on the oligomeric state of PLN. ATP2A2 inhibition is alleviated by PLN phosphorylation (By similarity). Also inhibits the activity of ATP2A3/SERCA3 (By similarity). Controls intracellular Ca(2+) levels in elongated spermatids and may play a role in germ cell differentiation (By similarity). In the thalamic reticular nucleus of the brain, plays a role in the regulation of sleep patterns and executive functioning (By similarity)", "gene_name": "PLN", "glycan_count": 0, "glycosylation_sites": [], "id": "P26678", "name": "Phospholamban (PLN)", "organism": "Homo sapiens", "uniprot_id": "P26678" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "various (PPP1CA: P62136)", "name": "Protein phosphatase 1 (PP1)", "organism": "", "uniprot_id": "" }, { "function": "Plays an important role in the regulation of glutamine catabolism. Promotes mitochondrial respiration and increases ATP generation in cells by catalyzing the synthesis of glutamate and alpha-ketoglutarate. Increases cellular anti-oxidant function via NADH and glutathione production. May play a role in preventing tumor proliferation", "gene_name": "GLS2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UI32", "name": "PP1 inhibitor 1 (I-1)", "organism": "Homo sapiens", "uniprot_id": "Q9UI32" }, { "function": "Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle (PubMed:28895244). Calcium ions are bound by clusters of acidic residues at the protein surface, often at the interface between subunits. Can bind around 80 Ca(2+) ions (PubMed:28895244). Regulates the release of lumenal Ca(2+) via the calcium release channel RYR1; this plays an important role in triggering muscle contraction. Negatively regulates store-operated Ca(2+) entry (SOCE) activity (PubMed:27185316)", "gene_name": "CASQ1", "glycan_count": 0, "glycosylation_sites": [ { "position": 350, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P31415", "name": "Calsequestrin", "organism": "Homo sapiens", "uniprot_id": "P31415" }, { "function": "", "gene_name": "SMCO4", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NRQ5", "name": "Thrombospondin-4", "organism": "Homo sapiens", "uniprot_id": "Q9NRQ5" }, { "function": "Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. LI-cadherin may have a role in the morphological organization of liver and intestine. Involved in intestinal peptide transport", "gene_name": "CDH17", "glycan_count": 6, "glycosylation_sites": [ { "position": 149, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 184, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 250, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 419, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 456, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 546, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 587, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 722, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q12864", "name": "Cadherin-17", "organism": "Homo sapiens", "uniprot_id": "Q12864" }, { "function": "Binds tightly to hydroxyapatite (PubMed:11459848). Appears to form an integral part of the mineralized matrix (PubMed:1818768). Probably important to cell-matrix interaction (PubMed:1818768). Promotes adhesion and migration of various cells via the alpha-V/beta-3 integrin receptor (ITGAV:ITGB3) (PubMed:10640428, PubMed:11459848, PubMed:24103036)", "gene_name": "IBSP", "glycan_count": 0, "glycosylation_sites": [ { "position": 104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 119, "type": "O-linked (GalNAc...) threonine" }, { "position": 122, "type": "O-linked (GalNAc...) threonine" }, { "position": 177, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 182, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 190, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 227, "type": "O-linked (GalNAc...) threonine" }, { "position": 228, "type": "O-linked (GalNAc...) threonine" }, { "position": 229, "type": "O-linked (GalNAc...) threonine" }, { "position": 238, "type": "O-linked (GalNAc...) threonine" }, { "position": 239, "type": "O-linked (GalNAc...) threonine" } ], "id": "P21815", "name": "Bone sialoprotein 2 (IBSP)", "organism": "Homo sapiens", "uniprot_id": "P21815" }, { "function": "May bind integrin alpha-8/beta-1 and play a role in hair follicle morphogenesis. Promotes matrix assembly (By similarity)", "gene_name": "EGFL6", "glycan_count": 1, "glycosylation_sites": [ { "position": 397, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8IUX8", "name": "Coiled-coil domain-containing protein 80 (CCDC80)", "organism": "Homo sapiens", "uniprot_id": "Q8IUX8" }, { "function": "Cytokine that binds to and signals through the IL1RL2/IL-36R receptor which in turn activates NF-kappa-B and MAPK signaling pathways in target cells linked to a pro-inflammatory response. Part of the IL-36 signaling system that is thought to be present in epithelial barriers and to take part in local inflammatory response; similar to the IL-1 system with which it shares the coreceptor IL1RAP. Seems to be involved in skin inflammatory response by acting on keratinocytes, dendritic cells and indirectly on T-cells to drive tissue infiltration, cell maturation and cell proliferation. In cultured keratinocytes induces the expression of macrophage, T-cell, and neutrophil chemokines, such as CCL3, CCL4, CCL5, CCL2, CCL17, CCL22, CL20, CCL5, CCL2, CCL17, CCL22, CXCL8, CCL20 and CXCL1, and the production of pro-inflammatory cytokines such as TNF-alpha, IL-8 and IL-6. In cultured monocytes up-regulates expression of IL-1A, IL-1B and IL-6. In myeloid dendritic cells involved in cell maturation by up-regulating surface expression of CD83, CD86 and HLA-DR. In monocyte-derived dendritic cells facilitates dendritic cell maturation and drives T-cell proliferation. May play a role in pro-inflammatory effects in the lung", "gene_name": "IL36A", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UHA7", "name": "Interleukin-36 alpha (IL36A)", "organism": "Homo sapiens", "uniprot_id": "Q9UHA7" }, { "function": "", "gene_name": "ART3", "glycan_count": 9, "glycosylation_sites": [ { "position": 248, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 346, "type": "O-linked (GalNAc...) threonine" } ], "id": "Q13508", "name": "Ecto-ADP-ribosyltransferase 3 (ART3)", "organism": "Homo sapiens", "uniprot_id": "Q13508" }, { "function": "Plays a role in the process of neurogenesis. Required throughout embryonic neurogenesis to maintain neural progenitor cells, also called radial glial cells (RGCs), by allowing their daughter cells to choose progenitor over neuronal cell fate. Not required for the proliferation of neural progenitor cells before the onset of embryonic neurogenesis. Also required postnatally in the subventricular zone (SVZ) neurogenesis by regulating SVZ neuroblasts survival and ependymal wall integrity. Negative regulator of NF-kappa-B signaling pathway. The inhibition of NF-kappa-B activation is mediated at least in part, by preventing MAP3K7IP2 to interact with polyubiquitin chains of TRAF6 and RIPK1 and by stimulating the 'Lys-48'-linked polyubiquitination and degradation of TRAF6 in cortical neurons", "gene_name": "NUMBL", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y6R0", "name": "NUMB", "organism": "Homo sapiens", "uniprot_id": "Q9Y6R0" }, { "function": "Regulates clathrin-mediated endocytosis by phosphorylating the AP2M1/mu2 subunit of the adaptor protein complex 2 (AP-2) which ensures high affinity binding of AP-2 to cargo membrane proteins during the initial stages of endocytosis (PubMed:11877457, PubMed:11877461, PubMed:12952931, PubMed:14617351, PubMed:17494869, PubMed:25653444). Isoform 1 and isoform 2 display similar levels of kinase activity towards AP2M1 (PubMed:17494869). Preferentially, may phosphorylate substrates on threonine residues (PubMed:11877457, PubMed:18657069). Regulates phosphorylation of other AP-2 subunits as well as AP-2 localization and AP-2-mediated internalization of ligand complexes (PubMed:12952931). Phosphorylates NUMB and regulates its cellular localization, promoting NUMB localization to endosomes (PubMed:18657069). Binds to and stabilizes the activated form of NOTCH1, increases its localization in endosomes and regulates its transcriptional activity (PubMed:21464124)", "gene_name": "AAK1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q2M2I8", "name": "AAK1", "organism": "Homo sapiens", "uniprot_id": "Q2M2I8" }, { "function": "Behaves as a myelinotrophic and neurotrophic factor, these effects are mediated by its G-protein-coupled receptors, GPR37 and GPR37L1, undergoing ligand-mediated internalization followed by ERK phosphorylation signaling", "gene_name": "Psap", "glycan_count": 25, "glycosylation_sites": [ { "position": 80, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 214, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 334, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 459, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q61207", "name": "Myelin oligodendrocyte glycoprotein", "organism": "Mus musculus", "uniprot_id": "Q61207" }, { "function": "Neurofilaments usually contain three intermediate filament proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of neuronal caliber. May additionally cooperate with the neuronal intermediate filament proteins PRPH and INA to form neuronal filamentous networks (PubMed:22723690)", "gene_name": "Nefl", "glycan_count": 1, "glycosylation_sites": [ { "position": 21, "type": "O-linked (GlcNAc) threonine" }, { "position": 27, "type": "O-linked (GlcNAc) serine" } ], "id": "P08551", "name": "Neurofilament light chain", "organism": "Mus musculus", "uniprot_id": "P08551" }, { "function": "RNA-binding protein that is involved in various steps of RNA biogenesis and processing. Preferentially binds, via its two RNA recognition motifs RRM1 and RRM2, to GU-repeats on RNA molecules predominantly localized within long introns and in the 3'UTR of mRNAs. In turn, regulates the splicing of many non-coding and protein-coding RNAs including proteins involved in neuronal survival, as well as mRNAs that encode proteins relevant for neurodegenerative diseases. Plays a role in maintaining mitochondrial homeostasis by regulating the processing of mitochondrial transcripts. Also regulates mRNA stability by recruiting CNOT7/CAF1 deadenylase on mRNA 3'UTR leading to poly(A) tail deadenylation and thus shortening. In response to oxidative insult, associates with stalled ribosomes localized to stress granules (SGs) and contributes to cell survival (By similarity). Also participates in the normal skeletal muscle formation and regeneration, forming cytoplasmic myo-granules and binding mRNAs that encode sarcomeric proteins (PubMed:30464263). Plays a role in the maintenance of the circadian clock periodicity via stabilization of the CRY1 and CRY2 proteins in a FBXL3-dependent manner (PubMed:27123980). Negatively regulates the expression of CDK6 (By similarity). Regulates the expression of HDAC6, ATG7 and VCP in a PPIA/CYPA-dependent manner (PubMed:25678563)", "gene_name": "Tardbp", "glycan_count": 1, "glycosylation_sites": [], "id": "Q921F2", "name": "Transactive response DNA binding protein 43 (TDP43)", "organism": "Mus musculus", "uniprot_id": "Q921F2" }, { "function": "Binds to type II regulatory subunits of protein kinase A and anchors/targets them to the membrane. May anchor the kinase to cytoskeletal and/or organelle-associated proteins (By similarity)", "gene_name": "NBEA", "glycan_count": 5, "glycosylation_sites": [], "id": "Q8NFP9", "name": "B4GALNT2", "organism": "Homo sapiens", "uniprot_id": "Q8NFP9" }, { "function": "Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to both the subterminal N-acetyl glucosamine (GlcNAc) of type 1 chain (beta-D-Gal-(1->3)-beta-D-GlcNAc) glycolipids and oligosaccharides via an alpha(1,4) linkage, and the subterminal glucose (Glc) or GlcNAc of type 2 chain (beta-D-Gal-(1->4)-beta-D-GlcNAc) oligosaccharides via an alpha(1,3) linkage, independently of the presence of terminal alpha-L-fucosyl-(1,2) moieties on the terminal galactose of these acceptors (PubMed:11058871, PubMed:12668675, PubMed:1977660). Through its catalytic activity, participates in the synthesis of antigens of the Lewis blood group system, i.e. Lewis a (Le(a)), lewis b (Le(b)), Lewis x/SSEA-1 (Le(x)) and lewis y (Le(y)) antigens (PubMed:11058871, PubMed:12668675, PubMed:1977660). Also catalyzes the transfer of L-fucose to subterminal GlcNAc of sialyl- and disialyl-lactotetraosylceramide to produce sialyl Lewis a (sLe(a)) and disialyl Lewis a via an alpha(1,4) linkage and therefore may regulate cell surface sLe(a) expression and consequently regulates adhesive properties to E-selectin, cell proliferation and migration (PubMed:11058871, PubMed:12668675, PubMed:27453266). Catalyzes the transfer of an L-fucose to 3'-sialyl-N-acetyllactosamine by an alpha(1,3) linkage, which allows the formation of sialyl-Lewis x structure and therefore may regulate the sialyl-Lewis x surface antigen expression and consequently adhesive properties to E-selectin (PubMed:11058871, PubMed:29593094). Prefers type 1 chain over type 2 acceptors (PubMed:7721776). Type 1 tetrasaccharide is a better acceptor than type 1 disaccharide suggesting that a beta anomeric configuration of GlcNAc in the substrate is preferred (PubMed:7721776). Lewis-positive (Le(+)) individuals have an active enzyme while Lewis-negative (Le(-)) individuals have an inactive enzyme (PubMed:1977660)", "gene_name": "FUT3", "glycan_count": 0, "glycosylation_sites": [ { "position": 154, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 185, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P21217", "name": "FUT3", "organism": "Homo sapiens", "uniprot_id": "P21217" }, { "function": "The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. Required for proper BBSome complex assembly and its ciliary localization", "gene_name": "BBS9", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y6A0", "name": "ST6GALNAC1", "organism": "Homo sapiens", "uniprot_id": "Q3SYG4" }, { "function": "Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFB and PGF, and plays an essential role in the development of embryonic vasculature, the regulation of angiogenesis, cell survival, cell migration, macrophage function, chemotaxis, and cancer cell invasion. Acts as a positive regulator of postnatal retinal hyaloid vessel regression (By similarity). May play an essential role as a negative regulator of embryonic angiogenesis by inhibiting excessive proliferation of endothelial cells. Can promote endothelial cell proliferation, survival and angiogenesis in adulthood. Its function in promoting cell proliferation seems to be cell-type specific. Promotes PGF-mediated proliferation of endothelial cells, proliferation of some types of cancer cells, but does not promote proliferation of normal fibroblasts (in vitro). Has very high affinity for VEGFA and relatively low protein kinase activity; may function as a negative regulator of VEGFA signaling by limiting the amount of free VEGFA and preventing its binding to KDR. Modulates KDR signaling by forming heterodimers with KDR. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leading to activation of phosphatidylinositol kinase and the downstream signaling pathway. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Phosphorylates SRC and YES1, and may also phosphorylate CBL. Promotes phosphorylation of AKT1 at 'Ser-473'. Promotes phosphorylation of PTK2/FAK1 (PubMed:16685275)", "gene_name": "FLT1", "glycan_count": 64, "glycosylation_sites": [ { "position": 100, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 164, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 196, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 251, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 323, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 402, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 417, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 474, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 547, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 597, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 620, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 625, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 666, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P17948", "name": "FLT1", "organism": "Homo sapiens", "uniprot_id": "P17948" }, { "function": "Multifunctional protein with controversial molecular function which plays an important role in cell protection against oxidative stress and cell death acting as oxidative stress sensor and redox-sensitive chaperone and protease (PubMed:12796482, PubMed:17015834, PubMed:18711745, PubMed:19229105, PubMed:20304780, PubMed:25416785, PubMed:26995087, PubMed:28993701). It is involved in neuroprotective mechanisms like the stabilization of NFE2L2 and PINK1 proteins, male fertility as a positive regulator of androgen signaling pathway as well as cell growth and transformation through, for instance, the modulation of NF-kappa-B signaling pathway (PubMed:12612053, PubMed:14749723, PubMed:15502874, PubMed:17015834, PubMed:18711745, PubMed:21097510). Has been described as a protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals (PubMed:25416785, PubMed:28596309). But this function is rebuted by other works (PubMed:27903648, PubMed:31653696). As a protein deglycase, repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) that cause irreversible damage (PubMed:25416785, PubMed:26995087, PubMed:28013050). Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair (PubMed:28596309). Protects histones from adduction by methylglyoxal, controls the levels of methylglyoxal-derived argininine modifications on chromatin (PubMed:30150385). Able to remove the glycations and restore histone 3, histone glycation disrupts both local and global chromatin architecture by altering histone-DNA interactions as well as histone acetylation and ubiquitination levels (PubMed:30150385, PubMed:30894531). Displays a very low glyoxalase activity that may reflect its deglycase activity (PubMed:22523093, PubMed:28993701, PubMed:31653696). Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death (PubMed:16390825). Required for correct mitochondrial morphology and function as well as for autophagy of dysfunctional mitochondria (PubMed:16632486, PubMed:19229105). Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking (PubMed:18711745). Regulates astrocyte inflammatory responses, may modulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells (PubMed:23847046). In pancreatic islets, involved in the maintenance of mitochondrial reactive oxygen species (ROS) levels and glucose homeostasis in an age- and diet dependent manner. Protects pancreatic beta cells from cell death induced by inflammatory and cytotoxic setting (By similarity). Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress (PubMed:18626009). Metal-binding protein able to bind copper as well as toxic mercury ions, enhances the cell protection mechanism against induced metal toxicity (PubMed:23792957). In macrophages, interacts with the NADPH oxidase subunit NCF1 to direct NADPH oxidase-dependent ROS production, and protects against sepsis (By similarity)", "gene_name": "PARK7", "glycan_count": 1, "glycosylation_sites": [], "id": "Q99497", "name": "PARK7", "organism": "Homo sapiens", "uniprot_id": "Q99497" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03437 (A/Michigan/45/2015)", "name": "Influenza Hemagglutinin (HA)", "organism": "", "uniprot_id": "" }, { "function": "Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate", "gene_name": "pheA", "glycan_count": 0, "glycosylation_sites": [], "id": "P0A9J8", "name": "Lumazine Synthase", "organism": "Escherichia coli (strain K12)", "uniprot_id": "P0A9J8" }, { "function": "Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively", "gene_name": "ilvD", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8DRT7", "name": "Sortase A (SrtA)", "organism": "Streptococcus mutans serotype c (strain ATCC 700610 / UA159)", "uniprot_id": "Q8DRT7" }, { "function": "Catalyzes the isomerization of L-xylulose-5-phosphate to L-ribulose-5-phosphate. Is involved in the anaerobic L-ascorbate utilization", "gene_name": "ulaE", "glycan_count": 0, "glycosylation_sites": [], "id": "P0C1B2", "name": "Pneumolysin (PLY)", "organism": "Shigella dysenteriae serotype 1 (strain Sd197)", "uniprot_id": "P0C1B2" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8NAU1 (precursor FNDC5)", "name": "Irisin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P19429 (cTnI)", "name": "Cardiac troponin (cTn)", "organism": "", "uniprot_id": "" }, { "function": "This is a non-secretory ribonuclease. It is a pyrimidine specific nuclease with a slight preference for U. Cytotoxin and helminthotoxin. Selectively chemotactic for dendritic cells. Possesses a wide variety of biological activities", "gene_name": "RNASE2", "glycan_count": 11, "glycosylation_sites": [ { "position": 34, "type": "C-linked (Man) tryptophan" }, { "position": 44, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 86, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 92, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 111, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 119, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P10153", "name": "RNASE2", "organism": "Homo sapiens", "uniprot_id": "P10153" }, { "function": "Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes", "gene_name": "PDE4D", "glycan_count": 1, "glycosylation_sites": [], "id": "Q08499", "name": "PTGDS", "organism": "Homo sapiens", "uniprot_id": "Q08499" }, { "function": "Receptor for interleukin-8 which is a powerful neutrophil chemotactic factor (PubMed:1891716). Binding of IL-8 to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system (PubMed:8662698). Binds to IL-8 with high affinity. Also binds with high affinity to CXCL3, GRO/MGSA and NAP-2", "gene_name": "CXCR2", "glycan_count": 0, "glycosylation_sites": [ { "position": 22, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P25025", "name": "CXCL2", "organism": "Homo sapiens", "uniprot_id": "P25025" }, { "function": "Promotes apoptosis, possibly via a pathway that involves the activation of NF-kappa-B. Can also promote apoptosis mediated by BAX and by the release of cytochrome c from the mitochondria into the cytoplasm. Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP). Negatively regulates oligodendrocyte survival, maturation and myelination. Plays a role in signaling cascades triggered by stimulation of T-cell receptors, in the adaptive immune response and in the regulation of T-cell differentiation and proliferation. Negatively regulates T-cell responses and the release of cytokines such as IL4, IL5, IL10, IL13 and IFNG by Th2 cells. Negatively regulates the production of IgG, IgM and IgM in response to antigens. May inhibit the activation of JNK in response to T-cell stimulation. Also acts as a regulator of pyroptosis: recruits CASP8 in response to reactive oxygen species (ROS) and subsequent oxidation, leading to activation of GSDMC (PubMed:34012073)", "gene_name": "TNFRSF21", "glycan_count": 10, "glycosylation_sites": [ { "position": 82, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 141, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 252, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 257, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 278, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 289, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O75509", "name": "TNFRSF21", "organism": "Homo sapiens", "uniprot_id": "O75509" }, { "function": "High-affinity receptor for immunoglobulin epsilon/IgE. Mediates IgE effector functions in myeloid cells. Upon IgE binding and antigen/allergen cross-linking initiates signaling pathways that lead to myeloid cell activation and differentiation. On mast cells, basophils and eosinophils stimulates the secretion of vasoactive amines, lipid mediators and cytokines that contribute to inflammatory response, tissue remodeling and cytotoxicity against microbes. Triggers the immediate hypersensitivity response to allergens as a host defense mechanism against helminth parasites, pathogenic bacteria and venom toxicity. When dysregulated, it can elicit harmful life-threatening allergic and anaphylactic reactions", "gene_name": "FCER1A", "glycan_count": 3, "glycosylation_sites": [ { "position": 46, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 67, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 75, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 99, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 160, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 165, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 191, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P12319", "name": "FCER1A", "organism": "Homo sapiens", "uniprot_id": "P12319" }, { "function": "Non-signaling receptor for IL1A, IL1B and IL1RN. Reduces IL1B activities. Serves as a decoy receptor by competitive binding to IL1B and preventing its binding to IL1R1. Also modulates cellular response through non-signaling association with IL1RAP after binding to IL1B. IL1R2 (membrane and secreted forms) preferentially binds IL1B and poorly IL1A and IL1RN. The secreted IL1R2 recruits secreted IL1RAP with high affinity; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors", "gene_name": "IL1R2", "glycan_count": 10, "glycosylation_sites": [ { "position": 66, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 72, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 112, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 219, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 277, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P27930", "name": "IL1R2", "organism": "Homo sapiens", "uniprot_id": "P27930" }, { "function": "Involved in pre-mRNA splicing as component of the spliceosome (PubMed:11991638, PubMed:28076346, PubMed:28502770, PubMed:33220177). PPIases accelerate the folding of proteins. Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (PubMed:16595688). Catalyzes prolyl peptide bond isomerization in CDC40/PRP17 (PubMed:33220177). Plays an important role in embryonic brain development; this function is independent of its isomerase activity (PubMed:33220177)", "gene_name": "PPIL1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y3C6", "name": "GOSR2", "organism": "Homo sapiens", "uniprot_id": "Q9Y3C6" }, { "function": "Mediates endoplasmic reticulum to Golgi transport. Together with p115/USO1 and GM130/GOLGA2, involved in vesicle tethering and fusion at the cis-Golgi membrane to maintain the stacked and inter-connected structure of the Golgi apparatus", "gene_name": "STX5", "glycan_count": 1, "glycosylation_sites": [], "id": "Q13190", "name": "Syntaxin-5", "organism": "Homo sapiens", "uniprot_id": "Q13190" }, { "function": "Seems to be a constitutive component of clathrin-coated pits that is required for receptor-mediated endocytosis. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR seems to require association with DAB2", "gene_name": "EPS15L1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UBC2", "name": "Bet1", "organism": "Homo sapiens", "uniprot_id": "Q9UBC2" }, { "function": "This endogenous retroviral envelope protein has retained its original fusogenic properties and participates in trophoblast fusion and the formation of a syncytium during placenta morphogenesis. May induce fusion through binding of SLC1A4 and SLC1A5 (PubMed:10708449, PubMed:12050356, PubMed:23492904)", "gene_name": "ERVW-1", "glycan_count": 0, "glycosylation_sites": [ { "position": 169, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 208, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 214, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 234, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 242, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 281, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 409, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UQF0", "name": "Desmocollin-3", "organism": "Homo sapiens", "uniprot_id": "Q9UQF0" }, { "function": "A component of desmosome cell-cell junctions which are required for positive regulation of cellular adhesion (By similarity). Required for desmosome adhesion strength between the granular layers of the epidermis, as a result moderates epidermal proliferation and differentiation (By similarity). Is therefore required to maintain postnatal epidermal barrier function and normal hair follicle morphology into adulthood (By similarity)", "gene_name": "DSC1", "glycan_count": 1, "glycosylation_sites": [ { "position": 165, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 546, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q08554", "name": "Desmocollin-2", "organism": "Homo sapiens", "uniprot_id": "Q08554" }, { "function": "May act as an inhibitor of TGF-beta signaling", "gene_name": "VASN", "glycan_count": 56, "glycosylation_sites": [ { "position": 101, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 117, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 273, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 500, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 528, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6EMK4", "name": "Vasorin", "organism": "Homo sapiens", "uniprot_id": "Q6EMK4" }, { "function": "Pattern recognition receptor (PRR) that detects bacterial peptidoglycan fragments and other danger signals and thus participates in both innate and adaptive immune responses (PubMed:11058605, PubMed:12791997, PubMed:12796777, PubMed:15044951, PubMed:16172124, PubMed:19043560, PubMed:22672233, PubMed:27099311). Specifically recognizes and binds gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP), a dipeptide present in peptidoglycan of Gram-negative bacteria (PubMed:12791997, PubMed:12796777, PubMed:12871942, PubMed:16172124, PubMed:16211083). Preferentially binds iE-DAP in tripeptide-containing muropeptides (MurNAc-TriDAP or TriDAP) (PubMed:16211083). Ligand binding triggers oligomerization that facilitates the binding and subsequent activation of the proximal adapter receptor-interacting RIPK2 (PubMed:12791997, PubMed:12796777, PubMed:17054981). Following recruitment, RIPK2 undergoes 'Met-1'- (linear) and 'Lys-63'-linked polyubiquitination by E3 ubiquitin-protein ligases XIAP, BIRC2, BIRC3 and the LUBAC complex, becoming a scaffolding protein for downstream effectors, triggering activation of the NF-kappa-B and MAP kinases signaling (PubMed:10880512, PubMed:12791997, PubMed:19043560). This in turn leads to the transcriptional activation of hundreds of genes involved in immune response (PubMed:10880512, PubMed:19043560). Also acts as a regulator of antiviral response elicited by dsRNA and the expression of RLR pathway members by targeting IFIH1 and TRAF3 to modulate the formation of IFIH1-MAVS and TRAF3-MAVS complexes leading to increased transcription of type I IFNs (PubMed:32169843). Also acts as a regulator of autophagy via its interaction with ATG16L1, possibly by recruiting ATG16L1 at the site of bacterial entry (By similarity). Besides recognizing pathogens, also involved in the endoplasmic reticulum stress response: acts by sensing and binding to the cytosolic metabolite sphingosine-1-phosphate generated in response to endoplasmic reticulum stress, initiating an inflammation process that leads to activation of the NF-kappa-B and MAP kinases signaling (PubMed:27007849, PubMed:33942347). In addition, plays a role in insulin trafficking in beta cells in a cell-autonomous manner (By similarity). Mechanistically, upon recognizing cognate ligands, NOD1 and RIPK2 localize to insulin vesicles where they recruit RAB1A to direct insulin trafficking through the cytoplasm (By similarity)", "gene_name": "NOD1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y239", "name": "NOD1", "organism": "Homo sapiens", "uniprot_id": "Q9Y239" }, { "function": "Pattern recognition receptor (PRR) that detects bacterial peptidoglycan fragments and other danger signals and plays an important role in gastrointestinal immunity (PubMed:12514169, PubMed:12527755, PubMed:12626759, PubMed:15044951, PubMed:15998797, PubMed:27283905, PubMed:27748583, PubMed:31649195). Specifically activated by muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan found in every bacterial peptidoglycan type (PubMed:12514169, PubMed:12527755, PubMed:12626759, PubMed:12871942, PubMed:15044951, PubMed:15198989, PubMed:15998797, PubMed:22857257, PubMed:23322906, PubMed:27748583, PubMed:36002575). NOD2 specifically recognizes and binds 6-O-phospho-MDP, the phosphorylated form of MDP, which is generated by NAGK (PubMed:36002575). 6-O-phospho-MDP-binding triggers oligomerization that facilitates the binding and subsequent activation of the proximal adapter receptor-interacting RIPK2 (PubMed:11087742, PubMed:17355968, PubMed:21887730, PubMed:23806334, PubMed:28436939). Following recruitment, RIPK2 undergoes 'Met-1'- (linear) and 'Lys-63'-linked polyubiquitination by E3 ubiquitin-protein ligases XIAP, BIRC2, BIRC3 and the LUBAC complex, becoming a scaffolding protein for downstream effectors, triggering activation of the NF-kappa-B and MAP kinases signaling (PubMed:11087742, PubMed:12514169, PubMed:12626759, PubMed:15198989, PubMed:21887730, PubMed:23322906, PubMed:23806334, PubMed:28436939). This in turn leads to the transcriptional activation of hundreds of genes involved in immune response (PubMed:15198989). Its ability to detect bacterial MDP plays a central role in maintaining the equilibrium between intestinal microbiota and host immune responses to control inflammation (By similarity). An imbalance in this relationship results in dysbiosis, whereby pathogenic bacteria prevail on commensals, causing damage in the intestinal epithelial barrier as well as allowing bacterial invasion and inflammation (By similarity). Acts as a regulator of appetite by sensing MDP in a subset of brain neurons: microbiota-derived MDP reach the brain, where they bind and activate NOD2 in inhibitory hypothalamic neurons, decreasing neuronal activity, thereby regulating satiety and body temperature (By similarity). NOD2-dependent MDP-sensing of bacterial cell walls in the intestinal epithelial compartment contributes to sustained postnatal growth upon undernutrition (By similarity). Also plays a role in antiviral response by acting as a sensor of single-stranded RNA (ssRNA) from viruses: upon ssRNA-binding, interacts with MAVS, leading to activation of interferon regulatory factor-3/IRF3 and expression of type I interferon (PubMed:19701189). Also acts as a regulator of autophagy in dendritic cells via its interaction with ATG16L1, possibly by recruiting ATG16L1 at the site of bacterial entry (PubMed:20637199). NOD2 activation in the small intestine crypt also contributes to intestinal stem cells survival and function: acts by promoting mitophagy via its association with ATG16L1 (By similarity). In addition to its main role in innate immunity, also regulates the adaptive immune system by acting as regulator of helper T-cell and regulatory T-cells (Tregs) (By similarity). Besides recognizing pathogens, also involved in the endoplasmic reticulum stress response: acts by sensing and binding to the cytosolic metabolite sphingosine-1-phosphate generated in response to endoplasmic reticulum stress, initiating an inflammation process that leads to activation of the NF-kappa-B and MAP kinases signaling (PubMed:27007849, PubMed:33942347). May also be involved in NLRP1 activation following activation by MDP, leading to CASP1 activation and IL1B release in macrophages (PubMed:18511561)", "gene_name": "NOD2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9HC29", "name": "NOD2", "organism": "Homo sapiens", "uniprot_id": "Q9HC29" }, { "function": "Proton-coupled amino-acid transporter that transports oligopeptides of 2 to 4 amino acids with a preference for dipeptides (PubMed:16434549, PubMed:18367661, PubMed:7756356). Transports neutral and anionic dipeptides with a proton to peptide stoichiometry of 2:1 or 3:1 (By similarity). In kidney, involved in the absorption of circulating di- and tripeptides from the glomerular filtrate (PubMed:7756356). Can also transport beta-lactam antibiotics, such as the aminocephalosporin cefadroxil, and other antiviral and anticancer drugs (PubMed:16434549). Transports the dipeptide-like aminopeptidase inhibitor bestatin (By similarity). Also able to transport carnosine (PubMed:31073693). Involved in innate immunity by promoting the detection of microbial pathogens by NOD-like receptors (NLRs) (By similarity). Mediates transport of bacterial peptidoglycans across the plasma membrane or, in macrophages, the phagosome membrane: catalyzes the transport of certain bacterial peptidoglycans, such as muramyl dipeptide (MDP), the NOD2 ligand (PubMed:20406817)", "gene_name": "SLC15A2", "glycan_count": 0, "glycosylation_sites": [ { "position": 435, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 472, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 528, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 567, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 587, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q16348", "name": "PepT1 (SLC15A1)", "organism": "Homo sapiens", "uniprot_id": "Q16348" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q16373", "name": "PepT2 (SLC15A2)", "organism": "", "uniprot_id": "Q16373" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01024, P08603", "name": "Complement proteins (C3a, C5a)", "organism": "", "uniprot_id": "" }, { "function": "GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has a substantial GAP activity toward CDC42 and RAC1 and less toward RHOA. Has a role in regulating adhesion of hematopoietic cells to the extracellular matrix. Binds phosphoinositides, and has the highest affinity for phosphatidylinositol 3,4,5-trisphosphate, followed by phosphatidylinositol 3,4-bisphosphate and phosphatidylinositol 4,5-bisphosphate", "gene_name": "ARHGAP9", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8TCJ3", "name": "OST-B (STT3B)", "organism": "Homo sapiens", "uniprot_id": "Q9BRR9" }, { "function": "Involved in melanosome biogenesis by ensuring the stability of GPR143. Plays a vital role in the expression, stability, trafficking, and processing of melanocyte protein PMEL, which is critical to the formation of stage II melanosomes", "gene_name": "MLANA", "glycan_count": 1, "glycosylation_sites": [], "id": "Q16655", "name": "Melan-A/MART-1", "organism": "Homo sapiens", "uniprot_id": "Q16655" }, { "function": "Plays a role in melanin biosynthesis (PubMed:16704458, PubMed:22556244, PubMed:23504663). Catalyzes the oxidation of 5,6-dihydroxyindole-2-carboxylic acid (DHICA) into indole-5,6-quinone-2-carboxylic acid in the presence of bound Cu(2+) ions, but not in the presence of Zn(2+) (PubMed:28661582). May regulate or influence the type of melanin synthesized (PubMed:16704458, PubMed:22556244). Also to a lower extent, capable of hydroxylating tyrosine and producing melanin (By similarity)", "gene_name": "TYRP1", "glycan_count": 6, "glycosylation_sites": [ { "position": 96, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 181, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 304, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 350, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 385, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P17643", "name": "TRP-1", "organism": "Homo sapiens", "uniprot_id": "P17643" }, { "function": "Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis (PubMed:17581632, PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation (PubMed:17581632). The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression (PubMed:25849773)", "gene_name": "EIF3K", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UBQ5", "name": "TRP-2", "organism": "Homo sapiens", "uniprot_id": "Q9UBQ5" }, { "function": "Essential for elastic fiber formation, is involved in the assembly of continuous elastin (ELN) polymer and promotes the interaction of microfibrils and ELN (PubMed:18185537). Stabilizes and organizes elastic fibers in the skin, lung and vasculature (By similarity). Promotes adhesion of endothelial cells through interaction of integrins and the RGD motif. Vascular ligand for integrin receptors which may play a role in vascular development and remodeling (PubMed:10428823). May act as an adapter that mediates the interaction between FBN1 and ELN (PubMed:17255108)", "gene_name": "FBLN5", "glycan_count": 84, "glycosylation_sites": [ { "position": 283, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 296, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UBX5", "name": "Microfibril-associated glycoprotein 4", "organism": "Homo sapiens", "uniprot_id": "Q9UBX5" }, { "function": "Adipocyte-secreted protein (adipokine) that regulates adipogenesis, metabolism and inflammation through activation of the chemokine-like receptor 1 (CMKLR1). Also acts as a ligand for CMKLR2. Can also bind to C-C chemokine receptor-like 2 (CCRL2), but with a lower affinity than it does to CMKLR1 or CMKLR2 (PubMed:27716822). Positively regulates adipocyte differentiation, modulates the expression of adipocyte genes involved in lipid and glucose metabolism and might play a role in angiogenesis, a process essential for the expansion of white adipose tissue. Also acts as a pro-inflammatory adipokine, causing an increase in secretion of pro-inflammatory and prodiabetic adipokines, which further impair adipose tissue metabolic function and have negative systemic effects including impaired insulin sensitivity, altered glucose and lipid metabolism, and a decrease in vascular function in other tissues. Can have both pro- and anti-inflammatory properties depending on the modality of enzymatic cleavage by different classes of proteases. Acts as a chemotactic factor for leukocyte populations expressing CMKLR1, particularly immature plasmacytoid dendritic cells, but also immature myeloid DCs, macrophages and natural killer cells. Exerts an anti-inflammatory role by preventing TNF/TNFA-induced VCAM1 expression and monocytes adhesion in vascular endothelial cells. The effect is mediated via inhibiting activation of NF-kappa-B and CRK/p38 through stimulation of AKT1/NOS3 signaling and nitric oxide production. Its dual role in inflammation and metabolism might provide a link between chronic inflammation and obesity, as well as obesity-related disorders such as type 2 diabetes and cardiovascular disease. Exhibits an antimicrobial function in the skin", "gene_name": "RARRES2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q99969", "name": "Keratocan", "organism": "Homo sapiens", "uniprot_id": "Q99969" }, { "function": "Required for lymphangioblast budding and angiogenic sprouting from venous endothelium during embryogenesis", "gene_name": "CCBE1", "glycan_count": 2, "glycosylation_sites": [ { "position": 142, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 182, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 385, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" } ], "id": "Q6UXH8", "name": "Olfactomedin-like protein 3", "organism": "Homo sapiens", "uniprot_id": "Q6UXH8" }, { "function": "", "gene_name": "ADAMTS18", "glycan_count": 1, "glycosylation_sites": [ { "position": 151, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 190, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 313, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 745, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 838, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 909, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8TE60", "name": "ADAMTS-like 2", "organism": "Homo sapiens", "uniprot_id": "Q8TE60" }, { "function": "Sulfotransferase that transfers sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to the C-6 hydroxyl group of the GalNAc 4-sulfate residue of chondroitin sulfate A and forms chondroitin sulfate E containing GlcA-GalNAc(4,6-SO(4)) repeating units. It also transfers sulfate to a unique non-reducing terminal sequence, GalNAc(4SO4)-GlcA(2SO4)-GalNAc(6SO4), to yield a highly sulfated structure similar to the structure found in thrombomodulin chondroitin sulfate. May also act as a B-cell receptor involved in BCR ligation-mediated early activation that mediate regulatory signals key to B-cell development and/or regulation of B-cell-specific RAG expression; however such results are unclear in vivo", "gene_name": "CHST15", "glycan_count": 2, "glycosylation_sites": [ { "position": 364, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q7LFX5", "name": "Carbohydrate sulfotransferase 15", "organism": "Homo sapiens", "uniprot_id": "Q7LFX5" }, { "function": "Receptor for IL1A, IL1B and IL1RN (PubMed:2950091, PubMed:37315560). After binding to interleukin-1 associates with the coreceptor IL1RAP to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B, MAPK and other pathways. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. Binds ligands with comparable affinity and binding of antagonist IL1RN prevents association with IL1RAP to form a signaling complex. Involved in IL1B-mediated costimulation of IFNG production from T-helper 1 (Th1) cells (PubMed:10653850)", "gene_name": "IL1R1", "glycan_count": 1, "glycosylation_sites": [ { "position": 100, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 193, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 233, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 249, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 263, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 297, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P14778", "name": "Interleukin-1 receptor", "organism": "Homo sapiens", "uniprot_id": "P14778" }, { "function": "Plays a role in cell attachment and migration. Interacts with extracellular matrix proteins and with the actin cytoskeleton and thereby plays an important role in normal extracellular matrix (ECM) homeostasis. Mediates adhesion of cells to type 1 collagen and gelatin, reorganization of the actin cytoskeleton and promotes cell spreading. Plays a role in the angiogenic response of cultured umbilical vein endothelial cells. May also act as a receptor for PLAU. Upon ligand binding, stimulates the phosphorylation of EGFR and ERK1/2 (PubMed:30241478)", "gene_name": "ANTXR1", "glycan_count": 2, "glycosylation_sites": [ { "position": 166, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 184, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 262, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9H6X2", "name": "SSR4", "organism": "Homo sapiens", "uniprot_id": "Q9H6X2" }, { "function": "Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis", "gene_name": "PRPS1", "glycan_count": 1, "glycosylation_sites": [], "id": "P60891", "name": "PRPS1", "organism": "Homo sapiens", "uniprot_id": "P60891" }, { "function": "Core component of the SMC5-SMC6 complex, a complex involved in DNA double-strand breaks by homologous recombination. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs). Required for recruitment of telomeres to PML nuclear bodies. SMC5-SMC6 complex may prevent transcription of episomal DNA, such as circular viral DNA genome (PubMed:26983541)", "gene_name": "SMC6", "glycan_count": 2, "glycosylation_sites": [], "id": "Q96SB8", "name": "OPHN1", "organism": "Homo sapiens", "uniprot_id": "Q96SB8" }, { "function": "Regulates ATP-dependent protein translocation into the mitochondrial matrix. Inhibits DNAJC19 stimulation of HSPA9/Mortalin ATPase activity", "gene_name": "PAM16", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y3D7", "name": "FTSJ1", "organism": "Homo sapiens", "uniprot_id": "Q9Y3D7" }, { "function": "3'-5'-exoribonuclease that specifically recognizes RNAs polyuridylated at their 3' end and mediates their degradation. Component of an exosome-independent RNA degradation pathway that mediates degradation of both mRNAs and miRNAs that have been polyuridylated by a terminal uridylyltransferase, such as ZCCHC11/TUT4. Mediates degradation of cytoplasmic mRNAs that have been deadenylated and subsequently uridylated at their 3'. Mediates degradation of uridylated pre-let-7 miRNAs, contributing to the maintenance of embryonic stem (ES) cells. Essential for correct mitosis, and negatively regulates cell proliferation", "gene_name": "DIS3L2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8IYB7", "name": "NEMF", "organism": "Homo sapiens", "uniprot_id": "Q8IYB7" }, { "function": "Essential component of the RMI complex, a complex that plays an important role in the processing of homologous recombination intermediates to limit DNA crossover formation in cells. Promotes TOP3A binding to double Holliday junctions (DHJ) and hence stimulates TOP3A-mediated dissolution. Required for BLM phosphorylation during mitosis. Within the BLM complex, required for BLM and TOP3A stability", "gene_name": "RMI1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H9A7", "name": "C5orf42", "organism": "Homo sapiens", "uniprot_id": "Q9H9A7" }, { "function": "Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity). Binds DNA non-specifically (PubMed:14982958, PubMed:15170388)", "gene_name": "ARID1B", "glycan_count": 2, "glycosylation_sites": [], "id": "Q8NFD5", "name": "ARID1B", "organism": "Homo sapiens", "uniprot_id": "Q8NFD5" }, { "function": "Key regulator of both differentiation and survival of T-lymphocytes during thymocyte development in mammals. Essential in controlling the responsiveness of hematopoietic stem cells to chemotactic signals by modulating the expression of the receptors CCR7 and CCR9, which direct the movement of progenitor cells from the bone marrow to the thymus (PubMed:27959755). Is a regulator of IL2 promoter and enhances IL2 expression in activated CD4(+) T-lymphocytes (PubMed:16809611). Tumor-suppressor that represses transcription through direct, TFCOUP2-independent binding to a GC-rich response element (By similarity). May also function in the P53-signaling pathway (By similarity)", "gene_name": "BCL11B", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9C0K0", "name": "BCL11B", "organism": "Homo sapiens", "uniprot_id": "Q9C0K0" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03468 (H1N1)", "name": "Neuraminidase (NA)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6DPL2 (H5N2)", "name": "Hemagglutinin (HA, H5)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6DPL3 (H5N2)", "name": "Neuraminidase (NA, H5)", "organism": "", "uniprot_id": "" }, { "function": "Component of the elastin-associated microfibrils", "gene_name": "MFAP2", "glycan_count": 2, "glycosylation_sites": [], "id": "P55001", "name": "MAGP-1 (Microfibril-associated glycoprotein-1)", "organism": "Homo sapiens", "uniprot_id": "P55001" }, { "function": "Multifunctional regulatory protein whose primary function is to antagonize members of the transforming growth factor beta (TGF-beta) superfamily including activin, myostatin, GDF11 or bone morphogenetic proteins (BMPs) (PubMed:11279126, PubMed:16482217, PubMed:18535106). Mechanistically, binds to these ligands in the extracellular space, blocking their type II receptor-binding site to inhibit downstream signaling (PubMed:16482217). Plays an essential role in muscle fiber formation and growth both by preventing the repressive effects of myostatin and through SMAD3/AKT/mTOR signaling independently of myostatin (By similarity). Also promotes neural differentiation by antagonizing the action BMP4 (By similarity). Acts as a specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (FSH) by sequestering activin A/INHBA (PubMed:11279126). On the other hand, translocates into the nucleus where it down-regulates rRNA synthesis and ribosome biogenesis to maintain cellular energy homeostasis by binding to rDNA", "gene_name": "FST", "glycan_count": 10, "glycosylation_sites": [ { "position": 124, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 288, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P19883", "name": "Follistatin", "organism": "Homo sapiens", "uniprot_id": "P19883" }, { "function": "Acts as an inhibitor of mitochondrial fission. Interacts with MFF and prevents DNM1L recruitment to mitochondria, promoting a more fused mitochondrial network", "gene_name": "MFI", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8NCR3", "name": "GALGT2 (\u03b21,4-N-acetylgalactosaminyltransferase-2)", "organism": "Homo sapiens", "uniprot_id": "Q8NCR3" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "LAMA4: Q16363, LAMA5: O15230", "name": "Laminin \u03b14/\u03b15", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P19838 (RELA)", "name": "NF-\u03baB", "organism": "", "uniprot_id": "" }, { "function": "Stimulatory receptor expressed in activated or antigen-experienced T-cells that plays an important role in the immune response (PubMed:9930702). Upon binding to its ligand ICOSL expressed on antigen presenting cells (APCs), delivers costimulatory signals that enhances all basic T-cell responses to a foreign antigen, namely proliferation, secretion of lymphokines including IL10, up-regulation of molecules that mediate cell-cell interaction, and effective help for antibody secretion by B-cells (PubMed:33033255). Also acts as a costimulatory receptor critical for the differentiation of T follicular regulatory cells upon immune challenges such as viral infection (PubMed:27135603). Mechanistically, potentiates TCR-induced calcium flux by augmenting PLCG1 activation and actin remodeling (By similarity). In addition, activates PI3K signaling pathways independently of calcium flux (PubMed:30523347). Essential both for efficient interaction between T and B-cells and for normal antibody responses to T-cell dependent antigens. Prevents the apoptosis of pre-activated T-cells. Plays a critical role in CD40-mediated class switching of immunoglobin isotypes (By similarity)", "gene_name": "ICOS", "glycan_count": 1, "glycosylation_sites": [ { "position": 89, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 110, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y6W8", "name": "ICOS", "organism": "Homo sapiens", "uniprot_id": "Q9Y6W8" }, { "function": "Catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine. Plays a role in maintaining acid-base homeostasis. Regulates the levels of the neurotransmitter glutamate, the main excitatory neurotransmitter in the brain (PubMed:30239721, PubMed:30575854, PubMed:30970188)", "gene_name": "GLS", "glycan_count": 7, "glycosylation_sites": [], "id": "O94925", "name": "GLS1", "organism": "Homo sapiens", "uniprot_id": "O94925" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "ITGA7: Q13683, ITGB1: P05556", "name": "Integrin \u03b17\u03b21", "organism": "", "uniprot_id": "" }, { "function": "Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state (PubMed:10383393, PubMed:20178975). Plays a role in stress resistance and actin organization (PubMed:19166925). Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins (PubMed:23728742)", "gene_name": "HSPB1", "glycan_count": 1, "glycosylation_sites": [], "id": "P04792", "name": "Heat Shock Protein 27 (HSP27)", "organism": "Homo sapiens", "uniprot_id": "P04792" }, { "function": "Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle (PubMed:18485873). The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (PubMed:18485873). The APC/C complex catalyzes assembly of branched 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on target proteins (PubMed:29033132)", "gene_name": "ANAPC1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H1A4", "name": "B4GALT2", "organism": "Homo sapiens", "uniprot_id": "Q9H1A4" }, { "function": "May play a role in intercellular signaling and in connecting cells with the extracellular matrix. May take part in the regulation of cell motility, growth and differentiation. Binds hyaluronic acid", "gene_name": "VCAN", "glycan_count": 91, "glycosylation_sites": [ { "position": 57, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 330, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 615, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 659, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 782, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 809, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1332, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1398, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1442, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1468, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1548, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 1631, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 1663, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1898, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1935, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 1959, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 2179, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2247, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 2254, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 2272, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2280, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2360, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2385, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2392, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2496, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2628, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2722, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 2723, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 2767, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 2934, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2941, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 3067, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3369, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3379, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P13611", "name": "Versican", "organism": "Homo sapiens", "uniprot_id": "P13611" }, { "function": "", "gene_name": "GALNS", "glycan_count": 33, "glycosylation_sites": [ { "position": 204, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 423, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P34059", "name": "N-acetylgalactosamine 6-sulfatase (GALNS)", "organism": "Homo sapiens", "uniprot_id": "P34059" }, { "function": "Lysosomal membrane glycoprotein which plays an important role in lysosome biogenesis, lysosomal pH regulation, autophagy and cholesterol homeostasis (PubMed:15121881). Acts as an important regulator of lysosomal lumen pH regulation by acting as a direct inhibitor of the proton channel TMEM175, facilitating lysosomal acidification for optimal hydrolase activity (By similarity). Also plays an important role in NK-cells cytotoxicity (PubMed:23847195). Mechanistically, participates in cytotoxic granule movement to the cell surface and perforin trafficking to the lytic granule (By similarity). In addition, protects NK-cells from degranulation-associated damage induced by their own cytotoxic granule content (PubMed:23847195). Presents carbohydrate ligands to selectins (By similarity). Also implicated in tumor cell metastasis (PubMed:2676155)", "gene_name": "Lamp1", "glycan_count": 39, "glycosylation_sites": [ { "position": 31, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 52, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 58, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 70, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 78, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 97, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 101, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 115, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 159, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 177, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 214, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 219, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 232, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 240, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 252, "type": "N-linked (GlcNAc...) (high mannose) asparagine" }, { "position": 282, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 296, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 311, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P11438", "name": "LAMP-1", "organism": "Mus musculus", "uniprot_id": "P11438" }, { "function": "Cleaves aggrecan, a cartilage proteoglycan, at the '392-Glu-|-Ala-393' site and may be involved in its turnover (PubMed:10356395, PubMed:10827174). Also cleaves COMP (PubMed:39672391). May play an important role in the destruction of aggrecan in arthritic diseases. Could be a critical factor in the exacerbation of neurodegeneration in Alzheimer disease", "gene_name": "ADAMTS4", "glycan_count": 3, "glycosylation_sites": [ { "position": 68, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O75173", "name": "Adamts4", "organism": "Homo sapiens", "uniprot_id": "O75173" }, { "function": "Connects cell membrane constituents to the actin cytoskeleton. May promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton. Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Various interactions and localizations of isoforms affect myotube morphology and myogenesis. Isoform 6 accelerates muscle differentiation in vitro", "gene_name": "FLNB", "glycan_count": 10, "glycosylation_sites": [], "id": "O75369", "name": "\u03b21D-integrin", "organism": "Homo sapiens", "uniprot_id": "O75369" }, { "function": "Catalyzes the reduction of glutathione disulfide (GSSG) to reduced glutathione (GSH). Constitutes the major mechanism to maintain a high GSH:GSSG ratio in the cytosol", "gene_name": "GSR", "glycan_count": 1, "glycosylation_sites": [], "id": "P00390", "name": "erythrocyte glutathione reductase", "organism": "Homo sapiens", "uniprot_id": "P00390" }, { "function": "Polycomb group (PcG) protein. Catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Required for embryonic stem cell derivation and self-renewal, suggesting that it is involved in safeguarding embryonic stem cell identity. Compared to EZH2-containing complexes, it is less abundant in embryonic stem cells, has weak methyltransferase activity and plays a less critical role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation", "gene_name": "EZH1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q92800", "name": "EZH1", "organism": "Homo sapiens", "uniprot_id": "Q92800" }, { "function": "Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex. Actin remodeling activity is regulated by RAC1. As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes", "gene_name": "NCKAP1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y2A7", "name": "GCNT3", "organism": "Homo sapiens", "uniprot_id": "Q9Y2A7" }, { "function": "Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor", "gene_name": "GALNT16", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8N428", "name": "GALNT7", "organism": "Homo sapiens", "uniprot_id": "Q8N428" }, { "function": "Hydrolyzes the non-reducing end N-acetyl-D-hexosamine and/or sulfated N-acetyl-D-hexosamine of glycoconjugates, such as the oligosaccharide moieties from proteins and neutral glycolipids, or from certain mucopolysaccharides (PubMed:11707436, PubMed:8123671, PubMed:8672428, PubMed:9694901). The isozyme B does not hydrolyze each of these substrates, however hydrolyzes efficiently neutral oligosaccharide (PubMed:11707436). Only the isozyme A is responsible for the degradation of GM2 gangliosides in the presence of GM2A (PubMed:8123671, PubMed:8672428, PubMed:9694901). During fertilization is responsible, at least in part, for the zona block to polyspermy. Present in the cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation and inactivates the sperm galactosyltransferase-binding site, accounting for the block in sperm binding to the zona pellucida (By similarity)", "gene_name": "HEXB", "glycan_count": 47, "glycosylation_sites": [ { "position": 84, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 142, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 190, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 327, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P07686", "name": "HEXB", "organism": "Homo sapiens", "uniprot_id": "P07686" }, { "function": "Catalyzes the transfer of Gal to GlcNAc-based acceptors with a preference for the core3 O-linked glycan GlcNAc(beta1,3)GalNAc structure. Can use glycolipid LC3Cer as an efficient acceptor", "gene_name": "B3GALT5", "glycan_count": 1, "glycosylation_sites": [ { "position": 130, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 174, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 231, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y2C3", "name": "B4GALT5", "organism": "Homo sapiens", "uniprot_id": "Q9Y2C3" }, { "function": "Shared alpha chain of the active heterodimeric glycoprotein hormones thyrotropin/thyroid stimulating hormone/TSH, lutropin/luteinizing hormone/LH, follitropin/follicle stimulating hormone/FSH and choriogonadotropin/CG. These hormones bind specific receptors on target cells that in turn activate downstream signaling pathways", "gene_name": "CGA", "glycan_count": 114, "glycosylation_sites": [ { "position": 76, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 102, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01215", "name": "CGA", "organism": "Homo sapiens", "uniprot_id": "P01215" }, { "function": "Mediates the transport of urea driven by a concentration gradient across the cell membrane of the renal inner medullary collecting duct which is critical to the urinary concentrating mechanism", "gene_name": "SLC14A2", "glycan_count": 0, "glycosylation_sites": [ { "position": 733, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q15849", "name": "UT-A1", "organism": "Homo sapiens", "uniprot_id": "Q15849" }, { "function": "Exonuclease that has both 3'-5' exoribonuclease and exodeoxyribonuclease activities, depending on the divalent metal cation used as cofactor (PubMed:29335528, PubMed:31127291). In presence of Mg(2+), only shows 3'-5' exoribonuclease activity, while it shows both exoribonuclease and exodeoxyribonuclease activities in presence of Mn(2+) (PubMed:29335528, PubMed:31127291). Acts as an exoribonuclease in mitochondrion, possibly by regulating ATP production and mitochondrial translation (PubMed:29335528). Also involved in the response to DNA damage (PubMed:26807646, PubMed:31255466). Acts as 3'-5' exodeoxyribonuclease for double-strand breaks resection and efficient homologous recombination (PubMed:20603073, PubMed:26807646). Plays a key role in controlling the initial steps of chromosomal break repair, it is recruited to chromatin in a damage-dependent manner and functionally interacts with the MRN complex to accelerate resection through its 3'-5' exonuclease activity, which efficiently processes double-stranded DNA substrates containing nicks (PubMed:26807646). Also involved in response to replicative stress: recruited to stalled forks and is required to stabilize and restart stalled replication forks by restraining excessive fork regression, thereby suppressing their degradation (PubMed:31255466)", "gene_name": "EXD2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NVH0", "name": "UT-A3", "organism": "Homo sapiens", "uniprot_id": "Q9NVH0" }, { "function": "Catalyzes the condensation of phosphoenolpyruvate (PEP) and N-acetylmannosamine 6-phosphate (ManNAc-6-P) to synthesize N-acetylneuraminate-9-phosphate (Neu5Ac-9-P) (PubMed:10749855). Also catalyzes the condensation of PEP and D-mannose 6-phosphate (Man-6-P) to produce 3-deoxy-D-glycero-beta-D-galacto-non-2-ulopyranosonate 9-phosphate (KDN-9-P) (PubMed:10749855). Neu5Ac-9-P and KDN-9-P are the phosphorylated forms of sialic acids N-acetylneuraminic acid (Neu5Ac) and deaminoneuraminic acid (KDN), respectively (PubMed:10749855). Required for brain and skeletal development (PubMed:27213289)", "gene_name": "NANS", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NR45", "name": "NEU3", "organism": "Homo sapiens", "uniprot_id": "Q9NR45" }, { "function": "Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,3- and alpha-2,6-linked sialic acid. Also binds disialogangliosides (disialogalactosyl globoside, disialyl lactotetraosylceramide and disialyl GalNAc lactotetraoslylceramide). The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Mediates inhibition of natural killer cells cytotoxicity. May play a role in hemopoiesis. Inhibits differentiation of CD34+ cell precursors towards myelomonocytic cell lineage and proliferation of leukemic myeloid cells (in vitro)", "gene_name": "SIGLEC7", "glycan_count": 33, "glycosylation_sites": [ { "position": 105, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 142, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 165, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 229, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 235, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 242, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 260, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 334, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y286", "name": "Siglec-7", "organism": "Homo sapiens", "uniprot_id": "Q9Y286" }, { "function": "Major glycoprotein component of a variety of mucus gels. Thought to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces. May be involved in ligand binding and intracellular signaling", "gene_name": "MUC3A", "glycan_count": 1, "glycosylation_sites": [], "id": "Q02505", "name": "MUC3", "organism": "Homo sapiens", "uniprot_id": "Q02505" }, { "function": "Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to the terminal galactose on both O- and N-linked glycans chains of cell surface glycoproteins and glycolipids and the resulting epitope regulates several processes such as cell-cell interaction including host-microbe interaction, cell surface expression and cell proliferation (PubMed:12692541, PubMed:7876235, PubMed:8018146). Preferentially fucosylates gangliosides GA1 and GM1 in the antrum, cecum and colon and in the female reproductive organs (By similarity). Fucosylated host glycoproteins or glycolipids mediate interaction with intestinal microbiota influencing its composition (PubMed:21625510, PubMed:22068912, PubMed:24733310). Creates a soluble precursor oligosaccharide FuC-alpha ((1,2)Galbeta-) called the H antigen which is an essential substrate for the final step in the soluble ABO blood group antigen synthesis pathway (PubMed:7876235)", "gene_name": "FUT2", "glycan_count": 0, "glycosylation_sites": [ { "position": 188, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 282, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 308, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q10981", "name": "FUT2", "organism": "Homo sapiens", "uniprot_id": "Q10981" }, { "function": "Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of internal galactose (Gal) residues of keratan. Cooperates with B4GALT4 and B3GNT7 glycosyltransferases and CHST6 sulfotransferase to construct and elongate disulfated disaccharide unit [->3(6-sulfoGalbeta)1->4(6-sulfoGlcNAcbeta)1->] within keratan sulfate polymer (PubMed:10642612, PubMed:17690104, PubMed:9405439). Has a preference for sulfating keratan sulfate, but it also transfers sulfate to the unsulfated polymer (PubMed:9405439). Involved in biosynthesis of phosphacan, a major keratan sulfate proteoglycan in the developing brain (By similarity). Involved in biosynthesis of 6-sulfoGalbeta-containing O-linked glycans in high endothelial venules of lymph nodes. May act in a synergistic manner with CHST4 to generate sialyl 6',6-disulfo Lewis X motif, a recognition determinant for immune cell receptors implicated in leukocyte trafficking (PubMed:10330415). Catalyzes sulfation of N-acetyllactosamine (LacNAc) oligosaccharides with highest efficiency for sialylated LacNAc structures (PubMed:10642612)", "gene_name": "CHST1", "glycan_count": 1, "glycosylation_sites": [ { "position": 56, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 145, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 189, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 334, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O43916", "name": "GlcNAc6ST-2/CHST4", "organism": "Homo sapiens", "uniprot_id": "O43916" }, { "function": "Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor (PubMed:10464263, PubMed:31932717). May participate in synthesis of oncofetal fibronectin (PubMed:10464263). Has activity toward MUC1A, MUC2, EA2 and fibronectin peptides (PubMed:10464263). Glycosylates FGF23 (PubMed:31932717)", "gene_name": "GALNT6", "glycan_count": 1, "glycosylation_sites": [ { "position": 86, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 476, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8NCL4", "name": "POMGNT2", "organism": "Homo sapiens", "uniprot_id": "Q8NCL4" }, { "function": "Serine protease component of the complement C1 complex, a multiprotein complex that initiates the classical pathway of the complement system, a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system (PubMed:17996945, PubMed:19473974, PubMed:29449492). C1R catalyzes the first enzymatic step in the classical complement pathway: it is activated by the C1Q subcomplex of the C1 complex, which associates with IgG or IgM immunoglobulins complexed with antigens to form antigen-antibody complexes on the surface of pathogens (PubMed:29449492, PubMed:34155115). Immunoglobulin-binding promotes the autocatalytic cleavage and activation of C1R (PubMed:11445589, PubMed:11673533, PubMed:17996945, PubMed:20178990, PubMed:6254570, PubMed:6271784). Activated C1R then cleaves and activates C1S, the second protease of the classical complement pathway (PubMed:11445589, PubMed:11673533, PubMed:6271784). It is unclear if C1R activates C1S within single, strained C1 complexes or between neighboring C1 complexes on surfaces (PubMed:28104818, PubMed:29311313, PubMed:29449492)", "gene_name": "C1R", "glycan_count": 60, "glycosylation_sites": [ { "position": 125, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 221, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 514, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 581, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P00736", "name": "Cetuximab", "organism": "Homo sapiens", "uniprot_id": "P00736" }, { "function": "Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine", "gene_name": "ADRB2", "glycan_count": 1, "glycosylation_sites": [ { "position": 6, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 15, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P07550", "name": "Beta-adrenergic receptor", "organism": "Homo sapiens", "uniprot_id": "P07550" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P11250/P11251", "name": "NDV-HN/F (Newcastle Disease Virus Hemagglutinin-Neuraminidase/Fusion)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8V8F6", "name": "LASV-GP (Lassa Virus Glycoprotein)", "organism": "JC polyomavirus", "uniprot_id": "Q8V8F6" }, { "function": "", "gene_name": "CDV3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UKY7", "name": "Utrophin", "organism": "Homo sapiens", "uniprot_id": "Q9UKY7" }, { "function": "Stratified squamous epithelial basement membrane protein that forms anchoring fibrils which may contribute to epithelial basement membrane organization and adherence by interacting with extracellular matrix (ECM) proteins such as type IV collagen", "gene_name": "COL7A1", "glycan_count": 2, "glycosylation_sites": [ { "position": 337, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 786, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1109, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2625, "type": "O-linked (Gal...) hydroxylysine; alternate" }, { "position": 2631, "type": "O-linked (Gal...) hydroxylysine; alternate" } ], "id": "Q02388", "name": "Collagen VII", "organism": "Homo sapiens", "uniprot_id": "Q02388" }, { "function": "Plays a role in formation of mast cell secretory granules and mediates storage of various compounds in secretory vesicles. Required for storage of some proteases in both connective tissue and mucosal mast cells and for storage of granzyme B in T-lymphocytes. Plays a role in localizing neutrophil elastase in azurophil granules of neutrophils. Mediates processing of MMP2. Plays a role in cytotoxic cell granule-mediated apoptosis by forming a complex with granzyme B which is delivered to cells by perforin to induce apoptosis. Regulates the secretion of TNF-alpha and may also regulate protease secretion. Inhibits bone mineralization", "gene_name": "SRGN", "glycan_count": 0, "glycosylation_sites": [ { "position": 94, "type": "O-linked (Xyl...) (glycosaminoglycan) serine" }, { "position": 96, "type": "O-linked (Xyl...) (glycosaminoglycan) serine" }, { "position": 100, "type": "O-linked (Xyl...) (glycosaminoglycan) serine" }, { "position": 102, "type": "O-linked (Xyl...) (glycosaminoglycan) serine" }, { "position": 104, "type": "O-linked (Xyl...) (glycosaminoglycan) serine" }, { "position": 106, "type": "O-linked (Xyl...) (glycosaminoglycan) serine" }, { "position": 108, "type": "O-linked (Xyl...) (glycosaminoglycan) serine" }, { "position": 110, "type": "O-linked (Xyl...) (glycosaminoglycan) serine" } ], "id": "P10124", "name": "Serglycin (SRGN)", "organism": "Homo sapiens", "uniprot_id": "P10124" }, { "function": "Cell surface proteoglycan that bears heparan sulfate. Putative cell surface coreceptor for growth factors, extracellular matrix proteins, proteases and anti-proteases (By similarity). Enhances migration and invasion of cancer cells through WNT5A signaling", "gene_name": "GPC6", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y625", "name": "Glypican-6 (GPC6)", "organism": "Homo sapiens", "uniprot_id": "Q9Y625" }, { "function": "Early post-infection, the reverse transcriptase converts the viral RNA genome into double-stranded viral DNA. The RNase H domain of the reverse transcriptase performs two functions. It degrades the RNA template and specifically removes the RNA primer from the RNA/DNA hybrid. Following nuclear import, the integrase catalyzes the insertion of the linear, double-stranded viral DNA into the host cell chromosome. Endogenous Pol proteins may have kept, lost or modified their original function during evolution", "gene_name": "ERVK-6", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9BXR3", "name": "CD301 (CLEC10A)", "organism": "Homo sapiens", "uniprot_id": "Q9BXR3" }, { "function": "Self assembles to form an icosahedral capsid. Most capsids appear to be large particles with an icosahedral symmetry of T=4 and consist of 240 copies of capsid protein, though a fraction forms smaller T=3 particles consisting of 180 capsid proteins. Entering capsids are transported along microtubules to the nucleus. Phosphorylation of the capsid is thought to induce exposure of nuclear localization signal in the C-terminal portion of the capsid protein that allows binding to the nuclear pore complex via the importin (karyopherin-) alpha and beta. Capsids are imported in intact form through the nuclear pore into the nuclear basket, where it probably binds NUP153. Only capsids that contain the mature viral genome can release the viral DNA and capsid protein into the nucleoplasm. Immature capsids get stuck in the basket. Capsids encapsulate the pre-genomic RNA and the P protein. Pre-genomic RNA is reverse-transcribed into DNA while the capsid is still in the cytoplasm. The capsid can then either be directed to the nucleus, providing more genomes for transcription, or bud through the endoplasmic reticulum to provide new virions", "gene_name": "C", "glycan_count": 0, "glycosylation_sites": [], "id": "P03147", "name": "HBsAg", "organism": "Hepatitis B virus genotype D subtype adw (isolate United Kingdom/adyw/1979)", "uniprot_id": "P03147" }, { "function": "Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin", "gene_name": "COL5A1", "glycan_count": 22, "glycosylation_sites": [], "id": "P20908", "name": "Collagen alpha-1(V) chain (COL5A1)", "organism": "Homo sapiens", "uniprot_id": "P20908" }, { "function": "F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein", "gene_name": "ACTN3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q08043", "name": "Alpha-actinin-3 (ACTN3)", "organism": "Homo sapiens", "uniprot_id": "Q08043" }, { "function": "AMP deaminase plays a critical role in energy metabolism", "gene_name": "AMPD1", "glycan_count": 1, "glycosylation_sites": [], "id": "P23109", "name": "Adenosine monophosphate deaminase 1 (AMPD1)", "organism": "Homo sapiens", "uniprot_id": "P23109" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P07359/P13224/P13022", "name": "Glycoprotein Ib-IX-V (GPIb-IX-V)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P23219/P17301", "name": "Glycoprotein Ia/IIa (GPIa/IIa)", "organism": "", "uniprot_id": "" }, { "function": "Large tegument protein that plays multiple roles in the viral cycle. During viral entry, remains associated with the capsid while most of the tegument is detached and participates in the capsid transport toward the host nucleus. Plays a role in the routing of the capsid at the nuclear pore complex and subsequent uncoating. Within the host nucleus, acts as a deneddylase and promotes the degradation of nuclear CRLs (cullin-RING ubiquitin ligases) and thereby stabilizes nuclear CRL substrates, while cytoplasmic CRLs remain unaffected. These modifications prevent host cell cycle S-phase progression and create a favorable environment allowing efficient viral genome replication. Participates later in the secondary envelopment of capsids. Indeed, plays a linker role for the association of the outer viral tegument to the capsids together with the inner tegument protein (By similarity). Counteracts host TLR-mediated NF-kappa-B activation through both MYD88 and TICAM1-dependent pathways by interfering with 'Lys-63'- and 'Lys-48'-linked ubiquitination of signaling intermediates such as TRAF6 and IKBKG (PubMed:24586164). Inhibits type I interferon production by forming a tri-molecular complex with host TRIM25 and 14-3-3 thereby promoting TRIM25 autoubiquitination and sequestration of the ligase into inactive protein aggregates (PubMed:31710640). In turn, host RIGI is recruited to the complex but ubiquitination is severely impaired leading to inhibition of the pathway (PubMed:29357390). Also catalyzes the removal of 'Lys-48'- and 'Lys-63'-linked ubiquitin chains on host TBK1 and STING1 suppressing cGAS-STING signaling in addition to the RIGI-MAVS pathway (PubMed:36802409). Inhibits selective autophagy by deubiquitinating host SQSTM1. In turn, decreased SQSTM1 ubiquitination fails to recruit LC3 to SQSTM1-positive aggregates (PubMed:34543352). In the host nucleus, deubiquitinates topoisomerase II subunits TOP2A and TOP2B thereby stabilizing SUMOylated TOP2 which halts the DNA damage response to TOP2-induced double strand DNA breaks and promotes cell survival (PubMed:34543352)", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03186", "name": "Epstein\u2013Barr virus gp350/220", "organism": "Epstein-Barr virus (strain B95-8)", "uniprot_id": "P03186" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9JXQ0 (NmB CSS, NMB0069)", "name": "CMP-sialic acid synthetase (CSS)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "GIP", "glycan_count": 0, "glycosylation_sites": [], "id": "P04146", "name": "Adenovirus Fiber Protein", "organism": "Drosophila melanogaster", "uniprot_id": "P04146" }, { "function": "Inactive precursor that is cleaved to give rise to the mature F1 and F2 fusion glycoproteins", "gene_name": "F", "glycan_count": 0, "glycosylation_sites": [ { "position": 57, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 172, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 353, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "Q6WB98", "name": "Human Metapneumovirus Fusion Glycoprotein", "organism": "Human metapneumovirus (strain CAN97-83)", "uniprot_id": "Q6WB98" }, { "function": "Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag-Pol, or to Gag-Pol binding host factors. Interaction with HECT ubiquitin ligases probably links the viral protein to the host ESCRT pathway and facilitates release", "gene_name": "pol", "glycan_count": 0, "glycosylation_sites": [], "id": "P11227", "name": "Parainfluenza Hemagglutinin-Neuraminidase", "organism": "Radiation murine leukemia virus", "uniprot_id": "P11227" }, { "function": "", "gene_name": "1D", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6X5K3", "name": "FREM1", "organism": "Foot-and-mouth disease virus serotype SAT-2", "uniprot_id": "Q6X5K3" }, { "function": "Has both helicase and E3 ubiquitin ligase activities. Possesses intrinsic ATP-dependent nucleosome-remodeling activity; This activity may be required for transcriptional activation or repression of specific target promoters (By similarity). These may include the SERPINE1 and HIV-1 promoters and the SV40 enhancer, to which this protein can bind directly. Plays a role in error-free postreplication repair (PRR) of damaged DNA and maintains genomic stability through acting as a ubiquitin ligase for 'Lys-63'-linked polyubiquitination of chromatin-bound PCNA", "gene_name": "HLTF", "glycan_count": 1, "glycosylation_sites": [], "id": "Q14527", "name": "HLTF", "organism": "Homo sapiens", "uniprot_id": "Q14527" }, { "function": "May promote proliferation of pancreatic cancer cells by favoring the transition from the S to G2/M phase. In myeloid leukemic cell lines, inhibits cell growth and induces cell differentiation and apoptosis. May play a role in the inhibition of EIF4EBP1 phosphorylation/deactivation. Facilitates cell adhesion, most probably through interaction with cell surface lectins and cadherin", "gene_name": "OLFM4", "glycan_count": 56, "glycosylation_sites": [ { "position": 72, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 136, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 253, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6UX06", "name": "Olfactomedin 4 (OLFM4)", "organism": "Homo sapiens", "uniprot_id": "Q6UX06" }, { "function": "Involved in sterol-regulated ubiquitination and degradation of HMG-CoA reductase HMGCR (PubMed:21343306). Involved in positive regulation of AMPA-selective glutamate receptor GRIA2 recycling to the cell surface (By similarity). Acts as a negative regulator of hepatocyte growth during regeneration (By similarity)", "gene_name": "TMUB1", "glycan_count": 4, "glycosylation_sites": [], "id": "Q9BVT8", "name": "TMEM59", "organism": "Homo sapiens", "uniprot_id": "Q9BVT8" }, { "function": "Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates ubiquitination of Ras (K-Ras/KRAS, N-Ras/NRAS and H-Ras/HRAS) (PubMed:30442762, PubMed:30442766, PubMed:30481304). Is a negative regulator of RAS-MAPK signaling that acts by controlling Ras levels and decreasing Ras association with membranes (PubMed:30442762, PubMed:30442766, PubMed:30481304)", "gene_name": "LZTR1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8N653", "name": "MLEC", "organism": "Homo sapiens", "uniprot_id": "Q8N653" }, { "function": "Transcription regulator. Forms a sequence-specific DNA-binding protein complex with MYC or MAD which recognizes the core sequence 5'-CAC[GA]TG-3'. The MYC:MAX complex is a transcriptional activator, whereas the MAD:MAX complex is a repressor. May repress transcription via the recruitment of a chromatin remodeling complex containing H3 'Lys-9' histone methyltransferase activity. Represses MYC transcriptional activity from E-box elements", "gene_name": "MAX", "glycan_count": 0, "glycosylation_sites": [], "id": "P61244", "name": "MAX", "organism": "Homo sapiens", "uniprot_id": "P61244" }, { "function": "May play a critical role in the development of respiratory control mechanisms and in the normal growth and maturation of the lung. Binds preferentially to methylated DNA (PubMed:28473536)", "gene_name": "LHX4", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8TCJ1", "name": "STT3B", "organism": "Homo sapiens", "uniprot_id": "Q969G2" }, { "function": "Multifunctional transcription factor that exhibits positive and negative control on a large number of cellular and viral genes by binding to sites overlapping the transcription start site (PubMed:15329343, PubMed:17721549, PubMed:24326773, PubMed:25787250). Binds to the consensus sequence 5'-CCGCCATNTT-3'; some genes have been shown to contain a longer binding motif allowing enhanced binding; the initial CG dinucleotide can be methylated greatly reducing the binding affinity (PubMed:15329343, PubMed:17721549, PubMed:24326773, PubMed:25787250). The effect on transcription regulation is depending upon the context in which it binds and diverse mechanisms of action include direct activation or repression, indirect activation or repression via cofactor recruitment, or activation or repression by disruption of binding sites or conformational DNA changes (PubMed:15329343, PubMed:17721549, PubMed:24326773, PubMed:25787250). Its activity is regulated by transcription factors and cytoplasmic proteins that have been shown to abrogate or completely inhibit YY1-mediated activation or repression (PubMed:15329343, PubMed:17721549, PubMed:24326773, PubMed:25787250). For example, it acts as a repressor in absence of adenovirus E1A protein but as an activator in its presence (PubMed:1655281). Acts synergistically with the SMAD1 and SMAD4 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression (PubMed:15329343). Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions (PubMed:15329343). May play an important role in development and differentiation. Proposed to recruit the PRC2/EED-EZH2 complex to target genes that are transcriptional repressed (PubMed:11158321). Involved in DNA repair (PubMed:18026119, PubMed:28575647). In vitro, binds to DNA recombination intermediate structures (Holliday junctions). Plays a role in regulating enhancer activation (PubMed:28575647). Recruits the PR-DUB complex to specific gene-regulatory regions (PubMed:20805357)", "gene_name": "YY1", "glycan_count": 1, "glycosylation_sites": [], "id": "P25490", "name": "Yin Yang 1 (YY1)", "organism": "Homo sapiens", "uniprot_id": "P25490" }, { "function": "The Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids", "gene_name": "B4GALT1", "glycan_count": 3, "glycosylation_sites": [ { "position": 113, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P15291", "name": "\u03b2-1,4-galactosyltransferase 1 (B4GALT1)", "organism": "Homo sapiens", "uniprot_id": "P15291" }, { "function": "", "gene_name": "TREM2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NZC2-2", "name": "Soluble TREM2", "organism": "Homo sapiens", "uniprot_id": "Q9NZC2-2" }, { "function": "Aquaglyceroporins form homotetrameric transmembrane channels, with each monomer independently mediating glycerol and water transport across the plasma membrane along their osmotic gradient (PubMed:12239222, PubMed:30420639). Could also be permeable to urea (By similarity). Also participates in cell permeability to H2O2 and H2O2-mediated signaling (PubMed:20724658). In skin, transports glycerol to the epidermis and stratum corneum, where it maintains hydration, elasticity, and supports lipid biosynthesis for barrier repair (By similarity). In kidney, contributes to the reabsorption of water, helping the body maintain proper fluid balance (By similarity)", "gene_name": "AQP3", "glycan_count": 0, "glycosylation_sites": [ { "position": 141, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q92482", "name": "Aquaporin-3 (AQP3)", "organism": "Homo sapiens", "uniprot_id": "Q92482" }, { "function": "May down-regulate host tetherin (BST2) by lysosomal degradation, thereby counteracting its antiviral activity", "gene_name": "S", "glycan_count": 17, "glycosylation_sites": [ { "position": 29, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 65, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 73, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 109, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 118, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 119, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 158, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 227, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 269, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 318, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 330, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 357, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 589, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 602, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 691, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 699, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 783, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1056, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1080, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1116, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1140, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1155, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1176, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P59594", "name": "SARS-CoV Spike Glycoprotein", "organism": "Severe acute respiratory syndrome coronavirus", "uniprot_id": "P59594" }, { "function": "Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vibronectin, tenascin, laminin, fibronectin, fibrin or casein. Also has dipeptidyl peptidase activity, exhibiting the ability to hydrolyze the prolyl bond two residues from the N-terminus of synthetic dipeptide substrates provided that the penultimate residue is proline, with a preference for Ala-Pro, Ile-Pro, Gly-Pro, Arg-Pro and Pro-Pro. Natural neuropeptide hormones for dipeptidyl peptidase are the neuropeptide Y (NPY), peptide YY (PYY), substance P (TAC1) and brain natriuretic peptide 32 (NPPB). The plasma membrane form, in association with either DPP4, PLAUR or integrins, is involved in the pericellular proteolysis of the extracellular matrix (ECM), and hence promotes cell adhesion, migration and invasion through the ECM. Plays a role in tissue remodeling during development and wound healing. Participates in the cell invasiveness towards the ECM in malignant melanoma cancers. Enhances tumor growth progression by increasing angiogenesis, collagen fiber degradation and apoptosis and by reducing antitumor response of the immune system. Promotes glioma cell invasion through the brain parenchyma by degrading the proteoglycan brevican. Acts as a tumor suppressor in melanocytic cells through regulation of cell proliferation and survival in a serine protease activity-independent manner", "gene_name": "Fap", "glycan_count": 3, "glycosylation_sites": [ { "position": 49, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 92, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 99, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 227, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 314, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 679, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P97321", "name": "Fibroblast Activation Protein (FAP)", "organism": "Mus musculus", "uniprot_id": "P97321" }, { "function": "Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity (PubMed:14699129, PubMed:14738735). Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore (PubMed:14699129, PubMed:14738735). The NDC80 complex synergistically enhances the affinity of the SKA1 complex for microtubules and may allow the NDC80 complex to track depolymerizing microtubules (PubMed:23085020)", "gene_name": "SPC25", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9HBM1", "name": "SET nuclear protein", "organism": "Homo sapiens", "uniprot_id": "Q9HBM1" }, { "function": "Has a strict specificity for hydrolysis of asparaginyl bonds (PubMed:23776206). Can also cleave aspartyl bonds slowly, especially under acidic conditions (PubMed:23776206). Involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system (PubMed:9872320). Also involved in MHC class I antigen presentation in cross-presenting dendritic cells by mediating cleavage and maturation of Perforin-2 (MPEG1), thereby promoting antigen translocation in the cytosol (By similarity). Required for normal lysosomal protein degradation in renal proximal tubules (By similarity). Required for normal degradation of internalized EGFR (By similarity). Plays a role in the regulation of cell proliferation via its role in EGFR degradation (By similarity)", "gene_name": "LGMN", "glycan_count": 31, "glycosylation_sites": [ { "position": 91, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 167, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 263, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 272, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q99538", "name": "Asparagine endopeptidase (AEP, Legumain)", "organism": "Homo sapiens", "uniprot_id": "Q99538" }, { "function": "Transcription factor that binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3') and displays two biological functions, as regulator of metabolic and redox processes under normal cellular conditions, and as master transcription factor during integrated stress response (ISR) (PubMed:16682973, PubMed:17684156, PubMed:31023583, PubMed:31444471, PubMed:32132707). Binds to asymmetric CRE's as a heterodimer and to palindromic CRE's as a homodimer (By similarity). Core effector of the ISR, which is required for adaptation to various stress such as endoplasmic reticulum (ER) stress, amino acid starvation, mitochondrial stress or oxidative stress (PubMed:31023583, PubMed:32132707). During ISR, ATF4 translation is induced via an alternative ribosome translation re-initiation mechanism in response to EIF2S1/eIF-2-alpha phosphorylation, and stress-induced ATF4 acts as a master transcription factor of stress-responsive genes in order to promote cell recovery (PubMed:31023583, PubMed:32132706, PubMed:32132707). Promotes the transcription of genes linked to amino acid sufficiency and resistance to oxidative stress to protect cells against metabolic consequences of ER oxidation (By similarity). Activates the transcription of NLRP1, possibly in concert with other factors in response to ER stress (PubMed:26086088). Activates the transcription of asparagine synthetase (ASNS) in response to amino acid deprivation or ER stress (PubMed:11960987). However, when associated with DDIT3/CHOP, the transcriptional activation of the ASNS gene is inhibited in response to amino acid deprivation (PubMed:18940792). Together with DDIT3/CHOP, mediates programmed cell death by promoting the expression of genes involved in cellular amino acid metabolic processes, mRNA translation and the terminal unfolded protein response (terminal UPR), a cellular response that elicits programmed cell death when ER stress is prolonged and unresolved (By similarity). Activates the expression of COX7A2L/SCAF1 downstream of the EIF2AK3/PERK-mediated unfolded protein response, thereby promoting formation of respiratory chain supercomplexes and increasing mitochondrial oxidative phosphorylation (PubMed:31023583). Together with DDIT3/CHOP, activates the transcription of the IRS-regulator TRIB3 and promotes ER stress-induced neuronal cell death by regulating the expression of BBC3/PUMA in response to ER stress (PubMed:15775988). May cooperate with the UPR transcriptional regulator QRICH1 to regulate ER protein homeostasis which is critical for cell viability in response to ER stress (PubMed:33384352). In the absence of stress, ATF4 translation is at low levels and it is required for normal metabolic processes such as embryonic lens formation, fetal liver hematopoiesis, bone development and synaptic plasticity (By similarity). Acts as a regulator of osteoblast differentiation in response to phosphorylation by RPS6KA3/RSK2: phosphorylation in osteoblasts enhances transactivation activity and promotes expression of osteoblast-specific genes and post-transcriptionally regulates the synthesis of Type I collagen, the main constituent of the bone matrix (PubMed:15109498). Cooperates with FOXO1 in osteoblasts to regulate glucose homeostasis through suppression of beta-cell production and decrease in insulin production (By similarity). Activates transcription of SIRT4 (By similarity). Regulates the circadian expression of the core clock component PER2 and the serotonin transporter SLC6A4 (By similarity). Binds in a circadian time-dependent manner to the cAMP response elements (CRE) in the SLC6A4 and PER2 promoters and periodically activates the transcription of these genes (By similarity). Mainly acts as a transcriptional activator in cellular stress adaptation, but it can also act as a transcriptional repressor: acts as a regulator of synaptic plasticity by repressing transcription, thereby inhibiting induction and maintenance of long-term memory (By similarity). Regulates synaptic functions via interaction with DISC1 in neurons, which inhibits ATF4 transcription factor activity by disrupting ATF4 dimerization and DNA-binding (PubMed:31444471)", "gene_name": "ATF4", "glycan_count": 1, "glycosylation_sites": [], "id": "P18848", "name": "ATF4", "organism": "Homo sapiens", "uniprot_id": "P18848" }, { "function": "Involved in the transfer of neutral lipids, including cholesteryl ester and triglyceride, among lipoprotein particles. Allows the net movement of cholesteryl ester from high density lipoproteins/HDL to triglyceride-rich very low density lipoproteins/VLDL, and the equimolar transport of triglyceride from VLDL to HDL (PubMed:24293641, PubMed:3281933, PubMed:3600759). Regulates the reverse cholesterol transport, by which excess cholesterol is removed from peripheral tissues and returned to the liver for elimination (PubMed:17237796)", "gene_name": "CETP", "glycan_count": 15, "glycosylation_sites": [ { "position": 105, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 257, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 358, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 413, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P11597", "name": "Cholesteryl ester transfer protein (CETP)", "organism": "Homo sapiens", "uniprot_id": "P11597" }, { "function": "Mediates the transfer of phospholipids and free cholesterol from triglyceride-rich lipoproteins (low density lipoproteins or LDL and very low density lipoproteins or VLDL) into high-density lipoproteins (HDL) as well as the exchange of phospholipids between triglyceride-rich lipoproteins themselves (PubMed:11013307, PubMed:19321130, PubMed:21515415, PubMed:29883800, PubMed:7654777, PubMed:9132017). Facilitates the transfer of a spectrum of different lipid molecules, including diacylglycerol, phosphatidic acid, sphingomyelin, phosphatidylcholine, phosphatidylinositol, phosphatidylglycerol, cerebroside and phosphatidyl ethanolamine (PubMed:9132017). Plays an important role in HDL remodeling which involves modulating the size and composition of HDL (PubMed:29883800). Also plays a key role in the uptake of cholesterol from peripheral cells and tissues that is subsequently transported to the liver for degradation and excretion (PubMed:21736953). Two distinct forms of PLTP exist in plasma: an active form that can transfer phosphatidylcholine from phospholipid vesicles to HDL, and an inactive form that lacks this capability (PubMed:11013307)", "gene_name": "PLTP", "glycan_count": 78, "glycosylation_sites": [ { "position": 64, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 94, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 117, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 143, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 245, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 398, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P55058", "name": "Phospholipid transfer protein (PLTP)", "organism": "Homo sapiens", "uniprot_id": "P55058" }, { "function": "Part of the TCR-CD3 complex present on T-lymphocyte cell surface that plays an essential role in adaptive immune response. When antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transmitted across the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3 chains contain immunoreceptor tyrosine-based activation motifs (ITAMs) in their cytoplasmic domain. Upon TCR engagement, these motifs become phosphorylated by Src family protein tyrosine kinases LCK and FYN, resulting in the activation of downstream signaling pathways (PubMed:2470098). In addition of this role of signal transduction in T-cell activation, CD3E plays an essential role in correct T-cell development. Initiates the TCR-CD3 complex assembly by forming the two heterodimers CD3D/CD3E and CD3G/CD3E. Also participates in internalization and cell surface down-regulation of TCR-CD3 complexes via endocytosis sequences present in CD3E cytosolic region (PubMed:10384095, PubMed:26507128). In addition to its role as a TCR coreceptor, it serves as a receptor for ITPRIPL1. Ligand recognition inhibits T-cell activation by promoting interaction with NCK1, which prevents CD3E-ZAP70 interaction and blocks the ERK-NFkB signaling cascade and calcium influx (PubMed:38614099)", "gene_name": "CD3E", "glycan_count": 1, "glycosylation_sites": [], "id": "P07766", "name": "CD3", "organism": "Homo sapiens", "uniprot_id": "P07766" }, { "function": "Tyrosine-protein kinase that acts as a cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of embryonic development, cell proliferation, differentiation and migration. Required for normal mesoderm patterning and correct axial organization during embryonic development, normal skeletogenesis and normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. Phosphorylates PLCG1, FRS2, GAB1 and SHB. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Promotes phosphorylation of SHC1, STAT1 and PTPN11/SHP2. In the nucleus, enhances RPS6KA1 and CREB1 activity and contributes to the regulation of transcription. FGFR1 signaling is down-regulated by IL17RD/SEF, and by FGFR1 ubiquitination, internalization and degradation", "gene_name": "FGFR1", "glycan_count": 15, "glycosylation_sites": [ { "position": 77, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 117, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 227, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 240, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 264, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 296, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 317, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 330, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P11362", "name": "FGFR1", "organism": "Homo sapiens", "uniprot_id": "P11362" }, { "function": "May be involved in processing of pneumocyte surfactant precursors", "gene_name": "NAPSA", "glycan_count": 76, "glycosylation_sites": [ { "position": 90, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 133, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 336, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O96009", "name": "Napsin A", "organism": "Homo sapiens", "uniprot_id": "O96009" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "varies by strain", "name": "Hemagglutinin (HA)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "multiple", "name": "Complement C5b-9 (MAC)", "organism": "", "uniprot_id": "" }, { "function": "Microtubule-associated protein with the capacity to bundle and stabilize microtubules (By similarity). May associate with chromosomes and promote the organization of mitotic spindle microtubules around them", "gene_name": "NUSAP1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9BXS6", "name": "Interleukin-32 (IL-32)", "organism": "Homo sapiens", "uniprot_id": "Q9BXS6" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P06756/P05106", "name": "Integrin \u03b1v\u03b23", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P06756/Q92626", "name": "Integrin \u03b1v\u03b26", "organism": "", "uniprot_id": "" }, { "function": "Cytosolic enzyme that catalyzes the carboxylation of acetyl-CoA to malonyl-CoA, the first and rate-limiting step of de novo fatty acid biosynthesis (PubMed:20457939, PubMed:20952656, PubMed:29899443). This is a 2 steps reaction starting with the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain followed by the transfer of the carboxyl group from carboxylated biotin to acetyl-CoA (PubMed:20457939, PubMed:20952656, PubMed:29899443)", "gene_name": "ACACA", "glycan_count": 1, "glycosylation_sites": [], "id": "Q13085", "name": "ACC (Acetyl-CoA carboxylase)", "organism": "Homo sapiens", "uniprot_id": "Q13085" }, { "function": "Key transcriptional regulator of type I interferon (IFN)-dependent immune responses which plays a critical role in the innate immune response against DNA and RNA viruses (PubMed:22394562, PubMed:24049179, PubMed:25636800, PubMed:27302953, PubMed:31340999, PubMed:36603579, PubMed:8524823). Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters (PubMed:11846977, PubMed:16846591, PubMed:16979567, PubMed:20049431, PubMed:32972995, PubMed:36603579, PubMed:8524823). Acts as a more potent activator of the IFN-beta (IFNB) gene than the IFN-alpha (IFNA) gene and plays a critical role in both the early and late phases of the IFNA/B gene induction (PubMed:16846591, PubMed:16979567, PubMed:20049431, PubMed:36603579). Found in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, is phosphorylated by IKBKE and TBK1 kinases (PubMed:22394562, PubMed:25636800, PubMed:27302953, PubMed:36603579). This induces a conformational change, leading to its dimerization and nuclear localization and association with CREB binding protein (CREBBP) to form dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I IFN and ISG genes (PubMed:16154084, PubMed:27302953, PubMed:33440148, PubMed:36603579). Can activate distinct gene expression programs in macrophages and can induce significant apoptosis in primary macrophages (PubMed:16846591). In response to Sendai virus infection, is recruited by TOMM70:HSP90AA1 to mitochondrion and forms an apoptosis complex TOMM70:HSP90AA1:IRF3:BAX inducing apoptosis (PubMed:25609812). Key transcription factor regulating the IFN response during SARS-CoV-2 infection (PubMed:33440148)", "gene_name": "IRF3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q14653", "name": "IRF3", "organism": "Homo sapiens", "uniprot_id": "Q14653" }, { "function": "Receptor for class I MHC antigens. Recognizes a broad spectrum of HLA-A, HLA-B, HLA-C, HLA-G and HLA-F alleles (PubMed:16455647, PubMed:28636952). Receptor for H301/UL18, a human cytomegalovirus class I MHC homolog. Ligand binding results in inhibitory signals and down-regulation of the immune response. Engagement of LILRB1 present on natural killer cells or T-cells by class I MHC molecules protects the target cells from lysis. Interaction with HLA-B or HLA-E leads to inhibition of FCER1A signaling and serotonin release. Inhibits FCGR1A-mediated phosphorylation of cellular proteins and mobilization of intracellular calcium ions (PubMed:11907092, PubMed:9285411, PubMed:9842885). Recognizes HLA-G in complex with B2M/beta-2 microglobulin and a nonamer self-peptide (PubMed:16455647). Upon interaction with peptide-bound HLA-G-B2M complex, triggers secretion of growth-promoting factors by decidual NK cells (PubMed:19304799, PubMed:29262349). Reprograms B cells toward an immune suppressive phenotype (PubMed:24453251)", "gene_name": "LILRB1", "glycan_count": 11, "glycosylation_sites": [ { "position": 281, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 302, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 341, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8NHL6", "name": "Leukocyte Immunoglobulin-Like Receptor Subfamily B2 (LILRB2)", "organism": "Homo sapiens", "uniprot_id": "Q8NHL6" }, { "function": "Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are DNA repair and redox regulation of transcriptional factors (PubMed:11118054, PubMed:11452037, PubMed:15831793, PubMed:18439621, PubMed:18579163, PubMed:21762700, PubMed:24079850, PubMed:8355688, PubMed:9108029, PubMed:9560228). Functions as an apurinic/apyrimidinic (AP) endodeoxyribonuclease in the base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Also incises at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules (PubMed:15380100, PubMed:16617147, PubMed:18439621, PubMed:19123919, PubMed:19188445, PubMed:19934257, PubMed:20699270, PubMed:21762700, PubMed:24079850, PubMed:8932375, PubMed:8995436, PubMed:9804799). Operates at switch sites of immunoglobulin (Ig) constant regions where it mediates Ig isotype class switch recombination. Processes AP sites induced by successive action of AICDA and UNG. Generates staggered nicks in opposite DNA strands resulting in the formation of double-strand DNA breaks that are finally resolved via non-homologous end joining repair pathway (By similarity). Has 3'-5' exodeoxyribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER (PubMed:11832948, PubMed:1719477). Possesses DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate and 8-oxoguanine) blocking the 3' side of DNA strand breaks (PubMed:15831793, PubMed:7516064). Also acts as an endoribonuclease involved in the control of single-stranded RNA metabolism. Plays a role in regulating MYC mRNA turnover by preferentially cleaving in between UA and CA dinucleotides of the MYC coding region determinant (CRD). In association with NMD1, plays a role in the rRNA quality control process during cell cycle progression (PubMed:19188445, PubMed:19401441, PubMed:21762700). Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB (PubMed:9207062). Exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR (PubMed:10023679, PubMed:11118054, PubMed:11452037, PubMed:18579163, PubMed:8355688, PubMed:9108029). Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs). Together with HNRNPL or the dimer XRCC5/XRCC6, associates with nCaRE, acting as an activator of transcriptional repression (PubMed:11809897, PubMed:14633989, PubMed:8621488). May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation (PubMed:21496894). Stimulates the YBX1-mediated MDR1 promoter activity, when acetylated at Lys-6 and Lys-7, leading to drug resistance (PubMed:18809583). Plays a role in protection from granzyme-mediated cellular repair leading to cell death (PubMed:18179823). Binds DNA and RNA. Associates, together with YBX1, on the MDR1 promoter. Together with NPM1, associates with rRNA (PubMed:19188445, PubMed:19401441, PubMed:20699270)", "gene_name": "APEX1", "glycan_count": 2, "glycosylation_sites": [], "id": "P27695", "name": "Apurinic/apyrimidinic endonuclease 1 (APE1)", "organism": "Homo sapiens", "uniprot_id": "P27695" }, { "function": "Potent inhibitor of the complement membrane attack complex (MAC) action, which protects human cells from damage during complement activation (PubMed:11882685, PubMed:1698710, PubMed:2475111, PubMed:2475570, PubMed:2606909, PubMed:9053451). Acts by binding to the beta-haipins of C8 (C8A and C8B) components of the assembling MAC, forming an intermolecular beta-sheet that prevents incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore (PubMed:11882685, PubMed:1698710, PubMed:36797260)", "gene_name": "CD59", "glycan_count": 226, "glycosylation_sites": [ { "position": 43, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 66, "type": "N-linked (Glc) (glycation) lysine" }, { "position": 76, "type": "O-linked (GalNAc...) threonine" }, { "position": 77, "type": "O-linked (GalNAc...) threonine" } ], "id": "P13987", "name": "CD59", "organism": "Homo sapiens", "uniprot_id": "P13987" }, { "function": "", "gene_name": "SED5", "glycan_count": 0, "glycosylation_sites": [], "id": "A7A0T2", "name": "Akkermansia muciniphila", "organism": "Saccharomyces cerevisiae (strain YJM789)", "uniprot_id": "A7A0T2" }, { "function": "", "gene_name": "DKFZp547P193", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UPU0", "name": "Transferrin Receptor 2 (TfR2)", "organism": "Homo sapiens", "uniprot_id": "Q9UPU0" }, { "function": "Inhibitory receptor for the CD200/OX2 cell surface glycoprotein. Limits inflammation by inhibiting the expression of pro-inflammatory molecules including TNF-alpha, interferons, and inducible nitric oxide synthase (iNOS) in response to selected stimuli. Also binds to HHV-8 K14 viral CD200 homolog with identical affinity and kinetics as the host CD200", "gene_name": "CD200R1", "glycan_count": 10, "glycosylation_sites": [ { "position": 31, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 60, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 69, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 116, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 122, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 185, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 218, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 233, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 247, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8TD46", "name": "CD200 Receptor 1", "organism": "Homo sapiens", "uniprot_id": "Q8TD46" }, { "function": "Acts both as a substrate recognition component of E3 ubiquitin-protein ligase complexes and as an atypical serine/threonine-protein kinase, playing key roles in various processes such as cell cycle, telomerase regulation and histone modification. Probable substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, named CUL4A-RBX1-DDB1-DCAF1/VPRBP complex, which mediates ubiquitination and proteasome-dependent degradation of proteins such as NF2 (PubMed:23063525). Involved in the turnover of methylated proteins: recognizes and binds methylated proteins via its chromo domain, leading to ubiquitination of target proteins by the RBX1-DDB1-DCAF1/VPRBP complex (PubMed:23063525). The CUL4A-RBX1-DDB1-DCAF1/VPRBP complex is also involved in B-cell development: DCAF1 is recruited by RAG1 to ubiquitinate proteins, leading to limit error-prone repair during V(D)J recombination (By similarity). Also part of the EDVP complex, an E3 ligase complex that mediates ubiquitination of proteins such as TERT, leading to TERT degradation and telomerase inhibition (PubMed:19287380, PubMed:23362280). The EDVP complex also mediates ubiquitination and degradation of CCP110 (PubMed:28242748, PubMed:34259627). Also acts as an atypical serine/threonine-protein kinase that specifically mediates phosphorylation of 'Thr-120' of histone H2A (H2AT120ph) in a nucleosomal context, thereby repressing transcription (PubMed:24140421). H2AT120ph is present in the regulatory region of many tumor suppresor genes, down-regulates their transcription and is present at high level in a number of tumors (PubMed:24140421). Involved in JNK-mediated apoptosis during cell competition process via its interaction with LLGL1 and LLGL2 (PubMed:20644714). By acting on TET dioxygenses, essential for oocyte maintenance at the primordial follicle stage, hence essential for female fertility (By similarity)", "gene_name": "DCAF1", "glycan_count": 3, "glycosylation_sites": [], "id": "Q9Y4B6", "name": "Exocyst complex component 3", "organism": "Homo sapiens", "uniprot_id": "Q9Y4B6" }, { "function": "Dual cyclooxygenase and peroxidase that plays an important role in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate, AA, C20:4(n-6)), with a particular role in the inflammatory response. The cyclooxygenase activity oxygenates AA to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide prostaglandin H2 (PGH2), the precursor of all 2-series prostaglandins and thromboxanes. This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons (PubMed:7947975). Involved in the constitutive production of prostanoids in particular in the stomach and platelets. In gastric epithelial cells, it is a key step in the generation of prostaglandins, such as prostaglandin E2 (PGE2), which plays an important role in cytoprotection. In platelets, it is involved in the generation of thromboxane A2 (TXA2), which promotes platelet activation and aggregation, vasoconstriction and proliferation of vascular smooth muscle cells (Probable). Can also use linoleate (LA, (9Z,12Z)-octadecadienoate, C18:2(n-6)) as substrate and produce hydroxyoctadecadienoates (HODEs) in a regio- and stereospecific manner, being (9R)-HODE ((9R)-hydroxy-(10E,12Z)-octadecadienoate) and (13S)-HODE ((13S)-hydroxy-(9Z,11E)-octadecadienoate) its major products (By similarity)", "gene_name": "PTGS1", "glycan_count": 7, "glycosylation_sites": [ { "position": 67, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 103, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 143, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P23219", "name": "PTGS1 (COX-1)", "organism": "Homo sapiens", "uniprot_id": "P23219" }, { "function": "Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [ { "position": 183, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 347, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 433, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 904, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 981, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1189, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 2302, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 2306, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 2458, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P33478", "name": "Dengue virus NS1 protein", "organism": "Dengue virus type 1 (strain Singapore/S275/1990)", "uniprot_id": "P33478" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8JIG5 (chicken)", "name": "Alpha-1-acid glycoprotein (AGP)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01876 (chicken)", "name": "Immunoglobulin A (IgA)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01871 (chicken)", "name": "Immunoglobulin M (IgM)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01756 (chicken)", "name": "Interferon-gamma (IFN-\u03b3)", "organism": "", "uniprot_id": "" }, { "function": "Coreceptor for IL1RL2 in the IL-36 signaling system (By similarity). Coreceptor with IL1R1 in the IL-1 signaling system. Associates with IL1R1 bound to IL1B to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B and other pathways. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. Recruits TOLLIP to the signaling complex. Does not bind to interleukin-1 alone; binding of IL1RN to IL1R1, prevents its association with IL1R1 to form a signaling complex. The cellular response is modulated through a non-signaling association with the membrane IL1R2 decoy receptor. Coreceptor for IL1RL1 in the IL-33 signaling system. Can bidirectionally induce pre- and postsynaptic differentiation of neurons by trans-synaptically binding to PTPRD (By similarity). May play a role in IL1B-mediated costimulation of IFNG production from T-helper 1 (Th1) cells (Probable)", "gene_name": "IL1RAP", "glycan_count": 20, "glycosylation_sites": [ { "position": 57, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 107, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 111, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 118, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 196, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 209, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 299, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NPH3", "name": "IL1RAP", "organism": "Homo sapiens", "uniprot_id": "Q9NPH3" }, { "function": "Adapter protein involved in the Toll-like receptor and IL-1 receptor signaling pathway in the innate immune response (PubMed:15361868, PubMed:18292575, PubMed:33718825, PubMed:37971847). Acts via IRAK1, IRAK2, IRF7 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (PubMed:15361868, PubMed:19506249, PubMed:24316379). Increases IL-8 transcription (PubMed:9013863). Involved in IL-18-mediated signaling pathway. Activates IRF1 resulting in its rapid migration into the nucleus to mediate an efficient induction of IFN-beta, NOS2/INOS, and IL12A genes. Upon TLR8 activation by GU-rich single-stranded RNA (GU-rich RNA) derived from viruses such as SARS-CoV-2, SARS-CoV and HIV-1, induces IL1B release through NLRP3 inflammasome activation (PubMed:33718825). MyD88-mediated signaling in intestinal epithelial cells is crucial for maintenance of gut homeostasis and controls the expression of the antimicrobial lectin REG3G in the small intestine (By similarity)", "gene_name": "MYD88", "glycan_count": 1, "glycosylation_sites": [], "id": "Q99836", "name": "MyD88", "organism": "Homo sapiens", "uniprot_id": "Q99836" }, { "function": "Binds EGFR, the EGF receptor, inducing EGFR autophosphorylation and the activation of downstream signaling pathways. May play a role in cell adhesion and migration. May function as a negative regulator of chondrocyte differentiation. In the olfactory epithelium, it may regulate glial cell migration, differentiation and the ability of glial cells to support neuronal neurite outgrowth", "gene_name": "EFEMP1", "glycan_count": 8, "glycosylation_sites": [ { "position": 249, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q12805", "name": "Fibulin-3", "organism": "Homo sapiens", "uniprot_id": "Q12805" }, { "function": "Histone chaperone that plays a role in the nuclear import of H2A-H2B and nucleosome assembly (PubMed:20002496, PubMed:21211722, PubMed:26841755). Also participates in several important DNA repair mechanisms: greatly enhances ERCC6-mediated chromatin remodeling which is essential for transcription-coupled nucleotide excision DNA repair (PubMed:28369616). Also stimulates homologous recombination (HR) by RAD51 and RAD54 which is essential in mitotic DNA double strand break (DSB) repair (PubMed:24798879). Plays a key role in the regulation of embryonic neurogenesis (By similarity). Promotes the proliferation of neural progenitors and inhibits neuronal differentiation during cortical development (By similarity). Regulates neurogenesis via the modulation of RASSF10; regulates RASSF10 expression by promoting SETD1A-mediated H3K4 methylation at the RASSF10 promoter (By similarity)", "gene_name": "NAP1L1", "glycan_count": 1, "glycosylation_sites": [], "id": "P55209", "name": "CD157", "organism": "Homo sapiens", "uniprot_id": "P55209" }, { "function": "", "gene_name": "MSLN", "glycan_count": 0, "glycosylation_sites": [], "id": "Q13421-2", "name": "Megakaryocyte Potentiating Factor (MPF)", "organism": "Homo sapiens", "uniprot_id": "Q13421-2" }, { "function": "Calcium-binding protein involved in calcium homeostasis and signal transduction. It plays a critical role in buffering intracellular calcium levels and modulating calcium-dependent signaling pathways (PubMed:2001709). Predominantly expressed in specific neuronal populations, influences synaptic plasticity and neuronal excitability, contributing to learning and memory (By similarity). During embryonic development, it facilitates neuronal differentiation and maturation (By similarity)", "gene_name": "CALB2", "glycan_count": 0, "glycosylation_sites": [], "id": "P22676", "name": "Calretinin", "organism": "Homo sapiens", "uniprot_id": "P22676" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P20701/P05107", "name": "LFA-1 (Integrin \u03b1L\u03b22)", "organism": "", "uniprot_id": "" }, { "function": "E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage (PubMed:10500182, PubMed:12887909, PubMed:12890688, PubMed:14976165, PubMed:16818604, PubMed:17525340, PubMed:19261748). It is unclear whether it also mediates the formation of other types of polyubiquitin chains (PubMed:12890688). The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability (PubMed:12890688, PubMed:14976165, PubMed:20351172). Regulates centrosomal microtubule nucleation (PubMed:18056443). Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle (PubMed:10724175, PubMed:11836499, PubMed:12183412, PubMed:19261748). Required for FANCD2 targeting to sites of DNA damage (PubMed:12887909). Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation (PubMed:16326698). Contributes to homologous recombination repair (HRR) via its direct interaction with PALB2, fine-tunes recombinational repair partly through its modulatory role in the PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks (PubMed:19369211). Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage via BRCA1-mediated ubiquitination of RBBP8 (PubMed:16818604). Acts as a transcriptional activator (PubMed:20160719)", "gene_name": "BRCA1", "glycan_count": 4, "glycosylation_sites": [], "id": "P38398", "name": "BRCA1", "organism": "Homo sapiens", "uniprot_id": "P38398" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P31749/P31751/P31751", "name": "Akt (Protein Kinase B)", "organism": "", "uniprot_id": "" }, { "function": "Endogenous F(1)F(o)-ATPase inhibitor limiting ATP depletion when the mitochondrial membrane potential falls below a threshold and the F(1)F(o)-ATP synthase starts hydrolyzing ATP to pump protons out of the mitochondrial matrix. Required to avoid the consumption of cellular ATP when the F(1)F(o)-ATP synthase enzyme acts as an ATP hydrolase. Indirectly acts as a regulator of heme synthesis in erythroid tissues: regulates heme synthesis by modulating the mitochondrial pH and redox potential, allowing FECH to efficiently catalyze the incorporation of iron into protoporphyrin IX to produce heme", "gene_name": "ATP5IF1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UII2", "name": "ATPase inhibitory factor 1 (IF1)", "organism": "Homo sapiens", "uniprot_id": "Q9UII2" }, { "function": "Widely expressed membrane-bound protein which acts as a ligand to stimulate an activating receptor KLRK1/NKG2D, expressed on the surface of essentially all human natural killer (NK), gammadelta T and CD8 alphabeta T-cells (PubMed:11491531, PubMed:11777960). Up-regulated in stressed conditions, such as viral and bacterial infections or DNA damage response, serves as signal of cellular stress, and engagement of KLRK1/NKG2D by MICA triggers NK-cells resulting in a range of immune effector functions, such as cytotoxicity and cytokine production (PubMed:10426993)", "gene_name": "MICA", "glycan_count": 7, "glycosylation_sites": [ { "position": 31, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 79, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 210, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 220, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 261, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q29983", "name": "MICA", "organism": "Homo sapiens", "uniprot_id": "Q29983" }, { "function": "Alcohol dehydrogenase. Exhibits high activity for ethanol oxidation and plays a major role in ethanol catabolism", "gene_name": "ADH1C", "glycan_count": 1, "glycosylation_sites": [], "id": "P00326", "name": "ADH1C", "organism": "Homo sapiens", "uniprot_id": "P00326" }, { "function": "Catalyzes the NAD-dependent oxidation of all-trans-retinol and its derivatives such as all-trans-4-hydroxyretinol and may participate in retinoid metabolism (PubMed:15369820, PubMed:16787387). In vitro can also catalyze the NADH-dependent reduction of all-trans-retinal and its derivatives such as all-trans-4-oxoretinal (PubMed:15369820, PubMed:16787387). Catalyzes in the oxidative direction with higher efficiency (PubMed:16787387). Has the same affinity for all-trans-4-hydroxyretinol and all-trans-4-oxoretinal (PubMed:15369820)", "gene_name": "ADH1B", "glycan_count": 1, "glycosylation_sites": [], "id": "P00325", "name": "ADH1B", "organism": "Homo sapiens", "uniprot_id": "P00325" }, { "function": "Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell", "gene_name": "CPS1", "glycan_count": 5, "glycosylation_sites": [ { "position": 537, "type": "O-linked (GlcNAc) serine; alternate" }, { "position": 1331, "type": "O-linked (GlcNAc) serine" }, { "position": 1332, "type": "O-linked (GlcNAc) threonine" } ], "id": "P31327", "name": "CPS1", "organism": "Homo sapiens", "uniprot_id": "P31327" }, { "function": "Catalyzes the GTP-dependent ribosomal translocation step during translation elongation (PubMed:26593721). During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively (PubMed:26593721). Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (PubMed:26593721)", "gene_name": "EEF2", "glycan_count": 3, "glycosylation_sites": [], "id": "P13639", "name": "EEF2", "organism": "Homo sapiens", "uniprot_id": "P13639" }, { "function": "Pyruvate kinase that catalyzes the conversion of phosphoenolpyruvate to pyruvate with the synthesis of ATP, and which plays a key role in glycolysis", "gene_name": "PKLR", "glycan_count": 1, "glycosylation_sites": [], "id": "P30613", "name": "PKLR", "organism": "Homo sapiens", "uniprot_id": "P30613" }, { "function": "", "gene_name": "sgta-prov", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6P2W1", "name": "RPL13A", "organism": "Xenopus tropicalis", "uniprot_id": "Q6P2W1" }, { "function": "Catalyzes the hydrolysis of nucleotide monophosphates, releasing inorganic phosphate and the corresponding nucleoside, with AMP being the preferred substrate (PubMed:21933152, PubMed:22997138, PubMed:23142347, PubMed:24887587, PubMed:34403084). Shows a preference for ribonucleotide monophosphates over their equivalent deoxyribose forms (PubMed:34403084). Other substrates include IMP, UMP, GMP, CMP, dAMP, dCMP, dTMP, NAD and NMN (PubMed:21933152, PubMed:22997138, PubMed:23142347, PubMed:24887587, PubMed:34403084)", "gene_name": "NT5E", "glycan_count": 25, "glycosylation_sites": [ { "position": 53, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 311, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 333, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 403, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P21589", "name": "NT5E", "organism": "Homo sapiens", "uniprot_id": "P21589" }, { "function": "Probable Na(+)/H(+) antiporter", "gene_name": "TMCO3", "glycan_count": 8, "glycosylation_sites": [ { "position": 206, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 230, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6UWJ1", "name": "LRG1", "organism": "Homo sapiens", "uniprot_id": "Q6UWJ1" }, { "function": "Catalyzes the transfer of a methyl group from methylcob(III)alamin (MeCbl) to homocysteine, yielding enzyme-bound cob(I)alamin and methionine in the cytosol (PubMed:16769880, PubMed:17288554, PubMed:27771510). MeCbl is an active form of cobalamin (vitamin B12) used as a cofactor for methionine biosynthesis. Cob(I)alamin form is regenerated to MeCbl by a transfer of a methyl group from 5-methyltetrahydrofolate (PubMed:16769880, PubMed:17288554, PubMed:27771510). The processing of cobalamin in the cytosol occurs in a multiprotein complex composed of at least MMACHC, MMADHC, MTRR (methionine synthase reductase) and MTR which may contribute to shuttle safely and efficiently cobalamin towards MTR in order to produce methionine (PubMed:16769880, PubMed:27771510)", "gene_name": "MTR", "glycan_count": 0, "glycosylation_sites": [], "id": "Q99723", "name": "MDK", "organism": "Homo sapiens", "uniprot_id": "Q99707" }, { "function": "Receptor for the chemotactic and inflammatory C3a, C4a and C5a anaphylatoxin peptides and also for their dearginated forms ASP/C3adesArg, C4adesArg and C5adesArg respectively. Couples weakly to G(i)-mediated signaling pathways", "gene_name": "C5AR2", "glycan_count": 0, "glycosylation_sites": [ { "position": 3, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9P296", "name": "GPR77 (C5aR2)", "organism": "Homo sapiens", "uniprot_id": "Q9P296" }, { "function": "Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types", "gene_name": "CDH3", "glycan_count": 0, "glycosylation_sites": [ { "position": 200, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 566, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P22223", "name": "P-cadherin", "organism": "Homo sapiens", "uniprot_id": "P22223" }, { "function": "Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P13548", "name": "N-cadherin", "organism": "Vigna radiata var. radiata", "uniprot_id": "P13548" }, { "function": "Nuclear receptor for calcitriol, the active form of vitamin D3 which mediates the action of this vitamin on cells (PubMed:10678179, PubMed:15728261, PubMed:16913708, PubMed:28698609, PubMed:37478846). Enters the nucleus upon vitamin D3 binding where it forms heterodimers with the retinoid X receptor/RXR (PubMed:28698609). The VDR-RXR heterodimers bind to specific response elements on DNA and activate the transcription of vitamin D3-responsive target genes (PubMed:28698609). Plays a central role in calcium homeostasis (By similarity). Also functions as a receptor for the secondary bile acid lithocholic acid (LCA) and its metabolites (PubMed:12016314, PubMed:32354638)", "gene_name": "VDR", "glycan_count": 1, "glycosylation_sites": [], "id": "P11473", "name": "VDR (Vitamin D Receptor)", "organism": "Homo sapiens", "uniprot_id": "P11473" }, { "function": "Transcription factor that plays a central role in developing and mature glia (By similarity). Specifically activates expression of myelin genes, during oligodendrocyte (OL) maturation, such as DUSP15 and MYRF, thereby playing a central role in oligodendrocyte maturation and CNS myelination (By similarity). Once induced, MYRF cooperates with SOX10 to implement the myelination program (By similarity). Transcriptional activator of MITF, acting synergistically with PAX3 (PubMed:21965087). Transcriptional activator of MBP, via binding to the gene promoter (By similarity)", "gene_name": "SOX10", "glycan_count": 0, "glycosylation_sites": [], "id": "P56693", "name": "SOX10", "organism": "Homo sapiens", "uniprot_id": "P56693" }, { "function": "Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and acts as a stem cell marker of the intestinal epithelium and the hair follicle. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. In contrast to classical G-protein coupled receptors, does not activate heterotrimeric G-proteins to transduce the signal. Involved in the development and/or maintenance of the adult intestinal stem cells during postembryonic development", "gene_name": "LGR5", "glycan_count": 0, "glycosylation_sites": [ { "position": 63, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 77, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 208, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 500, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 792, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O75473", "name": "LGR5", "organism": "Homo sapiens", "uniprot_id": "O75473" }, { "function": "Receptor for erythropoietin, which mediates erythropoietin-induced erythroblast proliferation and differentiation (PubMed:10388848, PubMed:2163695, PubMed:2163696, PubMed:8662939, PubMed:9774108). Upon EPO stimulation, EPOR dimerizes triggering the JAK2/STAT5 signaling cascade (By similarity). In some cell types, can also activate STAT1 and STAT3 (PubMed:11756159). May also activate the LYN tyrosine kinase (By similarity)", "gene_name": "EPOR", "glycan_count": 0, "glycosylation_sites": [ { "position": 76, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P19235", "name": "EPO Receptor (EPO-R)", "organism": "Homo sapiens", "uniprot_id": "P19235" }, { "function": "Protein kinase involved in the transduction of mitogenic signals from the cell membrane to the nucleus (Probable). Phosphorylates MAP2K1, and thereby activates the MAP kinase signal transduction pathway (PubMed:21441910, PubMed:29433126). Phosphorylates PFKFB2 (PubMed:36402789). May play a role in the postsynaptic responses of hippocampal neurons (PubMed:1508179)", "gene_name": "BRAF", "glycan_count": 0, "glycosylation_sites": [], "id": "P15056", "name": "BRAF", "organism": "Homo sapiens", "uniprot_id": "P15056" }, { "function": "Catalyzes the NADP(+)-dependent oxidative decarboxylation of isocitrate (D-threo-isocitrate) to 2-ketoglutarate (2-oxoglutarate), which is required by other enzymes such as the phytanoyl-CoA dioxygenase (PubMed:10521434, PubMed:19935646). Plays a critical role in the generation of NADPH, an important cofactor in many biosynthesis pathways (PubMed:10521434). May act as a corneal epithelial crystallin and may be involved in maintaining corneal epithelial transparency (By similarity)", "gene_name": "IDH1", "glycan_count": 2, "glycosylation_sites": [], "id": "O75874", "name": "Isocitrate dehydrogenase 1 (IDH1)", "organism": "Homo sapiens", "uniprot_id": "O75874" }, { "function": "Plays a role in intermediary metabolism and energy production (PubMed:19228619, PubMed:22416140). It may tightly associate or interact with the pyruvate dehydrogenase complex (PubMed:19228619, PubMed:22416140)", "gene_name": "IDH2", "glycan_count": 1, "glycosylation_sites": [], "id": "P48735", "name": "Isocitrate dehydrogenase 2 (IDH2)", "organism": "Homo sapiens", "uniprot_id": "P48735" }, { "function": "May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism", "gene_name": "APOA2", "glycan_count": 5, "glycosylation_sites": [], "id": "P02652", "name": "Low-Density Lipoprotein (LDL)", "organism": "Homo sapiens", "uniprot_id": "P02652" }, { "function": "Growth factor of the TGF-beta superfamily that plays essential roles in many developmental processes, including neurogenesis, vascular development, angiogenesis and osteogenesis (PubMed:31363885). Acts in concert with PTHLH/PTHRP to stimulate ductal outgrowth during embryonic mammary development and to inhibit hair follicle induction (By similarity). Initiates the canonical BMP signaling cascade by associating with type I receptor BMPR1A and type II receptor BMPR2 (PubMed:25868050, PubMed:8006002). Once all three components are bound together in a complex at the cell surface, BMPR2 phosphorylates and activates BMPR1A. In turn, BMPR1A propagates signal by phosphorylating SMAD1/5/8 that travel to the nucleus and act as activators and repressors of transcription of target genes (PubMed:25868050, PubMed:29212066). Positively regulates the expression of odontogenic development regulator MSX1 via inducing the IPO7-mediated import of SMAD1 to the nucleus (By similarity). Required for MSX1-mediated mesenchymal molar tooth bud development beyond the bud stage, via promoting Wnt signaling (By similarity). Acts as a positive regulator of odontoblast differentiation during mesenchymal tooth germ formation, expression is repressed during the bell stage by MSX1-mediated inhibition of CTNNB1 signaling (By similarity). Able to induce its own expression in dental mesenchymal cells and also in the neighboring dental epithelial cells via an MSX1-mediated pathway (By similarity). Can also signal through non-canonical BMP pathways such as ERK/MAP kinase, PI3K/Akt, or SRC cascades (PubMed:31363885). For example, induces SRC phosphorylation which, in turn, activates VEGFR2, leading to an angiogenic response (PubMed:31363885)", "gene_name": "BMP4", "glycan_count": 1, "glycosylation_sites": [ { "position": 143, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 208, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 350, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 365, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P12644", "name": "Bone Morphogenetic Protein 4 (BMP4)", "organism": "Homo sapiens", "uniprot_id": "P12644" }, { "function": "Transcriptional activator essential for osteoblast differentiation (PubMed:23457570). Binds to SP1 and EKLF consensus sequences and to other G/C-rich sequences (By similarity)", "gene_name": "SP7", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8TDD2", "name": "Osterix (OSX/SP7)", "organism": "Homo sapiens", "uniprot_id": "Q8TDD2" }, { "function": "Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins", "gene_name": "INHA", "glycan_count": 0, "glycosylation_sites": [ { "position": 146, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 268, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 302, "type": "N-linked (GlcNAc...) asparagine; partial" } ], "id": "P05111", "name": "Inhibin B", "organism": "Homo sapiens", "uniprot_id": "P05111" }, { "function": "", "gene_name": "4.3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9T125", "name": "VEGF-B", "organism": "Yersinia phage phiYeO3-12", "uniprot_id": "Q9T125" }, { "function": "Growth factor active in angiogenesis, lymphangiogenesis and endothelial cell growth, stimulating their proliferation and migration and also has effects on the permeability of blood vessels. May function in the formation of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentiated lymphatic endothelium in adults. Binds and activates VEGFR-2 (KDR/FLK1) and VEGFR-3 (FLT4) receptors", "gene_name": "VEGFD", "glycan_count": 1, "glycosylation_sites": [ { "position": 155, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 185, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 287, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O43915", "name": "VEGF-D", "organism": "Homo sapiens", "uniprot_id": "O43915" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01127/P01137", "name": "PDGF-AB/BB", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P08228 (rat)", "name": "Superoxide Dismutase (SOD)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P24270 (rat)", "name": "Catalase (CAT)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P00432 (rat)", "name": "Glutathione Peroxidase (GPx)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01308 (rat)", "name": "Insulin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02750 (human APOB)", "name": "Low-Density Lipoprotein (LDL)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02647 (human APOA1)", "name": "High-Density Lipoprotein (HDL)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02770 (rat)", "name": "Albumin", "organism": "", "uniprot_id": "" }, { "function": "Acts as a transcriptional coactivator of estrogen and progesterone receptors (ESR1 and PGR) upon hormone activation (PubMed:16772533). In presence of estrogen, binds to ESR1-responsive promoters (PubMed:16772533). Synergizes with YAP1 to enhance PGR activity (PubMed:16772533). Modulates expression of post-synaptic scaffolding proteins via regulation of ESR1, ESR2 and PGR (By similarity)", "gene_name": "WBP2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q969T9", "name": "Afamin", "organism": "Homo sapiens", "uniprot_id": "Q969T9" }, { "function": "Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negative regulator of osteogenesis. Blocks the nuclear translocation of the phosphorylated form (by AKT1) of SRPK2 and antagonizes its stimulatory effect on cyclin D1 expression resulting in blockage of neuronal apoptosis elicited by SRPK2. Negative regulator of signaling cascades that mediate activation of MAP kinases via AKAP13", "gene_name": "YWHAB", "glycan_count": 1, "glycosylation_sites": [], "id": "P31946", "name": "14-3-3 protein", "organism": "Homo sapiens", "uniprot_id": "P31946" }, { "function": "Immunophilin protein with PPIase and co-chaperone activities. Component of steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments. The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Also acts as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role against oxidative stress in mitochondria", "gene_name": "FKBP4", "glycan_count": 1, "glycosylation_sites": [], "id": "Q02790", "name": "Relaxin-2 (RLN2)", "organism": "Homo sapiens", "uniprot_id": "Q02790" }, { "function": "Plays a role in the structural integrity of cartilage via its interaction with other extracellular matrix proteins such as the collagens and fibronectin. Can mediate the interaction of chondrocytes with the cartilage extracellular matrix through interaction with cell surface integrin receptors (PubMed:16051604, PubMed:16542502). Could play a role in the pathogenesis of osteoarthritis (PubMed:16542502). Potent suppressor of apoptosis in both primary chondrocytes and transformed cells. Suppresses apoptosis by blocking the activation of caspase-3 and by inducing the IAP family of survival proteins (BIRC3, BIRC2, BIRC5 and XIAP) (PubMed:17993464). Essential for maintaining a vascular smooth muscle cells (VSMCs) contractile/differentiated phenotype under physiological and pathological stimuli. Maintains this phenotype of VSMCs by interacting with ITGA7 (By similarity)", "gene_name": "COMP", "glycan_count": 20, "glycosylation_sites": [ { "position": 121, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 742, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P49747", "name": "COMP (Cartilage Oligomeric Matrix Protein)", "organism": "Homo sapiens", "uniprot_id": "P49747" }, { "function": "Activity is required in presynaptic neurons, in a dose-dependent manner, for normal presynaptic development and morphology (PubMed:15707898). Plays a role in the formation of muscle connections, also called muscle arm extensions, between the body wall and the motor axons in the dorsal and ventral cord (PubMed:27123983)", "gene_name": "mkk-4", "glycan_count": 0, "glycosylation_sites": [], "id": "Q20347", "name": "CXCL9 (MIG)", "organism": "Caenorhabditis elegans", "uniprot_id": "Q20347" }, { "function": "Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species. Has also low oxidase activity towards aldehydes (in vitro)", "gene_name": "XDH", "glycan_count": 0, "glycosylation_sites": [], "id": "P47989", "name": "Xanthine oxidoreductase (XOR)", "organism": "Homo sapiens", "uniprot_id": "P47989" }, { "function": "May regulate the activity of kinases such as PKC and SRC via binding to integrin beta-1 (ITB1) and the receptor of activated protein C kinase 1 (RACK1). In complex with C1QBP is a high affinity receptor for kininogen-1/HMWK", "gene_name": "KRT1", "glycan_count": 5, "glycosylation_sites": [], "id": "P04264", "name": "Keratin", "organism": "Homo sapiens", "uniprot_id": "P04264" }, { "function": "Receptor for retinoic acid (PubMed:16417524, PubMed:19850744, PubMed:20215566, PubMed:21152046, PubMed:37478846). Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes (PubMed:21152046, PubMed:28167758, PubMed:37478846). The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 (PubMed:19398580, PubMed:28167758). In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone deacetylation, chromatin condensation and transcriptional suppression (PubMed:16417524). On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation (PubMed:19850744, PubMed:20215566, PubMed:37478846, PubMed:9267036). Formation of a complex with histone deacetylases might lead to inhibition of RARE DNA element binding and to transcriptional repression (PubMed:28167758). Transcriptional activation and RARE DNA element binding might be supported by the transcription factor KLF2 (PubMed:28167758). RARA plays an essential role in the regulation of retinoic acid-induced germ cell development during spermatogenesis (By similarity). Has a role in the survival of early spermatocytes at the beginning prophase of meiosis (By similarity). In Sertoli cells, may promote the survival and development of early meiotic prophase spermatocytes (By similarity). In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function (By similarity). Together with RXRA, positively regulates microRNA-10a expression, thereby inhibiting the GATA6/VCAM1 signaling response to pulsatile shear stress in vascular endothelial cells (PubMed:28167758). In association with HDAC3, HDAC5 and HDAC7 corepressors, plays a role in the repression of microRNA-10a and thereby promotes the inflammatory response (PubMed:28167758)", "gene_name": "RARA", "glycan_count": 0, "glycosylation_sites": [], "id": "P10276", "name": "Retinoic Acid Receptor", "organism": "Homo sapiens", "uniprot_id": "P10276" }, { "function": "Non-selective calcium permeant cation channel involved in detection of noxious chemical and thermal stimuli (PubMed:11050376, PubMed:11243859, PubMed:11226139, PubMed:12077606). Seems to mediate proton influx and may be involved in intracellular acidosis in nociceptive neurons. Involved in mediation of inflammatory pain and hyperalgesia. Sensitized by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases, which involves PKC isozymes and PCL. Activated by vanilloids, like capsaicin, and temperatures higher than 42 degrees Celsius (PubMed:37117175). Upon activation, exhibits a time- and Ca(2+)-dependent outward rectification, followed by a long-lasting refractory state. Mild extracellular acidic pH (6.5) potentiates channel activation by noxious heat and vanilloids, whereas acidic conditions (pH <6) directly activate the channel. Can be activated by endogenous compounds, including 12-hydroperoxytetraenoic acid and bradykinin. Acts as ionotropic endocannabinoid receptor with central neuromodulatory effects. Triggers a form of long-term depression (TRPV1-LTD) mediated by the endocannabinoid anandamine in the hippocampus and nucleus accumbens by affecting AMPA receptors endocytosis", "gene_name": "TRPV1", "glycan_count": 0, "glycosylation_sites": [ { "position": 604, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8NER1", "name": "TRPV1", "organism": "Homo sapiens", "uniprot_id": "Q8NER1" }, { "function": "Receptor for thymic stromal lymphopoietin (TSLP). Forms a functional complex with TSLP and IL7R which is capable of stimulating cell proliferation through activation of STAT3 and STAT5. Also activates JAK2 (By similarity). Implicated in the development of the hematopoietic system", "gene_name": "CRLF2", "glycan_count": 1, "glycosylation_sites": [ { "position": 47, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 55, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 101, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 169, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9HC73", "name": "CRLF2", "organism": "Homo sapiens", "uniprot_id": "Q9HC73" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P29016 (CD3E)", "name": "CD3", "organism": "", "uniprot_id": "" }, { "function": "Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate", "gene_name": "LTF", "glycan_count": 28, "glycosylation_sites": [ { "position": 252, "type": "N-linked (GlcNAc...) (high mannose) asparagine" }, { "position": 300, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 387, "type": "N-linked (GlcNAc...) (complex) asparagine; alternate" }, { "position": 387, "type": "N-linked (GlcNAc...) (high mannose) asparagine; alternate" }, { "position": 387, "type": "N-linked (GlcNAc...) (hybrid) asparagine; alternate" }, { "position": 495, "type": "N-linked (GlcNAc...) (complex) asparagine; alternate" }, { "position": 495, "type": "N-linked (GlcNAc...) (high mannose) asparagine; alternate" }, { "position": 495, "type": "N-linked (GlcNAc...) (hybrid) asparagine; alternate" }, { "position": 564, "type": "N-linked (GlcNAc...) (high mannose) asparagine" } ], "id": "P24627", "name": "Bovine Lactoferrin (bLf)", "organism": "Bos taurus", "uniprot_id": "P24627" }, { "function": "Ligand for tyrosine-protein kinase receptors AXL, TYRO3 and MER whose signaling is implicated in cell growth and survival, cell adhesion and cell migration. GAS6/AXL signaling plays a role in various processes such as endothelial cell survival during acidification by preventing apoptosis, optimal cytokine signaling during human natural killer cell development, hepatic regeneration, gonadotropin-releasing hormone neuron survival and migration, platelet activation, or regulation of thrombotic responses", "gene_name": "GAS6", "glycan_count": 6, "glycosylation_sites": [ { "position": 420, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q14393", "name": "Gas6", "organism": "Homo sapiens", "uniprot_id": "Q14393" }, { "function": "Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including LGALS3, TUB, TULP1 or GAS6. Regulates many physiological processes including cell survival, migration, differentiation, and phagocytosis of apoptotic cells (efferocytosis). Ligand binding at the cell surface induces autophosphorylation of MERTK on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with GRB2 or PLCG2 and induces phosphorylation of MAPK1, MAPK2, FAK/PTK2 or RAC1. MERTK signaling plays a role in various processes such as macrophage clearance of apoptotic cells, platelet aggregation, cytoskeleton reorganization and engulfment (PubMed:32640697). Functions in the retinal pigment epithelium (RPE) as a regulator of rod outer segments fragments phagocytosis. Also plays an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response by activating STAT1, which selectively induces production of suppressors of cytokine signaling SOCS1 and SOCS3", "gene_name": "MERTK", "glycan_count": 28, "glycosylation_sites": [ { "position": 114, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 170, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 207, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 215, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 234, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 294, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 316, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 329, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 336, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 354, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 389, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 395, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 442, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 454, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q12866", "name": "MerTK", "organism": "Homo sapiens", "uniprot_id": "Q12866" }, { "function": "Immunoglobulin-like cell surface receptor for CD47. Acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. Supports adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment. May play a key role in intracellular signaling during synaptogenesis and in synaptic function (By similarity). Involved in the negative regulation of receptor tyrosine kinase-coupled cellular responses induced by cell adhesion, growth factors or insulin. Mediates negative regulation of phagocytosis, mast cell activation and dendritic cell activation. CD47 binding prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells. Plays a role in antiviral immunity and limits new world arenavirus infection by decreasing virus internalization (By similarity). Receptor for THBS1 (PubMed:24511121). Interaction with THBS1 stimulates phosphorylation of SIRPA (By similarity). In response to THBS1, involved in ROS signaling in non-phagocytic cells, stimulating NADPH oxidase-derived ROS production (PubMed:24511121)", "gene_name": "SIRPA", "glycan_count": 49, "glycosylation_sites": [ { "position": 245, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 270, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 292, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 319, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P78324", "name": "SIRP\u03b1", "organism": "Homo sapiens", "uniprot_id": "P78324" }, { "function": "Heterodimerizes with PMS2 to form MutL alpha, a component of the post-replicative DNA mismatch repair system (MMR). DNA repair is initiated by MutS alpha (MSH2-MSH6) or MutS beta (MSH2-MSH3) binding to a dsDNA mismatch, then MutL alpha is recruited to the heteroduplex. Assembly of the MutL-MutS-heteroduplex ternary complex in presence of RFC and PCNA is sufficient to activate endonuclease activity of PMS2. It introduces single-strand breaks near the mismatch and thus generates new entry points for the exonuclease EXO1 to degrade the strand containing the mismatch. DNA methylation would prevent cleavage and therefore assure that only the newly mutated DNA strand is going to be corrected. MutL alpha (MLH1-PMS2) interacts physically with the clamp loader subunits of DNA polymerase III, suggesting that it may play a role to recruit the DNA polymerase III to the site of the MMR. Also implicated in DNA damage signaling, a process which induces cell cycle arrest and can lead to apoptosis in case of major DNA damages. Heterodimerizes with MLH3 to form MutL gamma which plays a role in meiosis", "gene_name": "MLH1", "glycan_count": 2, "glycosylation_sites": [], "id": "P40692", "name": "MLH1", "organism": "Homo sapiens", "uniprot_id": "P40692" }, { "function": "Component of the post-replicative DNA mismatch repair system (MMR). Forms two different heterodimers: MutS alpha (MSH2-MSH6 heterodimer) and MutS beta (MSH2-MSH3 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. When bound, heterodimers bend the DNA helix and shields approximately 20 base pairs. MutS alpha recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. MutS beta recognizes larger insertion-deletion loops up to 13 nucleotides long. After mismatch binding, MutS alpha or beta forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. Recruits DNA helicase MCM9 to chromatin which unwinds the mismatch containing DNA strand (PubMed:26300262). ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. In melanocytes may modulate both UV-B-induced cell cycle regulation and apoptosis", "gene_name": "MSH2", "glycan_count": 3, "glycosylation_sites": [], "id": "P43246", "name": "MSH2", "organism": "Homo sapiens", "uniprot_id": "P43246" }, { "function": "Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. Recruited on chromatin in G1 and early S phase via its PWWP domain that specifically binds trimethylated 'Lys-36' of histone H3 (H3K36me3): early recruitment to chromatin to be replicated allowing a quick identification of mismatch repair to initiate the DNA mismatch repair reaction", "gene_name": "MSH6", "glycan_count": 1, "glycosylation_sites": [], "id": "P52701", "name": "MSH6", "organism": "Homo sapiens", "uniprot_id": "P52701" }, { "function": "Component of the post-replicative DNA mismatch repair system (MMR) (PubMed:30653781, PubMed:35189042). Heterodimerizes with MLH1 to form MutL alpha. DNA repair is initiated by MutS alpha (MSH2-MSH6) or MutS beta (MSH2-MSH3) binding to a dsDNA mismatch, then MutL alpha is recruited to the heteroduplex. Assembly of the MutL-MutS-heteroduplex ternary complex in presence of RFC and PCNA is sufficient to activate endonuclease activity of PMS2. It introduces single-strand breaks near the mismatch and thus generates new entry points for the exonuclease EXO1 to degrade the strand containing the mismatch. DNA methylation would prevent cleavage and therefore assure that only the newly mutated DNA strand is going to be corrected. MutL alpha (MLH1-PMS2) interacts physically with the clamp loader subunits of DNA polymerase III, suggesting that it may play a role to recruit the DNA polymerase III to the site of the MMR. Also implicated in DNA damage signaling, a process which induces cell cycle arrest and can lead to apoptosis in case of major DNA damages. Possesses an ATPase activity, but in the absence of gross structural changes, ATP hydrolysis may not be necessary for proficient mismatch repair (PubMed:35189042)", "gene_name": "PMS2", "glycan_count": 1, "glycosylation_sites": [], "id": "P54278", "name": "PMS2", "organism": "Homo sapiens", "uniprot_id": "P54278" }, { "function": "Vascular endothelium glycoprotein that plays an important role in the regulation of angiogenesis (PubMed:21737454, PubMed:23300529). Required for normal structure and integrity of adult vasculature (PubMed:7894484). Regulates the migration of vascular endothelial cells (PubMed:17540773). Required for normal extraembryonic angiogenesis and for embryonic heart development (By similarity). May regulate endothelial cell shape changes in response to blood flow, which drive vascular remodeling and establishment of normal vascular morphology during angiogenesis (By similarity). May play a critical role in the binding of endothelial cells to integrins and/or other RGD receptors (PubMed:1692830). Acts as a TGF-beta coreceptor and is involved in the TGF-beta/BMP signaling cascade that ultimately leads to the activation of SMAD transcription factors (PubMed:21737454, PubMed:22347366, PubMed:23300529, PubMed:8370410). Required for GDF2/BMP9 signaling through SMAD1 in endothelial cells and modulates TGFB1 signaling through SMAD3 (PubMed:21737454, PubMed:22347366, PubMed:23300529)", "gene_name": "ENG", "glycan_count": 6, "glycosylation_sites": [ { "position": 88, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 102, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 121, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 134, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 307, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P17813", "name": "soluble endoglin", "organism": "Homo sapiens", "uniprot_id": "P17813" }, { "function": "Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin", "gene_name": "TUBA1C", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9BQE3", "name": "SPP2 (Secreted phosphoprotein 2)", "organism": "Homo sapiens", "uniprot_id": "Q9BQE3" }, { "function": "Cytokine that may play an important role during carcinogenesis and metanephric kidney organogenesis, as a BMP antagonist required for early limb outgrowth and patterning in maintaining the FGF4-SHH feedback loop. Down-regulates the BMP4 signaling in a dose-dependent manner (By similarity). Antagonist of BMP2; inhibits BMP2-mediated differentiation of osteoblasts (in vitro) (PubMed:27036124). Acts as inhibitor of monocyte chemotaxis. Can inhibit the growth or viability of normal cells but not transformed cells when is overexpressed (By similarity)", "gene_name": "GREM1", "glycan_count": 4, "glycosylation_sites": [ { "position": 42, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O60565", "name": "Gremlin-1 (GREM1)", "organism": "Homo sapiens", "uniprot_id": "O60565" }, { "function": "Granzyme B inhibitor", "gene_name": "SERPINB9", "glycan_count": 1, "glycosylation_sites": [], "id": "P50453", "name": "Serpine2", "organism": "Homo sapiens", "uniprot_id": "P50453" }, { "function": "Forms paracellular channels: polymerizes in tight junction strands with cation- and water-selective channels through the strands, conveying epithelial permeability in a process known as paracellular tight junction permeability (PubMed:20460438, PubMed:36008380). In intestinal epithelium, allows for sodium and water fluxes from the peritoneal side to the lumen of the intestine to regulate nutrient absorption and clear enteric pathogens as part of mucosal immune response (By similarity). In kidney, allows passive sodium and calcium reabsorption across proximal tubules from the lumen back to the bloodstream (By similarity). In the hepatobiliary tract, allows paracellular water and cation fluxes in the hepatic perivenous areas and biliary epithelium to generate bile flow and maintain osmotic gradients (By similarity)", "gene_name": "CLDN2", "glycan_count": 0, "glycosylation_sites": [], "id": "P57739", "name": "Cldn2", "organism": "Homo sapiens", "uniprot_id": "P57739" }, { "function": "May play a role in protection or detoxification", "gene_name": "SMR3A", "glycan_count": 0, "glycosylation_sites": [], "id": "Q99954", "name": "Osteoglycin (OGN)", "organism": "Homo sapiens", "uniprot_id": "Q99954" }, { "function": "Inhibitory receptor on lymphocytes that negatively regulates antigen receptor signaling via PTPN6/SHP-1 and PTPN11/SHP-2 (PubMed:12796776, PubMed:14652006, PubMed:15568026, PubMed:18193050). May interact in cis (on the same cell) or in trans (on other cells) with TNFRSF14 (PubMed:19915044). In cis interactions, appears to play an immune regulatory role inhibiting in trans interactions in naive T cells to maintain a resting state. In trans interactions, can predominate during adaptive immune response to provide survival signals to effector T cells (PubMed:19915044)", "gene_name": "BTLA", "glycan_count": 1, "glycosylation_sites": [ { "position": 75, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 94, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 110, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q7Z6A9", "name": "B- and T-lymphocyte attenuator (BTLA)", "organism": "Homo sapiens", "uniprot_id": "Q7Z6A9" }, { "function": "NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. In a non-canonical activation pathway, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B RelB-p52 complexes. The NF-kappa-B heterodimeric RelB-p52 complex is a transcriptional activator. The NF-kappa-B p52-p52 homodimer is a transcriptional repressor. NFKB2 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p100 and generation of p52 by a cotranslational processing. The proteasome-mediated process ensures the production of both p52 and p100 and preserves their independent function. p52 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. p52 and p100 are respectively the minor and major form; the processing of p100 being relatively poor. Isoform p49 is a subunit of the NF-kappa-B protein complex, which stimulates the HIV enhancer in synergy with p65. In concert with RELB, regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer", "gene_name": "NFKB2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q00653", "name": "NF-\u03baB2 (p100/p52)", "organism": "Homo sapiens", "uniprot_id": "Q00653" }, { "function": "Calcium-independent lectin displaying mannose-binding specificity and able to maintain carbohydrate recognition activity in an acidic environment. May be involved in inflammatory and metaplastic responses of the gastrointestinal epithelium", "gene_name": "REG4", "glycan_count": 0, "glycosylation_sites": [ { "position": 50, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9BYZ8", "name": "REG4", "organism": "Homo sapiens", "uniprot_id": "Q9BYZ8" }, { "function": "Uniporter involved in the facilitative transport of nucleosides and nucleobases, and contributes to maintaining their cellular homeostasis (PubMed:10722669, PubMed:10755314, PubMed:12527552, PubMed:14759222, PubMed:15037197, PubMed:17379602, PubMed:21795683, PubMed:26406980, PubMed:27995448, PubMed:35790189, PubMed:8986748). Functions as a Na(+)-independent transporter (PubMed:8986748). Involved in the transport of nucleosides such as adenosine, guanosine, inosine, uridine, thymidine and cytidine (PubMed:10722669, PubMed:10755314, PubMed:12527552, PubMed:14759222, PubMed:15037197, PubMed:17379602, PubMed:26406980, PubMed:8986748). Also transports purine nucleobases (hypoxanthine, adenine, guanine) and pyrimidine nucleobases (thymine, uracil) (PubMed:21795683, PubMed:27995448). Mediates basolateral nucleoside uptake into Sertoli cells, thereby regulating the transport of nucleosides in testis across the blood-testis barrier (By similarity). Regulates inosine levels in brown adipocytes tissues (BAT) and extracellular inosine levels, which controls BAT-dependent energy expenditure (PubMed:35790189)", "gene_name": "SLC29A1", "glycan_count": 11, "glycosylation_sites": [ { "position": 48, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q99808", "name": "Human equilibrative nucleoside transporter (hENT1)", "organism": "Homo sapiens", "uniprot_id": "Q99808" }, { "function": "Forms the heterodimeric complex core-binding factor (CBF) with CBFB. RUNX members modulate the transcription of their target genes through recognizing the core consensus binding sequence 5'-TGTGGT-3', or very rarely, 5'-TGCGGT-3', within their regulatory regions via their runt domain, while CBFB is a non-DNA-binding regulatory subunit that allosterically enhances the sequence-specific DNA-binding capacity of RUNX. The heterodimers bind to the core site of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM-CSF promoters (Probable). Essential for the development of normal hematopoiesis (PubMed:17431401). Acts synergistically with ELF4 to transactivate the IL-3 promoter and with ELF2 to transactivate the BLK promoter (PubMed:10207087, PubMed:14970218). Inhibits KAT6B-dependent transcriptional activation (By similarity). Involved in lineage commitment of immature T cell precursors. CBF complexes repress ZBTB7B transcription factor during cytotoxic (CD8+) T cell development. They bind to RUNX-binding sequence within the ZBTB7B locus acting as transcriptional silencer and allowing for cytotoxic T cell differentiation. CBF complexes binding to the transcriptional silencer is essential for recruitment of nuclear protein complexes that catalyze epigenetic modifications to establish epigenetic ZBTB7B silencing (By similarity). Controls the anergy and suppressive function of regulatory T-cells (Treg) by associating with FOXP3. Activates the expression of IL2 and IFNG and down-regulates the expression of TNFRSF18, IL2RA and CTLA4, in conventional T-cells (PubMed:17377532). Positively regulates the expression of RORC in T-helper 17 cells (By similarity)", "gene_name": "RUNX1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q01196", "name": "RUNX1", "organism": "Homo sapiens", "uniprot_id": "Q01196" }, { "function": "Sequence-specific RNA-binding protein which plays an important role in the establishment and maintenance of the early morphology of cortical neurons during embryonic development. Acts as a translation repressor and controls a translationally regulated cell morphology program to ensure proper structuring of the nervous system. Translational control depends on recognition of its binding element within target mRNAs which consists of a mandatory UAG trimer upstream of a U/A-rich motif. Associated with polysomes (PubMed:25737280)", "gene_name": "UNK", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9C0B0", "name": "ASXL1", "organism": "Homo sapiens", "uniprot_id": "Q9C0B0" }, { "function": "May play a role in preadipocyte differentiation and adipogenesis", "gene_name": "AAMDC", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H7C9", "name": "TM6SF2 (Transmembrane 6 superfamily member 2)", "organism": "Homo sapiens", "uniprot_id": "Q9H7C9" }, { "function": "Common subunit for the receptors for a variety of interleukins. Probably in association with IL15RA, involved in the stimulation of neutrophil phagocytosis by IL15 (PubMed:15123770)", "gene_name": "IL2RG", "glycan_count": 0, "glycosylation_sites": [ { "position": 24, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 71, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 75, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 84, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 159, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 249, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P31785", "name": "Common \u03b3 chain (\u03b3c)", "organism": "Homo sapiens", "uniprot_id": "P31785" }, { "function": "Effector protein for Rho-type GTPases that regulates actin filament reorganization via its interaction with the Arp2/3 complex (PubMed:12235133, PubMed:12769847, PubMed:16275905). Important for efficient actin polymerization (PubMed:12235133, PubMed:16275905, PubMed:8625410). Possible regulator of lymphocyte and platelet function (PubMed:9405671). Mediates actin filament reorganization and the formation of actin pedestals upon infection by pathogenic bacteria (PubMed:18650809). In addition to its role in the cytoplasmic cytoskeleton, also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA (PubMed:20574068). Promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs) (PubMed:29925947)", "gene_name": "WAS", "glycan_count": 0, "glycosylation_sites": [], "id": "P42768", "name": "Wiskott\u2013Aldrich syndrome protein (WASp)", "organism": "Homo sapiens", "uniprot_id": "P42768" }, { "function": "Involved in oxygen transport from the lung to the various peripheral tissues", "gene_name": "HBB", "glycan_count": 2, "glycosylation_sites": [ { "position": 2, "type": "N-linked (Glc) (glycation) valine; in Hb A1c" }, { "position": 9, "type": "N-linked (Glc) (glycation) lysine" }, { "position": 18, "type": "N-linked (Glc) (glycation) lysine" }, { "position": 67, "type": "N-linked (Glc) (glycation) lysine" }, { "position": 121, "type": "N-linked (Glc) (glycation) lysine" }, { "position": 145, "type": "N-linked (Glc) (glycation) lysine; alternate" } ], "id": "P68871", "name": "\u03b2-globin", "organism": "Homo sapiens", "uniprot_id": "P68871" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P69891/P69892", "name": "\u03b3-globin", "organism": "", "uniprot_id": "" }, { "function": "Hydrolyzes cerebroside sulfate", "gene_name": "ARSA", "glycan_count": 29, "glycosylation_sites": [ { "position": 158, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 184, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 350, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P15289", "name": "Aryl sulfatase A (ARSA)", "organism": "Homo sapiens", "uniprot_id": "P15289" }, { "function": "Transcription factor (PubMed:16704730, PubMed:29606353). Associated with the BAF SWI/SNF chromatin remodeling complex (PubMed:23644491, PubMed:39607926). Binds to the 5'-TGACCA-3' sequence motif in regulatory regions of target genes, including a distal promoter of the HBG1 hemoglobin subunit gamma-1 gene (PubMed:29606353, PubMed:39423807). Involved in regulation of the developmental switch from gamma- to beta-globin, probably via direct repression of HBG1; hence indirectly repressing fetal hemoglobin (HbF) level (PubMed:26375765, PubMed:29606353, PubMed:39423807, PubMed:39607926). Involved in brain development (PubMed:27453576). May play a role in hematopoiesis (By similarity). Essential factor in lymphopoiesis required for B-cell formation in fetal liver (By similarity). May function as a modulator of the transcriptional repression activity of NR2F2 (By similarity)", "gene_name": "BCL11A", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H165", "name": "BCL11A", "organism": "Homo sapiens", "uniprot_id": "Q9H165" }, { "function": "Acts with TAL1/SCL to regulate red blood cell development. Also acts with LDB1 to maintain erythroid precursors in an immature state", "gene_name": "LMO2", "glycan_count": 0, "glycosylation_sites": [], "id": "P25791", "name": "LMO2", "organism": "Homo sapiens", "uniprot_id": "P25791" }, { "function": "Binds DNA and functions as a transcriptional regulator (PubMed:12816872). Displays histone methyltransferase activity and monomethylates 'Lys-9' of histone H3 (H3K9me1) in vitro (By similarity). Probably catalyzes the monomethylation of free histone H3 in the cytoplasm which is then transported to the nucleus and incorporated into nucleosomes where SUV39H methyltransferases use it as a substrate to catalyze histone H3 'Lys-9' trimethylation (By similarity). Likely to be one of the primary histone methyltransferases along with MECOM/PRDM3 that direct cytoplasmic H3K9me1 methylation (By similarity). Functions in the differentiation of brown adipose tissue (BAT) which is specialized in dissipating chemical energy in the form of heat in response to cold or excess feeding while white adipose tissue (WAT) is specialized in the storage of excess energy and the control of systemic metabolism (By similarity). Together with CEBPB, regulates the differentiation of myoblastic precursors into brown adipose cells (By similarity). Functions as a repressor of TGF-beta signaling (PubMed:19049980)", "gene_name": "PRDM16", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9HAZ2", "name": "PRDM16", "organism": "Homo sapiens", "uniprot_id": "Q9HAZ2" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Composite (apo(a)+apoB100)", "name": "Lipoprotein(a) [Lp(a)]", "organism": "", "uniprot_id": "" }, { "function": "In association with beta-2 integrin heterodimer ITGAM/CD11b and ITGB2/CD18, mediates activation of TNF-alpha primed neutrophils including degranulation and superoxide production (PubMed:21193407). In addition, by preventing beta-2 integrin internalization and attenuating chemokine signaling favors adhesion over migration (PubMed:28807980). Heterophilic interaction with PECAM1 on endothelial cells plays a role in neutrophil transendothelial migration in vitro (PubMed:17580308). However, appears to be dispensable for neutrophil recruitment caused by bacterial infection in vivo (PubMed:23461681). Acts as a receptor for the mature form of protease PRTN3 allowing its display at the cell surface of neutrophils (PubMed:17244676, PubMed:18462208). By displaying PRTN3 at the neutrophil cell surface, may play a role in enhancing endothelial cell junctional integrity and thus vascular integrity during neutrophil diapedesis (PubMed:23202369)", "gene_name": "CD177", "glycan_count": 0, "glycosylation_sites": [ { "position": 189, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8N6Q3", "name": "CD177", "organism": "Homo sapiens", "uniprot_id": "Q8N6Q3" }, { "function": "Acts as a regulator of the Hippo signaling pathway (PubMed:28087714, PubMed:28169360). Negatively regulates the Hippo signaling pathway by mediating the interaction of MARK3 with STK3/4, bringing them together to promote MARK3-dependent hyperphosphorylation and inactivation of STK3 kinase activity toward LATS1 (PubMed:28087714). Positively regulates the Hippo signaling pathway by mediating the interaction of SCRIB with STK4/MST1 and LATS1 which is important for the activation of the Hippo signaling pathway. Involved in regulating cell proliferation, maintenance of epithelial polarity, epithelial-mesenchymal transition (EMT), cell migration and invasion (PubMed:28169360). Plays an important role in dendritic spine formation and synaptogenesis in cortical neurons; regulates synaptogenesis by enhancing the cell surface localization of N-cadherin. Acts as a positive regulator of hedgehog (Hh) signaling pathway. Plays a critical role in the early point of the SMO activity cycle by interacting with SMO at the ciliary base to induce the accumulation of KIF7 and GLI2 at the ciliary tip for GLI2 activation (By similarity)", "gene_name": "DLG5", "glycan_count": 2, "glycosylation_sites": [], "id": "Q8TDM6", "name": "DLG5", "organism": "Homo sapiens", "uniprot_id": "Q8TDM6" }, { "function": "The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis", "gene_name": "NQO2", "glycan_count": 0, "glycosylation_sites": [], "id": "P16083", "name": "NQO2", "organism": "Homo sapiens", "uniprot_id": "P16083" }, { "function": "Sodium-independent sulfate anion transporter (PubMed:12713736, PubMed:27125215). Can transport other anions including bicarbonate, thiosulfate and oxalate by mediating sulfate-thiosulfate, sulfate-hydrogencarbonate and sulfate-oxalate anion exchange (PubMed:12713736, PubMed:27125215). Mediates oxalate-hydrogencarbonate anion exchange (By similarity)", "gene_name": "SLC26A1", "glycan_count": 0, "glycosylation_sites": [ { "position": 158, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 163, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9H2B4", "name": "SLC26A8", "organism": "Homo sapiens", "uniprot_id": "Q9H2B4" }, { "function": "High affinity receptor for the Fc region of immunoglobulins gamma. Functions in both innate and adaptive immune responses. Mediates IgG effector functions on monocytes triggering antibody-dependent cellular cytotoxicity (ADCC) of virus-infected cells", "gene_name": "FCGR1A", "glycan_count": 39, "glycosylation_sites": [ { "position": 59, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 78, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 152, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 159, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 163, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 195, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 240, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P12314", "name": "FCGR1A", "organism": "Homo sapiens", "uniprot_id": "P12314" }, { "function": "Host-defense peptide that has antimicrobial activity against Gram-negative bacteria, and to a lesser extent also against Gram-positive bacteria and fungi (PubMed:15317502, PubMed:15616305, PubMed:2500436, PubMed:2501794, PubMed:30658057). Exhibits antimicrobial activity against Gram-negative E.coli and E.aerogenes and Gram-positive S.faecalis, S.aureus and B.cereus and the yeast C.albicans (in vitro) (PubMed:15317502, PubMed:15616305, PubMed:17088326, PubMed:2500436, PubMed:2501794, PubMed:30658057). Interacts with pathogenic surface proteins and toxins, such as HIV-1 surface protein gp120 and B.anthracis anthrax lethal factor lef (PubMed:15620707, PubMed:30658057). Protects blood cells against infection with HIV-1 (in vitro) (PubMed:15620707). Inhibits enzymatic activity of B.anthracis lef/anthrax lethal factor (in vitro) (PubMed:30658057). Inhibits corticotropin (ACTH)-stimulated corticosterone production (in vitro) (PubMed:2843187)", "gene_name": "DEFA4", "glycan_count": 0, "glycosylation_sites": [], "id": "P12838", "name": "DEFA4", "organism": "Homo sapiens", "uniprot_id": "P12838" }, { "function": "Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc (By similarity). Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (By similarity). The shared binding site between zinc and calcium at residue Asp-273 suggests a crosstalk between zinc and calcium transport in the blood (By similarity). The rank order of affinity is zinc > calcium > magnesium (By similarity). Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli (By similarity). Does not prevent iron uptake by the bacterial siderophore aerobactin (By similarity)", "gene_name": "Alb", "glycan_count": 0, "glycosylation_sites": [], "id": "P02770", "name": "Albumin", "organism": "Rattus norvegicus", "uniprot_id": "P02770" }, { "function": "Cleaves viral precursor proteins (pTP, pIIIa, pVI, pVII, pVIII, and pX) inside newly assembled particles giving rise to mature virions. Protease complexed to its cofactor slides along the viral DNA to specifically locate and cleave the viral precursors. Mature virions have a weakened organization compared to the unmature virions, thereby facilitating subsequent uncoating. Without maturation, the particle lacks infectivity and is unable to uncoat. Late in adenovirus infection, in the cytoplasm, may participate in the cytoskeleton destruction. Cleaves host cell cytoskeletal keratins K7 and K18", "gene_name": "L3", "glycan_count": 0, "glycosylation_sites": [], "id": "P19151", "name": "Alkaline phosphatase (ALP)", "organism": "Bovine adenovirus 7", "uniprot_id": "P19151" }, { "function": "Has reverse transcriptase activity required for target-primed reverse transcription of the LINE-1 element mRNA, a crucial step in LINE-1 retrotransposition (By similarity). Selectively binds and reversely transcribes RNA with a poly(A) tail consisting of at least 20 adenosines (By similarity). Also has endonuclease activity that allows the introduction of nicks in the chromosomal target DNA (By similarity). Cleaves DNA in AT-rich regions between a 5' stretch of purines and a 3' stretch of pyrimidines, corresponding to the sites of LINE-1 integration in the genome (By similarity). Conformational properties of the target DNA sequence rather than specific nucleotides are key determinants of the ORF2p capacity for sequence-specific DNA recognition (By similarity). Unlike related endonucleases, does not bend the DNA helix but causes compression near the cleavage site (By similarity)", "gene_name": "Pol", "glycan_count": 0, "glycosylation_sites": [], "id": "P11369", "name": "Aspartate aminotransferase (AST)", "organism": "Mus musculus", "uniprot_id": "P11369" }, { "function": "Required for the solubility and assembly of the heterotetramer 3-ketoacyl-[acyl carrier protein] (ACP) reductase functional complex (KAR or KAR1) that forms part of the mitochondrial fatty acid synthase (mtFAS). Alpha-subunit of the KAR complex, acts as scaffold protein, required for the stability of carbonyl reductase type-4 (CBR4, beta-subunit of the KAR complex) and for its 3-ketoacyl-ACP reductase activity, thereby participating in mitochondrial fatty acid biosynthesis. Catalyzes the NAD-dependent conversion of (3R)-3-hydroxyacyl-CoA into 3-ketoacyl-CoA (3-oxoacyl-CoA) with no chain length preference, this enzymatic activity is not needed for the KAR function. Prefers (3R)-3-hydroxyacyl-CoA over (3S)-3-hydroxyacyl-CoA and displays enzymatic activity only in the presence of NAD(+)(H). Cooperates with enoyl-CoA hydratase 1 in mitochondria, together they constitute an alternative route to the auxiliary enzyme pathways for the breakdown of Z-PUFA (cis polyunsaturated fatty acid) enoyl-esters (By similarity). NAD-dependent 17-beta-hydroxysteroid dehydrogenase with highest activity towards estradiol. It efficiently catalyzes the oxidation of estradiol (E2), testosterone, and dihydrotestosterone. Primarily an oxidative enzyme, it can switch to a reductive mode determined in the appropriate physiologic milieu and catalyze the reduction of estrone (E1) to form biologically active estradiol (E2) (PubMed:9712896)", "gene_name": "Hsd17b8", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Z1W2", "name": "Sclerostin", "organism": "Mus musculus", "uniprot_id": "P50171" }, { "function": "Involved in vesicular trafficking at the Golgi apparatus level. May play a role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with MACF1. Involved in endosome-to-Golgi trafficking", "gene_name": "Golga4", "glycan_count": 0, "glycosylation_sites": [], "id": "O70365", "name": "Osteoprotegerin (OPG)", "organism": "Mus musculus", "uniprot_id": "Q91VW5" }, { "function": "Acts specifically as a negative regulator of skeletal muscle growth", "gene_name": "Mstn", "glycan_count": 0, "glycosylation_sites": [ { "position": 72, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O08689", "name": "Myostatin", "organism": "Mus musculus", "uniprot_id": "O08689" }, { "function": "Growth factor of the TGF-beta superfamily that plays essential roles in many developmental processes, including cardiogenesis, neurogenesis, and osteogenesis. Induces cartilage and bone formation. Initiates the canonical BMP signaling cascade by associating with type I receptor BMPR1A and type II receptor BMPR2. Once all three components are bound together in a complex at the cell surface, BMPR2 phosphorylates and activates BMPR1A. In turn, BMPR1A propagates signal by phosphorylating SMAD1/5/8 that travel to the nucleus and act as activators and repressors of transcription of target genes. Also acts to promote expression of HAMP, via the interaction with its receptor BMPR1A/ALK3 (PubMed:31800957). Can also signal through non-canonical pathways such as ERK/MAP kinase signaling cascade that regulates osteoblast differentiation. Also stimulates the differentiation of myoblasts into osteoblasts via the EIF2AK3-EIF2A-ATF4 pathway by stimulating EIF2A phosphorylation which leads to increased expression of ATF4 which plays a central role in osteoblast differentiation. Acts as a positive regulator of odontoblast differentiation during mesenchymal tooth germ formation, expression is repressed during the bell stage by MSX1-mediated inhibition of CTNNB1 signaling (PubMed:29148101)", "gene_name": "Bmp2", "glycan_count": 3, "glycosylation_sites": [ { "position": 134, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 162, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 198, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 336, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P21274", "name": "BMP2", "organism": "Mus musculus", "uniprot_id": "P21274" }, { "function": "Cytokine that binds to TNFRSF11B/OPG and to TNFRSF11A/RANK. Osteoclast differentiation and activation factor (PubMed:22437732). Augments the ability of dendritic cells to stimulate naive T-cell proliferation. May be an important regulator of interactions between T-cells and dendritic cells and may play a role in the regulation of the T-cell-dependent immune response. May also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy (By similarity). Induces osteoclastogenesis by activating multiple signaling pathways in osteoclast precursor cells, chief among which is induction of long lasting oscillations in the intracellular concentration of Ca (2+) resulting in the activation of NFATC1, which translocates to the nucleus and induces osteoclast-specific gene transcription to allow differentiation of osteoclasts (PubMed:18586671, PubMed:24039232, PubMed:27336669). During osteoclast differentiation, in a TMEM64 and ATP2A2-dependent manner induces activation of CREB1 and mitochondrial ROS generation necessary for proper osteoclast generation (PubMed:23395171, PubMed:26644563)", "gene_name": "Tnfsf11", "glycan_count": 0, "glycosylation_sites": [ { "position": 197, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 262, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O35235", "name": "RANKL", "organism": "Mus musculus", "uniprot_id": "O35235" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8K3F0", "name": "Osterix (Osx)", "organism": "Rattus norvegicus", "uniprot_id": "Q8K3F0" }, { "function": "", "gene_name": "Ube-1c", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9R1R5", "name": "Atrogin-1 (FBXO32)", "organism": "Mus musculus", "uniprot_id": "Q9R1R5" }, { "function": "Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. It can phosphorylate a large number of proteins. Participates in Wnt signaling (By similarity)", "gene_name": "CSNK1A1L", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8N752", "name": "KLLN", "organism": "Homo sapiens", "uniprot_id": "Q8N752" }, { "function": "Exhibits a coumarin 7-hydroxylase activity. Active in the metabolic activation of hexamethylphosphoramide, N,N-dimethylaniline, 2'-methoxyacetophenone, N-nitrosomethylphenylamine, and the tobacco-specific carcinogen, 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone. Possesses phenacetin O-deethylation activity", "gene_name": "CYP2A13", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H2X2", "name": "SLC35A2 (UDP-galactose transporter)", "organism": "Homo sapiens", "uniprot_id": "Q16696" }, { "function": "Catalyzes the oxidative deamination of primary amines to the corresponding aldehydes with the concomitant production of hydrogen peroxide and ammonia (PubMed:12072962, PubMed:19764817, PubMed:239684, PubMed:8144586). Its preferred substrates are the diamines histamine and 1-methylhistamine and it could therefore play a role in allergic and immune responses (PubMed:12072962). Has a broad specificity for diamines and can also act on cadaverine and putrescine, two products of amino acid catabolism (PubMed:12072962). It could also act on polyamines, like spermidine and spermine though less efficiently, and regulate various biological processes (PubMed:12072962, PubMed:239684)", "gene_name": "AOC1", "glycan_count": 76, "glycosylation_sites": [ { "position": 110, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 168, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 538, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 745, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P19801", "name": "Diamine oxidase", "organism": "Homo sapiens", "uniprot_id": "P19801" }, { "function": "Acts as an inhibitory receptor for myeloid cells and mast cells (PubMed:15549731). Positively regulates the phagocytosis of apoptotic cells (efferocytosis) via phosphatidylserine (PS) recognition; recognizes and binds PS as a ligand which is expressed on the surface of apoptotic cells. Plays an important role in the maintenance of immune homeostasis, by promoting macrophage-mediated efferocytosis and by inhibiting dendritic cell-mediated efferocytosis (By similarity). Negatively regulates Fc epsilon receptor-dependent mast cell activation and allergic responses via binding to ceramide and sphingomyelin which act as ligands (PubMed:24035150). May act as a coreceptor for interleukin 4 (IL-4). Associates with and regulates IL-4 receptor alpha-mediated responses by augmenting IL-4- and IL-13-induced signaling (By similarity). Negatively regulates the Toll-like receptor (TLR) signaling mediated by MYD88 and TRIF through activation of PTPN6/SHP-1 and PTPN11/SHP-2 (PubMed:22043923). Inhibits osteoclast formation. Induces macrophage cell death upon engagement (By similarity)", "gene_name": "CD300LF", "glycan_count": 5, "glycosylation_sites": [ { "position": 88, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8TDQ1", "name": "CD200R (OX-2 receptor)", "organism": "Homo sapiens", "uniprot_id": "Q8TDQ1" }, { "function": "Receptor for secretory phospholipase A2 (sPLA2). Acts as a receptor for phospholipase sPLA2-IB/PLA2G1B but not sPLA2-IIA/PLA2G2A. Also able to bind to snake PA2-like toxins. Although its precise function remains unclear, binding of sPLA2 to its receptor participates in both positive and negative regulation of sPLA2 functions as well as clearance of sPLA2. Binding of sPLA2-IB/PLA2G1B induces various effects depending on the cell type, such as activation of the mitogen-activated protein kinase (MAPK) cascade to induce cell proliferation, the production of lipid mediators, selective release of arachidonic acid in bone marrow-derived mast cells. In neutrophils, binding of sPLA2-IB/PLA2G1B can activate p38 MAPK to stimulate elastase release and cell adhesion. May be involved in responses in pro-inflammatory cytokine productions during endotoxic shock. Also has endocytic properties and rapidly internalizes sPLA2 ligands, which is particularly important for the clearance of extracellular sPLA2s to protect their potent enzymatic activities. The soluble secretory phospholipase A2 receptor form is circulating and acts as a negative regulator of sPLA2 functions by blocking the biological functions of sPLA2-IB/PLA2G1B (PubMed:15611272, PubMed:7721806). In podocytes, binding of sPLA2-IB/PLA2G1B can regulate podocyte survival and glomerular homeostasis (PubMed:25335547)", "gene_name": "PLA2R1", "glycan_count": 2, "glycosylation_sites": [ { "position": 93, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 454, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1123, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13018", "name": "PLA2R (Phospholipase A2 receptor)", "organism": "Homo sapiens", "uniprot_id": "Q13018" }, { "function": "Plays a role in actin cytoskeleton rearrangement", "gene_name": "THSD7A", "glycan_count": 24, "glycosylation_sites": [ { "position": 234, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 332, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 450, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 500, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 679, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 717, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 968, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1043, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1182, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1225, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1276, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1366, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1500, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1547, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UPZ6", "name": "THSD7A (Thrombospondin type-1 domain-containing protein 7A)", "organism": "Homo sapiens", "uniprot_id": "Q9UPZ6" }, { "function": "A non-specific tyrosine phosphatase that dephosphorylates a diverse number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins (PubMed:10506173, PubMed:15280042, PubMed:20498373, PubMed:9584846). Has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma (PubMed:10506173, PubMed:15280042)", "gene_name": "ACP3", "glycan_count": 26, "glycosylation_sites": [ { "position": 94, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 220, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 333, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P15309", "name": "Folate Receptor Alpha (FR-\u03b1)", "organism": "Homo sapiens", "uniprot_id": "P15309" }, { "function": "One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell", "gene_name": "GJB5", "glycan_count": 0, "glycosylation_sites": [], "id": "O95377", "name": "DLL3", "organism": "Homo sapiens", "uniprot_id": "O95377" }, { "function": "Part of a multiprotein signaling complex which promotes phosphorylation of Raf family members and activation of downstream MAP kinases (By similarity). Independently of its kinase activity, acts as MAP2K1/MEK1 and MAP2K2/MEK2-dependent allosteric activator of BRAF; upon binding to MAP2K1/MEK1 or MAP2K2/MEK2, dimerizes with BRAF and promotes BRAF-mediated phosphorylation of MAP2K1/MEK1 and/or MAP2K2/MEK2 (PubMed:29433126). Promotes activation of MAPK1 and/or MAPK3, both in response to EGF and to cAMP (By similarity). Its kinase activity is unsure (By similarity). Some protein kinase activity has been detected in vitro, however the physiological relevance of this activity is unknown (By similarity)", "gene_name": "KSR1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8IVT5", "name": "KSR1 (Kinase suppressor of Ras 1)", "organism": "Homo sapiens", "uniprot_id": "Q8IVT5" }, { "function": "Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1 (PubMed:10679322, PubMed:12213813, PubMed:15117958, PubMed:16223362, PubMed:17360704, PubMed:18722121, PubMed:26158630, PubMed:35772404, PubMed:9430688). In fibroblast, is required for EGF-stimulated phosphorylation of CREB1, which results in the subsequent transcriptional activation of several immediate-early genes (PubMed:18508509, PubMed:18813292). In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP (PubMed:12213813, PubMed:16223362). Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity (PubMed:18508509, PubMed:18813292). Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the pre-initiation complex (PubMed:17360704). In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation (PubMed:16763566). Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway (PubMed:15342917). Also involved in feedback regulation of mTORC1 and mTORC2 by phosphorylating DEPTOR (PubMed:22017876). Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function (PubMed:10679322, PubMed:16213824). Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4) (PubMed:11684016). Mediates induction of hepatocyte prolifration by TGFA through phosphorylation of CEBPB (PubMed:18508509, PubMed:18813292). Is involved in cell cycle regulation by phosphorylating the CDK inhibitor CDKN1B, which promotes CDKN1B association with 14-3-3 proteins and prevents its translocation to the nucleus and inhibition of G1 progression (PubMed:18508509, PubMed:18813292). Phosphorylates EPHA2 at 'Ser-897', the RPS6KA-EPHA2 signaling pathway controls cell migration (PubMed:26158630). In response to mTORC1 activation, phosphorylates EIF4B at 'Ser-406' and 'Ser-422' which stimulates bicarbonate cotransporter SLC4A7 mRNA translation, increasing SLC4A7 protein abundance and function (PubMed:35772404)", "gene_name": "RPS6KA1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q15418", "name": "RSK1 (Ribosomal S6 Kinase 1)", "organism": "Homo sapiens", "uniprot_id": "Q15418" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Z1A4", "name": "NK1.1 (NKR-P1B)", "organism": "Rattus norvegicus", "uniprot_id": "Q9Z1A4" }, { "function": "This is a receptor for the anterior pituitary hormone prolactin (PRL). Acts as a prosurvival factor for spermatozoa by inhibiting sperm capacitation through suppression of SRC kinase activation and stimulation of AKT. Isoform 4 is unable to transduce prolactin signaling. Isoform 6 is unable to transduce prolactin signaling", "gene_name": "PRLR", "glycan_count": 0, "glycosylation_sites": [ { "position": 59, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 233, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P16471", "name": "PRLR", "organism": "Homo sapiens", "uniprot_id": "P16471" }, { "function": "Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form", "gene_name": "RGS12", "glycan_count": 0, "glycosylation_sites": [], "id": "O14924", "name": "GILZ", "organism": "Homo sapiens", "uniprot_id": "O14924" }, { "function": "Non-specific receptor for endothelin 1, 2, and 3. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system", "gene_name": "EDNRB", "glycan_count": 0, "glycosylation_sites": [ { "position": 59, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P24530", "name": "Endothelin B Receptor (ETBR)", "organism": "Homo sapiens", "uniprot_id": "P24530" }, { "function": "Non-amyloid component of senile plaques found in Alzheimer disease. Could act as a regulator of SNCA aggregation process. Protects neurons from staurosporine and 6-hydroxy dopamine (6OHDA)-stimulated caspase activation in a p53/TP53-dependent manner. Contributes to restore the SNCA anti-apoptotic function abolished by 6OHDA. Not found in the Lewy bodies associated with Parkinson disease", "gene_name": "SNCB", "glycan_count": 1, "glycosylation_sites": [], "id": "Q16143", "name": "Beta-synuclein", "organism": "Homo sapiens", "uniprot_id": "Q16143" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P33681/P42081", "name": "CD80/CD86", "organism": "", "uniprot_id": "" }, { "function": "Integrin alpha-1/beta-1 is a receptor for laminin and collagen. It recognizes the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Involved in anchorage-dependent, negative regulation of EGF-stimulated cell growth", "gene_name": "ITGA1", "glycan_count": 114, "glycosylation_sites": [ { "position": 74, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 100, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 105, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 112, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 217, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 317, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 341, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 402, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 418, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 460, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 532, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 699, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 748, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 780, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 840, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 883, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 908, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 915, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 939, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 966, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 974, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1008, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1073, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1083, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1102, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1113, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P56199", "name": "Integrin alpha-1 (ITGA1)", "organism": "Homo sapiens", "uniprot_id": "P56199" }, { "function": "Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance. NUP98 and NUP96 are involved in the bidirectional transport across the NPC (PubMed:33097660). May anchor NUP153 and TPR to the NPC. In cooperation with DHX9, plays a role in transcription and alternative splicing activation of a subset of genes (PubMed:28221134). Involved in the localization of DHX9 in discrete intranuclear foci (GLFG-body) (PubMed:28221134)", "gene_name": "NUP98", "glycan_count": 41, "glycosylation_sites": [], "id": "P52948", "name": "Nucleoporin 98 (NUP98)", "organism": "Homo sapiens", "uniprot_id": "P52948" }, { "function": "Plays a role in the nuclear pore complex (NPC) assembly and/or maintenance (PubMed:12552102, PubMed:15229283, PubMed:30179222). Required for the assembly of peripheral proteins into the NPC (PubMed:12552102, PubMed:15229283). May anchor NUP62 to the NPC (PubMed:15229283). Involved in nephrogenesis (PubMed:30179222)", "gene_name": "NUP107", "glycan_count": 2, "glycosylation_sites": [], "id": "P57740", "name": "Nucleoporin 107 (NUP107)", "organism": "Homo sapiens", "uniprot_id": "P57740" }, { "function": "Essential component of the nuclear pore complex (NPC) that seems to be required for NPC assembly and maintenance (PubMed:12718872). As part of the NPC Nup107-160 subcomplex plays a role in RNA export and in tethering NUP96/Nup98 and NUP153 to the nucleus (PubMed:12718872). The Nup107-160 complex seems to be required for spindle assembly during mitosis (PubMed:16807356). NUP85 is required for membrane clustering of CCL2-activated CCR2 (PubMed:15995708). Seems to be involved in CCR2-mediated chemotaxis of monocytes and may link activated CCR2 to the phosphatidyl-inositol 3-kinase-Rac-lammellipodium protrusion cascade (PubMed:15995708). Involved in nephrogenesis (PubMed:30179222)", "gene_name": "NUP85", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9BW27", "name": "Nucleoporin 85 (NUP85)", "organism": "Homo sapiens", "uniprot_id": "Q9BW27" }, { "function": "Regulator of pre-B-cell leukemia transcription factors (BPXs) function. Inhibits the binding of PBX1-HOX complex to DNA and blocks the transcriptional activity of E2A-PBX1. Tethers estrogen receptor-alpha (ESR1) to microtubules and allows them to influence estrogen receptors-alpha signaling", "gene_name": "PBXIP1", "glycan_count": 14, "glycosylation_sites": [], "id": "Q96AQ6", "name": "Nucleoporin 160 (NUP160)", "organism": "Homo sapiens", "uniprot_id": "Q96AQ6" }, { "function": "", "gene_name": "ADAM33", "glycan_count": 0, "glycosylation_sites": [ { "position": 109, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 145, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 231, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 276, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 448, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9BZ11", "name": "ADAM33 (A Disintegrin and Metalloproteinase Domain 33)", "organism": "Homo sapiens", "uniprot_id": "Q9BZ11" }, { "function": "May play a role in the cell adhesion to the extracellular matrix", "gene_name": "MUC15", "glycan_count": 0, "glycosylation_sites": [ { "position": 30, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 61, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 79, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 90, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 148, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 155, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 163, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 218, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 225, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8N387", "name": "MUC20 (Mucin 20)", "organism": "Homo sapiens", "uniprot_id": "Q8N387" }, { "function": "Salivary protein that stabilizes saliva supersaturated with calcium salts by inhibiting the precipitation of calcium phosphate salts. It also modulates hydroxyapatite crystal formation on the tooth surface", "gene_name": "STATH", "glycan_count": 0, "glycosylation_sites": [], "id": "P02808", "name": "STATH (Statherin)", "organism": "Homo sapiens", "uniprot_id": "P02808" }, { "function": "Catalyzes both the synthesis and degradation of fructose 2,6-bisphosphate", "gene_name": "PFKFB3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q16875", "name": "PFKFB3", "organism": "Homo sapiens", "uniprot_id": "Q16875" }, { "function": "Receptor for interleukin-2. This beta subunit is involved in receptor mediated endocytosis and transduces the mitogenic signals of IL2. Probably in association with IL15RA, involved in the stimulation of neutrophil phagocytosis by IL15 (PubMed:15123770, PubMed:31040185)", "gene_name": "IL2RB", "glycan_count": 5, "glycosylation_sites": [ { "position": 29, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 43, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 71, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 149, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P14784", "name": "Soluble interleukin-2 receptor (sIL-2R)", "organism": "Homo sapiens", "uniprot_id": "P14784" }, { "function": "Component of the large ribosomal subunit (PubMed:23636399, PubMed:32669547). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399, PubMed:32669547)", "gene_name": "RPL30", "glycan_count": 1, "glycosylation_sites": [], "id": "P62888", "name": "RPL30", "organism": "Homo sapiens", "uniprot_id": "P62888" }, { "function": "Catalyzes the reduction of the C14-unsaturated bond of lanosterol, as part of the metabolic pathway leading to cholesterol biosynthesis (PubMed:12618959, PubMed:16784888, PubMed:21327084, PubMed:27336722, PubMed:9630650). Plays a critical role in myeloid cell cholesterol biosynthesis which is essential to both myeloid cell growth and functional maturation (By similarity). Mediates the activation of NADPH oxidases, perhaps by maintaining critical levels of cholesterol required for membrane lipid raft formation during neutrophil differentiation (By similarity). Anchors the lamina and the heterochromatin to the inner nuclear membrane (PubMed:10828963)", "gene_name": "LBR", "glycan_count": 1, "glycosylation_sites": [], "id": "Q14739", "name": "Lamin B Receptor (LBR)", "organism": "Homo sapiens", "uniprot_id": "Q14739" }, { "function": "Essential component of the nuclear pore complex (PubMed:1915414). The N-terminal is probably involved in nucleocytoplasmic transport (PubMed:1915414). The C-terminal is involved in protein-protein interaction probably via coiled-coil formation, promotes its association with centrosomes and may function in anchorage of p62 to the pore complex (PubMed:1915414, PubMed:24107630). Plays a role in mitotic cell cycle progression by regulating centrosome segregation, centriole maturation and spindle orientation (PubMed:24107630). It might be involved in protein recruitment to the centrosome after nuclear breakdown (PubMed:24107630)", "gene_name": "NUP62", "glycan_count": 2, "glycosylation_sites": [ { "position": 373, "type": "O-linked (GlcNAc) threonine" }, { "position": 468, "type": "O-linked (GlcNAc) serine" } ], "id": "P37198", "name": "Nucleoporin p62", "organism": "Homo sapiens", "uniprot_id": "P37198" }, { "function": "Functions via its association with PML-nuclear bodies (PML-NBs) in a wide range of important cellular processes, including tumor suppression, transcriptional regulation, apoptosis, senescence, DNA damage response, and viral defense mechanisms. Acts as the scaffold of PML-NBs allowing other proteins to shuttle in and out, a process which is regulated by SUMO-mediated modifications and interactions. Inhibits EIF4E-mediated mRNA nuclear export by reducing EIF4E affinity for the 5' 7-methylguanosine (m7G) cap of target mRNAs (PubMed:11500381, PubMed:11575918, PubMed:18391071). Isoform PML-4 has a multifaceted role in the regulation of apoptosis and growth suppression: activates RB1 and inhibits AKT1 via interactions with PP1 and PP2A phosphatases respectively, negatively affects the PI3K pathway by inhibiting MTOR and activating PTEN, and positively regulates p53/TP53 by acting at different levels (by promoting its acetylation and phosphorylation and by inhibiting its MDM2-dependent degradation). Isoform PML-4 also: acts as a transcriptional repressor of TBX2 during cellular senescence and the repression is dependent on a functional RBL2/E2F4 repressor complex, regulates double-strand break repair in gamma-irradiation-induced DNA damage responses via its interaction with WRN, acts as a negative regulator of telomerase by interacting with TERT, and regulates PER2 nuclear localization and circadian function. Isoform PML-6 inhibits specifically the activity of the tetrameric form of PKM. The nuclear isoforms (isoform PML-1, isoform PML-2, isoform PML-3, isoform PML-4 and isoform PML-5) in concert with SATB1 are involved in local chromatin-loop remodeling and gene expression regulation at the MHC-I locus. Isoform PML-2 is required for efficient IFN-gamma induced MHC II gene transcription via regulation of CIITA. Cytoplasmic PML is involved in the regulation of the TGF-beta signaling pathway. PML also regulates transcription activity of ELF4 and can act as an important mediator for TNF-alpha- and IFN-alpha-mediated inhibition of endothelial cell network formation and migration", "gene_name": "PML", "glycan_count": 1, "glycosylation_sites": [], "id": "P29590", "name": "Promyelocytic Leukemia Protein (PML)", "organism": "Homo sapiens", "uniprot_id": "P29590" }, { "function": "This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine(PE)-stimulated ERK signaling in cardiac myocytes", "gene_name": "ADRA1A", "glycan_count": 1, "glycosylation_sites": [ { "position": 7, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 13, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 22, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P35348", "name": "\u03b11A-adrenoceptor", "organism": "Homo sapiens", "uniprot_id": "P35348" }, { "function": "Catalyzes one of the two ATP producing reactions in the glycolytic pathway via the reversible conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate (PubMed:30323285, PubMed:7391028). Both L- and D- forms of purine and pyrimidine nucleotides can be used as substrates, but the activity is much lower on pyrimidines (PubMed:18463139). In addition to its role as a glycolytic enzyme, it seems that PGK1 acts as a polymerase alpha cofactor protein (primer recognition protein) (PubMed:2324090). Acts as a protein kinase when localized to the mitochondrion where it phosphorylates pyruvate dehydrogenase kinase PDK1 to inhibit pyruvate dehydrogenase complex activity and suppress the formation of acetyl-coenzyme A from pyruvate, and consequently inhibit oxidative phosphorylation and promote glycolysis (PubMed:26942675, PubMed:36849569). May play a role in sperm motility (PubMed:26677959)", "gene_name": "PGK1", "glycan_count": 1, "glycosylation_sites": [], "id": "P00558", "name": "Phosphoglycerate kinase-1", "organism": "Homo sapiens", "uniprot_id": "P00558" }, { "function": "Microtubule-binding centrosomal protein required for centriole cohesion, independently of the centrosome-associated protein/CEP250 and rootletin/CROCC linker (PubMed:31789463). In interphase, required for anchoring microtubule at the mother centriole subdistal appendages and for centrosome positioning (PubMed:31789463). During mitosis, may be involved in spindle assembly and chromatin alignment by regulating the organization of spindle microtubules into a symmetrical structure (PubMed:30354798). Has been proposed to play a role in CEP170 recruitment to centrosomes (PubMed:30354798). However, this function could not be confirmed (PubMed:31789463). Plays a non-essential role in ciliogenesis (PubMed:31789463, PubMed:32375023)", "gene_name": "CCDC61", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y6R9", "name": "Zonulin", "organism": "Homo sapiens", "uniprot_id": "Q9Y6R9" }, { "function": "", "gene_name": "lacZ", "glycan_count": 0, "glycosylation_sites": [], "id": "P00722", "name": "\u03b2-galactosidase", "organism": "Escherichia coli (strain K12)", "uniprot_id": "P00722" }, { "function": "Abundant protease in the cytosolic granules of cytotoxic T-cells and NK-cells which activates caspase-independent pyroptosis when delivered into the target cell through the immunological synapse (PubMed:1985927, PubMed:3262682, PubMed:3263427). It cleaves after Asp (PubMed:1985927, PubMed:8258716). Once delivered into the target cell, acts by catalyzing cleavage of gasdermin-E (GSDME), releasing the pore-forming moiety of GSDME, thereby triggering pyroptosis and target cell death (PubMed:31953257, PubMed:32188940). Seems to be linked to an activation cascade of caspases (aspartate-specific cysteine proteases) responsible for apoptosis execution. Cleaves caspase-3, -9 and -10 (CASP3, CASP9 and CASP10, respectively) to give rise to active enzymes mediating apoptosis (PubMed:9852092). Cleaves and activates CASP7 in response to bacterial infection, promoting plasma membrane repair (By similarity)", "gene_name": "GZMB", "glycan_count": 2, "glycosylation_sites": [ { "position": 71, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 104, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P10144", "name": "Granzyme B (GzmB)", "organism": "Homo sapiens", "uniprot_id": "P10144" }, { "function": "Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-2 (TGF-beta-2) chains, which constitute the regulatory and active subunit of TGF-beta-2, respectively", "gene_name": "TGFB2", "glycan_count": 7, "glycosylation_sites": [ { "position": 72, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 140, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 241, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P61812", "name": "TGF\u03b22", "organism": "Homo sapiens", "uniprot_id": "P61812" }, { "function": "Receptor for thromboxane A2 (TXA2), a potent stimulator of platelet aggregation. The activity of this receptor is mediated by a G-protein that activates a phosphatidylinositol-calcium second messenger system. In the kidney, the binding of TXA2 to glomerular TP receptors causes intense vasoconstriction. Activates phospholipase C", "gene_name": "TBXA2R", "glycan_count": 1, "glycosylation_sites": [ { "position": 4, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 16, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P21731", "name": "Thromboxane A2 receptor", "organism": "Homo sapiens", "uniprot_id": "P21731" }, { "function": "Heme-containing oxidoreductase which catalyzes the conversion of thiocyanate (SCN(-)) into antimicrobial agent hypothiocyanous acid (OSCN(-)) in the presence of hydrogen peroxide (H2O2) (Probable) (PubMed:5338806). Also involved in the conversion of iodide (I(-)) into hypoiodite (IO(-)) in the presence of H2O2 (Probable) (PubMed:354515). Responsible for the inactivation of a wide range of micro-organisms and hence, important component of defense mechanism (PubMed:354515, PubMed:5338806). The lactoperoxidase-SCN(-)-H2O2 system shows antibacterial properties against some streptococci strains (PubMed:5338806). The lactoperoxidase-I(-)-H2O2 system shows antibacterial properties against E.coli (PubMed:354515). May protect the udder from infection and may promote growth in newborns (By similarity). May be implicated in airway host defense against infection (By similarity). May contribute to maintaining an appropriate H2O2 cellular level, therefore protecting cells from H2O2-caused injuries and inflammation (By similarity)", "gene_name": "LPO", "glycan_count": 0, "glycosylation_sites": [ { "position": 106, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 212, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 322, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 358, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 449, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P80025", "name": "Lactoperoxidase (LPO)", "organism": "Bos taurus", "uniprot_id": "P80025" }, { "function": "Structural component of lipid droplets, which is required for the formation and maintenance of lipid storage droplets", "gene_name": "PLIN2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q99541", "name": "Plin2 (Perilipin 2)", "organism": "Homo sapiens", "uniprot_id": "Q99541" }, { "function": "", "gene_name": "GYPA", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8WTS2", "name": "Plin5 (Perilipin 5)", "organism": "Homo sapiens", "uniprot_id": "Q8WTS2" }, { "function": "Catalyzes the initial step in triglyceride hydrolysis in adipocyte and non-adipocyte lipid droplets (PubMed:15364929, PubMed:15550674, PubMed:16150821, PubMed:16239926, PubMed:17603008, PubMed:34903883). Exhibits a strong preference for the hydrolysis of long-chain fatty acid esters at the sn-2 position of the glycerol backbone and acts coordinately with LIPE/HLS and DGAT2 within the lipolytic cascade (By similarity). Also possesses acylglycerol transacylase and phospholipase A2 activities (PubMed:15364929, PubMed:17032652, PubMed:17603008). Transfers fatty acid from triglyceride to retinol, hydrolyzes retinylesters, and generates 1,3-diacylglycerol from triglycerides (PubMed:17603008). Regulates adiposome size and may be involved in the degradation of adiposomes (PubMed:16239926). Catalyzes the formation of an ester bond between hydroxy fatty acids and fatty acids derived from triglycerides or diglycerides to generate fatty acid esters of hydroxy fatty acids (FAHFAs) in adipocytes (PubMed:35676490). Acts antagonistically with LDAH in regulation of cellular lipid stores (PubMed:28578400). Inhibits LDAH-stimulated lipid droplet fusion (PubMed:28578400). May play an important role in energy homeostasis (By similarity). May play a role in the response of the organism to starvation, enhancing hydrolysis of triglycerides and providing free fatty acids to other tissues to be oxidized in situations of energy depletion (By similarity)", "gene_name": "PNPLA2", "glycan_count": 2, "glycosylation_sites": [ { "position": 39, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q96AD5", "name": "ATGL (PNPLA2)", "organism": "Homo sapiens", "uniprot_id": "Q96AD5" }, { "function": "Integrin ITGAM/ITGB2 is implicated in various adhesive interactions of monocytes, macrophages and granulocytes as well as in mediating the uptake of complement-coated particles and pathogens (By similarity). It is identical with CR-3, the receptor for the iC3b fragment of the third complement component. It probably recognizes the R-G-D peptide in C3b. Integrin ITGAM/ITGB2 is also a receptor for fibrinogen, factor X and ICAM1. It recognizes P1 and P2 peptides of fibrinogen gamma chain. Regulates neutrophil migration. In association with beta subunit ITGB2/CD18, required for CD177-PRTN3-mediated activation of TNF primed neutrophils (By similarity). May regulate phagocytosis-induced apoptosis in extravasated neutrophils (By similarity). May play a role in mast cell development (By similarity). Required with TYROBP/DAP12 in microglia to control production of microglial superoxide ions which promote the neuronal apoptosis that occurs during brain development (PubMed:18685038)", "gene_name": "Itgam", "glycan_count": 7, "glycosylation_sites": [ { "position": 58, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 86, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 391, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 696, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 734, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 772, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 801, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 881, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 907, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 941, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 980, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 994, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1022, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1045, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1051, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1076, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P05555", "name": "CD11b", "organism": "Mus musculus", "uniprot_id": "P05555" }, { "function": "Acts as a ligand for C-C chemokine receptor CCR2 (By similarity). Signals through binding and activation of CCR2 and induces a strong chemotactic response and mobilization of intracellular calcium ions (By similarity). Exhibits a chemotactic activity for monocytes and basophils but not neutrophils or eosinophils (By similarity). Plays an important role in mediating peripheral nerve injury-induced neuropathic pain (PubMed:29993042). Increases NMDA-mediated synaptic transmission in both dopamine D1 and D2 receptor-containing neurons, which may be caused by MAPK/ERK-dependent phosphorylation of GRIN2B/NMDAR2B (PubMed:29993042)", "gene_name": "Ccl2", "glycan_count": 0, "glycosylation_sites": [ { "position": 126, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P10148", "name": "Ccl2 (MCP-1)", "organism": "Mus musculus", "uniprot_id": "P10148" }, { "function": "Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells", "gene_name": "Acta2", "glycan_count": 2, "glycosylation_sites": [], "id": "P62737", "name": "Acta2 (\u03b1-SMA)", "organism": "Mus musculus", "uniprot_id": "P62737" }, { "function": "Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14 (By similarity). Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling", "gene_name": "Timp1", "glycan_count": 1, "glycosylation_sites": [ { "position": 54, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 102, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P12032", "name": "Timp1", "organism": "Mus musculus", "uniprot_id": "P12032" }, { "function": "Apoptosis regulator that functions through different apoptotic signaling pathways (PubMed:23429263, PubMed:26015568, PubMed:26949185, PubMed:27098698, PubMed:9535847). Plays a roles as pro-apoptotic protein that positively regulates intrinsic apoptotic process in a BAX- and BAK1-dependent manner or in a BAX- and BAK1-independent manner (PubMed:23429263, PubMed:26015568, PubMed:26949185). In response to endoplasmic reticulum stress promotes mitochondrial apoptosis through downstream BAX/BAK1 activation and positive regulation of PERK-mediated unfolded protein response (PubMed:26015568). Activates apoptosis independently of heterodimerization with survival-promoting BCL2 and BCL2L1 through induction of mitochondrial outer membrane permeabilization, in a BAX- and BAK1-independent manner, in response to inhibition of ERAD-proteasome degradation system, resulting in cytochrome c release (PubMed:26949185, PubMed:9535847). In response to DNA damage, mediates intrinsic apoptotic process in a TP53-dependent manner. Plays a role in granulosa cell apoptosis by CASP3 activation (By similarity). Plays a roles as anti-apoptotic protein during neuronal apoptotic process, by negatively regulating poly ADP-ribose polymerase-dependent cell death through regulation of neuronal calcium homeostasis and mitochondrial bioenergetics in response to NMDA excitation (PubMed:27098698). In addition to its role in apoptosis, may regulate trophoblast cell proliferation during the early stages of placental development, by acting on G1/S transition through regulation of CCNE1 expression. May also play a role as an inducer of autophagy by disrupting interaction between MCL1 and BECN1 (By similarity)", "gene_name": "Bok", "glycan_count": 0, "glycosylation_sites": [], "id": "O35425", "name": "Srebp1c", "organism": "Mus musculus", "uniprot_id": "O35425" }, { "function": "ATP-driven pump that supplies the Golgi apparatus with Ca(2+) and Mn(2+) ions, both essential cofactors for processing and trafficking of newly synthesized proteins in the secretory pathway (PubMed:15677451, PubMed:15831496, PubMed:16332677, PubMed:30923126). Within a catalytic cycle, acquires Ca(2+) or Mn(2+) ions on the cytoplasmic side of the membrane and delivers them to the lumenal side. The transfer of ions across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing to outward-facing state (PubMed:15831496, PubMed:16332677). Induces Ca(2+) influx independently of its ATP-driven pump function. At the basolateral membrane of mammary epithelial cells, interacts with Ca(2+) channel ORAI1 and mediates Ca(2+) entry independently of the Ca(2+) content of endoplasmic reticulum or Golgi stores. May facilitate transepithelial transport of large quantities of Ca(2+) for milk secretion via activation of Ca(2+) influx channels at the plasma membrane and active Ca(2+) transport at the Golgi apparatus (PubMed:20887894, PubMed:23840669)", "gene_name": "ATP2C2", "glycan_count": 0, "glycosylation_sites": [], "id": "O75185", "name": "Plasma Membrane Ca2+-ATPase 3 (PMCA3)", "organism": "Homo sapiens", "uniprot_id": "O75185" }, { "function": "Polymerizes (R)-3-hydroxybutyryl-CoA to create polyhydroxybutyrate (PHB) which consists of thousands of hydroxybutyrate molecules linked end to end. PHB serves as an intracellular energy reserve material when cells grow under conditions of nutrient limitation", "gene_name": "phaC", "glycan_count": 0, "glycosylation_sites": [], "id": "P23608", "name": "Plasma Membrane Ca2+-ATPase 4 (PMCA4)", "organism": "Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)", "uniprot_id": "P23608" }, { "function": "Cytokine that affects the growth, movement, or activation state of cells that participate in immune and inflammatory response. Chemotactic for activated T-cells. Binds to CXCR3", "gene_name": "CXCL9", "glycan_count": 0, "glycosylation_sites": [], "id": "Q07325", "name": "CXCL9", "organism": "Homo sapiens", "uniprot_id": "Q07325" }, { "function": "Chemotactic for interleukin-activated T-cells but not unstimulated T-cells, neutrophils or monocytes. Induces calcium release in activated T-cells. Binds to CXCR3. May play an important role in CNS diseases which involve T-cell recruitment. May play a role in skin immune responses", "gene_name": "CXCL11", "glycan_count": 0, "glycosylation_sites": [], "id": "O14625", "name": "CXCL11", "organism": "Homo sapiens", "uniprot_id": "O14625" }, { "function": "Chromatin reader protein that recognizes and binds acetylated histones and plays a key role in transmission of epigenetic memory across cell divisions and transcription regulation (PubMed:20871596, PubMed:23086925, PubMed:23317504, PubMed:29176719, PubMed:29379197). Remains associated with acetylated chromatin throughout the entire cell cycle and provides epigenetic memory for postmitotic G1 gene transcription by preserving acetylated chromatin status and maintaining high-order chromatin structure (PubMed:22334664, PubMed:23317504, PubMed:23589332). During interphase, plays a key role in regulating the transcription of signal-inducible genes by associating with the P-TEFb complex and recruiting it to promoters (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). Also recruits P-TEFb complex to distal enhancers, so called anti-pause enhancers in collaboration with JMJD6 (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). BRD4 and JMJD6 are required to form the transcriptionally active P-TEFb complex by displacing negative regulators such as HEXIM1 and 7SKsnRNA complex from P-TEFb, thereby transforming it into an active form that can then phosphorylate the C-terminal domain (CTD) of RNA polymerase II (PubMed:16109376, PubMed:16109377, PubMed:19596240, PubMed:23589332, PubMed:24360279). Regulates differentiation of naive CD4(+) T-cells into T-helper Th17 by promoting recruitment of P-TEFb to promoters (By similarity). Promotes phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II (PubMed:23086925). According to a report, directly acts as an atypical protein kinase and mediates phosphorylation of 'Ser-2' of the C-terminal domain (CTD) of RNA polymerase II; these data however need additional evidences in vivo (PubMed:22509028). In addition to acetylated histones, also recognizes and binds acetylated RELA, leading to further recruitment of the P-TEFb complex and subsequent activation of NF-kappa-B (PubMed:19103749). Also acts as a regulator of p53/TP53-mediated transcription: following phosphorylation by CK2, recruited to p53/TP53 specific target promoters (PubMed:23317504)", "gene_name": "BRD4", "glycan_count": 2, "glycosylation_sites": [], "id": "O60885", "name": "BRD4", "organism": "Homo sapiens", "uniprot_id": "O60885" }, { "function": "Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Plays a central role in creating a multisubunit coactivator complex, which probably acts via remodeling of chromatin. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ER), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Displays histone acetyltransferase activity. Also involved in the coactivation of the NF-kappa-B pathway via its interaction with the NFKB1 subunit", "gene_name": "NCOA3", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9Y6Q9", "name": "NCOA3", "organism": "Homo sapiens", "uniprot_id": "Q9Y6Q9" }, { "function": "Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (PubMed:16762839, PubMed:17704056, PubMed:28497810). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (PubMed:16762839, PubMed:17704056). Histone deacetylases act via the formation of large multiprotein complexes (PubMed:16762839, PubMed:17704056). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:16428440, PubMed:28977666). As part of the SIN3B complex is recruited downstream of the constitutively active genes transcriptional start sites through interaction with histones and mitigates histone acetylation and RNA polymerase II progression within transcribed regions contributing to the regulation of transcription (PubMed:21041482). Also functions as a deacetylase for non-histone targets, such as NR1D2, RELA, SP1, SP3, STAT3 and TSHZ3 (PubMed:12837748, PubMed:16285960, PubMed:16478997, PubMed:17996965, PubMed:19343227). Deacetylates SP proteins, SP1 and SP3, and regulates their function (PubMed:12837748, PubMed:16478997). Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons (PubMed:19081374). Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation (PubMed:19081374). Deacetylates TSHZ3 and regulates its transcriptional repressor activity (PubMed:19343227). Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B (PubMed:17000776). Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression activity (PubMed:17996965). Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development (By similarity). Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-BMAL1 heterodimer (By similarity). Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation (By similarity). In addition to protein deacetylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase and delactylase by mediating decrotonylation ((2E)-butenoyl) and delactylation (lactoyl) of histones, respectively (PubMed:28497810, PubMed:35044827)", "gene_name": "HDAC1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q13547", "name": "HDAC1", "organism": "Homo sapiens", "uniprot_id": "Q13547" }, { "function": "Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes", "gene_name": "HDAC11", "glycan_count": 0, "glycosylation_sites": [], "id": "Q96DB2", "name": "HDAC11", "organism": "Homo sapiens", "uniprot_id": "Q96DB2" }, { "function": "NAD-dependent protein deacetylase, which deacetylates internal lysines on histone and alpha-tubulin as well as many other proteins such as key transcription factors (PubMed:12620231, PubMed:16648462, PubMed:18249187, PubMed:18332217, PubMed:18995842, PubMed:20543840, PubMed:20587414, PubMed:21081649, PubMed:21726808, PubMed:21949390, PubMed:22014574, PubMed:22771473, PubMed:23468428, PubMed:23908241, PubMed:24177535, PubMed:24681946, PubMed:24769394, PubMed:24940000). Participates in the modulation of multiple and diverse biological processes such as cell cycle control, genomic integrity, microtubule dynamics, cell differentiation, metabolic networks, and autophagy (PubMed:12620231, PubMed:16648462, PubMed:18249187, PubMed:18332217, PubMed:18995842, PubMed:20543840, PubMed:20587414, PubMed:21081649, PubMed:21726808, PubMed:21949390, PubMed:22014574, PubMed:22771473, PubMed:23468428, PubMed:23908241, PubMed:24177535, PubMed:24681946, PubMed:24769394, PubMed:24940000). Plays a major role in the control of cell cycle progression and genomic stability (PubMed:12697818, PubMed:16909107, PubMed:17488717, PubMed:17726514, PubMed:19282667, PubMed:23468428). Functions in the antephase checkpoint preventing precocious mitotic entry in response to microtubule stress agents, and hence allowing proper inheritance of chromosomes (PubMed:12697818, PubMed:16909107, PubMed:17488717, PubMed:17726514, PubMed:19282667, PubMed:23468428). Positively regulates the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase complex activity by deacetylating CDC20 and FZR1, then allowing progression through mitosis (PubMed:22014574). Associates both with chromatin at transcriptional start sites (TSSs) and enhancers of active genes (PubMed:23468428). Plays a role in cell cycle and chromatin compaction through epigenetic modulation of the regulation of histone H4 'Lys-20' methylation (H4K20me1) during early mitosis (PubMed:23468428). Specifically deacetylates histone H4 at 'Lys-16' (H4K16ac) between the G2/M transition and metaphase enabling H4K20me1 deposition by KMT5A leading to ulterior levels of H4K20me2 and H4K20me3 deposition throughout cell cycle, and mitotic S-phase progression (PubMed:23468428). Deacetylates KMT5A modulating KMT5A chromatin localization during the mitotic stress response (PubMed:23468428). Also deacetylates histone H3 at 'Lys-57' (H3K56ac) during the mitotic G2/M transition (PubMed:20587414). Upon bacterium Listeria monocytogenes infection, deacetylates 'Lys-18' of histone H3 in a receptor tyrosine kinase MET- and PI3K/Akt-dependent manner, thereby inhibiting transcriptional activity and promoting late stages of listeria infection (PubMed:23908241). During oocyte meiosis progression, may deacetylate histone H4 at 'Lys-16' (H4K16ac) and alpha-tubulin, regulating spindle assembly and chromosome alignment by influencing microtubule dynamics and kinetochore function (PubMed:24940000). Deacetylates histone H4 at 'Lys-16' (H4K16ac) at the VEGFA promoter and thereby contributes to regulate expression of VEGFA, a key regulator of angiogenesis (PubMed:24940000). Deacetylates alpha-tubulin at 'Lys-40' and hence controls neuronal motility, oligodendroglial cell arbor projection processes and proliferation of non-neuronal cells (PubMed:18332217, PubMed:18995842). Phosphorylation at Ser-368 by a G1/S-specific cyclin E-CDK2 complex inactivates SIRT2-mediated alpha-tubulin deacetylation, negatively regulating cell adhesion, cell migration and neurite outgrowth during neuronal differentiation (PubMed:17488717). Deacetylates PARD3 and participates in the regulation of Schwann cell peripheral myelination formation during early postnatal development and during postinjury remyelination (PubMed:21949390). Involved in several cellular metabolic pathways (PubMed:20543840, PubMed:21726808, PubMed:24769394). Plays a role in the regulation of blood glucose homeostasis by deacetylating and stabilizing phosphoenolpyruvate carboxykinase PCK1 activity in response to low nutrient availability (PubMed:21726808). Acts as a key regulator in the pentose phosphate pathway (PPP) by deacetylating and activating the glucose-6-phosphate G6PD enzyme, and therefore, stimulates the production of cytosolic NADPH to counteract oxidative damage (PubMed:24769394). Maintains energy homeostasis in response to nutrient deprivation as well as energy expenditure by inhibiting adipogenesis and promoting lipolysis (PubMed:20543840). Attenuates adipocyte differentiation by deacetylating and promoting FOXO1 interaction to PPARG and subsequent repression of PPARG-dependent transcriptional activity (PubMed:20543840). Plays a role in the regulation of lysosome-mediated degradation of protein aggregates by autophagy in neuronal cells (PubMed:20543840). Deacetylates FOXO1 in response to oxidative stress or serum deprivation, thereby negatively regulating FOXO1-mediated autophagy (PubMed:20543840). Deacetylates a broad range of transcription factors and co-regulators regulating target gene expression. Deacetylates transcriptional factor FOXO3 stimulating the ubiquitin ligase SCF(SKP2)-mediated FOXO3 ubiquitination and degradation (By similarity). Deacetylates HIF1A and therefore promotes HIF1A degradation and inhibition of HIF1A transcriptional activity in tumor cells in response to hypoxia (PubMed:24681946). Deacetylates RELA in the cytoplasm inhibiting NF-kappaB-dependent transcription activation upon TNF-alpha stimulation (PubMed:21081649). Inhibits transcriptional activation by deacetylating p53/TP53 and EP300 (PubMed:18249187, PubMed:18995842). Also deacetylates EIF5A (PubMed:22771473). Functions as a negative regulator on oxidative stress-tolerance in response to anoxia-reoxygenation conditions (PubMed:24769394). Plays a role as tumor suppressor (PubMed:22014574). In addition to protein deacetylase activity, also has activity toward long-chain fatty acyl groups and mediates protein-lysine demyristoylation and depalmitoylation of target proteins, such as ARF6 and KRAS, thereby regulating their association with membranes (PubMed:25704306, PubMed:29239724, PubMed:32103017)", "gene_name": "SIRT2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8IXJ6", "name": "SIRT2", "organism": "Homo sapiens", "uniprot_id": "Q8IXJ6" }, { "function": "NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins (PubMed:21908771, PubMed:22076378, PubMed:24703693, PubMed:29180469). Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation and deglutarylation of CPS1, thereby increasing CPS1 activity in response to elevated NAD levels during fasting (PubMed:22076378, PubMed:24703693). Activates SOD1 by mediating its desuccinylation, leading to reduced reactive oxygen species (PubMed:24140062). Activates SHMT2 by mediating its desuccinylation (PubMed:29180469). Modulates ketogenesis through the desuccinylation and activation of HMGCS2 (By similarity). Has weak NAD-dependent protein deacetylase activity; however this activity may not be physiologically relevant in vivo. Can deacetylate cytochrome c (CYCS) and a number of other proteins in vitro such as UOX", "gene_name": "SIRT5", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NXA8", "name": "SIRT5", "organism": "Homo sapiens", "uniprot_id": "Q9NXA8" }, { "function": "The METTL3-METTL14 heterodimer forms a N6-methyltransferase complex that methylates adenosine residues at the N(6) position of some RNAs and regulates various processes such as the circadian clock, differentiation of embryonic and hematopoietic stem cells, cortical neurogenesis, response to DNA damage, differentiation of T-cells and primary miRNA processing (PubMed:22575960, PubMed:24284625, PubMed:25719671, PubMed:25799998, PubMed:26321680, PubMed:26593424, PubMed:27281194, PubMed:27373337, PubMed:27627798, PubMed:28297716, PubMed:29348140, PubMed:29506078, PubMed:30428350, PubMed:9409616). In the heterodimer formed with METTL14, METTL3 constitutes the catalytic core (PubMed:27281194, PubMed:27373337, PubMed:27627798). N6-methyladenosine (m6A), which takes place at the 5'-[AG]GAC-3' consensus sites of some mRNAs, plays a role in mRNA stability, processing, translation efficiency and editing (PubMed:22575960, PubMed:24284625, PubMed:25719671, PubMed:25799998, PubMed:26321680, PubMed:26593424, PubMed:28297716, PubMed:9409616). M6A acts as a key regulator of mRNA stability: methylation is completed upon the release of mRNA into the nucleoplasm and promotes mRNA destabilization and degradation (PubMed:28637692). In embryonic stem cells (ESCs), m6A methylation of mRNAs encoding key naive pluripotency-promoting transcripts results in transcript destabilization, promoting differentiation of ESCs (By similarity). M6A regulates the length of the circadian clock: acts as an early pace-setter in the circadian loop by putting mRNA production on a fast-track for facilitating nuclear processing, thereby providing an early point of control in setting the dynamics of the feedback loop (By similarity). M6A also regulates circadian regulation of hepatic lipid metabolism (PubMed:30428350). M6A regulates spermatogonial differentiation and meiosis and is essential for male fertility and spermatogenesis (By similarity). Also required for oogenesis (By similarity). Involved in the response to DNA damage: in response to ultraviolet irradiation, METTL3 rapidly catalyzes the formation of m6A on poly(A) transcripts at DNA damage sites, leading to the recruitment of POLK to DNA damage sites (PubMed:28297716). M6A is also required for T-cell homeostasis and differentiation: m6A methylation of transcripts of SOCS family members (SOCS1, SOCS3 and CISH) in naive T-cells promotes mRNA destabilization and degradation, promoting T-cell differentiation (By similarity). Inhibits the type I interferon response by mediating m6A methylation of IFNB (PubMed:30559377). M6A also takes place in other RNA molecules, such as primary miRNA (pri-miRNAs) (PubMed:25799998). Mediates m6A methylation of Xist RNA, thereby participating in random X inactivation: m6A methylation of Xist leads to target YTHDC1 reader on Xist and promote transcription repression activity of Xist (PubMed:27602518). M6A also regulates cortical neurogenesis: m6A methylation of transcripts related to transcription factors, neural stem cells, the cell cycle and neuronal differentiation during brain development promotes their destabilization and decay, promoting differentiation of radial glial cells (By similarity). METTL3 mediates methylation of pri-miRNAs, marking them for recognition and processing by DGCR8 (PubMed:25799998). Acts as a positive regulator of mRNA translation independently of the methyltransferase activity: promotes translation by interacting with the translation initiation machinery in the cytoplasm (PubMed:27117702). Its overexpression in a number of cancer cells suggests that it may participate in cancer cell proliferation by promoting mRNA translation (PubMed:27117702). During human coronavirus SARS-CoV-2 infection, adds m6A modifications in SARS-CoV-2 RNA leading to decreased RIGI binding and subsequently dampening the sensing and activation of innate immune responses (PubMed:33961823)", "gene_name": "METTL3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q86U44", "name": "METTL3", "organism": "Homo sapiens", "uniprot_id": "Q86U44" }, { "function": "RNA demethylase that mediates oxidative demethylation of different RNA species, such as mRNAs, tRNAs and snRNAs, and acts as a regulator of fat mass, adipogenesis and energy homeostasis (PubMed:22002720, PubMed:25452335, PubMed:26457839, PubMed:26458103, PubMed:28002401, PubMed:30197295). Specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes (PubMed:22002720, PubMed:25452335, PubMed:26457839, PubMed:26458103, PubMed:30197295). M6A demethylation by FTO affects mRNA expression and stability (PubMed:30197295). Also able to demethylate m6A in U6 small nuclear RNA (snRNA) (PubMed:30197295). Mediates demethylation of N(6),2'-O-dimethyladenosine cap (m6A(m)), by demethylating the N(6)-methyladenosine at the second transcribed position of mRNAs and U6 snRNA (PubMed:28002401, PubMed:30197295). Demethylation of m6A(m) in the 5'-cap by FTO affects mRNA stability by promoting susceptibility to decapping (PubMed:28002401). Also acts as a tRNA demethylase by removing N(1)-methyladenine from various tRNAs (PubMed:30197295). Has no activity towards 1-methylguanine (PubMed:20376003). Has no detectable activity towards double-stranded DNA (PubMed:20376003). Also able to repair alkylated DNA and RNA by oxidative demethylation: demethylates single-stranded RNA containing 3-methyluracil, single-stranded DNA containing 3-methylthymine and has low demethylase activity towards single-stranded DNA containing 1-methyladenine or 3-methylcytosine (PubMed:18775698, PubMed:20376003). Ability to repair alkylated DNA and RNA is however unsure in vivo (PubMed:18775698, PubMed:20376003). Involved in the regulation of fat mass, adipogenesis and body weight, thereby contributing to the regulation of body size and body fat accumulation (PubMed:18775698, PubMed:20376003). Involved in the regulation of thermogenesis and the control of adipocyte differentiation into brown or white fat cells (PubMed:26287746). Regulates activity of the dopaminergic midbrain circuitry via its ability to demethylate m6A in mRNAs (By similarity). Plays an oncogenic role in a number of acute myeloid leukemias by enhancing leukemic oncogene-mediated cell transformation: acts by mediating m6A demethylation of target transcripts such as MYC, CEBPA, ASB2 and RARA, leading to promote their expression (PubMed:28017614, PubMed:29249359)", "gene_name": "FTO", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9C0B1", "name": "FTO", "organism": "Homo sapiens", "uniprot_id": "Q9C0B1" }, { "function": "Specifically recognizes and binds N6-methyladenosine (m6A)-containing mRNAs, and regulates their stability (PubMed:24284625, PubMed:26318451, PubMed:32492408, PubMed:39900921). M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing (PubMed:24284625, PubMed:32492408). Acts as a regulator of mRNA stability by promoting degradation of m6A-containing mRNAs via interaction with the CCR4-NOT complex (PubMed:32492408). The YTHDF paralogs (YTHDF1, YTHDF2 and YTHDF3) shares m6A-containing mRNAs targets and act redundantly to mediate mRNA degradation and cellular differentiation (PubMed:28106072, PubMed:32492408). Required to facilitate learning and memory formation in the hippocampus by binding to m6A-containing neuronal mRNAs (By similarity). Acts as a regulator of axon guidance by binding to m6A-containing ROBO3 transcripts (By similarity). Acts as a negative regulator of antigen cross-presentation in myeloid dendritic cells (By similarity). In the context of tumorigenesis, negative regulation of antigen cross-presentation limits the anti-tumor response by reducing efficiency of tumor-antigen cross-presentation (By similarity). Promotes formation of phase-separated membraneless compartments, such as P-bodies or stress granules, by undergoing liquid-liquid phase separation upon binding to mRNAs containing multiple m6A-modified residues: polymethylated mRNAs act as a multivalent scaffold for the binding of YTHDF proteins, juxtaposing their disordered regions and thereby leading to phase separation (PubMed:31292544, PubMed:31388144, PubMed:32451507). The resulting mRNA-YTHDF complexes then partition into different endogenous phase-separated membraneless compartments, such as P-bodies, stress granules or neuronal RNA granules (PubMed:31292544)", "gene_name": "YTHDF1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9BYJ9", "name": "YTHDF1", "organism": "Homo sapiens", "uniprot_id": "Q9BYJ9" }, { "function": "Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body (PubMed:7504305, PubMed:7531687, PubMed:7544004, PubMed:7682706). In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such PTGS2/COX2 (By similarity). As component of the iNOS-S100A8/9 transnitrosylase complex involved in the selective inflammatory stimulus-dependent S-nitrosylation of GAPDH on 'Cys-247' implicated in regulation of the GAIT complex activity and probably multiple targets including ANXA5, EZR, MSN and VIM (PubMed:25417112). Involved in inflammation, enhances the synthesis of pro-inflammatory mediators such as IL6 and IL8 (PubMed:19688109)", "gene_name": "NOS2", "glycan_count": 1, "glycosylation_sites": [], "id": "P35228", "name": "iNOS", "organism": "Homo sapiens", "uniprot_id": "P35228" }, { "function": "Essential antioxidant peroxidase that directly reduces phospholipid hydroperoxide even if they are incorporated in membranes and lipoproteins (PubMed:29290465). Can also reduce fatty acid hydroperoxide, cholesterol hydroperoxide and thymine hydroperoxide (By similarity). Plays a key role in protecting cells from oxidative damage by preventing membrane lipid peroxidation (PubMed:12566075). Required to prevent cells from ferroptosis, a non-apoptotic cell death resulting from an iron-dependent accumulation of lipid reactive oxygen species (PubMed:12566075, PubMed:24439385, PubMed:25402683, PubMed:25922076, PubMed:29290465). The presence of selenocysteine (Sec) versus Cys at the active site is essential for life: it provides resistance to overoxidation and prevents cells against ferroptosis (PubMed:29290465). The presence of Sec at the active site is also essential for the survival of a specific type of parvalbumin-positive interneurons, thereby preventing against fatal epileptic seizures (PubMed:29290465). May be required to protect cells from the toxicity of ingested lipid hydroperoxides (PubMed:12566075). Required for normal sperm development and male fertility (PubMed:19783653, PubMed:25922076). Essential for maturation and survival of photoreceptor cells (PubMed:22207760). Plays a role in a primary T-cell response to viral and parasitic infection by protecting T-cells from ferroptosis and by supporting T-cell expansion (PubMed:25824823). Plays a role of glutathione peroxidase in platelets in the arachidonic acid metabolism (By similarity). Reduces hydroperoxy ester lipids formed by a 15-lipoxygenase that may play a role as down-regulator of the cellular 15-lipoxygenase pathway (By similarity). Can also reduce small soluble hydroperoxides such as H2O2 and tert-butyl hydroperoxide (PubMed:12566075)", "gene_name": "Gpx4", "glycan_count": 2, "glycosylation_sites": [], "id": "O70325", "name": "GPX3 (Glutathione peroxidase 3)", "organism": "Mus musculus", "uniprot_id": "O70325" }, { "function": "Catalyzes the last step of the oxidative degradation of choline to glycine. Converts sarcosine into glycine", "gene_name": "Sardh", "glycan_count": 1, "glycosylation_sites": [], "id": "Q99LB7", "name": "GPX5 (Glutathione peroxidase 5)", "organism": "Mus musculus", "uniprot_id": "Q99LB7" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P15633", "name": "GSTT1 (Glutathione S-transferase theta-1)", "organism": "Soybean chlorotic mottle virus", "uniprot_id": "P15633" }, { "function": "Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the formation of glutathione conjugates of both prostaglandin A2 (PGA2) and prostaglandin J2 (PGJ2). Participates in the formation of novel hepoxilin regioisomers", "gene_name": "Gstm1", "glycan_count": 1, "glycosylation_sites": [], "id": "P10649", "name": "GSTM1 (Glutathione S-transferase mu-1)", "organism": "Mus musculus", "uniprot_id": "P10649" }, { "function": "Cytosolic calcium-activated calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytosol and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules (PubMed:11316255). Repeated very high-level exercise increases the open probability of the channel and leads to Ca(2+) leaking into the cytoplasm (By similarity). Can also mediate the release of Ca(2+) from intracellular stores in neurons, and may thereby promote prolonged Ca(2+) signaling in the brain. Required for normal embryonic development of muscle fibers and skeletal muscle. Required for normal heart morphogenesis, skin development and ossification during embryogenesis (By similarity)", "gene_name": "Ryr1", "glycan_count": 0, "glycosylation_sites": [], "id": "O35208", "name": "CYP27B1 (Vitamin D 1-alpha-hydroxylase)", "organism": "Rattus norvegicus", "uniprot_id": "F1LMY4" }, { "function": "Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Plays a role in mitotic spindle assembly and metaphase plate congression", "gene_name": "Dync1h1", "glycan_count": 4, "glycosylation_sites": [], "id": "Q9JHU4", "name": "CYB5R3 (NADH-cytochrome b5 reductase 3)", "organism": "Mus musculus", "uniprot_id": "Q9JHU4" }, { "function": "Catalyzes the final rate-limiting step of glycolysis by mediating the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival", "gene_name": "Pkm", "glycan_count": 1, "glycosylation_sites": [], "id": "P52480", "name": "PKM (Pyruvate kinase M1/2)", "organism": "Mus musculus", "uniprot_id": "P52480" }, { "function": "NADPH oxidase that catalyzes predominantly the reduction of oxygen to H2O2 (By similarity). Can also catalyze to a smaller extent, the reduction of oxygen to superoxide (PubMed:10869423, PubMed:11098048, PubMed:15638999). May function as an oxygen sensor regulating the KCNK3/TASK-1 potassium channel and HIF1A activity (By similarity). May regulate insulin signaling cascade (By similarity). May play a role in apoptosis, bone resorption and lipolysaccharide-mediated activation of NFKB (By similarity). May produce superoxide in the nucleus and play a role in regulating gene expression upon cell stimulation (By similarity). Promotes ferroptosis, reactive oxygen species production and reduced glutathione (GSH) levels by activating NLRP3 inflammasome activation and cytokine release (By similarity)", "gene_name": "Nox4", "glycan_count": 0, "glycosylation_sites": [ { "position": 133, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 230, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9JHI8", "name": "FAA H (Fatty acid amide hydrolase)", "organism": "Mus musculus", "uniprot_id": "Q9JHI8" }, { "function": "G protein-coupled receptor for follitropin, the follicle-stimulating hormone (PubMed:11847099, PubMed:24058690, PubMed:24692546). Through cAMP production activates the downstream PI3K-AKT and ERK1/ERK2 signaling pathways (PubMed:24058690)", "gene_name": "FSHR", "glycan_count": 0, "glycosylation_sites": [ { "position": 191, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 199, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 293, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 318, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P23945", "name": "FSH receptor (FSHR)", "organism": "Homo sapiens", "uniprot_id": "P23945" }, { "function": "Acts as a coreceptor with members of the frizzled family of seven-transmembrane spanning receptors to transduce signal by Wnt proteins (PubMed:11336703, PubMed:11448771, PubMed:11719191, PubMed:15778503, PubMed:15908424, PubMed:16252235). Activates the canonical Wnt signaling pathway that controls cell fate determination and self-renewal during embryonic development and adult tissue regeneration (PubMed:11336703, PubMed:11719191). In particular, may play an important role in the development of the posterior patterning of the epiblast during gastrulation (By similarity). During bone development, regulates osteoblast proliferation and differentiation thus determining bone mass (PubMed:11719191). Mechanistically, the formation of the signaling complex between Wnt ligand, frizzled receptor and LRP5 coreceptor promotes the recruitment of AXIN1 to LRP5, stabilizing beta-catenin/CTNNB1 and activating TCF/LEF-mediated transcriptional programs (PubMed:11336703, PubMed:14731402, PubMed:24706814, PubMed:25920554). Acts as a coreceptor for non-Wnt proteins, such as norrin/NDP. Binding of norrin/NDP to frizzled 4/FZD4-LRP5 receptor complex triggers beta-catenin/CTNNB1-dependent signaling known to be required for retinal vascular development (PubMed:16252235, PubMed:27228167). Plays a role in controlling postnatal vascular regression in retina via macrophage-induced endothelial cell apoptosis (By similarity)", "gene_name": "LRP5", "glycan_count": 4, "glycosylation_sites": [ { "position": 93, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 138, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 446, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 499, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 705, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 878, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O75197", "name": "Low-density lipoprotein receptor-related protein 5 (LRP5)", "organism": "Homo sapiens", "uniprot_id": "O75197" }, { "function": "Tyrosine-protein kinase that acts as a cell-surface receptor for the cytokine FLT3LG and regulates differentiation, proliferation and survival of hematopoietic progenitor cells and of dendritic cells. Promotes phosphorylation of SHC1 and AKT1, and activation of the downstream effector MTOR. Promotes activation of RAS signaling and phosphorylation of downstream kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation of FES, FER, PTPN6/SHP, PTPN11/SHP-2, PLCG1, and STAT5A and/or STAT5B. Activation of wild-type FLT3 causes only marginal activation of STAT5A or STAT5B. Mutations that cause constitutive kinase activity promote cell proliferation and resistance to apoptosis via the activation of multiple signaling pathways", "gene_name": "FLT3", "glycan_count": 1, "glycosylation_sites": [ { "position": 43, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 100, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 151, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 306, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 323, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 351, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 354, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 473, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 502, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 541, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P36888", "name": "FLT3", "organism": "Homo sapiens", "uniprot_id": "P36888" }, { "function": "Could be a T-cell-specific adapter protein involved in the control of T-cell activation. May play a role in the CD4-p56-LCK-dependent signal transduction pathway. Could also play an important role in normal and pathological angiogenesis. Could be an adapter protein that facilitates and regulates interaction of KDR with effector proteins important to endothelial cell survival and proliferation", "gene_name": "SH2D2A", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NP31", "name": "SH2D2A (T cell-specific adaptor protein, TSAd)", "organism": "Homo sapiens", "uniprot_id": "Q9NP31" }, { "function": "Orphan receptor involved in cell adhesion and probably in cell-cell interactions specifically involving cells of the immune system. May play a role in regulatory T-cells (Treg) development", "gene_name": "Adgre1", "glycan_count": 1, "glycosylation_sites": [ { "position": 148, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 167, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 229, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 269, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 283, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 405, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 417, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 474, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 498, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 706, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q61549", "name": "F4/80 (EMR1)", "organism": "Mus musculus", "uniprot_id": "Q61549" }, { "function": "Could coordinate an aspect of bone turnover", "gene_name": "SPP2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q13103", "name": "SRSF3", "organism": "Homo sapiens", "uniprot_id": "Q13103" }, { "function": "Necessary for the splicing of pre-mRNA. It is required for formation of the earliest ATP-dependent splicing complex and interacts with spliceosomal components bound to both the 5'- and 3'-splice sites during spliceosome assembly. It also is required for ATP-dependent interactions of both U1 and U2 snRNPs with pre-mRNA. Interacts with other spliceosomal components, via the RS domains, to form a bridge between the 5'- and 3'-splice site binding components, U1 snRNP and U2AF. Binds to purine-rich RNA sequences, either 5'-AGSAGAGTA-3' (S=C or G) or 5'-GTTCGAGTA-3'. Can bind to beta-globin mRNA and commit it to the splicing pathway. The phosphorylated form (by SRPK2) is required for cellular apoptosis in response to cisplatin treatment", "gene_name": "SRSF2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q01130", "name": "SRSF2", "organism": "Homo sapiens", "uniprot_id": "Q01130" }, { "function": "Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Cognate/functional ephrin ligands for this receptor include EFNB1, EFNB2 and EFNB3. During nervous system development, regulates retinal axon guidance redirecting ipsilaterally ventrotemporal retinal ganglion cells axons at the optic chiasm midline. This probably requires repulsive interaction with EFNB2. In the adult nervous system together with EFNB3, regulates chemotaxis, proliferation and polarity of the hippocampus neural progenitors. In addition to its role in axon guidance also plays an important redundant role with other ephrin-B receptors in development and maturation of dendritic spines and synapse formation. May also regulate angiogenesis. More generally, may play a role in targeted cell migration and adhesion. Upon activation by EFNB1 and probably other ephrin-B ligands activates the MAPK/ERK and the JNK signaling cascades to regulate cell migration and adhesion respectively. Involved in the maintenance of the pool of satellite cells (muscle stem cells) by promoting their self-renewal and reducing their activation and differentiation (By similarity)", "gene_name": "EPHB1", "glycan_count": 1, "glycosylation_sites": [ { "position": 334, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 426, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 480, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P54762", "name": "EPHB1", "organism": "Homo sapiens", "uniprot_id": "P54762" }, { "function": "Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation (PubMed:20667974). Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophobic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system (PubMed:20667974, PubMed:9475419). Involved in PLA2G3-dependent maturation of mast cells. PLA2G3 is secreted by immature mast cells and acts on nearby fibroblasts upstream to PTDGS to synthesize PGD2, which in turn promotes mast cell maturation and degranulation via PTGDR (By similarity)", "gene_name": "PTGDS", "glycan_count": 222, "glycosylation_sites": [ { "position": 29, "type": "O-linked (GalNAc...) serine" }, { "position": 51, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 78, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P41222", "name": "Beta trace protein (BTP, aka Prostaglandin D synthase)", "organism": "Homo sapiens", "uniprot_id": "P41222" }, { "function": "Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis", "gene_name": "CTSF", "glycan_count": 0, "glycosylation_sites": [ { "position": 160, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 195, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 367, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 378, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 440, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UKQ5", "name": "Emilin-1", "organism": "Homo sapiens", "uniprot_id": "Q9UBX1" }, { "function": "Catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism (PubMed:17307971, PubMed:17712357, PubMed:24563466, PubMed:37821951). In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation (PubMed:17307971, PubMed:17712357). AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators (PubMed:17307971, PubMed:17712357). Regulates lipid synthesis by phosphorylating and inactivating lipid metabolic enzymes such as ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and cholesterol synthesis by phosphorylating acetyl-CoA carboxylase (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, respectively (By similarity). Promotes lipolysis of lipid droplets by mediating phosphorylation of isoform 1 of CHKA (CHKalpha2) (PubMed:34077757). Regulates insulin-signaling and glycolysis by phosphorylating IRS1, PFKFB2 and PFKFB3 (By similarity). AMPK stimulates glucose uptake in muscle by increasing the translocation of the glucose transporter SLC2A4/GLUT4 to the plasma membrane, possibly by mediating phosphorylation of TBC1D4/AS160 (By similarity). Regulates transcription and chromatin structure by phosphorylating transcription regulators involved in energy metabolism such as CRTC2/TORC2, FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, p53/TP53, SREBF1, SREBF2 and PPARGC1A (PubMed:11518699, PubMed:11554766, PubMed:15866171, PubMed:17711846, PubMed:18184930). Acts as a key regulator of glucose homeostasis in liver by phosphorylating CRTC2/TORC2, leading to CRTC2/TORC2 sequestration in the cytoplasm (By similarity). In response to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), leading to promote transcription (By similarity). Acts as a key regulator of cell growth and proliferation by phosphorylating FNIP1, TSC2, RPTOR, WDR24 and ATG1/ULK1: in response to nutrient limitation, negatively regulates the mTORC1 complex by phosphorylating RPTOR component of the mTORC1 complex and by phosphorylating and activating TSC2 (PubMed:14651849, PubMed:18439900, PubMed:20160076, PubMed:21205641). Also phosphorylates and inhibits GATOR2 subunit WDR24 in response to nutrient limitation, leading to suppress glucose-mediated mTORC1 activation (PubMed:36732624). In response to energetic stress, phosphorylates FNIP1, inactivating the non-canonical mTORC1 signaling, thereby promoting nuclear translocation of TFEB and TFE3, and inducing transcription of lysosomal or autophagy genes (PubMed:37079666). In response to nutrient limitation, promotes autophagy by phosphorylating and activating ATG1/ULK1 (PubMed:21205641). In that process, it also activates WDR45/WIPI4 (PubMed:28561066). Phosphorylates CASP6, thereby preventing its autoprocessing and subsequent activation (PubMed:32029622). In response to nutrient limitation, phosphorylates transcription factor FOXO3 promoting FOXO3 mitochondrial import (By similarity). Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin (PubMed:17486097). AMPK also acts as a regulator of circadian rhythm by mediating phosphorylation of CRY1, leading to destabilize it (By similarity). May regulate the Wnt signaling pathway by phosphorylating CTNNB1, leading to stabilize it (By similarity). Also has tau-protein kinase activity: in response to amyloid beta A4 protein (APP) exposure, activated by CAMKK2, leading to phosphorylation of MAPT/TAU; however the relevance of such data remains unclear in vivo (By similarity). Also phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1 (PubMed:12519745, PubMed:20074060). Regulates hepatic lipogenesis. Activated via SIRT3, represses sterol regulatory element-binding protein (SREBP) transcriptional activities and ATP-consuming lipogenesis to restore cellular energy balance. Upon stress, regulates mitochondrial fragmentation through phosphorylation of MTFR1L (PubMed:36367943)", "gene_name": "PRKAA1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UNQ4", "name": "OAT3 (SLC22A8)", "organism": "Homo sapiens", "uniprot_id": "Q13131" }, { "function": "Transporter that mediates the transport of endogenous and microbial zwitterions and organic cations (PubMed:10215651, PubMed:15107849, PubMed:15795384, PubMed:16729965, PubMed:20601551, PubMed:22206629, PubMed:22569296, PubMed:29530864). Functions as a Na(+)-dependent and pH-dependent high affinity microbial symporter of potent food-derived antioxidant ergothioeine (PubMed:15795384, PubMed:29530864, PubMed:33124720). Transports one sodium ion with one ergothioeine molecule (By similarity). Involved in the absorption of ergothioneine from the luminal/apical side of the small intestine and renal tubular cells, and into non-parenchymal liver cells, thereby contributing to maintain steady-state ergothioneine level in the body (PubMed:20601551). Also mediates the bidirectional transport of acetycholine, although the exact transport mechanism has not been fully identified yet (PubMed:22206629). Most likely exports anti-inflammatory acetylcholine in non-neuronal tissues, thereby contributing to the non-neuronal cholinergic system (PubMed:22206629, PubMed:22569296). Displays a general physiological role linked to better survival by controlling inflammation and oxidative stress, which may be related to ergothioneine and acetycholine transports (PubMed:15795384, PubMed:22206629). May also function as a low-affinity Na(+)-dependent transporter of L-carnitine through the mitochondrial membrane, thereby maintaining intracellular carnitine homeostasis (PubMed:10215651, PubMed:15107849, PubMed:16729965). May contribute to regulate the transport of cationic compounds in testis across the blood-testis-barrier (PubMed:35307651)", "gene_name": "SLC22A4", "glycan_count": 1, "glycosylation_sites": [ { "position": 57, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 64, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 91, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9H015", "name": "OCTN1 (SLC22A4)", "organism": "Homo sapiens", "uniprot_id": "Q9H015" }, { "function": "Multidrug efflux pump that functions as a H(+)/organic cation antiporter. Mediates the efflux of cationic compounds, such as the model cations, tetraethylammonium (TEA) and 1-methyl-4-phenylpyridinium (MPP+), the platinum-based drug oxaliplatin or weak bases that are positively charged at physiological pH, cimetidine, the platinum-based drugs cisplatin and oxaliplatin or the antidiabetic drug metformin. Mediates the efflux of endogenous compounds such as, creatinine, thiamine and estrone-3-sulfate. Plays a physiological role in the excretion of drugs, toxins and endogenous metabolites through the kidney", "gene_name": "SLC47A2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q86VL8", "name": "MATE2-K (SLC47A2)", "organism": "Homo sapiens", "uniprot_id": "Q86VL8" }, { "function": "Required to promote assembly of the transition zone in primary cilia. Acts by specifically recognizing and binding the axonemal microtubule. Localizes to the distal ends of centrioles before ciliogenesis and directly binds to axonemal microtubule, thereby promoting and restricting transition zone formation specifically at the cilia base. Required to mediate CEP290 association with microtubules (By similarity)", "gene_name": "Cep162", "glycan_count": 1, "glycosylation_sites": [], "id": "Q6ZQ06", "name": "OATP4C1 (SLCO4C1)", "organism": "Mus musculus", "uniprot_id": "Q6ZQ06" }, { "function": "Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis (PubMed:11516652, PubMed:12925766, PubMed:14610074, PubMed:14722118, PubMed:29449677). The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly (PubMed:11516652, PubMed:12925766, PubMed:14610074, PubMed:14722118, PubMed:26829474). Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis (PubMed:15249581). Required for central/midzone spindle assembly and cleavage furrow formation (PubMed:12458200, PubMed:12686604). Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: phosphorylates CHMP4C, leading to retain abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis (PubMed:22422861, PubMed:24814515). AURKB phosphorylates the CPC complex subunits BIRC5/survivin, CDCA8/borealin and INCENP (PubMed:11516652, PubMed:12925766, PubMed:14610074). Phosphorylation of INCENP leads to increased AURKB activity (PubMed:11516652, PubMed:12925766, PubMed:14610074). Other known AURKB substrates involved in centromeric functions and mitosis are CENPA, DES/desmin, GPAF, KIF2C, NSUN2, RACGAP1, SEPTIN1, VIM/vimentin, HASPIN, and histone H3 (PubMed:11756469, PubMed:11784863, PubMed:11856369, PubMed:12689593, PubMed:14602875, PubMed:16103226, PubMed:21658950). A positive feedback loop involving HASPIN and AURKB contributes to localization of CPC to centromeres (PubMed:21658950). Phosphorylation of VIM controls vimentin filament segregation in cytokinetic process, whereas histone H3 is phosphorylated at 'Ser-10' and 'Ser-28' during mitosis (H3S10ph and H3S28ph, respectively) (PubMed:11784863, PubMed:11856369). AURKB is also required for kinetochore localization of BUB1 and SGO1 (PubMed:15020684, PubMed:17617734). Phosphorylation of p53/TP53 negatively regulates its transcriptional activity (PubMed:20959462). Key regulator of active promoters in resting B- and T-lymphocytes: acts by mediating phosphorylation of H3S28ph at active promoters in resting B-cells, inhibiting RNF2/RING1B-mediated ubiquitination of histone H2A and enhancing binding and activity of the USP16 deubiquitinase at transcribed genes (By similarity). Acts as an inhibitor of CGAS during mitosis: catalyzes phosphorylation of the N-terminus of CGAS during the G2-M transition, blocking CGAS liquid phase separation and activation, and thereby preventing CGAS-induced autoimmunity (PubMed:33542149). Phosphorylates KRT5 during anaphase and telophase (By similarity). Phosphorylates ATXN10 which promotes phosphorylation of ATXN10 by PLK1 and may play a role in the regulation of cytokinesis and stimulating the proteasomal degradation of ATXN10 (PubMed:25666058)", "gene_name": "AURKB", "glycan_count": 2, "glycosylation_sites": [], "id": "Q96GD4", "name": "Aurora B kinase", "organism": "Homo sapiens", "uniprot_id": "Q96GD4" }, { "function": "Microtubule (MT)-binding protein that plays a role in the formation and maintenance of the spindle poles and the alignement and the segregation of chromosomes during mitotic cell division (PubMed:17172455, PubMed:19255246, PubMed:24996901, PubMed:26195665, PubMed:27462074, PubMed:7769006). Functions to tether the minus ends of MTs at the spindle poles, which is critical for the establishment and maintenance of the spindle poles (PubMed:11956313, PubMed:12445386). Plays a role in the establishment of the mitotic spindle orientation during metaphase and elongation during anaphase in a dynein-dynactin-dependent manner (PubMed:23870127, PubMed:24109598, PubMed:24996901, PubMed:26765568). In metaphase, part of a ternary complex composed of GPSM2 and G(i) alpha proteins, that regulates the recruitment and anchorage of the dynein-dynactin complex in the mitotic cell cortex regions situated above the two spindle poles, and hence regulates the correct oritentation of the mitotic spindle (PubMed:22327364, PubMed:23027904, PubMed:23921553). During anaphase, mediates the recruitment and accumulation of the dynein-dynactin complex at the cell membrane of the polar cortical region through direct association with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), and hence participates in the regulation of the spindle elongation and chromosome segregation (PubMed:22327364, PubMed:23921553, PubMed:24371089, PubMed:24996901). Also binds to other polyanionic phosphoinositides, such as phosphatidylinositol 3-phosphate (PIP), lysophosphatidic acid (LPA) and phosphatidylinositol triphosphate (PIP3), in vitro (PubMed:24371089, PubMed:24996901). Also required for proper orientation of the mitotic spindle during asymmetric cell divisions (PubMed:21816348). Plays a role in mitotic MT aster assembly (PubMed:11163243, PubMed:11229403, PubMed:12445386). Involved in anastral spindle assembly (PubMed:25657325). Positively regulates TNKS protein localization to spindle poles in mitosis (PubMed:16076287). Highly abundant component of the nuclear matrix where it may serve a non-mitotic structural role, occupies the majority of the nuclear volume (PubMed:10075938). Required for epidermal differentiation and hair follicle morphogenesis (By similarity)", "gene_name": "NUMA1", "glycan_count": 1, "glycosylation_sites": [ { "position": 1844, "type": "O-linked (GlcNAc) serine; alternate" } ], "id": "Q14980", "name": "NuMA", "organism": "Homo sapiens", "uniprot_id": "Q14980" }, { "function": "Acts as a transcriptional activator: mediates transcriptional activation by binding to E box-containing promoter consensus core sequences 5'-CANNTG-3'. Associates with the p300/CBP transcription coactivator complex to stimulate transcription of the secretin gene as well as the gene encoding the cyclin-dependent kinase inhibitor CDKN1A. Contributes to the regulation of several cell differentiation pathways, like those that promote the formation of early retinal ganglion cells, inner ear sensory neurons, granule cells forming either the cerebellum or the dentate gyrus cell layer of the hippocampus, endocrine islet cells of the pancreas and enteroendocrine cells of the small intestine. Together with PAX6 or SIX3, is required for the regulation of amacrine cell fate specification. Also required for dendrite morphogenesis and maintenance in the cerebellar cortex. Associates with chromatin to enhancer regulatory elements in genes encoding key transcriptional regulators of neurogenesis (By similarity)", "gene_name": "NEUROD1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q13562", "name": "NeuroD1", "organism": "Homo sapiens", "uniprot_id": "Q13562" }, { "function": "Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a direct role in DNA repair when directly recruited to sites of DNA damage. As part of the SIN3B complex represses transcription and counteracts the histone acetyltransferase activity of EP300 through the recognition H3K27ac marks by PHF12 and the activity of the histone deacetylase HDAC2 (PubMed:12391155, PubMed:14966270, PubMed:37137925). SIN3B complex is recruited downstream of the constitutively active genes transcriptional start sites through interaction with histones and mitigates histone acetylation and RNA polymerase II progression within transcribed regions contributing to the regulation of transcription (PubMed:21041482). Required for homologous recombination repair (HRR) and resistance to mitomycin C (MMC). Involved in the localization of PALB2, BRCA2 and RAD51, but not BRCA1, to DNA-damage foci", "gene_name": "MORF4L1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UBU8", "name": "Host cell factor 1 (HCF1)", "organism": "Homo sapiens", "uniprot_id": "Q9UBU8" }, { "function": "Putative inactive protein kinase which regulates signaling downstream of immune receptors including IL1R and Toll-like receptors (PubMed:10383454, PubMed:29686383). Inhibits dissociation of IRAK1 and IRAK4 from the Toll-like receptor signaling complex by either inhibiting the phosphorylation of IRAK1 and IRAK4 or stabilizing the receptor complex (By similarity). Upon IL33-induced lung inflammation, positively regulates expression of IL6, CSF3, CXCL2 and CCL5 mRNAs in dendritic cells (PubMed:29686383)", "gene_name": "IRAK3", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9Y616", "name": "GATA2", "organism": "Homo sapiens", "uniprot_id": "Q9Y616" }, { "function": "Transcription factor that plays an essential role in both trophoblast giant cell differentiation and in cardiac morphogenesis (By similarity). Binds the DNA sequence 5'-NRTCTG-3' (non-canonical E-box) (By similarity). Acts as a transcriptional repressor of SOX15 (By similarity). In the adult, could be required for ongoing expression of cardiac-specific genes (PubMed:9931445)", "gene_name": "HAND1", "glycan_count": 0, "glycosylation_sites": [], "id": "O96004", "name": "HAND1", "organism": "Homo sapiens", "uniprot_id": "O96004" }, { "function": "Transcription factor involved in the control of expression of placental growth factor (PGF) and other placenta-specific genes (PubMed:10542267, PubMed:18160678). Binds to the trophoblast-specific element 2 (TSE2) of the aromatase gene enhancer (PubMed:10542267). Binds to the SYDE1 promoter (PubMed:27917469). Has a central role in mediating the differentiation of trophoblast cells along both the villous and extravillous pathways in placental development (PubMed:19219068)", "gene_name": "GCM1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NP62", "name": "GCM1", "organism": "Homo sapiens", "uniprot_id": "Q9NP62" }, { "function": "", "gene_name": "FBRS", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9HAH7", "name": "OVOL1", "organism": "Homo sapiens", "uniprot_id": "Q9HAH7" }, { "function": "May play a role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Directly binds piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. Besides their function in transposable elements repression, piRNAs are probably involved in other processes during meiosis such as translation regulation (By similarity)", "gene_name": "PIWIL3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q7Z3Z3", "name": "ERVFRD1 (syncytin-2)", "organism": "Homo sapiens", "uniprot_id": "Q7Z3Z3" }, { "function": "Deubiquitinase that plays a role in several cellular processes including transcriptional regulation, cell cycle progression or innate immunity. As part of the transcription regulatory histone acetylation (HAT) complex SAGA, catalyzes the deubiquitination of both histones H2A and H2B, thereby acting as a transcriptional coactivator (PubMed:18206972, PubMed:18206973, PubMed:18469533). Recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Facilitates cell-cycle progression by stabilizing CCNB1 and antagonizing its proteasome-mediated degradation in a cell cycle-specific manner (PubMed:27030811). Modulates cell cycle progression and apoptosis also by antagonizing TP53 transcriptional activation through deacetylase SIRT1 stabilization (PubMed:22542455). Plays multiple roles in immunity and inflammation. Participates in antiviral response by deubiquitinating the importin KPNA2, leading to IRF3 nuclear translocation and subsequent type I interferon production (PubMed:32130408). Acts as a central regulator of type III IFN signaling by negatively regulating STING1 activation and ubiquitination (PubMed:35933402). Inhibits NLRP3 inflammasome activation by promoting NLRP3 degradation through ATG5-dependent autophagy (By similarity). Deubiquitinates CD274 to induce its stabilization and thereby participates in maintenance of immune tolerance to self (PubMed:31399419). Controls necroptotic cell death by regulating RIPK3 phosphorylation and ubiquitination (PubMed:33369872). During bacterial infection, promotes pro-inflammatory response by targeting TRAF6 and removing its 'Lys-48'-linked polyubiquitination (By similarity)", "gene_name": "USP22", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UPT9", "name": "UBE4A (Ubiquitination factor E4A)", "organism": "Homo sapiens", "uniprot_id": "Q9UPT9" }, { "function": "Minor apolipoprotein mainly associated with HDL and to a lesser extent with VLDL. May also be associated with chylomicrons. Important determinant of plasma triglyceride (TG) levels by both being a potent stimulator of apo-CII lipoprotein lipase (LPL) TG hydrolysis and an inhibitor of the hepatic VLDL-TG production rate (without affecting the VLDL-apoB production rate) (By similarity). Activates poorly lecithin:cholesterol acyltransferase (LCAT) and does not enhance efflux of cholesterol from macrophages. Binds heparin (PubMed:17326667)", "gene_name": "APOA5", "glycan_count": 1, "glycosylation_sites": [], "id": "Q6Q788", "name": "Apolipoprotein A-V (apoA-V)", "organism": "Homo sapiens", "uniprot_id": "Q6Q788" }, { "function": "Methylates CpG residues. Preferentially methylates hemimethylated DNA. Associates with DNA replication sites in S phase maintaining the methylation pattern in the newly synthesized strand, that is essential for epigenetic inheritance. Associates with chromatin during G2 and M phases to maintain DNA methylation independently of replication. It is responsible for maintaining methylation patterns established in development. DNA methylation is coordinated with methylation of histones. Mediates transcriptional repression by direct binding to HDAC2. In association with DNMT3B and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9. Probably forms a corepressor complex required for activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) or other tumor-related genes in colorectal cancer (CRC) cells (PubMed:24623306). Also required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs) (PubMed:24623306). Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing (PubMed:24623306). Promotes tumor growth (PubMed:24623306)", "gene_name": "DNMT1", "glycan_count": 2, "glycosylation_sites": [], "id": "P26358", "name": "DNMT1", "organism": "Homo sapiens", "uniprot_id": "P26358" }, { "function": "Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development (PubMed:12138111, PubMed:16357870, PubMed:30478443). DNA methylation is coordinated with methylation of histones (PubMed:12138111, PubMed:16357870, PubMed:30478443). It modifies DNA in a non-processive manner and also methylates non-CpG sites (PubMed:12138111, PubMed:16357870, PubMed:30478443). May preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1 (By similarity). Plays a role in paternal and maternal imprinting (By similarity). Required for methylation of most imprinted loci in germ cells (By similarity). Acts as a transcriptional corepressor for ZBTB18 (By similarity). Recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites (By similarity). Can actively repress transcription through the recruitment of HDAC activity (By similarity). Also has weak auto-methylation activity on Cys-710 in absence of DNA (By similarity)", "gene_name": "DNMT3A", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y6K1", "name": "DNMT3A", "organism": "Homo sapiens", "uniprot_id": "Q9Y6K1" }, { "function": "Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNA methylation is coordinated with methylation of histones. May preferentially methylates nucleosomal DNA within the nucleosome core region. May function as transcriptional co-repressor by associating with CBX4 and independently of DNA methylation. Seems to be involved in gene silencing (By similarity). In association with DNMT1 and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9. Isoforms 4 and 5 are probably not functional due to the deletion of two conserved methyltransferase motifs. Functions as a transcriptional corepressor by associating with ZHX1. Required for DUX4 silencing in somatic cells (PubMed:27153398)", "gene_name": "DNMT3B", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UBC3", "name": "DNMT3B", "organism": "Homo sapiens", "uniprot_id": "Q9UBC3" }, { "function": "Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC) and plays a key role in active DNA demethylation. Has a preference for 5-hydroxymethylcytosine in CpG motifs. Also mediates subsequent conversion of 5hmC into 5-formylcytosine (5fC), and conversion of 5fC to 5-carboxylcytosine (5caC). Conversion of 5mC into 5hmC, 5fC and 5caC probably constitutes the first step in cytosine demethylation. Methylation at the C5 position of cytosine bases is an epigenetic modification of the mammalian genome which plays an important role in transcriptional regulation. In addition to its role in DNA demethylation, also involved in the recruitment of the O-GlcNAc transferase OGT to CpG-rich transcription start sites of active genes, thereby promoting histone H2B GlcNAcylation by OGT", "gene_name": "TET2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q6N021", "name": "TET2", "organism": "Homo sapiens", "uniprot_id": "Q6N021" }, { "function": "Dioxygenase that catalyzes the conversion of the modified genomic base 5-methylcytosine (5mC) into 5-hydroxymethylcytosine (5hmC) and plays a key role in epigenetic chromatin reprogramming in the zygote following fertilization (PubMed:31928709). Also mediates subsequent conversion of 5hmC into 5-formylcytosine (5fC), and conversion of 5fC to 5-carboxylcytosine (5caC). Conversion of 5mC into 5hmC, 5fC and 5caC probably constitutes the first step in cytosine demethylation (By similarity). Selectively binds to the promoter region of target genes and contributes to regulate the expression of numerous developmental genes (PubMed:23217707). In zygotes, DNA demethylation occurs selectively in the paternal pronucleus before the first cell division, while the adjacent maternal pronucleus and certain paternally-imprinted loci are protected from this process. Participates in DNA demethylation in the paternal pronucleus by mediating conversion of 5mC into 5hmC, 5fC and 5caC. Does not mediate DNA demethylation of maternal pronucleus because of the presence of DPPA3/PGC7 on maternal chromatin that prevents TET3-binding to chromatin (By similarity). In addition to its role in DNA demethylation, also involved in the recruitment of the O-GlcNAc transferase OGT to CpG-rich transcription start sites of active genes, thereby promoting histone H2B GlcNAcylation by OGT (PubMed:23353889). Binds preferentially to DNA containing cytidine-phosphate-guanosine (CpG) dinucleotides over CpH (H=A, T, and C), hemimethylated-CpG and hemimethylated-hydroxymethyl-CpG (PubMed:29276034)", "gene_name": "TET3", "glycan_count": 1, "glycosylation_sites": [], "id": "O43151", "name": "TET3", "organism": "Homo sapiens", "uniprot_id": "O43151" }, { "function": "Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone", "gene_name": "NDUFB8", "glycan_count": 1, "glycosylation_sites": [], "id": "O95169", "name": "Complex I subunit NDUFB8", "organism": "Homo sapiens", "uniprot_id": "O95169" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9U3D0", "name": "OGT-1", "organism": "Caenorhabditis elegans", "uniprot_id": "Q9U3D0" }, { "function": "Required for neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes. Neddylation of cullins play an essential role in the regulation of SCF-type complexes activity. Does not act by preventing deneddylation, but rather facilitates neddylation, possibly by acting with rbx-1 to recruit the Nedd8-charged E2 enzyme to the cullin component of SCF-type complexes", "gene_name": "dcn-1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9U3C9", "name": "OGA-1", "organism": "Caenorhabditis elegans", "uniprot_id": "Q9U3C8" }, { "function": "", "gene_name": "nep-23", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9U2T1", "name": "NPR-1", "organism": "Caenorhabditis elegans", "uniprot_id": "Q9U2T1" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9U2S9", "name": "NPR-8", "organism": "", "uniprot_id": "Q9U2S9" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9U2T2", "name": "OCTR-1", "organism": "Caenorhabditis elegans", "uniprot_id": "Q9U2T2" }, { "function": "", "gene_name": "nccd-1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9U2T3", "name": "TOL-1", "organism": "Caenorhabditis elegans", "uniprot_id": "Q9U2T3" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9U2T4", "name": "DAF-2", "organism": "", "uniprot_id": "Q9U2T4" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9U2T5", "name": "DAF-7", "organism": "", "uniprot_id": "Q9U2T5" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9U2T6", "name": "LIN-1", "organism": "", "uniprot_id": "Q9U2T6" }, { "function": "Ceramide synthase that catalyzes the transfer of the acyl chain from acyl-CoA to a sphingoid base, with high selectivity toward palmitoyl-CoA (hexadecanoyl-CoA; C16:0-CoA) (PubMed:17609214, PubMed:17977534, PubMed:23530041, PubMed:26887952, PubMed:31916624). Can use other acyl donors, but with less efficiency (By similarity). N-acylates sphinganine and sphingosine bases to form dihydroceramides and ceramides in de novo synthesis and salvage pathways, respectively (PubMed:17977534, PubMed:23530041, PubMed:26887952, PubMed:31916624). Ceramides generated by CERS6 play a role in inflammatory response (By similarity). Acts as a regulator of metabolism and hepatic lipid accumulation (By similarity). Under high fat diet, palmitoyl- (C16:0-) ceramides generated by CERS6 specifically bind the mitochondrial fission factor MFF, thereby promoting mitochondrial fragmentation and contributing to the development of obesity (By similarity)", "gene_name": "CERS6", "glycan_count": 9, "glycosylation_sites": [ { "position": 18, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6ZMG9", "name": "Ceramide synthase 6 (CerS6)", "organism": "Homo sapiens", "uniprot_id": "Q6ZMG9" }, { "function": "", "gene_name": "TTC33", "glycan_count": 0, "glycosylation_sites": [], "id": "O95105", "name": "Pref-1 (preadipocyte factor-1/DLK1)", "organism": "Homo sapiens", "uniprot_id": "Q6PID6" }, { "function": "Mitochondrial aminoacyl-tRNA synthetase that catalyzes the specific attachment of the asparagine amino acid (aa) to the homologous transfer RNA (tRNA), further participating in protein synthesis (PubMed:25385316). The reaction occurs in a two steps: asparagine is first activated by ATP to form Asn-AMP and then transferred to the acceptor end of tRNA(Asn) (Probable)", "gene_name": "NARS2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96I59", "name": "GMPPA (mannose-1-phosphate guanyltransferase alpha)", "organism": "Homo sapiens", "uniprot_id": "Q96I59" }, { "function": "", "gene_name": "NARS2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q96I59-2", "name": "GMPPB (GDP-mannose pyrophosphorylase B)", "organism": "Homo sapiens", "uniprot_id": "Q96I59-2" }, { "function": "Converts guanidinoacetate to creatine, using S-adenosylmethionine as the methyl donor (PubMed:24415674, PubMed:26003046, PubMed:26319512). Important in nervous system development (PubMed:24415674)", "gene_name": "GAMT", "glycan_count": 1, "glycosylation_sites": [], "id": "Q14353", "name": "GFAT2 (Glutamine:fructose-6-phosphate amidotransferase 2)", "organism": "Homo sapiens", "uniprot_id": "Q14353" }, { "function": "Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (PubMed:29987188). Exists in two complexes, either with EIF1 or with EIF4E (mutually exclusive) (PubMed:29987188). Together with EIF1, is required for leaky scanning, in particular for avoiding cap-proximal start codon (PubMed:29987188). Together with EIF4E, antagonizes the scanning promoted by EIF1-EIF4G1 and locates the start codon (through a TISU element) without scanning (PubMed:29987188). As a member of the eIF4F complex, required for endoplasmic reticulum stress-induced ATF4 mRNA translation (PubMed:29062139)", "gene_name": "EIF4G1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q04637", "name": "eIF4G1", "organism": "Homo sapiens", "uniprot_id": "Q04637" }, { "function": "Nuclear receptor that exhibits a ligand-dependent transcriptional activation activity (PubMed:19481530, PubMed:25661920, PubMed:37478846). Interaction with retinoic acid receptor (RXR) shifts RXR from its role as a silent DNA-binding partner to an active ligand-binding subunit in mediating retinoid responses through target genes defined by LXRES (PubMed:37478846). LXRES are DR4-type response elements characterized by direct repeats of two similar hexanuclotide half-sites spaced by four nucleotides (By similarity). Plays an important role in the regulation of cholesterol homeostasis, regulating cholesterol uptake through MYLIP-dependent ubiquitination of LDLR, VLDLR and LRP8 (PubMed:19481530). Interplays functionally with RORA for the regulation of genes involved in liver metabolism (By similarity). Induces LPCAT3-dependent phospholipid remodeling in endoplasmic reticulum (ER) membranes of hepatocytes, driving SREBF1 processing and lipogenesis (By similarity). Via LPCAT3, triggers the incorporation of arachidonate into phosphatidylcholines of ER membranes, increasing membrane dynamics and enabling triacylglycerols transfer to nascent very low-density lipoprotein (VLDL) particles. Via LPCAT3 also counteracts lipid-induced ER stress response and inflammation, likely by modulating SRC kinase membrane compartmentalization and limiting the synthesis of lipid inflammatory mediators (By similarity)", "gene_name": "NR1H3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q13133", "name": "Liver X Receptor (LXR)", "organism": "Homo sapiens", "uniprot_id": "Q13133" }, { "function": "Receptor for hormone LEP/leptin (Probable) (PubMed:22405007). On ligand binding, mediates LEP central and peripheral effects through the activation of different signaling pathways such as JAK2/STAT3 and MAPK cascade/FOS. In the hypothalamus, LEP acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption by inducing anorexinogenic factors and suppressing orexigenic neuropeptides, also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones (By similarity) (PubMed:9537324). In the periphery, increases basal metabolism, influences reproductive function, regulates pancreatic beta-cell function and insulin secretion, is pro-angiogenic and affects innate and adaptive immunity (PubMed:12504075, PubMed:25060689, PubMed:8805376). Control of energy homeostasis and melanocortin production (stimulation of POMC and full repression of AgRP transcription) is mediated by STAT3 signaling, whereas distinct signals regulate NPY and the control of fertility, growth and glucose homeostasis. Involved in the regulation of counter-regulatory response to hypoglycemia by inhibiting neurons of the parabrachial nucleus. Has a specific effect on T lymphocyte responses, differentially regulating the proliferation of naive and memory T -ells. Leptin increases Th1 and suppresses Th2 cytokine production (By similarity)", "gene_name": "LEPR", "glycan_count": 22, "glycosylation_sites": [ { "position": 23, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 41, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 56, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 73, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 81, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 98, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 187, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 206, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 276, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 347, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 397, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 516, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 624, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 659, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 688, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 697, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 728, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 750, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P48357", "name": "Leptin receptor (LepR)", "organism": "Homo sapiens", "uniprot_id": "P48357" }, { "function": "In complex with CRLF1, forms a heterodimeric neurotropic cytokine that plays a crucial role during neuronal development (Probable). Also stimulates B-cells. Binds to and activates the ILST/gp130 receptor", "gene_name": "CLCF1", "glycan_count": 0, "glycosylation_sites": [ { "position": 29, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UBD9", "name": "SSR4 (Translocon-associated protein subunit delta, TRAP-\u03b4)", "organism": "Homo sapiens", "uniprot_id": "Q9UBD9" }, { "function": "The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids. HSD VII is active against four 7-alpha-hydroxylated sterols. Does not metabolize several different C(19/21) steroids as substrates. Involved in bile acid synthesis (PubMed:11067870). Plays a key role in cell positioning and movement in lymphoid tissues by mediating degradation of 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC): 7-alpha,25-OHC acts as a ligand for the G protein-coupled receptor GPR183/EBI2, a chemotactic receptor for a number of lymphoid cells (By similarity)", "gene_name": "HSD3B7", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H2F3", "name": "SRD5A3 (Steroid 5\u03b1-reductase type 3)", "organism": "Homo sapiens", "uniprot_id": "Q9H2F3" }, { "function": "Converts inositol hexakisphosphate (InsP6) to diphosphoinositol pentakisphosphate (InsP7/PP-InsP5). Converts 1,3,4,5,6-pentakisphosphate (InsP5) to PP-InsP4", "gene_name": "IP6K1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q92551", "name": "Inositol hexakisphosphate kinase 1 (IP6K1)", "organism": "Homo sapiens", "uniprot_id": "Q92551" }, { "function": "Subunit of heteromeric glycine-gated chloride channels (PubMed:15302677, PubMed:16144831, PubMed:2155780, PubMed:23895467, PubMed:25445488, PubMed:26370147, PubMed:34473954). Plays a role in synaptic plasticity (By similarity). Contributes to the generation of inhibitory postsynaptic currents, and is involved in the down-regulation of neuronal excitability (PubMed:25445488). Plays a role in cellular responses to ethanol (PubMed:23895467)", "gene_name": "GLRA2", "glycan_count": 1, "glycosylation_sites": [ { "position": 72, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 103, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P23416", "name": "Glycine receptor alpha 2 (GlyR\u03b12)", "organism": "Homo sapiens", "uniprot_id": "P23416" }, { "function": "Glycine receptors are ligand-gated chloride channels. Channel opening is triggered by extracellular glycine (PubMed:26416729, PubMed:9677400). Channel characteristics depend on the subunit composition; heteropentameric channels display faster channel closure (By similarity). Plays an important role in the down-regulation of neuronal excitability (By similarity). Contributes to the generation of inhibitory postsynaptic currents (By similarity). Contributes to increased pain perception in response to increased prostaglandin E2 levels (By similarity). Plays a role in cellular responses to ethanol (By similarity)", "gene_name": "GLRA3", "glycan_count": 1, "glycosylation_sites": [ { "position": 71, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O75311", "name": "Glycine receptor alpha 3 (GlyR\u03b13)", "organism": "Homo sapiens", "uniprot_id": "O75311" }, { "function": "Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD3/SMAD4 complex, activates transcription. Also can form a SMAD3/SMAD4/JUN/FOS complex at the AP-1/SMAD site to regulate TGF-beta-mediated transcription. Has an inhibitory effect on wound healing probably by modulating both growth and migration of primary keratinocytes and by altering the TGF-mediated chemotaxis of monocytes. This effect on wound healing appears to be hormone-sensitive. Regulator of chondrogenesis and osteogenesis and inhibits early healing of bone fractures. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator", "gene_name": "SMAD3", "glycan_count": 1, "glycosylation_sites": [], "id": "P84022", "name": "SMAD3", "organism": "Homo sapiens", "uniprot_id": "P84022" }, { "function": "Calcium/calmodulin-dependent myosin light chain kinase implicated in smooth muscle contraction via phosphorylation of myosin light chains (MLC). Also regulates actin-myosin interaction through a non-kinase activity. Phosphorylates PTK2B/PYK2 and myosin light-chains. Involved in the inflammatory response (e.g. apoptosis, vascular permeability, leukocyte diapedesis), cell motility and morphology, airway hyperreactivity and other activities relevant to asthma. Required for tonic airway smooth muscle contraction that is necessary for physiological and asthmatic airway resistance. Necessary for gastrointestinal motility. Implicated in the regulation of endothelial as well as vascular permeability, probably via the regulation of cytoskeletal rearrangements. In the nervous system it has been shown to control the growth initiation of astrocytic processes in culture and to participate in transmitter release at synapses formed between cultured sympathetic ganglion cells. Critical participant in signaling sequences that result in fibroblast apoptosis. Plays a role in the regulation of epithelial cell survival. Required for epithelial wound healing, especially during actomyosin ring contraction during purse-string wound closure. Mediates RhoA-dependent membrane blebbing. Triggers TRPC5 channel activity in a calcium-dependent signaling, by inducing its subcellular localization at the plasma membrane. Promotes cell migration (including tumor cells) and tumor metastasis. PTK2B/PYK2 activation by phosphorylation mediates ITGB2 activation and is thus essential to trigger neutrophil transmigration during acute lung injury (ALI). May regulate optic nerve head astrocyte migration. Probably involved in mitotic cytoskeletal regulation. Regulates tight junction probably by modulating ZO-1 exchange in the perijunctional actomyosin ring. Mediates burn-induced microvascular barrier injury; triggers endothelial contraction in the development of microvascular hyperpermeability by phosphorylating MLC. Essential for intestinal barrier dysfunction. Mediates Giardia spp.-mediated reduced epithelial barrier function during giardiasis intestinal infection via reorganization of cytoskeletal F-actin and tight junctional ZO-1. Necessary for hypotonicity-induced Ca(2+) entry and subsequent activation of volume-sensitive organic osmolyte/anion channels (VSOAC) in cervical cancer cells. Responsible for high proliferative ability of breast cancer cells through anti-apoptosis", "gene_name": "MYLK", "glycan_count": 1, "glycosylation_sites": [], "id": "Q15746", "name": "MYLK", "organism": "Homo sapiens", "uniprot_id": "Q15746" }, { "function": "Antigen-presenting major histocompatibility complex class I (MHCI) molecule. In complex with B2M/beta 2 microglobulin displays primarily viral and tumor-derived peptides on antigen-presenting cells for recognition by alpha-beta T cell receptor (TCR) on HLA-B-restricted CD8-positive T cells, guiding antigen-specific T cell immune response to eliminate infected or transformed cells (PubMed:23209413, PubMed:25808313, PubMed:29531227, PubMed:9620674). May also present self-peptides derived from the signal sequence of secreted or membrane proteins, although T cells specific for these peptides are usually inactivated to prevent autoreactivity (PubMed:18991276, PubMed:7743181). Both the peptide and the MHC molecule are recognized by TCR, the peptide is responsible for the fine specificity of antigen recognition and MHC residues account for the MHC restriction of T cells (PubMed:24600035, PubMed:29531227, PubMed:9620674). Typically presents intracellular peptide antigens of 8 to 13 amino acids that arise from cytosolic proteolysis via constitutive proteasome and IFNG-induced immunoproteasome (PubMed:23209413). Can bind different peptides containing allele-specific binding motifs, which are mainly defined by anchor residues at position 2 and 9 (PubMed:25808313, PubMed:29531227)", "gene_name": "HLA-B", "glycan_count": 0, "glycosylation_sites": [ { "position": 110, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P03989", "name": "HLA-B", "organism": "Homo sapiens", "uniprot_id": "P01889" }, { "function": "Caspase inhibitor. Acts as a regulator of procaspase-1/CASP1 activation implicated in the regulation of the proteolytic maturation of pro-interleukin-1 beta (IL1B) and its release during inflammation. Inhibits the release of IL1B in response to LPS in monocytes. Also induces NF-kappa-B activation during the pro-inflammatory cytokine response. Also able to inhibit CASP1-mediated neuronal cell death, TNF-alpha, hypoxia-, UV-, and staurosporine-mediated cell death but not ER stress-mediated cell death. Acts by preventing activation of caspases CASP1 and CASP4, possibly by preventing the interaction between CASP1 and RIPK2", "gene_name": "CARD16", "glycan_count": 0, "glycosylation_sites": [], "id": "Q5EG05", "name": "Kif11", "organism": "Homo sapiens", "uniprot_id": "Q5EG05" }, { "function": "Bifunctional zinc metalloenzyme that comprises both epoxide hydrolase (EH) and aminopeptidase activities. Acts as an epoxide hydrolase to catalyze the conversion of LTA4 to the pro-inflammatory mediator leukotriene B4 (LTB4) (PubMed:11917124, PubMed:12207002, PubMed:15078870, PubMed:18804029, PubMed:1897988, PubMed:1975494, PubMed:2244921). Also has aminopeptidase activity, with high affinity for N-terminal arginines of various synthetic tripeptides (PubMed:18804029, PubMed:20813919). In addition to its pro-inflammatory EH activity, may also counteract inflammation by its aminopeptidase activity, which inactivates by cleavage another neutrophil attractant, the tripeptide Pro-Gly-Pro (PGP), a bioactive fragment of collagen generated by the action of matrix metalloproteinase-9 (MMP9) and prolylendopeptidase (PREPL) (PubMed:20813919, PubMed:24591641). Involved also in the biosynthesis of resolvin E1 and 18S-resolvin E1 from eicosapentaenoic acid, two lipid mediators that show potent anti-inflammatory and pro-resolving actions (PubMed:21206090)", "gene_name": "LTA4H", "glycan_count": 2, "glycosylation_sites": [], "id": "P09960", "name": "LTA4H", "organism": "Homo sapiens", "uniprot_id": "P09960" }, { "function": "Receptor for granulocyte colony-stimulating factor (CSF3), essential for granulocytic maturation. Plays a crucial role in the proliferation, differentiation and survival of cells along the neutrophilic lineage. In addition it may function in some adhesion or recognition events at the cell surface", "gene_name": "CSF3R", "glycan_count": 0, "glycosylation_sites": [ { "position": 51, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 93, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 128, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 134, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 389, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 474, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 579, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 610, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q99062", "name": "CSF3R", "organism": "Homo sapiens", "uniprot_id": "Q99062" }, { "function": "Catalyzes the hydrolysis of triglycerides and phospholipids present in circulating plasma lipoproteins, including chylomicrons, intermediate density lipoproteins (IDL), low density lipoproteins (LDL) of large size and high density lipoproteins (HDL), releasing free fatty acids (FFA) and smaller lipoprotein particles (PubMed:12032167, PubMed:26193433, PubMed:7592706, PubMed:8798474). Also exhibits lysophospholipase activity (By similarity). Can hydrolyze both neutral lipid and phospholipid substrates but shows a greater binding affinity for neutral lipid substrates than phospholipid substrates (By similarity). In native LDL, preferentially hydrolyzes the phosphatidylcholine species containing polyunsaturated fatty acids at sn-2 position (PubMed:26193433)", "gene_name": "LIPC", "glycan_count": 27, "glycosylation_sites": [ { "position": 42, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 78, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 362, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 397, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P11150", "name": "Lipase", "organism": "Homo sapiens", "uniprot_id": "P11150" }, { "function": "Integrin ITGAM/ITGB2 is implicated in various adhesive interactions of monocytes, macrophages and granulocytes as well as in mediating the uptake of complement-coated particles and pathogens (PubMed:20008295, PubMed:9558116). It is identical with CR-3, the receptor for the iC3b fragment of the third complement component. It probably recognizes the R-G-D peptide in C3b. Integrin ITGAM/ITGB2 is also a receptor for fibrinogen, factor X and ICAM1. It recognizes P1 and P2 peptides of fibrinogen gamma chain. Regulates neutrophil migration (PubMed:28807980). In association with beta subunit ITGB2/CD18, required for CD177-PRTN3-mediated activation of TNF primed neutrophils (PubMed:21193407). May regulate phagocytosis-induced apoptosis in extravasated neutrophils (By similarity). May play a role in mast cell development (By similarity). Required with TYROBP/DAP12 in microglia to control production of microglial superoxide ions which promote the neuronal apoptosis that occurs during brain development (By similarity)", "gene_name": "ITGAM", "glycan_count": 39, "glycosylation_sites": [ { "position": 86, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 240, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 391, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 469, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 692, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 696, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 734, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 801, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 880, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 900, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 911, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 940, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 946, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 978, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 993, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1021, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1044, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1050, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1075, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P11215", "name": "ITGAM", "organism": "Homo sapiens", "uniprot_id": "P11215" }, { "function": "Sorting receptor that directs prohormones to the regulated secretory pathway. Also acts as a prohormone processing enzyme in neuro/endocrine cells, removing dibasic residues from the C-terminal end of peptide hormone precursors after initial endoprotease cleavage", "gene_name": "CPE", "glycan_count": 22, "glycosylation_sites": [ { "position": 139, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 390, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P16870", "name": "Carboxypeptidase E", "organism": "Homo sapiens", "uniprot_id": "P16870" }, { "function": "Zinc endopeptidase with endothelin-3-converting enzyme activity. Cleaves EDN1, EDN2 and EDN3, with a marked preference for EDN3", "gene_name": "KEL", "glycan_count": 2, "glycosylation_sites": [ { "position": 94, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 115, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 191, "type": "N-linked (GlcNAc...) asparagine; in KEL2 antigen" }, { "position": 345, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 627, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P23276", "name": "Kell antigen (K)", "organism": "Homo sapiens", "uniprot_id": "P23276" }, { "function": "May be part of an oligomeric complex which is likely to have a transport or channel function in the erythrocyte membrane", "gene_name": "RHD", "glycan_count": 0, "glycosylation_sites": [], "id": "Q02161", "name": "RhD antigen", "organism": "Homo sapiens", "uniprot_id": "Q02161" }, { "function": "This protein is the basis of the ABO blood group system. The histo-blood group ABO involves three carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity that converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals lack such activity", "gene_name": "ABO", "glycan_count": 0, "glycosylation_sites": [ { "position": 113, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P16442", "name": "A antigen (ABO)", "organism": "Homo sapiens", "uniprot_id": "P16442" }, { "function": "Cell surface proteoglycan that bears heparan sulfate. Binds, via the heparan sulfate side chains, alpha-4 (V) collagen and participates in Schwann cell myelination (By similarity). May act as a catalyst in increasing the rate of conversion of prion protein PRPN(C) to PRNP(Sc) via associating (via the heparan sulfate side chains) with both forms of PRPN, targeting them to lipid rafts and facilitating their interaction. Required for proper skeletal muscle differentiation by sequestering FGF2 in lipid rafts preventing its binding to receptors (FGFRs) and inhibiting the FGF-mediated signaling", "gene_name": "GPC1", "glycan_count": 18, "glycosylation_sites": [ { "position": 79, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 116, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 486, "type": "O-linked (Xyl...) (heparan sulfate) serine" }, { "position": 488, "type": "O-linked (Xyl...) (heparan sulfate) serine" }, { "position": 490, "type": "O-linked (Xyl...) (heparan sulfate) serine" } ], "id": "P35052", "name": "Glypican-1 (GPC1)", "organism": "Homo sapiens", "uniprot_id": "P35052" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P05260", "name": "ALT", "organism": "", "uniprot_id": "" }, { "function": "Specifically binds vasopressin", "gene_name": "AVP", "glycan_count": 0, "glycosylation_sites": [ { "position": 131, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01185", "name": "Antidiuretic hormone (ADH, also called vasopressin)", "organism": "Homo sapiens", "uniprot_id": "P01185" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q99523-variant", "name": "Sortilin (truncated splice variant, Sort_T)", "organism": "", "uniprot_id": "" }, { "function": "Converts inositol hexakisphosphate (InsP6) to diphosphoinositol pentakisphosphate (InsP7/PP-InsP5)", "gene_name": "IP6K2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UHH9", "name": "Inositol polyphosphate multikinase (IPMK)", "organism": "Homo sapiens", "uniprot_id": "Q9UHH9" }, { "function": "Neuroendocrine peptide which is a critical regulator of cellular and organ growth, development, migration, differentiation and survival and of epithelial calcium ion transport (PubMed:12538599, PubMed:35932760, PubMed:3616618). Acts by binding to its receptor, PTH1R, activating G protein-coupled receptor signaling (PubMed:19674967, PubMed:35932760). Regulates endochondral bone development and epithelial-mesenchymal interactions during the formation of the mammary glands and teeth (By similarity). Required for skeletal homeostasis (PubMed:12538599). Promotes mammary mesenchyme differentiation and bud outgrowth by modulating mesenchymal cell responsiveness to BMPs (PubMed:12538599). Up-regulates BMPR1A expression in the mammary mesenchyme and this increases the sensitivity of these cells to BMPs and allows them to respond to BMP4 in a paracrine and/or autocrine fashion (By similarity). BMP4 signaling in the mesenchyme, in turn, triggers epithelial outgrowth and augments MSX2 expression, which causes the mammary mesenchyme to inhibit hair follicle formation within the nipple sheath (By similarity). Promotes colon cancer cell migration and invasion in an integrin alpha-6/beta-1-dependent manner through activation of Rac1 (PubMed:20637541)", "gene_name": "PTHLH", "glycan_count": 2, "glycosylation_sites": [], "id": "P12272", "name": "Parathyroid hormone-related protein (PTHrP)", "organism": "Homo sapiens", "uniprot_id": "P12272" }, { "function": "Plays a regulatory role in the organization of neuroendocrine signals accessing the anterior pituitary gland. Stimulates water drinking and food intake. May play a role in the hypothalamic response to stress (By similarity). NPW23 activates GPR7 and GPR8 more efficiently than NPW30", "gene_name": "NPW", "glycan_count": 0, "glycosylation_sites": [ { "position": 133, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" } ], "id": "Q8N729", "name": "Spexin (Neuropeptide Q)", "organism": "Homo sapiens", "uniprot_id": "Q8N729" }, { "function": "DNA repair protein involved in DNA non-homologous end joining (NHEJ); it is required for double-strand break (DSB) repair and V(D)J recombination and is also involved in telomere maintenance (PubMed:16439204, PubMed:16439205, PubMed:17317666, PubMed:17470781, PubMed:17717001, PubMed:18158905, PubMed:18644470, PubMed:20558749, PubMed:26100018, PubMed:28369633). Plays a key role in NHEJ by promoting the ligation of various mismatched and non-cohesive ends (PubMed:17470781, PubMed:17717001, PubMed:19056826). Together with PAXX, collaborates with DNA polymerase lambda (POLL) to promote joining of non-cohesive DNA ends (PubMed:25670504, PubMed:30250067). May act in concert with XRCC5-XRCC6 (Ku) to stimulate XRCC4-mediated joining of blunt ends and several types of mismatched ends that are non-complementary or partially complementary (PubMed:16439204, PubMed:16439205, PubMed:17317666, PubMed:17470781). In some studies, has been shown to associate with XRCC4 to form alternating helical filaments that bridge DNA and act like a bandage, holding together the broken DNA until it is repaired (PubMed:21768349, PubMed:21775435, PubMed:22228831, PubMed:22287571, PubMed:26100018, PubMed:27437582, PubMed:28500754). Alternatively, it has also been shown that rather than forming filaments, a single NHEJ1 dimer interacts through both head domains with XRCC4 to promote the close alignment of DNA ends (By similarity). The XRCC4-NHEJ1/XLF subcomplex binds to the DNA fragments of a DSB in a highly diffusive manner and robustly bridges two independent DNA molecules, holding the broken DNA fragments in close proximity to one other (PubMed:27437582, PubMed:28500754). The mobility of the bridges ensures that the ends remain accessible for further processing by other repair factors (PubMed:27437582). Binds DNA in a length-dependent manner (PubMed:17317666, PubMed:18158905)", "gene_name": "NHEJ1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H9Q4", "name": "IL21R", "organism": "Homo sapiens", "uniprot_id": "Q9H9Q4" }, { "function": "Receptor for the C-X-C chemokine CXCL16. Used as a coreceptor by SIVs and by strains of HIV-2 and m-tropic HIV-1", "gene_name": "CXCR6", "glycan_count": 0, "glycosylation_sites": [ { "position": 16, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O00574", "name": "CXCR6", "organism": "Homo sapiens", "uniprot_id": "O00574" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P46531 (NOTCH1)", "name": "NOTCH", "organism": "", "uniprot_id": "" }, { "function": "Nucleolar protein which is involved in the integration of the 5S RNP into the ribosomal large subunit during ribosome biogenesis (PubMed:24120868). In ribosome biogenesis, may also play a role in rRNA transcription (PubMed:27729611). Also functions as a nucleolar sensor that regulates the activation of p53/TP53 in response to ribosome biogenesis perturbation, DNA damage and other stress conditions (PubMed:21741933, PubMed:24120868, PubMed:27829214). DNA damage or perturbation of ribosome biogenesis disrupt the interaction between NOP53 and RPL11 allowing RPL11 transport to the nucleoplasm where it can inhibit MDM2 and allow p53/TP53 activation (PubMed:24120868, PubMed:27829214). It may also positively regulate the function of p53/TP53 in cell cycle arrest and apoptosis through direct interaction, preventing its MDM2-dependent ubiquitin-mediated proteasomal degradation (PubMed:22522597). Originally identified as a tumor suppressor, it may also play a role in cell proliferation and apoptosis by positively regulating the stability of PTEN, thereby antagonizing the PI3K-AKT/PKB signaling pathway (PubMed:15355975, PubMed:16971513, PubMed:27729611). May also inhibit cell proliferation and increase apoptosis through its interaction with NF2 (PubMed:21167305). May negatively regulate NPM1 by regulating its nucleoplasmic localization, oligomerization and ubiquitin-mediated proteasomal degradation (PubMed:25818168). Thereby, may prevent NPM1 interaction with MYC and negatively regulate transcription mediated by the MYC-NPM1 complex (PubMed:25956029). May also regulate cellular aerobic respiration (PubMed:24556985). In the cellular response to viral infection, may play a role in the attenuation of interferon-beta through the inhibition of RIGI (PubMed:27824081)", "gene_name": "NOP53", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NZM5", "name": "NINJ2", "organism": "Homo sapiens", "uniprot_id": "Q9NZM5" }, { "function": "Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Represses MEF2-dependent transcription", "gene_name": "HDAC9", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UKV0", "name": "HDAC9", "organism": "Homo sapiens", "uniprot_id": "Q9UKV0" }, { "function": "P4-ATPase flippase which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation also seems to be implicated in vesicle formation and in uptake of lipid signaling molecules. May be responsible for the maintenance of asymmetric distribution of phosphatidylserine (PS) in spermatozoa membranes. Involved in acrosome reactions and binding of spermatozoa to zona pellucida", "gene_name": "ATP8B3", "glycan_count": 0, "glycosylation_sites": [], "id": "O60423", "name": "ALOX5AP", "organism": "Homo sapiens", "uniprot_id": "O60423" }, { "function": "Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX and participates to the sixth step in the heme biosynthetic pathway", "gene_name": "CPOX", "glycan_count": 2, "glycosylation_sites": [], "id": "P36551", "name": "CYP4A11", "organism": "Homo sapiens", "uniprot_id": "P36551" }, { "function": "Transcriptional regulator which can act as an activator or a repressor. Inhibits the enhancer element of the AFP gene by binding to its AT-rich core sequence. In concert with SMAD-dependent TGF-beta signaling can repress the transcription of AFP via its interaction with SMAD2/3 (PubMed:25105025). Regulates the circadian locomotor rhythms via transcriptional activation of neuropeptidergic genes which are essential for intercellular synchrony and rhythm amplitude in the suprachiasmatic nucleus (SCN) of the brain (By similarity). Regulator of myoblasts differentiation through the binding to the AT-rich sequence of MYF6 promoter and promoter repression (PubMed:11312261). Down-regulates the MUC5AC promoter in gastric cancer (PubMed:17330845). In association with RUNX3, up-regulates CDKN1A promoter activity following TGF-beta stimulation (PubMed:20599712). Inhibits estrogen receptor (ESR1) function by selectively competing with coactivator NCOA3 for binding to ESR1 in ESR1-positive breast cancer cells (PubMed:20720010)", "gene_name": "ZFHX3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q15911", "name": "ZFHX3", "organism": "Homo sapiens", "uniprot_id": "Q15911" }, { "function": "", "gene_name": "C1orf74", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96LT6", "name": "LGI1", "organism": "Homo sapiens", "uniprot_id": "Q96LT6" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P08648 (ITGA5), P05556 (ITGB1)", "name": "Integrin \u03b15\u03b21", "organism": "", "uniprot_id": "" }, { "function": "Plays a role in the cellular response to UV irradiation. Mediates G2/M cell cycle arrest, MEK autoactivation and ERK1/2-signaling pathway activation in response to UV irradiation. In ciliated cells of airways, it is involved in the regulation of mucociliary transport (PubMed:31959991)", "gene_name": "NEK10", "glycan_count": 1, "glycosylation_sites": [], "id": "Q6ZWH5", "name": "G6b-B", "organism": "Homo sapiens", "uniprot_id": "Q6ZWH5" }, { "function": "Inactivates MAP kinases. Has a specificity for the ERK family", "gene_name": "DUSP9", "glycan_count": 0, "glycosylation_sites": [], "id": "Q99956", "name": "Tissue Factor Pathway Inhibitor 2 (TFPI2)", "organism": "Homo sapiens", "uniprot_id": "Q99956" }, { "function": "Receptor for the Fc region of immunoglobulins gamma. Low affinity receptor. Binds complexed or aggregated IgG and also monomeric IgG. Contrary to III-A, is not capable to mediate antibody-dependent cytotoxicity and phagocytosis. May serve as a trap for immune complexes in the peripheral circulation which does not activate neutrophils", "gene_name": "FCGR3B", "glycan_count": 40, "glycosylation_sites": [ { "position": 56, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 63, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 82, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 92, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 180, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 187, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O75015", "name": "FCGR3B", "organism": "Homo sapiens", "uniprot_id": "O75015" }, { "function": "Tyrosine-protein kinase that acts as a cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation, migration and apoptosis, and in the regulation of embryonic development. Required for normal embryonic patterning, trophoblast function, limb bud development, lung morphogenesis, osteogenesis and skin development. Plays an essential role in the regulation of osteoblast differentiation, proliferation and apoptosis, and is required for normal skeleton development. Promotes cell proliferation in keratinocytes and immature osteoblasts, but promotes apoptosis in differentiated osteoblasts. Phosphorylates PLCG1, FRS2 and PAK4. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. FGFR2 signaling is down-regulated by ubiquitination, internalization and degradation. Mutations that lead to constitutive kinase activation or impair normal FGFR2 maturation, internalization and degradation lead to aberrant signaling. Over-expressed FGFR2 promotes activation of STAT1", "gene_name": "FGFR2", "glycan_count": 7, "glycosylation_sites": [ { "position": 83, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 123, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 228, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 241, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 265, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 297, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 318, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 331, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P21802", "name": "FGFR2", "organism": "Homo sapiens", "uniprot_id": "P21802" }, { "function": "The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). RAB6C may be involved in the regulation of centrosome duplication and cell cycle progression", "gene_name": "RAB6C", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H0N0", "name": "RBEL1A (Rab-like protein 1A)", "organism": "Homo sapiens", "uniprot_id": "Q9H0N0" }, { "function": "Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:10066435, PubMed:10497169, PubMed:10644755, PubMed:10835356, PubMed:11158290, PubMed:11238952, PubMed:11359933, PubMed:11994270, PubMed:12791267, PubMed:12902344, PubMed:14603323, PubMed:14681206, PubMed:14988407, PubMed:15448698, PubMed:15917222, PubMed:16371461, PubMed:22017875, PubMed:22017876, PubMed:22017877, PubMed:22087322, PubMed:25503564, PubMed:25704143, PubMed:36608670, PubMed:9859996, PubMed:9990852). Recognizes and binds to phosphorylated target proteins (PubMed:10066435, PubMed:10497169, PubMed:10644755, PubMed:10835356, PubMed:11158290, PubMed:11238952, PubMed:11359933, PubMed:11994270, PubMed:12791267, PubMed:12902344, PubMed:14603323, PubMed:14681206, PubMed:14988407, PubMed:15448698, PubMed:15917222, PubMed:16371461, PubMed:22017875, PubMed:22017876, PubMed:22017877, PubMed:22087322, PubMed:25503564, PubMed:25704143, PubMed:36608670, PubMed:9859996, PubMed:9990852). SCF(BTRC) mediates the ubiquitination of CTNNB1 and participates in Wnt signaling (PubMed:12077367, PubMed:12820959). SCF(BTRC) mediates the ubiquitination of phosphorylated NFKB1, ATF4, CDC25A, DLG1, FBXO5, PER1, SMAD3, SMAD4, SNAI1 and probably NFKB2 (PubMed:10835356, PubMed:11238952, PubMed:14603323, PubMed:14681206). SCF(BTRC) mediates the ubiquitination of NFKBIA, NFKBIB and NFKBIE; the degradation frees the associated NFKB1 to translocate into the nucleus and to activate transcription (PubMed:10066435, PubMed:10497169, PubMed:10644755, PubMed:9859996). Ubiquitination of NFKBIA occurs at 'Lys-21' and 'Lys-22' (PubMed:10066435). The SCF(FBXW11) complex also regulates NF-kappa-B by mediating ubiquitination of phosphorylated NFKB1: specifically ubiquitinates the p105 form of NFKB1, leading to its degradation (PubMed:10835356, PubMed:11158290, PubMed:14673179). SCF(BTRC) mediates the ubiquitination of CEP68; this is required for centriole separation during mitosis (PubMed:25503564, PubMed:25704143). SCF(BTRC) mediates the ubiquitination and subsequent degradation of nuclear NFE2L1 (By similarity). Has an essential role in the control of the clock-dependent transcription via degradation of phosphorylated PER1 and PER2 (PubMed:15917222). May be involved in ubiquitination and subsequent proteasomal degradation through a DBB1-CUL4 E3 ubiquitin-protein ligase. Required for activation of NFKB-mediated transcription by IL1B, MAP3K14, MAP3K1, IKBKB and TNF. Required for proteolytic processing of GLI3 (PubMed:16371461). Mediates ubiquitination of REST, thereby leading to its proteasomal degradation (PubMed:18354482, PubMed:21258371). SCF(BTRC) mediates the ubiquitination and subsequent proteasomal degradation of KLF4; thereby negatively regulating cell pluripotency maintenance and embryogenesis (By similarity). SCF(BTRC) acts as a regulator of mTORC1 signaling pathway by catalyzing ubiquitination and subsequent proteasomal degradation of phosphorylated DEPTOR, TFE3 and MITF (PubMed:22017875, PubMed:22017876, PubMed:22017877, PubMed:33110214, PubMed:36608670). SCF(BTRC) directs 'Lys-48'-linked ubiquitination of UBR2 in the T-cell receptor signaling pathway (PubMed:38225265)", "gene_name": "BTRC", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y297", "name": "\u03b2-TrCP", "organism": "Homo sapiens", "uniprot_id": "Q9Y297" }, { "function": "Essential for the control of the cell cycle at the G1/S (start) transition", "gene_name": "CCNE1", "glycan_count": 0, "glycosylation_sites": [], "id": "P24864", "name": "Cyclin E", "organism": "Homo sapiens", "uniprot_id": "P24864" }, { "function": "Essential for the control of the cell cycle at the G2/M (mitosis) transition", "gene_name": "CCNB1", "glycan_count": 1, "glycosylation_sites": [], "id": "P14635", "name": "Cyclin B1", "organism": "Homo sapiens", "uniprot_id": "P14635" }, { "function": "", "gene_name": "CDR2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q01850", "name": "Yo antigen (CDR2)", "organism": "Homo sapiens", "uniprot_id": "Q01850" }, { "function": "May play a role in maintenance of cell cycle integrity by regulating mitosis or cytokinesis", "gene_name": "MPLKIP", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8TAP9", "name": "Ma2 antigen (PNMA2)", "organism": "Homo sapiens", "uniprot_id": "Q8TAP9" }, { "function": "Upon acetylcholine binding, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane", "gene_name": "CHRNA1", "glycan_count": 7, "glycosylation_sites": [ { "position": 161, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P02708", "name": "Acetylcholine Receptor (AChR)", "organism": "Homo sapiens", "uniprot_id": "P02708" }, { "function": "Phosphatidylinositol-4-phosphate-binding protein that links Golgi membranes to the cytoskeleton and may participate in the tensile force required for vesicle budding from the Golgi. Thereby, may play a role in Golgi membrane trafficking and could indirectly give its flattened shape to the Golgi apparatus. May also bind to the coatomer to regulate Golgi membrane trafficking. May play a role in anterograde transport from the Golgi to the plasma membrane and regulate secretion. Has also been involved in the control of the localization of Golgi enzymes through interaction with their cytoplasmic part. May play an indirect role in cell migration. Has also been involved in the modulation of mTOR signaling. May also be involved in the regulation of mitochondrial lipids biosynthesis", "gene_name": "GOLPH3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H4A6", "name": "GMPPB", "organism": "Homo sapiens", "uniprot_id": "Q9H4A6" }, { "function": "Serine protease with a variety of targets, including extracellular matrix proteins such as fibronectin. HTRA1-generated fibronectin fragments further induce synovial cells to up-regulate MMP1 and MMP3 production. May also degrade proteoglycans, such as aggrecan, decorin and fibromodulin. Through cleavage of proteoglycans, may release soluble FGF-glycosaminoglycan complexes that promote the range and intensity of FGF signals in the extracellular space. Regulates the availability of insulin-like growth factors (IGFs) by cleaving IGF-binding proteins. Inhibits signaling mediated by TGF-beta family members. This activity requires the integrity of the catalytic site, although it is unclear whether TGF-beta proteins are themselves degraded. By acting on TGF-beta signaling, may regulate many physiological processes, including retinal angiogenesis and neuronal survival and maturation during development. Intracellularly, degrades TSC2, leading to the activation of TSC2 downstream targets", "gene_name": "HTRA1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q92743", "name": "HTRA1", "organism": "Homo sapiens", "uniprot_id": "Q92743" }, { "function": "After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane", "gene_name": "CHRNE", "glycan_count": 3, "glycosylation_sites": [ { "position": 86, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 161, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q04844", "name": "CHRNE", "organism": "Homo sapiens", "uniprot_id": "Q04844" }, { "function": "Necessary for efficient 3-hydroxylation of fibrillar collagen prolyl residues", "gene_name": "CRTAP", "glycan_count": 22, "glycosylation_sites": [ { "position": 87, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 363, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O75718", "name": "COLQ", "organism": "Homo sapiens", "uniprot_id": "O75718" }, { "function": "Electrogenic antiporter that exchanges one cholinergic neurotransmitter, acetylcholine or choline, with two intravesicular protons across the membrane of synaptic vesicles. Uses the electrochemical proton gradient established by the V-type proton-pump ATPase to store neurotransmitters inside the vesicles prior to their release via exocytosis (By similarity) (PubMed:20225888, PubMed:8910293). Determines cholinergic vesicular quantal size at presynaptic nerve terminals in developing neuro-muscular junctions with an impact on motor neuron differentiation and innervation pattern (By similarity). Part of forebrain cholinergic system, regulates hippocampal synapse transmissions that underlie spatial memory formation (By similarity). Can transport serotonin", "gene_name": "SLC18A3", "glycan_count": 0, "glycosylation_sites": [ { "position": 89, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 96, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q16572", "name": "SLC18A3", "organism": "Homo sapiens", "uniprot_id": "Q16572" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "GAD65: Q05329", "name": "Anti-GAD65 antibody", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P29459 (human)", "name": "Interleukin-12 (IL-12)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q14116 (human)", "name": "Interleukin-18 (IL-18)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01579 (human)", "name": "Interferon gamma (IFN-\u03b3)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P22301 (human)", "name": "Interleukin-10 (IL-10)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01375 (human)", "name": "Tumor necrosis factor alpha (TNF-\u03b1)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P05112 (human)", "name": "Interleukin-4 (IL-4)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01562 (human)", "name": "Interferon alpha (IFN-\u03b1)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01574 (human)", "name": "Interferon beta (IFN-\u03b2)", "organism": "", "uniprot_id": "" }, { "function": "May be a negative regulator of NF-kappa-B and p53-mediated gene transcription", "gene_name": "STK40", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8N2I9", "name": "Glial cell adhesion molecule (GlialCAM)", "organism": "Homo sapiens", "uniprot_id": "Q8N2I9" }, { "function": "Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems (PubMed:14976160, PubMed:20978020). Extracellular ligand for the NTRK1 and NGFR receptors, activates cellular signaling cascades to regulate neuronal proliferation, differentiation and survival (Probable) (PubMed:20978020). The immature NGF precursor (proNGF) functions as a ligand for the heterodimeric receptor formed by SORCS2 and NGFR, and activates cellular signaling cascades that lead to inactivation of RAC1 and/or RAC2, reorganization of the actin cytoskeleton and neuronal growth cone collapse. In contrast to mature NGF, the precursor form (proNGF) promotes neuronal apoptosis (in vitro) (By similarity). Inhibits metalloproteinase-dependent proteolysis of platelet glycoprotein VI (PubMed:20164177). Binds lysophosphatidylinositol and lysophosphatidylserine between the two chains of the homodimer. The lipid-bound form promotes histamine relase from mast cells, contrary to the lipid-free form (By similarity)", "gene_name": "NGF", "glycan_count": 1, "glycosylation_sites": [ { "position": 69, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 114, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01138", "name": "Nerve growth factor (NGF)", "organism": "Homo sapiens", "uniprot_id": "P01138" }, { "function": "Type I interferon cytokine that plays a key role in the innate immune response to infection, developing tumors and other inflammatory stimuli (PubMed:10049744, PubMed:10556041, PubMed:6157094, PubMed:6171735, PubMed:7665574, PubMed:8027027, PubMed:8969169). Signals via binding to high-affinity (IFNAR2) and low-affinity (IFNAR1) heterodimeric receptor, activating the canonical Jak-STAT signaling pathway resulting in transcriptional activation or repression of interferon-regulated genes that encode the effectors of the interferon response, such as antiviral proteins, regulators of cell proliferation and differentiation, and immunoregulatory proteins (PubMed:10049744, PubMed:10556041, PubMed:7665574, PubMed:8027027, PubMed:8969169). Signals mostly via binding to a IFNAR1-IFNAR2 heterodimeric receptor, but can also function with IFNAR1 alone and independently of Jak-STAT pathways (By similarity). Elicits a wide variety of responses, including antiviral and antibacterial activities, and can regulate the development of B-cells, myelopoiesis and lipopolysaccharide (LPS)-inducible production of tumor necrosis factor (By similarity). Plays a role in neuronal homeostasis by regulating dopamine turnover and protecting dopaminergic neurons: acts by promoting neuronal autophagy and alpha-synuclein clearance, thereby preventing dopaminergic neuron loss (By similarity). IFNB1 is more potent than interferon-alpha (IFN-alpha) in inducing the apoptotic and antiproliferative pathways required for control of tumor cell growth (By similarity)", "gene_name": "IFNB1", "glycan_count": 2, "glycosylation_sites": [ { "position": 101, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01574", "name": "IFN-\u03b2", "organism": "Homo sapiens", "uniprot_id": "P01574" }, { "function": "The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (PubMed:15601896, PubMed:15689490, PubMed:17462998, PubMed:19542231, PubMed:20026645, PubMed:20890297, PubMed:21282656, PubMed:26032412). The small Rab GTPase RAB11A regulates endocytic recycling (PubMed:20026645). Forms a functional Rab11/RAB11FIP3/dynein complex that regulates the movement of peripheral sorting endosomes (SE) along microtubule tracks toward the microtubule organizing center/centrosome, generating the endosomal recycling compartment (ERC) (PubMed:20026645). Acts as a major regulator of membrane delivery during cytokinesis (PubMed:15601896). Together with MYO5B and RAB8A participates in epithelial cell polarization (PubMed:21282656). Together with Rabin8/RAB3IP, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis (PubMed:20890297). Together with MYO5B participates in CFTR trafficking to the plasma membrane and TF (Transferrin) recycling in nonpolarized cells (PubMed:17462998). Required in a complex with MYO5B and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane (PubMed:19542231). Participates in the sorting and basolateral transport of CDH1 from the Golgi apparatus to the plasma membrane (PubMed:15689490). Regulates the recycling of FCGRT (receptor of Fc region of monomeric IgG) to basolateral membranes (By similarity). May also play a role in melanosome transport and release from melanocytes (By similarity). Promotes Rabin8/RAB3IP preciliary vesicular trafficking to mother centriole by forming a ciliary targeting complex containing Rab11, ASAP1, Rabin8/RAB3IP, RAB11FIP3 and ARF4, thereby regulating ciliogenesis initiation (PubMed:25673879, PubMed:31204173). On the contrary, upon LPAR1 receptor signaling pathway activation, interaction with phosphorylated WDR44 prevents Rab11-RAB3IP-RAB11FIP3 complex formation and cilia growth (PubMed:31204173). Participates in the export of a subset of neosynthesized proteins through a Rab8-Rab10-Rab11-endososomal dependent export route via interaction with WDR44 (PubMed:32344433)", "gene_name": "RAB11A", "glycan_count": 1, "glycosylation_sites": [ { "position": 4, "type": "(Microbial infection) N-beta-linked (GlcNAc) arginine" } ], "id": "P62491", "name": "Ras-related protein Rab11a", "organism": "Homo sapiens", "uniprot_id": "P62491" }, { "function": "May be involved in collagen fiber assembly", "gene_name": "BGN", "glycan_count": 276, "glycosylation_sites": [ { "position": 42, "type": "O-linked (Xyl...) (glycosaminoglycan) serine" }, { "position": 47, "type": "O-linked (Xyl...) (glycosaminoglycan) serine" }, { "position": 180, "type": "O-linked (Xyl...) (glycosaminoglycan) serine" }, { "position": 198, "type": "O-linked (Xyl...) (glycosaminoglycan) serine" }, { "position": 270, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 311, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P21810", "name": "BGN", "organism": "Homo sapiens", "uniprot_id": "P21810" }, { "function": "Death-promoting transcriptional repressor. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA", "gene_name": "BCLAF1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9NYF8", "name": "CLDN9", "organism": "Homo sapiens", "uniprot_id": "Q9NYF8" }, { "function": "Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell motility, cell cycle progression, apoptosis or proliferation (PubMed:12853446, PubMed:16617111, PubMed:19273597, PubMed:19923322, PubMed:33693784, PubMed:7744004, PubMed:9171063). Acts as a downstream effector of the small GTPases CDC42 and RAC1 (PubMed:7744004). Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues (PubMed:7744004). Full-length PAK2 stimulates cell survival and cell growth (PubMed:7744004). Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration (PubMed:21317288). Phosphorylates JUN and plays an important role in EGF-induced cell proliferation (PubMed:21177766). Phosphorylates many other substrates including histone H4 to promote assembly of H3.3 and H4 into nucleosomes, BAD, ribosomal protein S6, or MBP (PubMed:21724829). Phosphorylates CASP7, thereby preventing its activity (PubMed:21555521, PubMed:27889207). Additionally, associates with ARHGEF7 and GIT1 to perform kinase-independent functions such as spindle orientation control during mitosis (PubMed:19273597, PubMed:19923322). On the other hand, apoptotic stimuli such as DNA damage lead to caspase-mediated cleavage of PAK2, generating PAK-2p34, an active p34 fragment that translocates to the nucleus and promotes cellular apoptosis involving the JNK signaling pathway (PubMed:12853446, PubMed:16617111, PubMed:9171063). Caspase-activated PAK2 phosphorylates MKNK1 and reduces cellular translation (PubMed:15234964)", "gene_name": "PAK2", "glycan_count": 2, "glycosylation_sites": [], "id": "Q13177", "name": "PAK2", "organism": "Homo sapiens", "uniprot_id": "Q13177" }, { "function": "Dual specificity phosphatase that dephosphorylates MAP kinase MAPK1/ERK2 on both 'Thr-183' and 'Tyr-185', regulating its activity during the meiotic cell cycle", "gene_name": "DUSP1", "glycan_count": 0, "glycosylation_sites": [], "id": "P28562", "name": "DUSP1", "organism": "Homo sapiens", "uniprot_id": "P28562" }, { "function": "Component of the U5 snRNP complex that is required for spliceosome assembly and for pre-mRNA splicing", "gene_name": "AAR2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y312", "name": "EFNA3", "organism": "Homo sapiens", "uniprot_id": "Q9Y312" }, { "function": "Component of the nuclear pore complex that has a direct role in nuclear protein import (PubMed:20016008). Actively displaces NLSs from importin-alpha, and facilitates disassembly of the importin-alpha:beta-cargo complex and importin recycling (PubMed:20016008). Interacts with regulatory proteins of cell cycle progression including CDKN1B (By similarity). This interaction is required for correct intracellular transport and degradation of CDKN1B (By similarity)", "gene_name": "NUP50", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9UKX7", "name": "NUP50", "organism": "Homo sapiens", "uniprot_id": "Q9UKX7" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "derived from FNDC5", "name": "Irisin", "organism": "", "uniprot_id": "" }, { "function": "Receptor activated by multiple ligands, including osteocalcin (BGLAP), basic amino acids, and various cations (PubMed:15576628). Activated by amino acids with a preference for basic amino acids such as L-Lys, L-Arg and L-ornithine but also by small and polar amino acids (PubMed:15576628). The L-alpha amino acids respond is augmented by divalent cations Ca(2+) and Mg(2+) (By similarity). Seems to act through a G(q)/G(11) and G(i)-coupled pathway (By similarity). Regulates testosterone production by acting as a ligand for uncarboxylated osteocalcin hormone: osteocalcin-binding at the surface of Leydig cells initiates a signaling response that promotes the expression of enzymes required for testosterone synthesis in a CREB-dependent manner (By similarity). Mediates the non-genomic effects of androgens in multiple tissue (By similarity). May coordinate nutritional and hormonal anabolic signals through the sensing of extracellular amino acids, osteocalcin, divalent ions and its responsiveness to anabolic steroids (PubMed:20947496)", "gene_name": "GPRC6A", "glycan_count": 0, "glycosylation_sites": [ { "position": 121, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 259, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 332, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 378, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 452, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 555, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 567, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 590, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 733, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q5T6X5", "name": "Gpr158", "organism": "Homo sapiens", "uniprot_id": "Q5T6X5" }, { "function": "Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling. During ubiquitination, the acceptor ubiquitin is positioned in the active site via direct interaction with the E2 ubiquitin-conjugating enzymes such as UBE2R2 (PubMed:38326650). As a monoubiquitin, its C-terminal glycine is recognized as a C-degron by Cul2-RING (CRL2) E3 ubiquitin-protein ligase complexes (PubMed:39548056)", "gene_name": "UBC", "glycan_count": 1, "glycosylation_sites": [], "id": "P0CG48", "name": "UBB (Polyubiquitin-B)", "organism": "Homo sapiens", "uniprot_id": "P0CG48" }, { "function": "Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Binds to the C-terminus of CDKN1A and thereby mediates its degradation. Negatively regulates the membrane trafficking of the cell-surface thromboxane A2 receptor (TBXA2R) isoform 2", "gene_name": "PSMA3", "glycan_count": 2, "glycosylation_sites": [], "id": "P25788", "name": "PSMA3 (Proteasome subunit alpha type-3)", "organism": "Homo sapiens", "uniprot_id": "P25788" }, { "function": "Acetylates histones, giving a specific tag for transcriptional activation (PubMed:21131905, PubMed:24616510). Mediates acetylation of histone H3 at 'Lys-18' and 'Lys-27' (H3K18ac and H3K27ac, respectively) (PubMed:21131905). Also acetylates non-histone proteins, like DDX21, FBL, IRF2, MAFG, NCOA3, POLR1E/PAF53 and FOXO1 (PubMed:10490106, PubMed:11154691, PubMed:12738767, PubMed:12929931, PubMed:24207024, PubMed:28790157, PubMed:30540930, PubMed:35675826, PubMed:9707565). Binds specifically to phosphorylated CREB and enhances its transcriptional activity toward cAMP-responsive genes. Acts as a coactivator of ALX1. Acts as a circadian transcriptional coactivator which enhances the activity of the circadian transcriptional activators: NPAS2-BMAL1 and CLOCK-BMAL1 heterodimers (PubMed:14645221). Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER) (PubMed:24939902). Acetylates POLR1E/PAF53, leading to decreased association of RNA polymerase I with the rDNA promoter region and coding region (PubMed:24207024). Acetylates DDX21, thereby inhibiting DDX21 helicase activity (PubMed:28790157). Acetylates FBL, preventing methylation of 'Gln-105' of histone H2A (H2AQ104me) (PubMed:30540930). In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as lactoyl-CoA, and is able to mediate protein lactylation (PubMed:38128537). Catalyzes lactylation of MRE11 in response to DNA damage, thereby promoting DNA double-strand breaks (DSBs) via homologous recombination (HR) (PubMed:38128537). Functions as a transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway (PubMed:25514493)", "gene_name": "CREBBP", "glycan_count": 2, "glycosylation_sites": [], "id": "Q92793", "name": "CREBBP (CREB-binding protein)", "organism": "Homo sapiens", "uniprot_id": "Q92793" }, { "function": "Functions as a histone acetyltransferase and regulates transcription via chromatin remodeling (PubMed:23415232, PubMed:23934153, PubMed:8945521). Acetylates all four core histones in nucleosomes (PubMed:23415232, PubMed:23934153, PubMed:8945521). Histone acetylation gives an epigenetic tag for transcriptional activation (PubMed:23415232, PubMed:23934153, PubMed:8945521). Mediates acetylation of histone H3 at 'Lys-122' (H3K122ac), a modification that localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability (PubMed:23415232). Mediates acetylation of histone H3 at 'Lys-18' and 'Lys-27' (H3K18ac and H3K27ac, respectively) (PubMed:21131905, PubMed:23911289). Also able to acetylate histone lysine residues that are already monomethylated on the same side chain to form N6-acetyl-N6-methyllysine (Kacme), an epigenetic mark of active chromatin associated with increased transcriptional initiation (PubMed:37731000). Catalyzes formation of histone H4 acetyl-methylated at 'Lys-5' and 'Lys-12' (H4K5acme and H4K12acme, respectively) (PubMed:37731000). Also functions as acetyltransferase for non-histone targets, such as ALX1, HDAC1, PRMT1, SIRT2, STAT3 or GLUL (PubMed:12929931, PubMed:15653507, PubMed:16285960, PubMed:16762839, PubMed:18722353, PubMed:18782771, PubMed:26990986). Acetylates 'Lys-131' of ALX1 and acts as its coactivator (PubMed:12929931). Acetylates SIRT2 and is proposed to indirectly increase the transcriptional activity of p53/TP53 through acetylation and subsequent attenuation of SIRT2 deacetylase function (PubMed:18722353). Following DNA damage, forms a stress-responsive p53/TP53 coactivator complex with JMY which mediates p53/TP53 acetylation, thereby increasing p53/TP53-dependent transcription and apoptosis (PubMed:11511361, PubMed:15448695). Promotes chromatin acetylation in heat shock responsive HSP genes during the heat shock response (HSR), thereby stimulating HSR transcription (PubMed:18451878). Acetylates HDAC1 leading to its inactivation and modulation of transcription (PubMed:16762839). Acetylates 'Lys-247' of EGR2 (By similarity). Acts as a TFAP2A-mediated transcriptional coactivator in presence of CITED2 (PubMed:12586840). Plays a role as a coactivator of NEUROD1-dependent transcription of the secretin and p21 genes and controls terminal differentiation of cells in the intestinal epithelium. Promotes cardiac myocyte enlargement (PubMed:14752053). Can also mediate transcriptional repression. Acetylates FOXO1 and enhances its transcriptional activity (PubMed:15890677). Acetylates STAT3 at different sites, promoting both STAT3 dimerization and activation and recruitment to chromatin (PubMed:15653507, PubMed:16285960, PubMed:18782771). Acetylates BCL6 which disrupts its ability to recruit histone deacetylases and hinders its transcriptional repressor activity (PubMed:12402037). Participates in CLOCK or NPAS2-regulated rhythmic gene transcription; exhibits a circadian association with CLOCK or NPAS2, correlating with increase in PER1/2 mRNA and histone H3 acetylation on the PER1/2 promoter (PubMed:14645221). Acetylates MTA1 at 'Lys-626' which is essential for its transcriptional coactivator activity (PubMed:16617102). Acetylates XBP1 isoform 2; acetylation increases protein stability of XBP1 isoform 2 and enhances its transcriptional activity (PubMed:20955178). Acetylates PCNA; acetylation promotes removal of chromatin-bound PCNA and its degradation during nucleotide excision repair (NER) (PubMed:24939902). Acetylates MEF2D (PubMed:21030595). Acetylates and stabilizes ZBTB7B protein by antagonizing ubiquitin conjugation and degradation, this mechanism may be involved in CD4/CD8 lineage differentiation (PubMed:20810990). Acetylates GABPB1, impairing GABPB1 heterotetramerization and activity (By similarity). Acetylates PCK1 and promotes PCK1 anaplerotic activity (PubMed:30193097). Acetylates RXRA and RXRG (PubMed:17761950). Acetylates isoform M2 of PKM (PKM2), promoting its homodimerization and conversion into a protein kinase (PubMed:24120661). Acetylates RPTOR in response to leucine, leading to activation of the mTORC1 complex (PubMed:30197302, PubMed:32561715). Acetylates RICTOR, leading to activation of the mTORC2 complex (PubMed:22084251). Mediates cAMP-gene regulation by binding specifically to phosphorylated CREBBP (PubMed:8917528). In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as (2E)-butenoyl-CoA (crotonyl-CoA), butanoyl-CoA (butyryl-CoA), 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA), lactoyl-CoA or propanoyl-CoA (propionyl-CoA), and is able to mediate protein crotonylation, butyrylation, 2-hydroxyisobutyrylation, lactylation or propionylation, respectively (PubMed:17267393, PubMed:25818647, PubMed:29775581, PubMed:31645732). Acts as a histone crotonyltransferase; crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors (PubMed:25818647). Histone crotonyltransferase activity is dependent on the concentration of (2E)-butenoyl-CoA (crotonyl-CoA) substrate and such activity is weak when (2E)-butenoyl-CoA (crotonyl-CoA) concentration is low (PubMed:25818647). Also acts as a histone butyryltransferase; butyrylation marks active promoters (PubMed:17267393). Catalyzes histone lactylation in macrophages by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription (PubMed:31645732). Acts as a protein-lysine 2-hydroxyisobutyryltransferase; regulates glycolysis by mediating 2-hydroxyisobutyrylation of glycolytic enzymes (PubMed:29775581). Functions as a transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway (PubMed:25514493)", "gene_name": "EP300", "glycan_count": 1, "glycosylation_sites": [], "id": "Q09472", "name": "EP300 (Histone acetyltransferase p300)", "organism": "Homo sapiens", "uniprot_id": "Q09472" }, { "function": "Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues", "gene_name": "GH1", "glycan_count": 0, "glycosylation_sites": [], "id": "P19795", "name": "HBV DNA polymerase", "organism": "Neovison vison", "uniprot_id": "P19795" }, { "function": "Orphan receptor", "gene_name": "GPR160", "glycan_count": 0, "glycosylation_sites": [ { "position": 8, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UJ42", "name": "Kidney injury molecule-1 (KIM-1)", "organism": "Homo sapiens", "uniprot_id": "Q9UJ42" }, { "function": "Mitotic serine/threonine kinase that contributes to the regulation of cell cycle progression (PubMed:11039908, PubMed:12390251, PubMed:17125279, PubMed:17360485, PubMed:18615013, PubMed:26246606). Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle, centrosome duplication, centrosome separation as well as maturation, chromosomal alignment, spindle assembly checkpoint, and cytokinesis (PubMed:14523000, PubMed:26246606). Required for normal spindle positioning during mitosis and for the localization of NUMA1 and DCTN1 to the cell cortex during metaphase (PubMed:27335426). Required for initial activation of CDK1 at centrosomes (PubMed:13678582, PubMed:15128871). Phosphorylates numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3, p53/TP53 and TPX2 (PubMed:11551964, PubMed:14702041, PubMed:15128871, PubMed:15147269, PubMed:15987997, PubMed:17604723, PubMed:18056443, PubMed:18615013). Phosphorylates MCRS1 which is required for MCRS1-mediated kinetochore fiber assembly and mitotic progression (PubMed:27192185). Regulates KIF2A tubulin depolymerase activity (PubMed:19351716). Important for microtubule formation and/or stabilization (PubMed:18056443). Required for normal axon formation (PubMed:19812038). Plays a role in microtubule remodeling during neurite extension (PubMed:19668197). Also acts as a key regulatory component of the p53/TP53 pathway, and particularly the checkpoint-response pathways critical for oncogenic transformation of cells, by phosphorylating and destabilizing p53/TP53 (PubMed:14702041). Phosphorylates its own inhibitors, the protein phosphatase type 1 (PP1) isoforms, to inhibit their activity (PubMed:11551964). Inhibits cilia outgrowth (By similarity). Required for cilia disassembly via phosphorylation of HDAC6 and subsequent deacetylation of alpha-tubulin (PubMed:17604723, PubMed:20643351). Regulates protein levels of the anti-apoptosis protein BIRC5 by suppressing the expression of the SCF(FBXL7) E3 ubiquitin-protein ligase substrate adapter FBXL7 through the phosphorylation of the transcription factor FOXP1 (PubMed:28218735)", "gene_name": "AURKA", "glycan_count": 1, "glycosylation_sites": [], "id": "O14965", "name": "Aurora A (AURKA)", "organism": "Homo sapiens", "uniprot_id": "O14965" }, { "function": "Cell-cycle-regulated enzyme of importance in nucleotide metabolism (PubMed:9575153). Catalyzes the first enzymatic step in the salvage pathway converting thymidine into thymidine monophosphate (PubMed:22385435). Transcriptional regulation limits expression to the S phase of the cell cycle and transient expression coincides with the oscillation in the intracellular dTTP concentration (Probable). Also important for the activation of anticancer and antiviral nucleoside analog prodrugs such as 1-b-d-arabinofuranosylcytosine (AraC) and 3c-azido-3c-deoxythymidine (AZT) (PubMed:22385435)", "gene_name": "TK1", "glycan_count": 1, "glycosylation_sites": [], "id": "P04183", "name": "Thymidine kinase 1 (TK1)", "organism": "Homo sapiens", "uniprot_id": "P04183" }, { "function": "Non-classical major histocompatibility class Ib molecule involved in immune regulatory processes at the maternal-fetal interface (PubMed:19304799, PubMed:23184984, PubMed:29262349). In complex with B2M/beta-2 microglobulin binds a limited repertoire of nonamer self-peptides derived from intracellular proteins including histones and ribosomal proteins (PubMed:7584149, PubMed:8805247). Peptide-bound HLA-G-B2M complex acts as a ligand for inhibitory/activating KIR2DL4, LILRB1 and LILRB2 receptors on uterine immune cells to promote fetal development while maintaining maternal-fetal tolerance (PubMed:16366734, PubMed:19304799, PubMed:20448110, PubMed:23184984, PubMed:27859042, PubMed:29262349). Upon interaction with KIR2DL4 and LILRB1 receptors on decidual NK cells, it triggers NK cell senescence-associated secretory phenotype as a molecular switch to promote vascular remodeling and fetal growth in early pregnancy (PubMed:16366734, PubMed:19304799, PubMed:23184984, PubMed:29262349). Through interaction with KIR2DL4 receptor on decidual macrophages induces pro-inflammatory cytokine production mainly associated with tissue remodeling (PubMed:19304799). Through interaction with LILRB2 receptor triggers differentiation of type 1 regulatory T cells and myeloid-derived suppressor cells, both of which actively maintain maternal-fetal tolerance (PubMed:20448110, PubMed:27859042). May play a role in balancing tolerance and antiviral-immunity at maternal-fetal interface by keeping in check the effector functions of NK, CD8+ T cells and B cells (PubMed:10190900, PubMed:11290782, PubMed:24453251). Reprograms B cells toward an immune suppressive phenotype via LILRB1 (PubMed:24453251). May induce immune activation/suppression via intercellular membrane transfer (trogocytosis), likely enabling interaction with KIR2DL4, which resides mostly in endosomes (PubMed:20179272, PubMed:26460007). Through interaction with the inhibitory receptor CD160 on endothelial cells may control angiogenesis in immune privileged sites (PubMed:16809620)", "gene_name": "HLA-G", "glycan_count": 0, "glycosylation_sites": [ { "position": 110, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P17693", "name": "HLA-G", "organism": "Homo sapiens", "uniprot_id": "P17693" }, { "function": "May be involved in transcriptional regulation through interaction with SNW1 and recruiting histone deactelyase HDAC1. May inhibit notch intracellular domain (NICD) transactivation. May play a role in embryonal development and tumor transformation or aspects of tumor progression. Antigen recognized on a melanoma by autologous cytolytic T-lymphocytes", "gene_name": "MAGEA1", "glycan_count": 0, "glycosylation_sites": [], "id": "P43355", "name": "MAGE-A3", "organism": "Homo sapiens", "uniprot_id": "P43355" }, { "function": "May function as an inhibitor of Wnt/beta-catenin signaling by indirectly interacting with LRP6 and blocking Wnt3a-dependent LRP6 internalization", "gene_name": "TPBG", "glycan_count": 22, "glycosylation_sites": [ { "position": 81, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 124, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 275, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13641", "name": "5T4", "organism": "Homo sapiens", "uniprot_id": "Q13641" }, { "function": "Assembly factor that mediates the formation of some mitochondrial respiratory supercomplexes (respirasomes), thereby promoting oxidative phosphorylation and energy metabolism (PubMed:27545886, PubMed:30428348, PubMed:33727070, PubMed:36198313). Acts as a molecular adapter that associates with both mitochondrial respiratory complexes III (CIII) and IV (CIV), promoting their association (PubMed:27545886, PubMed:36198313). Mediates the formation of various mitochondrial respiratory supercomplexes, such as MCIII(2)IV(2), composed of two CIII and two CIV, and the CS-respirasome (MCI(1)III(2)IV(2)), composed of one CI, two CIII and two CIV (PubMed:27545886, PubMed:30428348). Not involved in the formation of the canonical respirasome (MCI(1)III(2)IV(1)), composed of one CI, two CIII and one CIV (By similarity). The formation of different respirasomes is important for cell adaptation to oxygen conditions and prevent metabolic exhaustion: supercomplexes mediated by COX7A2L/SCAF1 are required to maintain oxidative phosphorylation upon low oxygen conditions and promote metabolic rewiring toward glycolysis (PubMed:36198313)", "gene_name": "COX7A2L", "glycan_count": 0, "glycosylation_sites": [], "id": "O14548", "name": "STAT3 (STT3)", "organism": "Homo sapiens", "uniprot_id": "O14548" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01275-2", "name": "Glucagon-like peptide 2 (GLP-2)", "organism": "", "uniprot_id": "" }, { "function": "Exo-alpha-sialidase that catalyzes the hydrolytic cleavage of the terminal sialic acid (N-acetylneuraminic acid, Neu5Ac) of a glycan moiety in the catabolism of glycolipids, glycoproteins and oligosacharides. Displays high catalytic efficiency for gangliosides including alpha-(2->3)-sialylated GD1a and GM3 and alpha-(2->8)-sialylated GD3 (PubMed:10405317, PubMed:10861246, PubMed:11298736, PubMed:12011038, PubMed:15847605, PubMed:20511247, PubMed:28646141). Plays a role in the regulation of transmembrane signaling through the modulation of ganglioside content of the lipid bilayer and by direct interaction with signaling receptors, such as EGFR (PubMed:17334392, PubMed:25922362). Desialylates EGFR and activates downstream signaling in proliferating cells (PubMed:25922362). Contributes to clathrin-mediated endocytosis by regulating sorting of endocytosed receptors to early and recycling endosomes (PubMed:26251452)", "gene_name": "NEU3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UQ49", "name": "NEU3 (Sialidase-3)", "organism": "Homo sapiens", "uniprot_id": "Q9UQ49" }, { "function": "Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(q) proteins which activate a phosphatidylinositol-calcium second messenger system. May play a role as an important modulator of renal function. Implicated the smooth muscle contractile response to PGE2 in various tissues", "gene_name": "PTGER1", "glycan_count": 0, "glycosylation_sites": [ { "position": 8, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 25, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P34995", "name": "Prostaglandin E2 receptor EP3", "organism": "Homo sapiens", "uniprot_id": "P34995" }, { "function": "Human saliva appears to contain several cysteine proteinase inhibitors that are immunologically related to cystatin S but that differ in their specificity due to amino acid sequence differences. Cystatin SN, with a pI of 7.5, is a much better inhibitor of papain and dipeptidyl peptidase I than is cystatin S, although both inhibit ficin equally well", "gene_name": "CST1", "glycan_count": 0, "glycosylation_sites": [], "id": "P01037", "name": "Cystatin SN (CST1)", "organism": "Homo sapiens", "uniprot_id": "P01037" }, { "function": "Thiol protease inhibitor", "gene_name": "CST2", "glycan_count": 0, "glycosylation_sites": [], "id": "P09228", "name": "Cystatin SA (CST2)", "organism": "Homo sapiens", "uniprot_id": "P09228" }, { "function": "This protein strongly inhibits papain and ficin, partially inhibits stem bromelain and bovine cathepsin C, but does not inhibit porcine cathepsin B or clostripain. Papain is inhibited non-competitively", "gene_name": "CST4", "glycan_count": 0, "glycosylation_sites": [], "id": "P01036", "name": "Cystatin S (CST4)", "organism": "Homo sapiens", "uniprot_id": "P01036" }, { "function": "Cysteine proteinase inhibitor that possibly plays a protective role against proteinases present in the oral cavity. The order of preference for inhibition is cathepsin S > cathepsin H > cathepsin L > cathepsin B", "gene_name": "CST5", "glycan_count": 0, "glycosylation_sites": [], "id": "P28325", "name": "Cystatin D (CST5)", "organism": "Homo sapiens", "uniprot_id": "P28325" }, { "function": "Glycosyltransferase required for the biosynthesis of heparan-sulfate and responsible for the alternating addition of beta-1-4-linked glucuronic acid (GlcA) and alpha-1-4-linked N-acetylglucosamine (GlcNAc) units to nascent heparan sulfate chains", "gene_name": "EXTL2", "glycan_count": 4, "glycosylation_sites": [ { "position": 74, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UBQ6", "name": "Cystatin F (CST7)", "organism": "Homo sapiens", "uniprot_id": "Q9UBQ6" }, { "function": "Pro-inflammatory cytokine involved in the innate immune response to bacterial pathogens (PubMed:15908412, PubMed:17443469, PubMed:23776208). The expression of MIF at sites of inflammation suggests a role as mediator in regulating the function of macrophages in host defense (PubMed:15908412, PubMed:17443469, PubMed:23776208). Counteracts the anti-inflammatory activity of glucocorticoids (PubMed:15908412, PubMed:17443469, PubMed:23776208). Has phenylpyruvate tautomerase and dopachrome tautomerase activity (in vitro), but the physiological substrate is not known (PubMed:11439086, PubMed:17526494). It is not clear whether the tautomerase activity has any physiological relevance, and whether it is important for cytokine activity (PubMed:11439086, PubMed:17526494)", "gene_name": "MIF", "glycan_count": 2, "glycosylation_sites": [], "id": "P14174", "name": "Macrophage migration inhibitory factor", "organism": "Homo sapiens", "uniprot_id": "P14174" }, { "function": "TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:16129888). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Binds and recruits PATJ to tight junctions where it connects and stabilizes apical and lateral components of tight junctions (PubMed:16129888). Promotes cell-cycle progression through the sequestration of cyclin D1 (CCND1) at tight junctions during mitosis which prevents CCND1 degradation during M-phase and enables S-phase transition (PubMed:21411630). With TJP1 and TJP2, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity). Contrary to TJP2, TJP3 is dispensable for individual viability, embryonic development, epithelial differentiation, and the establishment of TJs, at least in the laboratory environment (By similarity)", "gene_name": "TJP3", "glycan_count": 1, "glycosylation_sites": [], "id": "O95049", "name": "Claudin 2 (CLDN2)", "organism": "Homo sapiens", "uniprot_id": "O95049" }, { "function": "", "gene_name": "N", "glycan_count": 0, "glycosylation_sites": [], "id": "Q66525", "name": "E2", "organism": "Equine arteritis virus", "uniprot_id": "Q66525" }, { "function": "Packages viral RNA to form a viral nucleocapsid, and promotes virion budding (Probable). Participates in the viral particle production as a result of its interaction with the non-structural protein 5A (By similarity). Binds RNA and may function as a RNA chaperone to induce the RNA structural rearrangements taking place during virus replication (By similarity). Modulates viral translation initiation by interacting with viral IRES and 40S ribosomal subunit (By similarity). Affects various cell signaling pathways, host immunity and lipid metabolism (Probable). Prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) and IFN-gamma signaling pathways and by blocking the formation of phosphorylated STAT1 and promoting ubiquitin-mediated proteasome-dependent degradation of STAT1 (By similarity). Activates STAT3 leading to cellular transformation (By similarity). Regulates the activity of cellular genes, including c-myc and c-fos (By similarity). May repress the promoter of p53, and sequester CREB3 and SP110 isoform 3/Sp110b in the cytoplasm (By similarity). Represses cell cycle negative regulating factor CDKN1A, thereby interrupting an important check point of normal cell cycle regulation (By similarity). Targets transcription factors involved in the regulation of inflammatory responses and in the immune response: suppresses TNF-induced NF-kappa-B activation, and activates AP-1 (By similarity). Binds to dendritic cells (DCs) via C1QR1, resulting in down-regulation of T-lymphocytes proliferation (By similarity). Alters lipid metabolism by interacting with hepatocellular proteins involved in lipid accumulation and storage (By similarity). Induces up-regulation of FAS promoter activity, and thereby contributes to the increased triglyceride accumulation in hepatocytes (steatosis) (By similarity)", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [ { "position": 196, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 209, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 234, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 305, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 417, "type": "N-linked (GlcNAc...) (high mannose) asparagine; by host" }, { "position": 423, "type": "N-linked (GlcNAc...) (high mannose) asparagine; by host" }, { "position": 430, "type": "N-linked (GlcNAc...) (high mannose) asparagine; by host" }, { "position": 448, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 476, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 533, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 557, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 623, "type": "N-linked (GlcNAc...) (high mannose) asparagine; by host" }, { "position": 645, "type": "N-linked (GlcNAc...) (high mannose) asparagine; by host" } ], "id": "O39929", "name": "NS1 (p7)", "organism": "Hepatitis C virus genotype 4a (isolate ED43)", "uniprot_id": "O39929" }, { "function": "", "gene_name": "NS5b", "glycan_count": 0, "glycosylation_sites": [], "id": "O39930", "name": "NS2", "organism": "Hepacivirus hominis", "uniprot_id": "O39930" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O39931/O39932", "name": "NS3/NS4A", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "RNA polymerase gene", "glycan_count": 0, "glycosylation_sites": [], "id": "O39933", "name": "NS4B", "organism": "Norovirus isolates", "uniprot_id": "O39933" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O39934", "name": "NS5A", "organism": "Hepatitis delta virus", "uniprot_id": "O39934" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O39935", "name": "NS5B", "organism": "Hepatitis delta virus", "uniprot_id": "O39935" }, { "function": "Receptor for the chemotactic and inflammatory peptide anaphylatoxin C5a (PubMed:10636859, PubMed:15153520, PubMed:1847994, PubMed:29300009, PubMed:7622471, PubMed:8182049, PubMed:9553099). The ligand interacts with at least two sites on the receptor: a high-affinity site on the extracellular N-terminus, and a second site in the transmembrane region which activates downstream signaling events (PubMed:7622471, PubMed:8182049, PubMed:9553099). Receptor activation stimulates chemotaxis, granule enzyme release, intracellular calcium release and superoxide anion production (PubMed:10636859, PubMed:15153520)", "gene_name": "C5AR1", "glycan_count": 0, "glycosylation_sites": [ { "position": 5, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P21730", "name": "Complement C5a receptor (C5aR1)", "organism": "Homo sapiens", "uniprot_id": "P21730" }, { "function": "Acts as a guanine-nucleotide releasing factor (GEF) for Rab GTPases by promoting the conversion of inactive RAB-GDP to the active form RAB-GTP (PubMed:27103069, PubMed:27193190, PubMed:27617292, PubMed:28195531, PubMed:37821429). Acts as a GEF for RAB39A which enables HOPS-mediated autophagosome-lysosome membrane tethering and fusion in mammalian autophagy (PubMed:37821429). Component of the C9orf72-SMCR8 complex where both subunits display GEF activity and that regulates autophagy (PubMed:27103069, PubMed:27193190, PubMed:27617292, PubMed:28195531). As part of the C9orf72-SMCR8-WDR41 (CSW) complex, functions as GEF for RAB8A and RAB39B, thereby promoting autophagosome maturation (PubMed:27103069). As part of the C9orf72-SMCR8 complex, also functions as GTPase activating protein (GAP) for RAB8A and RAB11A in vitro (PubMed:32303654). The C9orf72-SMCR8 complex also acts as a regulator of autophagy initiation by interacting with the ULK1/ATG1 kinase complex and modulating its protein kinase activity (PubMed:27617292). Promotes initiation of autophagy by regulating the RAB1A-dependent trafficking of the ULK1/ATG1 kinase complex to the phagophore which leads to autophagosome formation (PubMed:27334615). Acts as a regulator of mTORC1 signaling by promoting phosphorylation of mTORC1 substrates (PubMed:27559131). Plays a role in endosomal trafficking (PubMed:24549040). May be involved in regulating the maturation of phagosomes to lysosomes (By similarity). Promotes the lysosomal localization and lysosome-mediated degradation of CARM1 which leads to inhibition of starvation-induced lipid metabolism (By similarity). Regulates actin dynamics in motor neurons by inhibiting the GTP-binding activity of ARF6, leading to ARF6 inactivation (PubMed:27723745). This reduces the activity of the LIMK1 and LIMK2 kinases which are responsible for phosphorylation and inactivation of cofilin, leading to CFL1/cofilin activation (PubMed:27723745). Positively regulates axon extension and axon growth cone size in spinal motor neurons (PubMed:27723745). Required for SMCR8 protein expression and localization at pre- and post-synaptic compartments in the forebrain, also regulates protein abundance of RAB3A and GRIA1/GLUR1 in post-synaptic compartments in the forebrain and hippocampus (By similarity). Plays a role within the hematopoietic system in restricting inflammation and the development of autoimmunity (By similarity)", "gene_name": "C9orf72", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96LT7", "name": "C9ORF72", "organism": "Homo sapiens", "uniprot_id": "Q96LT7" }, { "function": "May act as a GTPase regulator. Controls survival and growth of spinal motoneurons (By similarity)", "gene_name": "ALS2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96Q42", "name": "Alsin (ALS2)", "organism": "Homo sapiens", "uniprot_id": "Q96Q42" }, { "function": "Endoplasmic reticulum (ER)-anchored protein that mediates the formation of contact sites between the ER and endosomes via interaction with FFAT motif-containing proteins such as STARD3 or WDR44 (PubMed:32344433, PubMed:33124732). Interacts with STARD3 in a FFAT motif phosphorylation dependent manner (PubMed:33124732). Via interaction with WDR44 participates in neosynthesized protein export (PubMed:32344433). Participates in the endoplasmic reticulum unfolded protein response (UPR) by inducing ERN1/IRE1 activity (PubMed:16891305, PubMed:20940299). Involved in cellular calcium homeostasis regulation (PubMed:22131369)", "gene_name": "VAPB", "glycan_count": 1, "glycosylation_sites": [], "id": "O95292", "name": "VAPB", "organism": "Homo sapiens", "uniprot_id": "O95292" }, { "function": "Plays an important role in the maintenance of the Golgi complex, in membrane trafficking, in exocytosis, through its interaction with myosin VI and Rab8 (PubMed:27534431). Links myosin VI to the Golgi complex and plays an important role in Golgi ribbon formation (PubMed:27534431). Plays a role in the activation of innate immune response during viral infection. Mechanistically, recruits TBK1 at the Golgi apparatus, promoting its trans-phosphorylation after RLR or TLR3 stimulation (PubMed:27538435). In turn, activated TBK1 phosphorylates its downstream partner IRF3 to produce IFN-beta/IFNB1. Plays a neuroprotective role in the eye and optic nerve. May act by regulating membrane trafficking and cellular morphogenesis via a complex that contains Rab8 and huntingtin (HD). Mediates the interaction of Rab8 with the probable GTPase-activating protein TBC1D17 during Rab8-mediated endocytic trafficking, such as that of transferrin receptor (TFRC/TfR); regulates Rab8 recruitment to tubules emanating from the endocytic recycling compartment (PubMed:22854040). Autophagy receptor that interacts directly with both the cargo to become degraded and an autophagy modifier of the MAP1 LC3 family; targets ubiquitin-coated bacteria (xenophagy), such as cytoplasmic Salmonella enterica, and appears to function in the same pathway as SQSTM1 and CALCOCO2/NDP52", "gene_name": "OPTN", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96CV9", "name": "Optineurin (OPTN)", "organism": "Homo sapiens", "uniprot_id": "Q96CV9" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P24043/P55268", "name": "Laminin \u03b12/\u03b22", "organism": "", "uniprot_id": "" }, { "function": "Has weak activities on human monocytes and acts via receptors that also recognize MIP-1 alpha. It induces intracellular Ca(2+) changes and enzyme release, but no chemotaxis, at concentrations of 100-1,000 nM, and is inactive on T-lymphocytes, neutrophils, and eosinophil leukocytes. Enhances the proliferation of CD34 myeloid progenitor cells. The processed form HCC-1(9-74) is a chemotactic factor that attracts monocytes, eosinophils, and T-cells and is a ligand for CCR1, CCR3 and CCR5", "gene_name": "CCL14", "glycan_count": 1, "glycosylation_sites": [ { "position": 26, "type": "O-linked (GalNAc...) serine; partial" } ], "id": "Q16627", "name": "Chemokine (C-C motif) ligand 14 (CCL14)", "organism": "Homo sapiens", "uniprot_id": "Q16627" }, { "function": "Inhibits gastrointestinal motility and gastric acid secretion. Could function as a structural component of gastric mucus, possibly by stabilizing glycoproteins in the mucus gel through interactions with carbohydrate side chains (By similarity)", "gene_name": "TFF2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q03403", "name": "Soluble urokinase plasminogen activator receptor (suPAR)", "organism": "Homo sapiens", "uniprot_id": "Q03403" }, { "function": "Non-classical major histocompatibility class Ib molecule postulated to play a role in immune surveillance, immune tolerance and inflammation. Functions in two forms, as a heterotrimeric complex with B2M/beta-2 microglobulin and a peptide (peptide-bound HLA-F-B2M) and as an open conformer (OC) devoid of peptide and B2M (peptide-free OC). In complex with B2M, presents non-canonical self-peptides carrying post-translational modifications, particularly phosphorylated self-peptides. Peptide-bound HLA-F-B2M acts as a ligand for LILRB1 inhibitory receptor, a major player in maternal-fetal tolerance. Peptide-free OC acts as a ligand for KIR3DS1 and KIR3DL2 receptors (PubMed:28636952). Upon interaction with activating KIR3DS1 receptor on NK cells, triggers NK cell degranulation and anti-viral cytokine production (PubMed:27455421). Through interaction with KIR3DL2 receptor, inhibits NK and T cell effector functions (PubMed:24018270). May interact with other MHC class I OCs to cross-present exogenous viral, tumor or minor histompatibility antigens to cytotoxic CD8+ T cells, triggering effector and memory responses (PubMed:23851683). May play a role in inflammatory responses in the peripheral nervous system. Through interaction with KIR3DL2, may protect motor neurons from astrocyte-induced toxicity (PubMed:26928464)", "gene_name": "HLA-F", "glycan_count": 8, "glycosylation_sites": [ { "position": 107, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P30511", "name": "HLA-F", "organism": "Homo sapiens", "uniprot_id": "P30511" }, { "function": "Binds to actin filaments in muscle and non-muscle cells (PubMed:23170982). Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction (PubMed:23170982). Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments", "gene_name": "TPM1", "glycan_count": 1, "glycosylation_sites": [], "id": "P09493", "name": "Tropomyosin", "organism": "Homo sapiens", "uniprot_id": "P09493" }, { "function": "", "gene_name": "KRT3", "glycan_count": 1, "glycosylation_sites": [], "id": "P12035", "name": "C/EBP\u03b1", "organism": "Homo sapiens", "uniprot_id": "P12035" }, { "function": "Mediates the Na(+)-independent high affinity transport of organic anions such as the thyroid hormones L-thyroxine (T4), L-thyroxine sulfate (T4S), and 3,3',5'-triiodo-L-thyronine (reverse T3, rT3) at the plasma membrane (PubMed:12351693, PubMed:18566113, PubMed:19129463). Regulates T4 levels in different brain regions by transporting T4, and also by serving as an export pump for T4S, which is a source of T4 after hydrolysis by local sulfatases (PubMed:18566113). Increases the access of these substrates to the intracellular sites where they are metabolized by the deiodinases (PubMed:18566113). Other potential substrates, such as triiodothyronine (T3), 17-beta-glucuronosyl estradiol (17beta-estradiol 17-O-(beta-D-glucuronate)), estrone-3-sulfate (E1S) and sulfobromophthalein (BSP) are transported with much lower efficiency (PubMed:12351693, PubMed:19129463). Transports T4 and E1S in a pH-insensitive manner (PubMed:19129463). Facilitates the transport of thyroid hormones across the blood-brain barrier and into glia and neuronal cells in the brain (PubMed:30296914)", "gene_name": "SLCO1C1", "glycan_count": 1, "glycosylation_sites": [ { "position": 146, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 510, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 520, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 533, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NYB5", "name": "OATP1A4", "organism": "Homo sapiens", "uniprot_id": "Q9NYB5" }, { "function": "ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds and xenobiotics from cells. Transports a range of endogenous molecules that have a key role in cellular communication and signaling, including cyclic nucleotides such as cyclic AMP (cAMP) and cyclic GMP (cGMP), bile acids, steroid conjugates, urate, and prostaglandins (PubMed:11856762, PubMed:12523936, PubMed:12835412, PubMed:12883481, PubMed:15364914, PubMed:15454390, PubMed:16282361, PubMed:17959747, PubMed:18300232, PubMed:26721430). Mediates the ATP-dependent efflux of glutathione conjugates such as leukotriene C4 (LTC4) and leukotriene B4 (LTB4) too. The presence of GSH is necessary for the ATP-dependent transport of LTB4, whereas GSH is not required for the transport of LTC4 (PubMed:17959747). Mediates the cotransport of bile acids with reduced glutathione (GSH) (PubMed:12523936, PubMed:12883481, PubMed:16282361). Transports a wide range of drugs and their metabolites, including anticancer, antiviral and antibiotics molecules (PubMed:11856762, PubMed:12105214, PubMed:15454390, PubMed:17344354, PubMed:18300232). Confers resistance to anticancer agents such as methotrexate (PubMed:11106685)", "gene_name": "ABCC4", "glycan_count": 6, "glycosylation_sites": [ { "position": 746, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 754, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O15439", "name": "MRP4", "organism": "Homo sapiens", "uniprot_id": "O15439" }, { "function": "Nucleoporin essential for nuclear pore assembly and fusion, nuclear pore spacing, as well as structural integrity", "gene_name": "NUP210", "glycan_count": 23, "glycosylation_sites": [ { "position": 44, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 337, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 405, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 484, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 681, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 801, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 926, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1039, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1116, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1135, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1362, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1441, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8TEM1", "name": "Anti-gp210", "organism": "Homo sapiens", "uniprot_id": "Q8TEM1" }, { "function": "Histone H3-like nucleosomal protein that is specifically found in centromeric nucleosomes (PubMed:11756469, PubMed:14667408, PubMed:15282608, PubMed:15475964, PubMed:15702419, PubMed:17651496, PubMed:19114591, PubMed:20739937, PubMed:27499292, PubMed:7962047, PubMed:9024683). Replaces conventional H3 in the nucleosome core of centromeric chromatin that serves as an assembly site for the inner kinetochore (PubMed:18072184). The presence of CENPA subtly modifies the nucleosome structure and the way DNA is wrapped around the nucleosome and gives rise to protruding DNA ends that are less well-ordered and rigid compared to nucleosomes containing histone H3 (PubMed:26878239, PubMed:27499292). May serve as an epigenetic mark that propagates centromere identity through replication and cell division (PubMed:15282608, PubMed:15475964, PubMed:20739937, PubMed:21478274, PubMed:26878239). Required for recruitment and assembly of kinetochore proteins, and as a consequence required for progress through mitosis, chromosome segregation and cytokinesis (PubMed:11756469, PubMed:14667408, PubMed:18072184, PubMed:23818633, PubMed:25556658, PubMed:27499292)", "gene_name": "CENPA", "glycan_count": 0, "glycosylation_sites": [], "id": "P49450", "name": "Anti-centromere protein A (CENP-A)", "organism": "Homo sapiens", "uniprot_id": "P49450" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01185-2", "name": "Copeptin", "organism": "", "uniprot_id": "" }, { "function": "Mitochondrial protein required for adaptation of miochondrial dynamics to metabolic changes. Regulates mitochondrial morphology at steady state and mediates AMPK-dependent stress-induced mitochondrial fragmentation via the control of OPA1 levels", "gene_name": "MTFR1L", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H019", "name": "Leucyl and cystinyl aminopeptidase (LNPEP/vasopressinase)", "organism": "Homo sapiens", "uniprot_id": "Q9H019" }, { "function": "May affect the movement of lipids in the cytoplasm or allow the binding of lipids to organelles", "gene_name": "APOL6", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9BWW8", "name": "Testican-2", "organism": "Homo sapiens", "uniprot_id": "Q9BWW8" }, { "function": "LIF has the capacity to induce terminal differentiation in leukemic cells. Its activities include the induction of hematopoietic differentiation in normal and myeloid leukemia cells, the induction of neuronal cell differentiation, and the stimulation of acute-phase protein synthesis in hepatocytes", "gene_name": "LIF", "glycan_count": 1, "glycosylation_sites": [ { "position": 31, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 56, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 85, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 95, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 118, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 138, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P15018", "name": "Leukemia Inhibitory Factor (LIF)", "organism": "Homo sapiens", "uniprot_id": "P15018" }, { "function": "Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TEFb complex) that will in turn hyperphosphorylate the RNA polymerase II to allow efficient elongation. The CDK9 component of P-TEFb and other Tat-activated kinases hyperphosphorylate the C-terminus of RNA Pol II that becomes stabilized and much more processive. Other factors such as HTATSF1/Tat-SF1, SUPT5H/SPT5, and HTATIP2 are also important for Tat's function. Besides its effect on RNA Pol II processivity, Tat induces chromatin remodeling of proviral genes by recruiting the histone acetyltransferases (HATs) CREBBP, EP300 and PCAF to the chromatin. This also contributes to the increase in proviral transcription rate, especially when the provirus integrates in transcriptionally silent region of the host genome. To ensure maximal activation of the LTR, Tat mediates nuclear translocation of NF-kappa-B by interacting with host RELA. Through its interaction with host TBP, Tat may also modulate transcription initiation. Tat can reactivate a latently infected cell by penetrating in it and transactivating its LTR promoter. In the cytoplasm, Tat is thought to act as a translational activator of HIV-1 mRNAs", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04612", "name": "Tat", "organism": "Human immunodeficiency virus type 1 group M subtype B (isolate BH5)", "uniprot_id": "P04612" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P00488 (A), P05160 (B)", "name": "Factor XIII", "organism": "", "uniprot_id": "" }, { "function": "Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein) (PubMed:10993067, PubMed:12679784, PubMed:25043039, PubMed:26280335, PubMed:30598546, PubMed:30630874). The gamma-secretase complex plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins, and by regulating cytosolic CTNNB1 levels", "gene_name": "NCSTN", "glycan_count": 31, "glycosylation_sites": [ { "position": 45, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 55, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 187, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 200, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 204, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 264, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 387, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 417, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 435, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 464, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 506, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 530, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 562, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 573, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 580, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 612, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q92542", "name": "Nicastrin (NCT)", "organism": "Homo sapiens", "uniprot_id": "Q92542" }, { "function": "Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P0DTC1", "name": "3CLpro (Main protease, nsp5)", "organism": "Severe acute respiratory syndrome coronavirus 2", "uniprot_id": "P0DTC1" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P19838 (RelA)", "name": "NF-\u03baB", "organism": "", "uniprot_id": "" }, { "function": "Monokine with inflammatory and chemokinetic properties. Binds to CCR1, CCR4 and CCR5. One of the major HIV-suppressive factors produced by CD8+ T-cells. Recombinant MIP-1-alpha induces a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV)", "gene_name": "Ccl3", "glycan_count": 0, "glycosylation_sites": [], "id": "P10855", "name": "Ccl3", "organism": "Mus musculus", "uniprot_id": "P10855" }, { "function": "Monokine with inflammatory and chemokinetic properties", "gene_name": "Ccl4", "glycan_count": 0, "glycosylation_sites": [], "id": "P14097", "name": "Ccl4", "organism": "Mus musculus", "uniprot_id": "P14097" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P41754", "name": "Cxcl2", "organism": "Phytophthora capsici", "uniprot_id": "P41754" }, { "function": "ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds and xenobiotics from cells. Plays a role in physiological processes involving bile acids, conjugated steroids and cyclic nucleotides, including cAMP and cGMP (PubMed:12764137, PubMed:15537867). Mediates the ATP-dependent efflux of a range of physiological lipophilic anions, including the glutathione S-conjugates leukotriene C4 and dinitrophenyl S-glutathione, steroid sulfates, such as dehydroepiandrosterone 3-sulfate (DHEAS) and estrone 3-sulfate, glucuronides such as estradiol 17-beta-D-glucuronide (E(2)17betaG), the monoanionic bile acids glycocholate and taurocholate, and methotrexate (PubMed:15537867, PubMed:16359813, PubMed:25896536). Plays a role in the transport of earwax components (PubMed:16444273, PubMed:19383836). Participates in the secretion of odorants and their precursors from the apocrine sweat glands, including the secretion of glutamine conjugates, as well as the Cys-Gly-(S) conjugates of 3-methyl-3-sulfanyl-hexanol (PubMed:19710689). Involved in the cellular extrusion of nucleotide analogs, hence confering resistance to various drugs, including clinically relevant drugs such as 5-fluorouracil (5-FU) and methotrexate (PubMed:12764137, PubMed:15537867, PubMed:25896536)", "gene_name": "ABCC11", "glycan_count": 0, "glycosylation_sites": [ { "position": 838, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 844, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q96J66", "name": "ABCC11 (MRP8)", "organism": "Homo sapiens", "uniprot_id": "Q96J66" }, { "function": "Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation (By similarity). Induces insulin resistance in adipocytes via inhibition of insulin-induced IRS1 tyrosine phosphorylation and insulin-induced glucose uptake. Induces GKAP42 protein degradation in adipocytes which is partially responsible for TNF-induced insulin resistance (By similarity). Plays a role in angiogenesis by inducing VEGF production synergistically with IL1B and IL6 (By similarity). Promotes osteoclastogenesis and therefore mediates bone resorption (By similarity)", "gene_name": "Tnf", "glycan_count": 0, "glycosylation_sites": [ { "position": 83, "type": "O-linked (GalNAc...) serine; in soluble form" }, { "position": 86, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P16599", "name": "Interleukin-1 beta (IL1\u03b2)", "organism": "Rattus norvegicus", "uniprot_id": "P16599" }, { "function": "Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues (By similarity)", "gene_name": "Mmp2", "glycan_count": 0, "glycosylation_sites": [ { "position": 575, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 644, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P33436", "name": "Matrix metalloproteinase-2 (MMP2)", "organism": "Rattus norvegicus", "uniprot_id": "P33436" }, { "function": "Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion", "gene_name": "Mmp13", "glycan_count": 0, "glycosylation_sites": [ { "position": 118, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 153, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 410, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P33435", "name": "Matrix metalloproteinase-3 (MMP3)", "organism": "Mus musculus", "uniprot_id": "P33435" }, { "function": "Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration (By similarity). Could play a role in bone osteoclastic resorption (By similarity). Cleaves KiSS1 at a Gly-|-Leu bond (By similarity). Cleaves NINJ1 to generate the Secreted ninjurin-1 form (By similarity). Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide (By similarity)", "gene_name": "Mmp9", "glycan_count": 0, "glycosylation_sites": [ { "position": 39, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 121, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P50282", "name": "Matrix metalloproteinase-9 (MMP9)", "organism": "Rattus norvegicus", "uniprot_id": "P50282" }, { "function": "Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. Binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. May play a role in increasing vascular permeability during lactation, when increased transport of molecules from the blood is required for efficient milk protein synthesis. Binding to NRP1 receptor initiates a signaling pathway needed for motor neuron axon guidance and cell body migration, including for the caudal migration of facial motor neurons from rhombomere 4 to rhombomere 6 during embryonic development (By similarity). Also binds the DEAR/FBXW7-AS1 receptor (By similarity)", "gene_name": "Vegfa", "glycan_count": 0, "glycosylation_sites": [ { "position": 100, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P16612", "name": "Vascular endothelial growth factor (VEGF)", "organism": "Rattus norvegicus", "uniprot_id": "P16612" }, { "function": "The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover", "gene_name": "CHRM3", "glycan_count": 1, "glycosylation_sites": [ { "position": 5, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 6, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 15, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 41, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 48, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P20309", "name": "M3 muscarinic receptor", "organism": "Homo sapiens", "uniprot_id": "P20309" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q02817 (mouse)", "name": "Muc2", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01584 (mouse)", "name": "IL-1\u03b2", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P18893 (mouse)", "name": "IL-10", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P05109 (S100A8), P06702 (S100A9)", "name": "Calprotectin", "organism": "", "uniprot_id": "" }, { "function": "The heterodimer with SLC3A2 functions as a sodium-independent, high-affinity transporter that mediates uptake of large neutral amino acids such as phenylalanine, tyrosine, leucine, histidine, methionine, tryptophan, valine, isoleucine and alanine (PubMed:10049700, PubMed:10574970, PubMed:11557028, PubMed:11564694, PubMed:12117417, PubMed:12225859, PubMed:15769744, PubMed:18262359, PubMed:25998567, PubMed:30867591, PubMed:9751058). The heterodimer with SLC3A2 mediates the uptake of L-DOPA (By similarity). Functions as an amino acid exchanger (PubMed:11557028, PubMed:12117417, PubMed:12225859, PubMed:30867591). May play a role in the transport of L-DOPA across the blood-brain barrier (By similarity). May act as the major transporter of tyrosine in fibroblasts (Probable). May mediate blood-to-retina L-leucine transport across the inner blood-retinal barrier (By similarity). Can mediate the transport of thyroid hormones diiodothyronine (T2), triiodothyronine (T3) and thyroxine (T4) across the cell membrane (PubMed:11564694). When associated with LAPTM4B, the heterodimer formed by SLC3A2 and SLC7A5 is recruited to lysosomes to promote leucine uptake into these organelles, and thereby mediates mTORC1 activation (PubMed:25998567). Involved in the uptake of toxic methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes (PubMed:12117417). Involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the membrane (PubMed:15769744)", "gene_name": "SLC7A5", "glycan_count": 1, "glycosylation_sites": [], "id": "Q01650", "name": "Neutral amino acid transporter B0AT1", "organism": "Homo sapiens", "uniprot_id": "Q01650" }, { "function": "Antibacterial protein which inhibits the growth of E.coli and S.aureus", "gene_name": "Wfdc15b", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9JHY4", "name": "Prestin", "organism": "Mus musculus", "uniprot_id": "Q9JHY4" }, { "function": "Catalyzes erythromycin N-demethylation, nifedipine oxidation and testosterone 6 beta-hydroxylation", "gene_name": "Cyp3a11", "glycan_count": 0, "glycosylation_sites": [], "id": "Q64459", "name": "Cytochrome P450 2c29 (Cyp2c29)", "organism": "Mus musculus", "uniprot_id": "Q64459" }, { "function": "Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics", "gene_name": "16aoh-b", "glycan_count": 0, "glycosylation_sites": [], "id": "Q64460", "name": "Cytochrome P450 2c50 (Cyp2c50)", "organism": "Mus musculus", "uniprot_id": "Q64460" }, { "function": "The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity)", "gene_name": "Copa", "glycan_count": 5, "glycosylation_sites": [], "id": "Q8CIE6", "name": "Cytochrome P450 2j5 (Cyp2j5)", "organism": "Mus musculus", "uniprot_id": "Q8CIE6" }, { "function": "A cytochrome P450 monooxygenase that selectively catalyzes the epoxidation of 14,15 double bond of (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (arachidonate) forming 14,15-epoxyeicosatrienoic acid (14,15-EET) regioisomer. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH--hemoprotein reductase)", "gene_name": "Cyp2c29", "glycan_count": 1, "glycosylation_sites": [], "id": "Q64458", "name": "Cytochrome P450 2a4 (Cyp2a4)", "organism": "Mus musculus", "uniprot_id": "Q64458" }, { "function": "Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen", "gene_name": "Col4a4", "glycan_count": 0, "glycosylation_sites": [ { "position": 43, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 134, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 661, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q64457", "name": "Cytochrome P450 2a5 (Cyp2a5)", "organism": "Mus musculus", "uniprot_id": "Q9QZR9" }, { "function": "This proteoglycan is a major component of extracellular matrix of cartilagenous tissues. A major function of this protein is to resist compression in cartilage. It binds avidly to hyaluronic acid via an N-terminal globular region. May play a regulatory role in the matrix assembly of the cartilage", "gene_name": "Acan", "glycan_count": 6, "glycosylation_sites": [ { "position": 126, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 239, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 333, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 371, "type": "O-linked (Xyl...) (keratan sulfate) threonine" }, { "position": 376, "type": "O-linked (Xyl...) (keratan sulfate) threonine" }, { "position": 387, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 611, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 667, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1150, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 1186, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 1200, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 1206, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 1210, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 1220, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 1322, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 1675, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1880, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q61282", "name": "Cytochrome P450 7a1 (Cyp7a1)", "organism": "Mus musculus", "uniprot_id": "Q61282" }, { "function": "Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) and in neurons (Ih) (PubMed:10962006, PubMed:11096117, PubMed:11459060, PubMed:11741901, PubMed:12034718, PubMed:12193608, PubMed:12968185, PubMed:17562314, PubMed:21347269, PubMed:21903816, PubMed:23103389). Can also transport ammonium in the distal nephron (By similarity). Involved in the initiation of neuropathic pain in sensory neurons (PubMed:21903816)", "gene_name": "Hcn2", "glycan_count": 1, "glycosylation_sites": [ { "position": 380, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O88703", "name": "Bile salt export pump (Abcb11)", "organism": "Mus musculus", "uniprot_id": "O88703" }, { "function": "Catalyzes the first irreversible step in ketogenesis, condensing acetyl-CoA to acetoacetyl-CoA to form HMG-CoA, which is converted by HMG-CoA reductase (HMGCR) into mevalonate", "gene_name": "HMGCS2", "glycan_count": 1, "glycosylation_sites": [], "id": "P54868", "name": "Hydroxymethylglutaryl-CoA synthase (HMGCS1)", "organism": "Homo sapiens", "uniprot_id": "P54868" }, { "function": "Dual specificity protein phosphatase involved in the inactivation of MAP kinases. Dephosphorylates MAPK10 bound to ARRB2", "gene_name": "DUSP16", "glycan_count": 3, "glycosylation_sites": [], "id": "Q9BY84", "name": "Dual specificity protein phosphatase 13 isoform A (DUSP13A)", "organism": "Homo sapiens", "uniprot_id": "Q9BY84" }, { "function": "Multifunctional glycoprotein that acts as a receptor for a broad range of ligands. Ligands can be of proteinaceous nature like thrombospondin, fibronectin, collagen or amyloid-beta as well as of lipidic nature such as oxidized low-density lipoprotein (oxLDL), anionic phospholipids, long-chain fatty acids and bacterial diacylated lipopeptides. They are generally multivalent and can therefore engage multiple receptors simultaneously, the resulting formation of CD36 clusters initiates signal transduction and internalization of receptor-ligand complexes. The dependency on coreceptor signaling is strongly ligand specific. Cellular responses to these ligands are involved in angiogenesis, inflammatory response, fatty acid metabolism, taste and dietary fat processing in the intestine (By similarity) (PubMed:8320718). Binds long-chain fatty acids and facilitates their transport into cells, thus participating in muscle lipid utilization, adipose energy storage, and gut fat absorption (By similarity) (PubMed:8320718). Mechanistically, binding of fatty acids activates downstream kinase LYN, which phosphorylates the palmitoyltransferase ZDHHC5 and inactivates it, resulting in the subsequent depalmitoylation of CD36 and caveolar endocytosis (By similarity). In the small intestine, plays a role in proximal absorption of dietary fatty acid and cholesterol for optimal chylomicron formation, possibly through the activation of MAPK1/3 (ERK1/2) signaling pathway (By similarity) (PubMed:16276419, PubMed:21610069). Involved in oral fat perception and preferences (By similarity) (PubMed:16276419). Detection into the tongue of long-chain fatty acids leads to a rapid and sustained rise in flux and protein content of pancreatobiliary secretions (By similarity) (PubMed:16276419). In taste receptor cells, mediates the induction of an increase in intracellular calcium levels by long-chain fatty acids, leading to the activation of the gustatory neurons in the nucleus of the solitary tract (By similarity). Important factor in both ventromedial hypothalamus neuronal sensing of long-chain fatty acid and the regulation of energy and glucose homeostasis (By similarity) (PubMed:23557700). Receptor for thrombospondins, THBS1 and THBS2, mediating their antiangiogenic effects (By similarity). As a coreceptor for TLR4:TLR6 heterodimer, promotes inflammation in monocytes/macrophages. Upon ligand binding, such as oxLDL or amyloid-beta 42, interacts with the heterodimer TLR4:TLR6, the complex is internalized and triggers inflammatory response, leading to NF-kappa-B-dependent production of CXCL1, CXCL2 and CCL9 cytokines, via MYD88 signaling pathway, and CCL5 cytokine, via TICAM1 signaling pathway, as well as IL1B secretion, through the priming and activation of the NLRP3 inflammasome. Selective and nonredundant sensor of microbial diacylated lipopeptide that signal via TLR2:TLR6 heterodimer, this cluster triggers signaling from the cell surface, leading to the NF-kappa-B-dependent production of TNF, via MYD88 signaling pathway and subsequently is targeted to the Golgi in a lipid-raft dependent pathway (By similarity)", "gene_name": "Cd36", "glycan_count": 0, "glycosylation_sites": [ { "position": 79, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 102, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 134, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 205, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 220, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 235, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 247, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 321, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 417, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q07969", "name": "CD36", "organism": "Rattus norvegicus", "uniprot_id": "Q07969" }, { "function": "Involved in the biosynthesis of highly unsaturated fatty acids (HUFA) from the essential polyunsaturated fatty acids (PUFA) linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3) precursors, acting as a fatty acyl-coenzyme A (CoA) desaturase that introduces a cis double bond at carbon 6 of the fatty acyl chain. Catalyzes the first and rate limiting step in this pathway which is the desaturation of LA (18:2n-6) and ALA (18:3n-3) into gamma-linoleate (GLA) (18:3n-6) and stearidonate (18:4n-3), respectively (PubMed:10049752, PubMed:11988075, PubMed:14563830, PubMed:22216341, PubMed:24070791). Subsequently, in the biosynthetic pathway of HUFA n-3 series, it desaturates tetracosapentaenoate (24:5n-3) to tetracosahexaenoate (24:6n-3), which is then converted to docosahexaenoate (DHA)(22:6n-3), an important lipid for nervous system function (PubMed:11988075). It can also desaturate (11E)-octadecenoate (trans-vaccenoate) at carbon 6 generating (6Z,11E)-octadecadienoate (PubMed:24070791). In addition to Delta-6 activity, this enzyme exhibits Delta-8 activity with slight biases toward n-3 fatty acyl-CoA substrates (By similarity)", "gene_name": "Fads2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Z122", "name": "FADS2", "organism": "Rattus norvegicus", "uniprot_id": "Q9Z122" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "2IIK", "name": "ACAA1", "organism": "", "uniprot_id": "" }, { "function": "Calcium-activated selective cation channel that mediates membrane depolarization (PubMed:12015988, PubMed:12842017, PubMed:29211723, PubMed:30528822). While it is activated by increase in intracellular Ca(2+), it is impermeable to it (PubMed:12015988). Mediates transport of monovalent cations (Na(+) > K(+) > Cs(+) > Li(+)), leading to depolarize the membrane (PubMed:12015988). It thereby plays a central role in cadiomyocytes, neurons from entorhinal cortex, dorsal root and vomeronasal neurons, endocrine pancreas cells, kidney epithelial cells, cochlea hair cells etc. Participates in T-cell activation by modulating Ca(2+) oscillations after T lymphocyte activation, which is required for NFAT-dependent IL2 production. Involved in myogenic constriction of cerebral arteries. Controls insulin secretion in pancreatic beta-cells. May also be involved in pacemaking or could cause irregular electrical activity under conditions of Ca(2+) overload. Affects T-helper 1 (Th1) and T-helper 2 (Th2) cell motility and cytokine production through differential regulation of calcium signaling and NFATC1 localization. Enhances cell proliferation through up-regulation of the beta-catenin signaling pathway. Plays a role in keratinocyte differentiation (PubMed:30528822)", "gene_name": "TRPM4", "glycan_count": 0, "glycosylation_sites": [ { "position": 992, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8TD43", "name": "TRPM4", "organism": "Homo sapiens", "uniprot_id": "Q8TD43" }, { "function": "Plays a role in fertilization by controlling binding of sperm to zona pellucida and migration of spermatozoa into the oviduct (By similarity). May play a role in signal transduction and promote protein tyrosine phosphorylation (PubMed:11809740)", "gene_name": "Tex101", "glycan_count": 0, "glycosylation_sites": [ { "position": 45, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 110, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 134, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 160, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q924B5", "name": "TEX101", "organism": "Rattus norvegicus", "uniprot_id": "Q924B5" }, { "function": "Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione. May constitute a glutathione peroxidase-like protective system against peroxide damage in sperm membrane lipids", "gene_name": "Gpx5", "glycan_count": 0, "glycosylation_sites": [], "id": "P30710", "name": "GPX5", "organism": "Rattus norvegicus", "uniprot_id": "P30710" }, { "function": "Serine protease inhibitor that plays an essential role in male reproduction and fertility. Modulates the hydrolysis of SEMG1 by KLK3/PSA (a serine protease), provides antimicrobial protection for spermatozoa in the ejaculate coagulum, and binds SEMG1 thereby inhibiting sperm motility (By similarity)", "gene_name": "Eppin", "glycan_count": 0, "glycosylation_sites": [], "id": "D4A2Z2", "name": "EPPIN", "organism": "Rattus norvegicus", "uniprot_id": "D4A2Z2" }, { "function": "Can bind protoporphyrin IX and may play a role in the transport of porphyrins and heme (By similarity). Promotes the transport of cholesterol across mitochondrial membranes and may play a role in lipid metabolism (PubMed:24814875), but its precise physiological role is controversial. It is apparently not required for steroid hormone biosynthesis. Was initially identified as peripheral-type benzodiazepine receptor; can also bind isoquinoline carboxamides (PubMed:1847678)", "gene_name": "TSPO", "glycan_count": 1, "glycosylation_sites": [], "id": "P30536", "name": "Translocator protein (TSPO)", "organism": "Homo sapiens", "uniprot_id": "P30536" }, { "function": "Processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament. Can hydrolyze ATP in the presence of actin, which is essential for its function as a motor protein (PubMed:10448864). Involved in melanosome transport. Also mediates the transport of vesicles to the plasma membrane (By similarity). May also be required for some polarization process involved in dendrite formation (By similarity)", "gene_name": "MYO5A", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y4I1", "name": "MYO5B (Myosin Vb)", "organism": "Homo sapiens", "uniprot_id": "Q9Y4I1" }, { "function": "Binds mRNA and regulates the stability of target mRNA. Binds single-stranded DNA (in vitro)", "gene_name": "CARHSP1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y2V2", "name": "FCGBP", "organism": "Homo sapiens", "uniprot_id": "Q9Y2V2" }, { "function": "Calcium-binding protein that plays a role in various cellular processes including motility, angiogenesis, cell differentiation, apoptosis, and autophagy (PubMed:16707441, PubMed:23752197, PubMed:30713770). Increases cell motility and invasiveness by interacting with non-muscle myosin heavy chain (NMMHC) IIA/MYH9 (PubMed:16707441). Mechanistically, promotes filament depolymerization and increases the amount of soluble myosin-IIA, resulting in the formation of stable protrusions facilitating chemotaxis (By similarity). Also modulates the pro-apoptotic function of TP53 by binding to its C-terminal transactivation domain within the nucleus and reducing its protein levels (PubMed:23752197). Within the extracellular space, stimulates cytokine production including granulocyte colony-stimulating factor and CCL24 from T-lymphocytes (By similarity). In addition, stimulates T-lymphocyte chemotaxis by acting as a chemoattractant complex with PGLYRP1 that promotes lymphocyte migration via CCR5 and CXCR3 receptors (PubMed:26654597, PubMed:30713770)", "gene_name": "S100A4", "glycan_count": 1, "glycosylation_sites": [], "id": "P26447", "name": "S100A4", "organism": "Homo sapiens", "uniprot_id": "P26447" }, { "function": "Component of the large ribosomal subunit (PubMed:25901680). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:25901680). Binds directly to 26S ribosomal RNA (PubMed:25901680)", "gene_name": "RPL12", "glycan_count": 1, "glycosylation_sites": [], "id": "P30050", "name": "RPL12", "organism": "Homo sapiens", "uniprot_id": "P30050" }, { "function": "Component of the small ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. Required for proper rRNA processing and maturation of 18S rRNAs. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome", "gene_name": "rps27", "glycan_count": 0, "glycosylation_sites": [], "id": "P47904", "name": "RPL29", "organism": "Xenopus laevis", "uniprot_id": "P47904" }, { "function": "Component of the large ribosomal subunit (PubMed:23636399, PubMed:32669547). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399, PubMed:32669547)", "gene_name": "RPL31", "glycan_count": 1, "glycosylation_sites": [], "id": "P62899", "name": "RPL31", "organism": "Homo sapiens", "uniprot_id": "P62899" }, { "function": "Component of the small ribosomal subunit (PubMed:23636399). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399). Required for pre-rRNA processing and maturation of 40S ribosomal subunits (PubMed:16990592). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797)", "gene_name": "RPS19", "glycan_count": 1, "glycosylation_sites": [], "id": "P39019", "name": "RPS19", "organism": "Homo sapiens", "uniprot_id": "P39019" }, { "function": "Phosphorylates PPP1C, phosphorylase b and CFTR", "gene_name": "LMTK2", "glycan_count": 3, "glycosylation_sites": [], "id": "Q8IWU2", "name": "Asprosin", "organism": "Homo sapiens", "uniprot_id": "Q8IWU2" }, { "function": "Orphan receptor involved in cell adhesion and probably in cell-cell interactions specifically involving cells of the immune system. May play a role in regulatory T-cells (Treg) development", "gene_name": "ADGRE1", "glycan_count": 1, "glycosylation_sites": [ { "position": 94, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 99, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 127, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 167, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 189, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 194, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 232, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 258, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 312, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 366, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 375, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 448, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q14246", "name": "F4/80 (EMR1)", "organism": "Homo sapiens", "uniprot_id": "Q14246" }, { "function": "Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. This isozyme has a high catalytic efficiency with 4-hydroxyalkenals such as 4-hydroxynonenal (4-HNE)", "gene_name": "GSTA4", "glycan_count": 0, "glycosylation_sites": [], "id": "O15217", "name": "GCLM", "organism": "Homo sapiens", "uniprot_id": "O15217" }, { "function": "", "gene_name": "FAM174A", "glycan_count": 6, "glycosylation_sites": [ { "position": 83, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8TBP5", "name": "HSD17B13", "organism": "Homo sapiens", "uniprot_id": "Q8TBP5" }, { "function": "Galactose-specific lectin which binds IgE. May mediate with the alpha-3, beta-1 integrin the stimulation by CSPG4 of endothelial cells migration (PubMed:15181153). Together with DMBT1, required for terminal differentiation of columnar epithelial cells during early embryogenesis. In the nucleus: acts as a pre-mRNA splicing factor. Involved in acute inflammatory responses including neutrophil activation and adhesion, chemoattraction of monocytes macrophages, opsonization of apoptotic neutrophils, and activation of mast cells. Together with TRIM16, coordinates the recognition of membrane damage with mobilization of the core autophagy regulators ATG16L1 and BECN1 in response to damaged endomembranes (By similarity). When secreted, interacts with NK cell-activating receptor NCR3/NKp30 acting as an inhibitory ligand which antagonizes NK cell attack (By similarity)", "gene_name": "Lgals3", "glycan_count": 1, "glycosylation_sites": [], "id": "P16110", "name": "Galectin-3 (Gal3)", "organism": "Mus musculus", "uniprot_id": "P16110" }, { "function": "Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen", "gene_name": "Col4a2", "glycan_count": 0, "glycosylation_sites": [ { "position": 138, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1270, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08122", "name": "Collagen alpha-2(I) chain (Col1a2)", "organism": "Mus musculus", "uniprot_id": "P08122" }, { "function": "Transforming growth factor beta-1 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains, which constitute the regulatory and active subunit of TGF-beta-1, respectively", "gene_name": "Tgfb1", "glycan_count": 1, "glycosylation_sites": [ { "position": 82, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 136, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 176, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P04202", "name": "Transforming growth factor beta-1 (TGF\u03b21)", "organism": "Mus musculus", "uniprot_id": "P04202" }, { "function": "Involved in the Notch signaling pathway as Notch ligand (PubMed:11134954). Activates NOTCH1 and NOTCH4. Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting (PubMed:20616313). Essential for retinal progenitor proliferation. Required for suppressing rod fates in late retinal progenitors as well as for proper generation of other retinal cell types (By similarity). During spinal cord neurogenesis, inhibits V2a interneuron fate (PubMed:17728344)", "gene_name": "DLL4", "glycan_count": 1, "glycosylation_sites": [ { "position": 108, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 183, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 205, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 393, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NR61", "name": "Delta-like canonical Notch ligand 4 (Dll4)", "organism": "Homo sapiens", "uniprot_id": "Q9NR61" }, { "function": "Transcriptional repressor of genes that require a bHLH protein for their transcription. May act as a negative regulator of myogenesis by inhibiting the functions of MYOD1 and ASH1. Binds DNA on N-box motifs: 5'-CACNAG-3' with high affinity and on E-box motifs: 5'-CANNTG-3' with low affinity (By similarity). May play a role in a functional FA core complex response to DNA cross-link damage, being required for the stability and nuclear localization of FA core complex proteins, as well as for FANCD2 monoubiquitination in response to DNA damage", "gene_name": "HES1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q14469", "name": "Hairy Enhancer of Split-1 (Hes1)", "organism": "Homo sapiens", "uniprot_id": "Q14469" }, { "function": "Transcriptional coactivator for steroid receptors and nuclear receptors (PubMed:23508108, PubMed:8670870, PubMed:9430642, PubMed:22504882, PubMed:26553876). Coactivator of the steroid binding domain (AF-2) but not of the modulating N-terminal domain (AF-1) (PubMed:23508108, PubMed:8670870, PubMed:9430642). Required with NCOA1 to control energy balance between white and brown adipose tissues (PubMed:23508108, PubMed:8670870, PubMed:9430642). Critical regulator of glucose metabolism regulation, acts as a RORA coactivator to specifically modulate G6PC1 expression (PubMed:23508108, PubMed:8670870, PubMed:9430642). Involved in the positive regulation of the transcriptional activity of the glucocorticoid receptor NR3C1 by sumoylation enhancer RWDD3 (PubMed:23508108). Positively regulates the circadian clock by acting as a transcriptional coactivator for the CLOCK-BMAL1 heterodimer (By similarity)", "gene_name": "NCOA2", "glycan_count": 4, "glycosylation_sites": [], "id": "Q15596", "name": "Small heterodimer partner (SHP)", "organism": "Homo sapiens", "uniprot_id": "Q15596" }, { "function": "Muscle-specific type III intermediate filament essential for proper muscular structure and function. Plays a crucial role in maintaining the structure of sarcomeres, inter-connecting the Z-disks and forming the myofibrils, linking them not only to the sarcolemmal cytoskeleton, but also to the nucleus and mitochondria, thus providing strength for the muscle fiber during activity. In adult striated muscle they form a fibrous network connecting myofibrils to each other and to the plasma membrane from the periphery of the Z-line structures. May act as a sarcomeric microtubule-anchoring protein: specifically associates with detyrosinated tubulin-alpha chains, leading to buckled microtubules and mechanical resistance to contraction. Required for nuclear membrane integrity, via anchoring at the cell tip and nuclear envelope, resulting in maintenance of microtubule-derived intracellular mechanical forces (By similarity). Contributes to the transcriptional regulation of the NKX2-5 gene in cardiac progenitor cells during a short period of cardiomyogenesis and in cardiac side population stem cells in the adult. Plays a role in maintaining an optimal conformation of nebulette (NEB) on heart muscle sarcomeres to bind and recruit cardiac alpha-actin", "gene_name": "Des", "glycan_count": 1, "glycosylation_sites": [], "id": "P48675", "name": "Desmin", "organism": "Rattus norvegicus", "uniprot_id": "P48675" }, { "function": "", "gene_name": "GATA-6", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9WUZ3", "name": "Transgelin (Tagln)", "organism": "Mus musculus", "uniprot_id": "Q9WUZ3" }, { "function": "Binds to actin filaments in muscle and non-muscle cells (PubMed:22812662, PubMed:7568216). Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction (PubMed:22812662). Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments. The non-muscle isoform may have a role in agonist-mediated receptor internalization (By similarity)", "gene_name": "Tpm2", "glycan_count": 1, "glycosylation_sites": [], "id": "P58775", "name": "Tropomyosin beta chain (Tpm2)", "organism": "Rattus norvegicus", "uniprot_id": "P58775" }, { "function": "The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. STRAP plays a role in the cellular distribution of the SMN complex. Negatively regulates TGF-beta signaling but positively regulates the PDPK1 kinase activity by enhancing its autophosphorylation and by significantly reducing the association of PDPK1 with 14-3-3 protein (By similarity)", "gene_name": "Strap", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Z1Z2", "name": "Cysteine and glycine-rich protein 1 (Csrp1)", "organism": "Mus musculus", "uniprot_id": "Q9Z1Z2" }, { "function": "Functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs. May regulate branching morphogenesis in the developing vascular system (By similarity)", "gene_name": "NOTCH4", "glycan_count": 3, "glycosylation_sites": [ { "position": 664, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 714, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 964, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1143, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q99466", "name": "Notch4", "organism": "Homo sapiens", "uniprot_id": "Q99466" }, { "function": "Putative Notch ligand involved in the mediation of Notch signaling. Involved in limb development (By similarity)", "gene_name": "JAG2", "glycan_count": 2, "glycosylation_sites": [ { "position": 153, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 570, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 619, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 752, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1058, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y219", "name": "Jagged2 (Jag2)", "organism": "Homo sapiens", "uniprot_id": "Q9Y219" }, { "function": "Transmembrane ligand protein of NOTCH1, NOTCH2 and NOTCH3 receptors that binds the extracellular domain (ECD) of Notch receptor in a cis and trans fashion manner (PubMed:11006133). Following transinteraction, ligand cells produce mechanical force that depends of a clathrin-mediated endocytosis, requiring ligand ubiquitination, EPN1 interaction, and actin polymerisation; these events promote Notch receptor extracellular domain (NECD) transendocytosis and triggers Notch signaling through induction of cleavage, hyperphosphorylation, and nuclear accumulation of the intracellular domain of Notch receptors (NICD) (By similarity). Is required for embryonic development and maintenance of adult stem cells in many different tissues and immune systeme; the DLL1-induced Notch signaling is mediated through an intercellular communication that regulates cell lineage, cell specification, cell patterning and morphogenesis through effects on differentiation and proliferation (PubMed:11581320). Plays a role in brain development at different level, namely by regulating neuronal differentiation of neural precursor cells via cell-cell interaction, most likely through the lateral inhibitory system in an endogenous level dependent-manner. During neocortex development, Dll1-Notch signaling transmission is mediated by dynamic interactions between intermediate neurogenic progenitors and radial glia; the cell-cell interactions are mediated via dynamic and transient elongation processes, likely to reactivate/maintain Notch activity in neighboring progenitors, and coordinate progenitor cell division and differentiation across radial and zonal boundaries. During cerebellar development, regulates Bergmann glial monolayer formation and its morphological maturation through a Notch signaling pathway. At the retina and spinal cord level, regulates neurogenesis by preventing the premature differentiation of neural progenitors and also by maintaining progenitors in spinal cord through Notch signaling pathway. Also controls neurogenesis of the neural tube in a progenitor domain-specific fashion along the dorsoventral axis. Maintains quiescence of neural stem cells and plays a role as a fate determinant that segregates asymmetrically to one daughter cell during neural stem cells mitosis, resulting in neuronal differentiation in Dll1-inheriting cell. Plays a role in immune systeme development, namely the development of all T-cells and marginal zone (MZ) B-cells (By similarity). Blocks the differentiation of progenitor cells into the B-cell lineage while promoting the emergence of a population of cells with the characteristics of a T-cell/NK-cell precursor (PubMed:11581320). Also plays a role during muscle development. During early development, inhibits myoblasts differentiation from the medial dermomyotomal lip and later regulates progenitor cell differentiation. Directly modulates cell adhesion and basal lamina formation in satellite cells through Notch signaling. Maintains myogenic progenitors pool by suppressing differentiation through down-regulation of MYOD1 and is required for satellite cell homing and PAX7 expression. During craniofacial and trunk myogenesis suppresses differentiation of cranial mesoderm-derived and somite-derived muscle via MYOD1 regulation but in cranial mesoderm-derived progenitors, is neither required for satellite cell homing nor for PAX7 expression. Also plays a role during pancreatic cell development. During type B pancreatic cell development, may be involved in the initiation of proximodistal patterning in the early pancreatic epithelium. Stimulates multipotent pancreatic progenitor cells proliferation and pancreatic growth by maintaining HES1 expression and PTF1A protein levels. During fetal stages of development, is required to maintain arterial identity and the responsiveness of arterial endothelial cells for VEGFA through regulation of KDR activation and NRP1 expression. Controls sprouting angiogenesis and subsequent vertical branch formation through regulation on tip cell differentiation. Negatively regulates goblet cell differentiation in intestine and controls secretory fat commitment through lateral inhibition in small intestine. Plays a role during inner ear development; negatively regulates auditory hair cell differentiation. Plays a role during nephron development through Notch signaling pathway. Regulates growth, blood pressure and energy homeostasis (By similarity)", "gene_name": "DLL1", "glycan_count": 1, "glycosylation_sites": [ { "position": 477, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O00548", "name": "Delta-like ligand 1 (Dll1)", "organism": "Homo sapiens", "uniprot_id": "O00548" }, { "function": "Inhibits primary neurogenesis. May be required to divert neurons along a specific differentiation pathway. Plays a role in the formation of somite boundaries during segmentation of the paraxial mesoderm (By similarity)", "gene_name": "DLL3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NYJ7", "name": "Delta-like ligand 3 (Dll3)", "organism": "Homo sapiens", "uniprot_id": "Q9NYJ7" }, { "function": "May play a role in an as yet undefined retina-specific signal transduction. Could bind to photoactivated-phosphorylated red/green opsins", "gene_name": "ARR3", "glycan_count": 0, "glycosylation_sites": [], "id": "P36575", "name": "CD103 (\u03b1E integrin)", "organism": "Homo sapiens", "uniprot_id": "P36575" }, { "function": "Cytoplasmic poly(A) RNA polymerase that adds successive AMP monomers to the 3'-end of specific RNAs, forming a poly(A) tail (PubMed:15070731, PubMed:31792053). In contrast to the canonical nuclear poly(A) RNA polymerase, it only adds poly(A) to selected cytoplasmic mRNAs (PubMed:15070731). Does not play a role in replication-dependent histone mRNA degradation (PubMed:18172165). Adds a single nucleotide to the 3' end of specific miRNAs, monoadenylation stabilizes and prolongs the activity of some but not all miRNAs (PubMed:23200856, PubMed:31792053)", "gene_name": "TENT2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q6PIY7", "name": "SERAC1", "organism": "Homo sapiens", "uniprot_id": "Q6PIY7" }, { "function": "Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of a wide variety of acceptor molecules bearing a hydroxyl or an amine group. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Displays broad substrate specificity for small phenolic compounds. Plays an important role in the sulfonation of endogenous molecules such as steroid hormones (PubMed:12471039, PubMed:16221673, PubMed:21723874, PubMed:22069470, PubMed:7834621). Mediates the sulfate conjugation of a variety of xenobiotics, including the drugs acetaminophen and minoxidil (By similarity). Mediates also the metabolic activation of carcinogenic N-hydroxyarylamines leading to highly reactive intermediates capable of forming DNA adducts, potentially resulting in mutagenesis (PubMed:7834621). May play a role in gut microbiota-host metabolic interaction. O-sulfonates 4-ethylphenol (4-EP), a dietary tyrosine-derived metabolite produced by gut bacteria. The product 4-EPS crosses the blood-brain barrier and may negatively regulate oligodendrocyte maturation and myelination, affecting the functional connectivity of different brain regions associated with the limbic system (PubMed:35165440). Catalyzes the sulfate conjugation of dopamine (PubMed:8093002). Catalyzes the sulfation of T4 (L-thyroxine/3,5,3',5'-tetraiodothyronine), T3 (3,5,3'-triiodothyronine), rT3 (3,3',5'-triiodothyronine) and 3,3'-T2 (3,3'-diiodothyronine), with a substrate preference of 3,3'-T2 > rT3 > T3 > T4 (PubMed:10199779)", "gene_name": "SULT1A1", "glycan_count": 1, "glycosylation_sites": [], "id": "P50225", "name": "SULT1A1", "organism": "Homo sapiens", "uniprot_id": "P50225" }, { "function": "Atypical sulfotransferase family member with very low affinity for 3'-phospho-5'-adenylyl sulfate (PAPS) and very low catalytic activity towards L-triiodothyronine, thyroxine, estrone, p-nitrophenol, 2-naphthylamine, and 2-beta-naphthol. May have a role in the metabolism of drugs and neurotransmitters in the CNS", "gene_name": "SULT4A1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9BR01", "name": "SULT1C4", "organism": "Homo sapiens", "uniprot_id": "Q9BR01" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P08684/P20815", "name": "Cytochrome P450 3A4/5 (CYP3A4/5)", "organism": "", "uniprot_id": "" }, { "function": "PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P24294", "name": "Alanine aminotransferase (ALT)", "organism": "Eristicophis macmahoni", "uniprot_id": "P24294" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P07359 (GPIb alpha)", "name": "Glycoprotein Ib-IX-V complex", "organism": "", "uniprot_id": "" }, { "function": "Cadherins are calcium-dependent cell adhesion proteins (PubMed:11976333). They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells (PubMed:11976333). Promotes organization of radial actin fiber structure and cellular response to contractile forces, via its interaction with AMOTL2 which facilitates anchoring of radial actin fibers to CDH1 junction complexes at the cell membrane (By similarity). Plays a role in the early stages of desmosome cell-cell junction formation via facilitating the recruitment of DSG2 and DSP to desmosome plaques (By similarity). Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7 (By similarity)", "gene_name": "Cdh1", "glycan_count": 1, "glycosylation_sites": [ { "position": 282, "type": "O-linked (Man...) serine" }, { "position": 287, "type": "O-linked (Man...) serine" }, { "position": 360, "type": "O-linked (Man...) threonine" }, { "position": 472, "type": "O-linked (Man...) threonine" }, { "position": 474, "type": "O-linked (Man...) threonine" }, { "position": 511, "type": "O-linked (Man...) threonine" }, { "position": 560, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 578, "type": "O-linked (Man...) threonine" }, { "position": 580, "type": "O-linked (Man...) threonine" }, { "position": 582, "type": "O-linked (Man...) threonine" }, { "position": 639, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P09803", "name": "E-cadherin (E-cad)", "organism": "Mus musculus", "uniprot_id": "P09803" }, { "function": "Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome", "gene_name": "rpsK", "glycan_count": 0, "glycosylation_sites": [], "id": "P10789", "name": "Alkaline phosphatase (ALP)", "organism": "Geobacillus stearothermophilus", "uniprot_id": "P10789" }, { "function": "Involved in oxygen transport from the lung to the various peripheral tissues", "gene_name": "HBA", "glycan_count": 0, "glycosylation_sites": [], "id": "P01958", "name": "Hemoglobin", "organism": "Equus caballus", "uniprot_id": "P01958" }, { "function": "Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc (By similarity). Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (By similarity). The shared binding site between zinc and calcium at residue Asp-272 suggests a crosstalk between zinc and calcium transport in the blood (By similarity). The rank order of affinity is zinc > calcium > magnesium (By similarity). Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli (By similarity). Does not prevent iron uptake by the bacterial siderophore aerobactin (By similarity)", "gene_name": "ALB", "glycan_count": 0, "glycosylation_sites": [], "id": "P35747", "name": "Albumin", "organism": "Equus caballus", "uniprot_id": "P35747" }, { "function": "Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1D gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, and by benzothiazepines", "gene_name": "CACNA1D", "glycan_count": 4, "glycosylation_sites": [ { "position": 155, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 225, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 329, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q01668", "name": "Peripheral Myelin Protein 22 (PMP22)", "organism": "Homo sapiens", "uniprot_id": "Q01668" }, { "function": "May play a role in lipid transport protein in Schwann cells. May bind cholesterol", "gene_name": "PMP2", "glycan_count": 0, "glycosylation_sites": [], "id": "P02689", "name": "Myelin Protein P2", "organism": "Homo sapiens", "uniprot_id": "P02689" }, { "function": "Component of N-methyl-D-aspartate (NMDA) receptors (NMDARs) that function as heterotetrameric, ligand-gated cation channels with high calcium permeability and voltage-dependent block by Mg(2+) (PubMed:1350383, PubMed:1388270, PubMed:1834949, PubMed:8428958). NMDARs participate in synaptic plasticity for learning and memory formation by contributing to the long-term potentiation (LTP) (By similarity). Channel activation requires binding of the neurotransmitter L-glutamate to the GluN2 subunit, glycine or D-serine binding to the GluN1 subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+) (PubMed:11823786, PubMed:1350383, PubMed:1388270, PubMed:15996549, PubMed:18177891, PubMed:1834949, PubMed:24876489, PubMed:27135925, PubMed:27618671, PubMed:28384476, PubMed:28468946, PubMed:8428958). NMDARs mediate simultaneously the potasium efflux and the influx of calcium and sodium (By similarity). Each GluN2 or GluN3 subunit confers differential attributes to channel properties, including activation, deactivation and desensitization kinetics, pH sensitivity, Ca2(+) permeability, and binding to allosteric modulators (PubMed:10436042, PubMed:11160393, PubMed:11929923, PubMed:28384476, PubMed:9463421). Forms excitatory glycinergic receptor complexes with GluN3 alone which are activated by glycine binding to the GluN1 and GluN3 subunits (PubMed:11823786, PubMed:11929923, PubMed:12391275)", "gene_name": "Grin1", "glycan_count": 13, "glycosylation_sites": [ { "position": 61, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 203, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 239, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 276, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 300, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 350, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 368, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 440, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 471, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 491, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 674, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 771, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P35439", "name": "NMDA receptor", "organism": "Rattus norvegicus", "uniprot_id": "P35439" }, { "function": "Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase (PubMed:21645528). Positively regulates postnatal regression of retinal hyaloid vessels via suppression of VEGFR2/KDR activity, downstream of OPN5 (By similarity)", "gene_name": "DRD2", "glycan_count": 0, "glycosylation_sites": [ { "position": 5, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 17, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 23, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P14416", "name": "Antipsychotic targets (e.g., dopamine receptor D2)", "organism": "Homo sapiens", "uniprot_id": "P14416" }, { "function": "Serum protease that plays an important role in the activation of the complement system via mannose-binding lectin. After activation by auto-catalytic cleavage it cleaves C2 and C4, leading to their activation and to the formation of C3 convertase", "gene_name": "MASP2", "glycan_count": 1, "glycosylation_sites": [], "id": "O00187", "name": "MASP-2", "organism": "Homo sapiens", "uniprot_id": "O00187" }, { "function": "A positive regulator of the alternate pathway (AP) of complement (PubMed:16301317, PubMed:20382442, PubMed:28264884, PubMed:9748277). It binds to and stabilizes the C3- and C5-convertase enzyme complexes (PubMed:16301317, PubMed:20382442, PubMed:28264884, PubMed:9748277). Inhibits CFI-CFH mediated degradation of Complement C3 beta chain (C3b) (PubMed:31507604)", "gene_name": "CFP", "glycan_count": 4, "glycosylation_sites": [ { "position": 83, "type": "C-linked (Man) tryptophan" }, { "position": 86, "type": "C-linked (Man) tryptophan" }, { "position": 92, "type": "O-linked (Fuc...) threonine" }, { "position": 139, "type": "C-linked (Man) tryptophan" }, { "position": 142, "type": "C-linked (Man) tryptophan" }, { "position": 145, "type": "C-linked (Man) tryptophan" }, { "position": 151, "type": "O-linked (Fuc...) threonine" }, { "position": 196, "type": "C-linked (Man) tryptophan" }, { "position": 199, "type": "C-linked (Man) tryptophan" }, { "position": 202, "type": "C-linked (Man) tryptophan" }, { "position": 208, "type": "O-linked (Fuc...) serine" }, { "position": 260, "type": "C-linked (Man) tryptophan" }, { "position": 263, "type": "C-linked (Man) tryptophan" }, { "position": 272, "type": "O-linked (Fuc...) threonine" }, { "position": 321, "type": "C-linked (Man) tryptophan" }, { "position": 324, "type": "C-linked (Man) tryptophan" }, { "position": 382, "type": "C-linked (Man) tryptophan" }, { "position": 385, "type": "C-linked (Man) tryptophan" }, { "position": 388, "type": "C-linked (Man) tryptophan" }, { "position": 428, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P27918", "name": "Properdin", "organism": "Homo sapiens", "uniprot_id": "P27918" }, { "function": "Thiol protease important for the overall degradation of proteins in lysosomes (Probable). Plays a critical for normal cellular functions such as general protein turnover, antigen processing and bone remodeling. Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen (By similarity). In neuroendocrine chromaffin cells secretory vesicles, catalyzes the prohormone proenkephalin processing to the active enkephalin peptide neurotransmitter (By similarity). In thymus, regulates CD4(+) T cell positive selection by generating the major histocompatibility complex class II (MHCII) bound peptide ligands presented by cortical thymic epithelial cells. Also mediates invariant chain processing in cortical thymic epithelial cells (By similarity). Major elastin-degrading enzyme at neutral pH. Accumulates as a mature and active enzyme in the extracellular space of antigen presenting cells (APCs) to regulate degradation of the extracellular matrix in the course of inflammation (By similarity). Secreted form generates endostatin from COL18A1 (PubMed:10716919). Critical for cardiac morphology and function. Plays an important role in hair follicle morphogenesis and cycling, as well as epidermal differentiation (By similarity). Required for maximal stimulation of steroidogenesis by TIMP1 (By similarity)", "gene_name": "CTSL", "glycan_count": 25, "glycosylation_sites": [ { "position": 221, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P07711", "name": "Cathepsin L", "organism": "Homo sapiens", "uniprot_id": "P07711" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "varies (influenza)", "name": "Hemagglutinin", "organism": "", "uniprot_id": "" }, { "function": "Lipid transporter involved in lipid countertransport between the Golgi complex and membranes of the endoplasmic reticulum: specifically exchanges sterol with phosphatidylinositol 4-phosphate (PI4P), delivering sterol to the Golgi in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the endoplasmic reticulum (PubMed:24209621). Binds cholesterol and a range of oxysterols including 25-hydroxycholesterol (PubMed:15746430, PubMed:17428193). Cholesterol binding promotes the formation of a complex with PP2A and a tyrosine phosphatase which dephosphorylates ERK1/2, whereas 25-hydroxycholesterol causes its disassembly (PubMed:15746430). Regulates cholesterol efflux by decreasing ABCA1 stability (PubMed:18450749)", "gene_name": "OSBP", "glycan_count": 1, "glycosylation_sites": [], "id": "P22059", "name": "OSBP1", "organism": "Homo sapiens", "uniprot_id": "P22059" }, { "function": "Acyl-CoA binding protein which acts as the peroxisome receptor for pexophagy but is dispensable for aggrephagy and nonselective autophagy. Binds medium- and long-chain acyl-CoA esters", "gene_name": "ACBD5", "glycan_count": 2, "glycosylation_sites": [], "id": "Q5T8D3", "name": "ACBD5", "organism": "Homo sapiens", "uniprot_id": "Q5T8D3" }, { "function": "Acts as a Ca(2+) sensor that gates two major inward rectifying Ca(2+) channels at the plasma membrane: Ca(2+) release-activated Ca(2+) (CRAC) channels and arachidonate-regulated Ca(2+)-selective (ARC) channels (PubMed:15866891, PubMed:16005298, PubMed:16208375, PubMed:16537481, PubMed:16733527, PubMed:16766533, PubMed:16807233, PubMed:18854159, PubMed:19182790, PubMed:19249086, PubMed:19622606, PubMed:19706554, PubMed:22464749, PubMed:24069340, PubMed:24351972, PubMed:24591628, PubMed:25326555, PubMed:26322679, PubMed:28219928, PubMed:32415068). Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Upon Ca(2+) depletion, translocates from the endoplasmic reticulum to the plasma membrane where it activates CRAC channel pore-forming subunits ORA1, ORA2 and ORAI3 to generate sustained and oscillatory Ca(2+) entry (PubMed:16208375, PubMed:16537481, PubMed:32415068). Involved in enamel formation (PubMed:24621671)", "gene_name": "STIM1", "glycan_count": 12, "glycosylation_sites": [ { "position": 131, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 171, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13586", "name": "STIM1", "organism": "Homo sapiens", "uniprot_id": "Q13586" }, { "function": "Pore-forming subunit of two major inward rectifying Ca(2+) channels at the plasma membrane: Ca(2+) release-activated Ca(2+) (CRAC) channels and arachidonate-regulated Ca(2+)-selective (ARC) channels (Probable) (PubMed:16645049, PubMed:16733527, PubMed:16807233, PubMed:16921383, PubMed:19249086, PubMed:19706554, PubMed:23307288, PubMed:26956484, PubMed:28219928). Assembles with ORAI2 and ORAI3 to form hexameric CRAC channels that mediate Ca(2+) influx upon depletion of endoplasmic reticulum Ca(2+) store and channel activation by Ca(2+) sensor STIM1, a process known as store-operated Ca(2+) entry (SOCE). Various pore subunit combinations may account for distinct CRAC channel spatiotemporal and cell-type specific dynamics. ORAI1 mainly contributes to the generation of Ca(2+) plateaus involved in sustained Ca(2+) entry and is dispensable for cytosolic Ca(2+) oscillations, whereas ORAI2 and ORAI3 generate oscillatory patterns. CRAC channels assemble in Ca(2+) signaling microdomains where Ca(2+) influx is coupled to calmodulin and calcineurin signaling and activation of NFAT transcription factors recruited to ORAI1 via AKAP5. Activates NFATC2/NFAT1 and NFATC3/NFAT4-mediated transcriptional responses. CRAC channels are the main pathway for Ca(2+) influx in T cells and promote the immune response to pathogens by activating NFAT-dependent cytokine and chemokine transcription (PubMed:16582901, PubMed:17442569, PubMed:19182790, PubMed:20354224, PubMed:22641696, PubMed:26221052, PubMed:32415068, PubMed:33941685). Assembles with ORAI3 to form channels that mediate store-independent Ca(2+) influx in response to inflammatory metabolites arachidonate or its derivative leukotriene C4, termed ARC and LRC channels respectively (PubMed:19622606, PubMed:32415068). Plays a prominent role in Ca(2+) influx at the basolateral membrane of mammary epithelial cells independently of the Ca(2+) content of endoplasmic reticulum or Golgi stores. May mediate transepithelial transport of large quantities of Ca(2+) for milk secretion (By similarity) (PubMed:20887894)", "gene_name": "ORAI1", "glycan_count": 0, "glycosylation_sites": [ { "position": 223, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q96D31", "name": "ORAI1", "organism": "Homo sapiens", "uniprot_id": "Q96D31" }, { "function": "Component of a heteromeric calcium-permeable ion channel formed by PKD1 and PKD2 that is activated by interaction between PKD1 and a Wnt family member, such as WNT3A and WNT9B (PubMed:27214281). Both PKD1 and PKD2 are required for channel activity (PubMed:27214281). Involved in renal tubulogenesis (PubMed:12482949). Involved in fluid-flow mechanosensation by the primary cilium in renal epithelium (By similarity). Acts as a regulator of cilium length, together with PKD2 (By similarity). The dynamic control of cilium length is essential in the regulation of mechanotransductive signaling (By similarity). The cilium length response creates a negative feedback loop whereby fluid shear-mediated deflection of the primary cilium, which decreases intracellular cAMP, leads to cilium shortening and thus decreases flow-induced signaling (By similarity). May be an ion-channel regulator. Involved in adhesive protein-protein and protein-carbohydrate interactions. Likely to be involved with polycystin-1-interacting protein 1 in the detection, sequestration and exocytosis of senescent mitochondria (PubMed:37681898)", "gene_name": "PKD1", "glycan_count": 8, "glycosylation_sites": [ { "position": 50, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 89, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 116, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 121, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 187, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 621, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 632, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 746, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 810, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 841, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 854, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 890, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 921, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1004, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1010, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1034, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1072, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1113, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1178, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1194, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1240, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1269, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1336, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1348, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1382, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1450, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1455, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1474, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1518, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1541, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1554, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1563, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1647, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1661, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1733, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1791, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1834, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1867, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1880, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1991, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2050, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2074, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2125, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2248, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2353, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2395, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2412, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2567, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2578, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2645, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2718, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2754, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2841, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2878, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2925, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2956, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2994, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3738, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3790, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3845, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P98161", "name": "Polycystin-1 (PC-1)", "organism": "Homo sapiens", "uniprot_id": "P98161" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "OLR1_HUMAN (P78380)", "name": "LOX-1", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "TLR4_HUMAN (O00206)", "name": "TLR4", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "PCSK9_HUMAN (Q8NBP7)", "name": "PCSK9", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "HMGB1_HUMAN (P09429)", "name": "HMGB1", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "LDLR_HUMAN (P01130)", "name": "LDLR", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "CD36_HUMAN (P16671)", "name": "CD36", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "MSR1_HUMAN (Q13291)", "name": "SR-A", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "ICAM1_HUMAN (P05362)", "name": "ICAM-1", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "VCAM1_HUMAN (P19320)", "name": "VCAM-1", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "SELE_HUMAN (P16581)", "name": "E-selectin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01009 (E342K variant)", "name": "Mutant Z-AAT", "organism": "", "uniprot_id": "" }, { "function": "Multifunctional adapter protein involved in diverse array of functions including trafficking of transmembrane proteins, neuro and immunomodulation, exosome biogenesis, and tumorigenesis (PubMed:26291527). Positively regulates TGFB1-mediated SMAD2/3 activation and TGFB1-induced epithelial-to-mesenchymal transition (EMT) and cell migration in various cell types. May increase TGFB1 signaling by enhancing cell-surface expression of TGFR1 by preventing the interaction between TGFR1 and CAV1 and subsequent CAV1-dependent internalization and degradation of TGFR1 (PubMed:25893292). In concert with SDC1/4 and PDCD6IP, regulates exosome biogenesis (PubMed:22660413). Regulates migration, growth, proliferation, and cell cycle progression in a variety of cancer types (PubMed:26539120). In adherens junctions may function to couple syndecans to cytoskeletal proteins or signaling components. Seems to couple transcription factor SOX4 to the IL-5 receptor (IL5RA) (PubMed:11498591). May also play a role in vesicular trafficking (PubMed:11179419). Seems to be required for the targeting of TGFA to the cell surface in the early secretory pathway (PubMed:10230395)", "gene_name": "SDCBP", "glycan_count": 1, "glycosylation_sites": [], "id": "O00560", "name": "NUP153", "organism": "Homo sapiens", "uniprot_id": "O00560" }, { "function": "Involved in poly(A)+ RNA transport. Involved in nephrogenesis (PubMed:30179222)", "gene_name": "NUP133", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8WUM0", "name": "NUP133", "organism": "Homo sapiens", "uniprot_id": "Q8WUM0" }, { "function": "Substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:15601820, PubMed:21199876). Negatively regulates nitric oxide (NO) production and limits cellular toxicity in activated macrophages by mediating the ubiquitination and proteasomal degradation of NOS2 (PubMed:21199876). Acts as a bridge which links NOS2 with the ECS E3 ubiquitin ligase complex components ELOC and CUL5 (PubMed:21199876)", "gene_name": "SPSB2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q99619", "name": "NUP155", "organism": "Homo sapiens", "uniprot_id": "Q99619" }, { "function": "Interferon-induced dynamin-like GTPase with potent antiviral activity against human immunodeficiency virus type 1 (HIV-1). Acts by targeting the viral capsid and affects the nuclear uptake and/or stability of the HIV-1 replication complex and the subsequent chromosomal integration of the proviral DNA. Exhibits antiviral activity also against simian immunodeficiency virus (SIV-mnd). May play a role in regulating nucleocytoplasmic transport and cell-cycle progression", "gene_name": "MX2", "glycan_count": 0, "glycosylation_sites": [], "id": "P20592", "name": "MX2", "organism": "Homo sapiens", "uniprot_id": "P20592" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "various (main: APOB P04114)", "name": "Low-density lipoprotein (LDL)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "Abo", "glycan_count": 0, "glycosylation_sites": [ { "position": 92, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9EQW3", "name": "Siglec-F", "organism": "Mus musculus", "uniprot_id": "P38649" }, { "function": "Plays a role in growth cones guidance. May function to pattern sensory projections by selectively repelling axons that normally terminate dorsally. Involved in the development of the olfactory system and in neuronal control of puberty (By similarity)", "gene_name": "Sema3a", "glycan_count": 1, "glycosylation_sites": [ { "position": 53, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 125, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 591, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O08665", "name": "Thrombopoietin (TPO)", "organism": "Mus musculus", "uniprot_id": "O08665" }, { "function": "Receptor for the chemokine CCL1/SCYA1/I-309. May regulate monocyte chemotaxis and thymic cell line apoptosis. Alternative coreceptor with CD4 for HIV-1 infection", "gene_name": "CCR8", "glycan_count": 0, "glycosylation_sites": [], "id": "P51685", "name": "CCR8", "organism": "Homo sapiens", "uniprot_id": "P51685" }, { "function": "", "gene_name": "HBB", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6V0K9", "name": "CD36", "organism": "Homo sapiens", "uniprot_id": "Q6V0K9" }, { "function": "Catalytic subunit of the NuA4 histone acetyltransferase complex, a multiprotein complex involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H2A and H4 (PubMed:12776177, PubMed:14966270, PubMed:15042092, PubMed:15121871, PubMed:15310756, PubMed:16387653, PubMed:19909775, PubMed:25865756, PubMed:27153538, PubMed:29174981, PubMed:29335245, PubMed:32822602, PubMed:33076429). Histone acetylation alters nucleosome-DNA interactions and promotes interaction of the modified histones with other proteins which positively regulate transcription (PubMed:12776177, PubMed:14966270, PubMed:15042092, PubMed:15121871, PubMed:15310756). The NuA4 histone acetyltransferase complex is required for the activation of transcriptional programs associated with proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair (PubMed:17709392, PubMed:19783983, PubMed:32832608). The NuA4 complex plays a direct role in repair of DNA double-strand breaks (DSBs) by promoting homologous recombination (HR): the complex inhibits TP53BP1 binding to chromatin via MBTD1, which recognizes and binds histone H4 trimethylated at 'Lys-20' (H4K20me), and KAT5 that catalyzes acetylation of 'Lys-15' of histone H2A (H2AK15ac), thereby blocking the ubiquitination mark required for TP53BP1 localization at DNA breaks (PubMed:27153538, PubMed:32832608). Also involved in DSB repair by mediating acetylation of 'Lys-5' of histone H2AX (H2AXK5ac), promoting NBN/NBS1 assembly at the sites of DNA damage (PubMed:17709392, PubMed:26438602). The NuA4 complex plays a key role in hematopoietic stem cell maintenance and is required to maintain acetylated H2A.Z/H2AZ1 at MYC target genes (By similarity). The NuA4 complex is also required for spermatid development by promoting acetylation of histones: histone hyperacetylation is required for histone replacement during the transition from round to elongating spermatids (By similarity). Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AZ1 from the nucleosome (PubMed:24463511). Also acetylates non-histone proteins, such as BMAL1, ATM, AURKB, CHKA, CGAS, ERCC4/XPF, LPIN1, TP53/p53, NDC80/HEC1, NR1D2, RAN, SOX4, FOXP3, SQSTM1, ULK1 and RUBCNL/Pacer (PubMed:16141325, PubMed:17189187, PubMed:17360565, PubMed:17996965, PubMed:24835996, PubMed:26829474, PubMed:29040603, PubMed:30409912, PubMed:30704899, PubMed:31857589, PubMed:32034146, PubMed:32817552, PubMed:34077757). Directly acetylates and activates ATM (PubMed:16141325). Promotes nucleotide excision repair (NER) by mediating acetylation of ERCC4/XPF, thereby promoting formation of the ERCC4-ERCC1 complex (PubMed:32034146). Relieves NR1D2-mediated inhibition of APOC3 expression by acetylating NR1D2 (PubMed:17996965). Acts as a regulator of regulatory T-cells (Treg) by catalyzing FOXP3 acetylation, thereby promoting FOXP3 transcriptional repressor activity (PubMed:17360565, PubMed:24835996). Involved in skeletal myoblast differentiation by mediating acetylation of SOX4 (PubMed:26291311). Catalyzes acetylation of APBB1/FE65, increasing its transcription activator activity (PubMed:33938178). Promotes transcription elongation during the activation phase of the circadian cycle by catalyzing acetylation of BMAL1, promoting elongation of circadian transcripts (By similarity). Together with GSK3 (GSK3A or GSK3B), acts as a regulator of autophagy: phosphorylated at Ser-86 by GSK3 under starvation conditions, leading to activate acetyltransferase activity and promote acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer (PubMed:30704899). Acts as a regulator of the cGAS-STING innate antiviral response by catalyzing acetylation the N-terminus of CGAS, thereby promoting CGAS DNA-binding and activation (PubMed:32817552). Also regulates lipid metabolism by mediating acetylation of CHKA or LPIN1 (PubMed:34077757). Promotes lipolysis of lipid droplets following glucose deprivation by mediating acetylation of isoform 1 of CHKA, thereby promoting monomerization of CHKA and its conversion into a tyrosine-protein kinase (PubMed:34077757). Acts as a regulator of fatty-acid-induced triacylglycerol synthesis by catalyzing acetylation of LPIN1, thereby promoting the synthesis of diacylglycerol (PubMed:29765047). In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as (2E)-butenoyl-CoA (crotonyl-CoA), S-lactoyl-CoA (lactyl-CoA) and 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA), and is able to mediate protein crotonylation, lactylation and 2-hydroxyisobutyrylation, respectively (PubMed:29192674, PubMed:34608293, PubMed:38961290). Acts as a key regulator of chromosome segregation and kinetochore-microtubule attachment during mitosis by mediating acetylation or crotonylation of target proteins (PubMed:26829474, PubMed:29040603, PubMed:30409912, PubMed:34608293). Catalyzes acetylation of AURKB at kinetochores, increasing AURKB activity and promoting accurate chromosome segregation in mitosis (PubMed:26829474). Acetylates RAN during mitosis, promoting microtubule assembly at mitotic chromosomes (PubMed:29040603). Acetylates NDC80/HEC1 during mitosis, promoting robust kinetochore-microtubule attachment (PubMed:30409912). Catalyzes crotonylation of MAPRE1/EB1, thereby ensuring accurate spindle positioning in mitosis (PubMed:34608293). Catalyzes lactylation of NBN/NBS1 in response to DNA damage, thereby promoting DNA double-strand breaks (DSBs) via homologous recombination (HR) (PubMed:38961290)", "gene_name": "KAT5", "glycan_count": 0, "glycosylation_sites": [], "id": "Q92993", "name": "TIP60", "organism": "Homo sapiens", "uniprot_id": "Q92993" }, { "function": "Proto-oncogene that may play a role in differentiation and lymphopoiesis. NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. The NF-kappa-B heterodimer RELA/p65-c-Rel is a transcriptional activator", "gene_name": "REL", "glycan_count": 2, "glycosylation_sites": [], "id": "Q04864", "name": "c-Rel", "organism": "Homo sapiens", "uniprot_id": "Q04864" }, { "function": "Component of the membrane attack complex (MAC), a multiprotein complex activated by the complement cascade, which inserts into a target cell membrane and forms a pore, leading to target cell membrane rupture and cell lysis (PubMed:26841837, PubMed:27052168, PubMed:30552328). The MAC is initiated by proteolytic cleavage of C5 into complement C5b in response to the classical, alternative, lectin and GZMK complement pathways (PubMed:30552328). The complement pathways consist in a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system (PubMed:30552328). C8G, together with C8A and C8B, inserts into the target membrane, but does not form pores by itself (PubMed:30552328). During MAC assembly, associates with C5b, C6 and C7 to form the C5b8 intermediate complex that inserts into the target membrane and traverses the bilayer increasing membrane rigidity (PubMed:30552328, PubMed:6833260)", "gene_name": "C8G", "glycan_count": 0, "glycosylation_sites": [], "id": "P07360", "name": "Complement component C8 gamma chain", "organism": "Homo sapiens", "uniprot_id": "P07360" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P35439 (NR1 subunit)", "name": "N-methyl D-aspartate receptor (NMDAR)", "organism": "", "uniprot_id": "" }, { "function": "Presents phospholipase and nuclease activities, depending on the different physiological conditions (PubMed:17028579, PubMed:21397847, PubMed:28063496). Interaction with Mitoguardin (MIGA1 or MIGA2) affects the dimer conformation, facilitating the lipase activity over the nuclease activity (PubMed:26711011). Plays a key role in mitochondrial fusion and fission via its phospholipase activity (PubMed:17028579, PubMed:24599962, PubMed:26678338). In its phospholipase role, it uses the mitochondrial lipid cardiolipin as substrate to generate phosphatidate (PA or 1,2-diacyl-sn-glycero-3-phosphate), a second messenger signaling lipid (PubMed:17028579, PubMed:26711011). Production of PA facilitates Mitofusin-mediated fusion, whereas the cleavage of PA by the Lipin family of phosphatases produces diacylgycerol (DAG) which promotes mitochondrial fission (PubMed:24599962). Both Lipin and DAG regulate mitochondrial dynamics and membrane fusion/fission, important processes for adapting mitochondrial metabolism to changes in cell physiology. Mitochondrial fusion enables cells to cope with the increased nucleotide demand during DNA synthesis (PubMed:26678338). Mitochondrial function and dynamics are closely associated with biological processes such as cell growth, proliferation, and differentiation (PubMed:21397848). Mediator of MYC activity, promotes mitochondrial fusion and activates AMPK which in turn inhibits YAP/TAZ, thereby inducing cell growth and proliferation (PubMed:26678338). The endonuclease activity plays a critical role in PIWI-interacting RNA (piRNA) biogenesis during spermatogenesis (PubMed:21397847, PubMed:21397848). Implicated in spermatogenesis and sperm fertility in testicular germ cells, its single strand-specific nuclease activity is critical for the biogenesis/maturation of PIWI-interacting RNA (piRNA). MOV10L1 selectively binds to piRNA precursors and funnels them to the endonuclease that catalyzes the first cleavage step of piRNA processing to generate piRNA intermediate fragments that are subsequently loaded to Piwi proteins. Cleaves either DNA or RNA substrates with similar affinity, producing a 5' phosphate end, in this way it participates in the processing of primary piRNA transcripts. piRNAs provide essential protection against the activity of mobile genetic elements. piRNA-mediated transposon silencing is thus critical for maintaining genome stability, in particular in germline cells when transposons are mobilized as a consequence of wide-spread genomic demethylation (By similarity). PA may act as signaling molecule in the recognition/transport of the precursor RNAs of primary piRNAs (PubMed:21397847). Interacts with tesmin in testes, suggesting a role in spermatogenesis via association with its interacting partner (By similarity)", "gene_name": "PLD6", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8N2A8", "name": "IgLON family member 5 (IgLON5)", "organism": "Homo sapiens", "uniprot_id": "Q8N2A8" }, { "function": "Functional component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors (PubMed:14966521, PubMed:15694321). Is also an important negative regulator of oligodentrocyte differentiation and axonal myelination (PubMed:15895088). Acts in conjunction with RTN4 and RTN4R in regulating neuronal precursor cell motility during cortical development (By similarity)", "gene_name": "LINGO1", "glycan_count": 3, "glycosylation_sites": [ { "position": 144, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 202, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 264, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 274, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 293, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 341, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 492, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 505, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 526, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 542, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q96FE5", "name": "Leucine-rich glioma inactivated 1 (LGI1)", "organism": "Homo sapiens", "uniprot_id": "Q96FE5" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P42261 (GluA1)", "name": "Alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR)", "organism": "", "uniprot_id": "" }, { "function": "G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling activates a phosphatidylinositol-calcium second messenger system and generates a calcium-activated chloride current. Plays an important role in the regulation of synaptic plasticity and the modulation of the neural network activity", "gene_name": "GRM5", "glycan_count": 3, "glycosylation_sites": [ { "position": 88, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 210, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 378, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 382, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 445, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 734, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P41594", "name": "Metabotropic glutamate receptor 5 (mGluR5)", "organism": "Homo sapiens", "uniprot_id": "P41594" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P07359 (GP1BA), P14770 (GP1BB), P17927 (GP9)", "name": "GPIb-V-IX complex", "organism": "", "uniprot_id": "" }, { "function": "May play a role in the regulation of hemostasis. The soluble form may have inhibitory properties towards coagulation factors. May interact with cellular G-protein signaling pathways. May bind to the DNA 5'-GTCACATG-3'(CDEI box). Inhibits trypsin, chymotrypsin, plasmin, factor XIA and plasma and glandular kallikrein. Modulates the Cu/Zn nitric oxide-catalyzed autodegradation of GPC1 heparan sulfate side chains in fibroblasts (By similarity)", "gene_name": "APLP2", "glycan_count": 24, "glycosylation_sites": [ { "position": 626, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" } ], "id": "Q06481", "name": "APLP2", "organism": "Homo sapiens", "uniprot_id": "Q06481" }, { "function": "RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation (By similarity). Preferentially binds to N6-methyladenosine (m6A)-containing mRNAs and increases their stability (PubMed:29476152). Binds to the 5'-UTR of the insulin-like growth factor 2 (IGF2) mRNAs (PubMed:9891060). Binding is isoform-specific. Binds to beta-actin/ACTB and MYC transcripts. Increases MYC mRNA stability by binding to the coding region instability determinant (CRD) and binding is enhanced by m6A-modification of the CRD (PubMed:29476152)", "gene_name": "IGF2BP2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y6M1", "name": "IGF2BP2", "organism": "Homo sapiens", "uniprot_id": "Q9Y6M1" }, { "function": "Pyridoxal 5'-phosphate (PLP)-binding protein, which may be involved in intracellular homeostatic regulation of pyridoxal 5'-phosphate (PLP), the active form of vitamin B6", "gene_name": "PLPBP", "glycan_count": 1, "glycosylation_sites": [], "id": "O94903", "name": "APLP1", "organism": "Homo sapiens", "uniprot_id": "O94903" }, { "function": "Receptor subunit for interferon gamma/INFG that plays crucial roles in antimicrobial, antiviral, and antitumor responses by activating effector immune cells and enhancing antigen presentation (PubMed:20015550). Associates with transmembrane accessory factor IFNGR2 to form a functional receptor (PubMed:10986460, PubMed:2971451, PubMed:7615558, PubMed:7617032, PubMed:7673114). Upon ligand binding, the intracellular domain of IFNGR1 opens out to allow association of downstream signaling components JAK1 and JAK2. In turn, activated JAK1 phosphorylates IFNGR1 to form a docking site for STAT1. Subsequent phosphorylation of STAT1 leads to dimerization, translocation to the nucleus, and stimulation of target gene transcription (PubMed:28883123). STAT3 can also be activated in a similar manner although activation seems weaker. IFNGR1 intracellular domain phosphorylation also provides a docking site for SOCS1 that regulates the JAK-STAT pathway by competing with STAT1 binding to IFNGR1 (By similarity)", "gene_name": "IFNGR1", "glycan_count": 13, "glycosylation_sites": [ { "position": 34, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 79, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 86, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 179, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 240, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P15260", "name": "IFNGR1", "organism": "Homo sapiens", "uniprot_id": "P15260" }, { "function": "", "gene_name": "KRT15", "glycan_count": 0, "glycosylation_sites": [], "id": "P19012", "name": "K15 (Keratin 15)", "organism": "Homo sapiens", "uniprot_id": "P19012" }, { "function": "Is a positive regulator of nascent focal adhesion assembly, involved in the modulation of endothelial cell attachment to the extracellular matrix", "gene_name": "THSD1", "glycan_count": 2, "glycosylation_sites": [ { "position": 39, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 53, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 58, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 69, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 80, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 135, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 304, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NS62", "name": "Lhx2", "organism": "Homo sapiens", "uniprot_id": "Q9NS62" }, { "function": "Inhibitor of the Wnt signaling pathway. Down-regulates beta-catenin. Probably facilitate the phosphorylation of beta-catenin and APC by GSK3B", "gene_name": "AXIN2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y2T1", "name": "Axin2", "organism": "Homo sapiens", "uniprot_id": "Q9Y2T1" }, { "function": "Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2 or IL-4 gene transcription. Also controls gene expression in embryonic cardiac cells. Could regulate not only the activation and proliferation but also the differentiation and programmed death of T-lymphocytes as well as lymphoid and non-lymphoid cells (PubMed:10358178). Required for osteoclastogenesis and regulates many genes important for osteoclast differentiation and function (By similarity)", "gene_name": "NFATC1", "glycan_count": 1, "glycosylation_sites": [], "id": "O95644", "name": "Nfatc1", "organism": "Homo sapiens", "uniprot_id": "O95644" }, { "function": "Regulatory subunit of multiple voltage-gated sodium (Nav) channels directly mediating the depolarization of excitable membranes. Navs, also called VGSCs (voltage-gated sodium channels) or VDSCs (voltage-dependent sodium channels), operate by switching between closed and open conformations depending on the voltage difference across the membrane. In the open conformation they allow Na(+) ions to selectively pass through the pore, along their electrochemical gradient. The influx of Na+ ions provokes membrane depolarization, initiating the propagation of electrical signals throughout cells and tissues. The accessory beta subunits participate in localization and functional modulation of the Nav channels (PubMed:20558140, PubMed:21051419). Modulates the activity of SCN2A/Nav1.2, causing a hyperpolarizing shift in the voltage-dependence of inactivation of the channel and increasing the fraction of channels operating in the fast gating mode (By similarity). Modulates the activity of SCN5A/Nav1.5 (PubMed:20558140, PubMed:21051419, PubMed:24567321, PubMed:31950564). Could also regulate the atypical sodium channel SCN7A/Nav2.1 (PubMed:35301303). Modulates the activity of SCN10A/Nav1.8, regulating its oligomerization and accelerating the recovery from inactivation (PubMed:14975698)", "gene_name": "SCN3B", "glycan_count": 0, "glycosylation_sites": [ { "position": 95, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 109, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 113, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 121, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NY72", "name": "Nav\u03b23 (SCN3B)", "organism": "Homo sapiens", "uniprot_id": "Q9NY72" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P00533 (EGFR)", "name": "EGFRvIII", "organism": "", "uniprot_id": "" }, { "function": "Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties", "gene_name": "GPH1", "glycan_count": 0, "glycosylation_sites": [], "id": "P06738", "name": "Cluster of Differentiation 11b (CD11b)", "organism": "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "uniprot_id": "P06738" }, { "function": "Transmembrane serine/threonine kinase activin type-2 receptor forming an activin receptor complex with activin type-1 serine/threonine kinase receptors (ACVR1, ACVR1B or ACVR1c). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, the type-2 receptors act as a primary activin receptors (binds activin-A/INHBA, activin-B/INHBB as well as inhibin-A/INHA-INHBA). The type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine-threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor. Once activated, the type-1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal tail. Soon after their association with the activin receptor and subsequent phosphorylation, SMAD2 and SMAD3 are released into the cytoplasm where they interact with the common partner SMAD4. This SMAD complex translocates into the nucleus where it mediates activin-induced transcription. Inhibitory SMAD7, which is recruited to ACVR1B through FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. Activin signal transduction is also antagonized by the binding to the receptor of inhibin-B via the IGSF1 inhibin coreceptor", "gene_name": "ACVR2B", "glycan_count": 1, "glycosylation_sites": [ { "position": 42, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 65, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13705", "name": "ACVR2B", "organism": "Homo sapiens", "uniprot_id": "Q13705" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q13067", "name": "GAGE1", "organism": "", "uniprot_id": "Q13067" }, { "function": "Nuclear lamina-associated inner nuclear membrane protein that is involved in nuclear structure organization, maintenance of nuclear envelope (NE) integrity and NE reformation after mitosis (PubMed:16339967, PubMed:17097643, PubMed:28242692, PubMed:32494070). Plays a role as transmembrane adapter for the endosomal sorting complexes required for transport (ESCRT), and is thereby involved in ESCRT-mediated NE reformation (PubMed:28242692, PubMed:32494070). Promotes ESCRT-mediated NE closure by recruiting CHMP7 and downstream ESCRT-III proteins IST1/CHMP8 and CHMP2A to the reforming NE during anaphase (PubMed:28242692). During nuclear reassembly, condenses into a liquid-like coating around microtubule spindles and coassembles with CHMP7 to form a macromolecular O-ring seal at the confluence between membranes, chromatin, and the spindle to facilitate early nuclear sealing (PubMed:32494070). Plays a role in the organization of heterochromatin associated with the NE and in the maintenance of NE organization under mechanical stress (By similarity). Required for embryonic development and involved in regulation of several signaling pathways such as MAPK and AKT (By similarity). Required for myoblast differentiation involving regulation of ERK signaling (By similarity). Essential for cardiac homeostasis and proper heart function (By similarity)", "gene_name": "LEMD2", "glycan_count": 10, "glycosylation_sites": [], "id": "Q8NC56", "name": "LEMD1", "organism": "Homo sapiens", "uniprot_id": "Q8NC56" }, { "function": "Proposed to enhance ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases. In vitro enhances ubiquitin ligase activity of TRIM28 and stimulates p53/TP53 ubiquitination in presence of Ubl-conjugating enzyme UBE2H leading to p53/TP53 degradation. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzymes (E2) at the E3:substrate complex", "gene_name": "MAGEC2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UBF1", "name": "MAGEB1", "organism": "Homo sapiens", "uniprot_id": "Q9UBF1" }, { "function": "Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (By similarity). Involved in normal vectorial acid transport into the urine by the kidney (PubMed:10973252, PubMed:12414817)", "gene_name": "ATP6V0A4", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9HBG4", "name": "PAGE1", "organism": "Homo sapiens", "uniprot_id": "Q9HBG4" }, { "function": "Required during ciliogenesis for tubulin glutamylation in cilium. Probably acts by participating in the transport of TTLL6, a tubulin polyglutamylase, between the basal body and the cilium", "gene_name": "CEP41", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9BYV8", "name": "MAGEA10", "organism": "Homo sapiens", "uniprot_id": "Q9BYV8" }, { "function": "", "gene_name": "TCP11L1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NUJ3", "name": "PLEKHA5", "organism": "Homo sapiens", "uniprot_id": "Q9NUJ3" }, { "function": "Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence of ligand, acts mainly as an activator of gene expression due to weak binding to corepressors. Required for limb bud development. In concert with RARA or RARB, required for skeletal growth, matrix homeostasis and growth plate function (By similarity)", "gene_name": "RARG", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9BYX8", "name": "XAGE3aV1", "organism": "Homo sapiens", "uniprot_id": "P13631" }, { "function": "Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Binds to receptor tyrosine kinase including EPHA4, EPHA3 and EPHB4. Together with EPHB4 plays a central role in heart morphogenesis and angiogenesis through regulation of cell adhesion and cell migration. EPHB4-mediated forward signaling controls cellular repulsion and segregation from EFNB2-expressing cells. May play a role in constraining the orientation of longitudinally projecting axons", "gene_name": "EFNB2", "glycan_count": 17, "glycosylation_sites": [ { "position": 36, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 139, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P52799", "name": "EFNB2", "organism": "Homo sapiens", "uniprot_id": "P52799" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P13232-fusion", "name": "IL-7-hyFc (efineptakin alfa)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P0DTC2-2", "name": "Receptor Binding Domain (RBD) of Spike Protein", "organism": "", "uniprot_id": "" }, { "function": "Protects cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione", "gene_name": "GPX3", "glycan_count": 0, "glycosylation_sites": [], "id": "P22352", "name": "GPX3", "organism": "Homo sapiens", "uniprot_id": "P22352" }, { "function": "Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids", "gene_name": "MT1G", "glycan_count": 10, "glycosylation_sites": [], "id": "P13640", "name": "Metallothionein 1G (MT1G)", "organism": "Homo sapiens", "uniprot_id": "P13640" }, { "function": "A NAD(P)H-dependent oxidoreductase that acts as a key inhibitor of ferroptosis (PubMed:31634899, PubMed:31634900, PubMed:35922516, PubMed:39881208). At the plasma membrane, catalyzes reduction of coenzyme Q/ubiquinone-10 to ubiquinol-10, a lipophilic radical-trapping antioxidant that prevents lipid oxidative damage and consequently ferroptosis (PubMed:31634899, PubMed:31634900). Acts in parallel to GPX4 to suppress phospholipid peroxidation and ferroptosis (PubMed:31634899, PubMed:31634900). This anti-ferroptotic function is independent of cellular glutathione levels (PubMed:31634899, PubMed:31634900). Also acts as a potent radical-trapping antioxidant by mediating warfarin-resistant vitamin K reduction in the canonical vitamin K cycle: catalyzes NAD(P)H-dependent reduction of vitamin K (phylloquinone, menaquinone-4 and menadione) to hydroquinone forms (PubMed:35922516). Hydroquinones act as potent radical-trapping antioxidants inhibitor of phospholipid peroxidation and ferroptosis (PubMed:35922516). May play a role in mitochondrial stress signaling (PubMed:26689472). Upon oxidative stress, associates with the lipid peroxidation end product 4-hydroxy-2-nonenal (HNE) forming a lipid adduct devoid of oxidoreductase activity, which then translocates from mitochondria into the nucleus triggering DNA damage and cell death (PubMed:26689472). Capable of DNA binding in a non-sequence specific way (PubMed:15958387)", "gene_name": "AIFM2", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9BRQ8", "name": "AIFM2/FSP1", "organism": "Homo sapiens", "uniprot_id": "Q9BRQ8" }, { "function": "Specifically binds unfolded proteins and may recruit protein disulfide isomerase PDIA3 to unfolded substrates (PubMed:16940051, PubMed:23192347). Binds protein substrates via a hydrophobic pocket in the C-terminal domain (PubMed:16940051, PubMed:23192347). May play a role in the unfolded stress response (PubMed:23192347)", "gene_name": "ERP27", "glycan_count": 0, "glycosylation_sites": [ { "position": 100, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q96DN0", "name": "TXNDC12", "organism": "Homo sapiens", "uniprot_id": "Q96DN0" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01236 (human)", "name": "Prolactin (PRL)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01282 (human)", "name": "Vasoactive Intestinal Peptide (VIP)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P49763 (human)", "name": "Placental Growth Factor (PGF)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01225 (human)", "name": "Follicle Stimulating Hormone subunit beta (FSHB)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01133 (human)", "name": "Epidermal Growth Factor (EGF)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01215 (human)", "name": "Glycoprotein hormones, alpha polypeptide (CGA)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01189 (human)", "name": "Proopiomelanocortin (POMC)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P07492 (human)", "name": "Gastrin-releasing peptide (GRP)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01303 (human)", "name": "Neuropeptide Y (NPY)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01019 (human)", "name": "Angiotensinogen (AGT)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8I7T7", "name": "gp63 (Leishmania surface glycoprotein)", "organism": "Podocoryna carnea", "uniprot_id": "Q8I7T7" }, { "function": "Catalyzes the hydrolysis of both di- and triphosphate nucleotides (NDPs and NTPs) and hydrolyze NTPs to nucleotide monophosphates (NMPs) in two distinct successive phosphate-releasing steps, with NDPs as intermediates and participates in the regulation of extracellular levels of nucleotides (Probable) (PubMed:8529670, PubMed:8626624, PubMed:8955160, PubMed:8996251). By hydrolyzing proinflammatory ATP and platelet-activating ADP to AMP, it blocks platelet aggregation and supports blood flow (PubMed:8955160, PubMed:8996251)", "gene_name": "ENTPD1", "glycan_count": 30, "glycosylation_sites": [ { "position": 73, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 227, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 292, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 334, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 371, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 457, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P49961", "name": "CD39", "organism": "Homo sapiens", "uniprot_id": "P49961" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P45373", "name": "CD73", "organism": "Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D)", "uniprot_id": "P45373" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P08107 (human homolog)", "name": "Heat Shock Protein 70 (HSP70)", "organism": "", "uniprot_id": "" }, { "function": "Flippase that catalyzes in an ATP-dependent manner the transport of retinal-phosphatidylethanolamine conjugates like 11-cis and all-trans isomers of N-retinylidene-phosphatidylethanolamine (N-Ret-PE) from the lumen to the cytoplasmic leaflet of photoreceptor outer segment disk membranes, where 11-cis-retinylidene-phosphatidylethanolamine is then isomerized to its all-trans isomer and reduced by RDH8 to produce all-trans-retinol. This transport activity ensures that all-trans-retinal generated from photoexcitation and 11-cis-retinal not needed for the regeneration of rhodopsin and cone opsins are effectively cleared from the photoreceptors, therefore preventing their accumulation and the formation of toxic bisretinoid (PubMed:10075733, PubMed:20404325, PubMed:22735453, PubMed:23144455, PubMed:24097981, PubMed:29847635, PubMed:33375396). Displays ATPase activity in vitro in absence of retinal substrate (PubMed:33605212, PubMed:39128720, PubMed:29847635, PubMed:33375396). May display GTPase activity that is strongly influenced by the lipid environment and the presence of retinoid compounds (PubMed:22735453). Binds the unprotonated form of N-retinylidene-phosphatidylethanolamine with high affinity in the absence of ATP, and ATP binding and hydrolysis induce a protein conformational change that causes N-retinylidene-phosphatidylethanolamine release (By similarity)", "gene_name": "ABCA4", "glycan_count": 2, "glycosylation_sites": [ { "position": 98, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 415, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 444, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 504, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1469, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1529, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1588, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1662, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P78363", "name": "ABCA4", "organism": "Homo sapiens", "uniprot_id": "P78363" }, { "function": "Transfers the acyl group from the sn-1 position of phosphatidylcholine to all-trans retinol, producing all-trans retinyl esters (PubMed:9920938). Retinyl esters are storage forms of vitamin A (Probable). LRAT plays a critical role in vision (Probable). It provides the all-trans retinyl ester substrates for the isomerohydrolase which processes the esters into 11-cis-retinol in the retinal pigment epithelium; due to a membrane-associated alcohol dehydrogenase, 11 cis-retinol is oxidized and converted into 11-cis-retinaldehyde which is the chromophore for rhodopsin and the cone photopigments (Probable). Required for the survival of cone photoreceptors and correct rod photoreceptor cell morphology (By similarity)", "gene_name": "LRAT", "glycan_count": 0, "glycosylation_sites": [], "id": "O95237", "name": "LRAT", "organism": "Homo sapiens", "uniprot_id": "O95237" }, { "function": "Plays a role in photoreceptor morphogenesis in the retina (By similarity). May maintain cell polarization and adhesion (By similarity)", "gene_name": "CRB1", "glycan_count": 1, "glycosylation_sites": [ { "position": 30, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 41, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 42, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 215, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 287, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 313, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 322, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 418, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 427, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 453, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 550, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 561, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 657, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 757, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 871, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 880, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 968, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 975, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1000, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1190, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1243, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1265, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1273, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P82279", "name": "CRB1", "organism": "Homo sapiens", "uniprot_id": "P82279" }, { "function": "Low affinity receptor for N-formyl-methionyl peptides, which are powerful neutrophil chemotactic factors (PubMed:1374236). Binding of FMLP to the receptor causes activation of neutrophils (PubMed:1374236). This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system (PubMed:1374236). The activation of LXA4R could result in an anti-inflammatory outcome counteracting the actions of pro-inflammatory signals such as LTB4 (leukotriene B4) (PubMed:9547339). Receptor for the chemokine-like protein FAM19A5, mediating FAM19A5-stimulated macrophage chemotaxis and the inhibitory effect on TNFSF11/RANKL-induced osteoclast differentiation (By similarity). Acts as a receptor for humanin (PubMed:15465011)", "gene_name": "FPR2", "glycan_count": 0, "glycosylation_sites": [ { "position": 4, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P25090", "name": "Formyl peptide receptor 2 (FPR2)", "organism": "Homo sapiens", "uniprot_id": "P25090" }, { "function": "Potent stimulator of insulin secretion and relatively poor inhibitor of gastric acid secretion", "gene_name": "GIP", "glycan_count": 0, "glycosylation_sites": [], "id": "P09681", "name": "GIP (Gastric inhibitory polypeptide)", "organism": "Homo sapiens", "uniprot_id": "P09681" }, { "function": "Promotes formation and maturation of oligodendrocytes, especially within the brain. Cooperates with OLIG2 to establish the pMN domain of the embryonic neural tube (By similarity)", "gene_name": "OLIG1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8TAK6", "name": "OLIG1", "organism": "Homo sapiens", "uniprot_id": "Q8TAK6" }, { "function": "Controls the classical pathway of complement activation. It binds as a cofactor to C3b/C4b inactivator (C3bINA), which then hydrolyzes the complement fragment C4b. It also accelerates the degradation of the C4bC2a complex (C3 convertase) by dissociating the complement fragment C2a. Alpha chain binds C4b. It also interacts with anticoagulant protein S and with serum amyloid P component", "gene_name": "C4BPA", "glycan_count": 28, "glycosylation_sites": [ { "position": 221, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 506, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 528, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P04003", "name": "C4b-binding protein alpha chain", "organism": "Homo sapiens", "uniprot_id": "P04003" }, { "function": "Major acute phase reactant", "gene_name": "SAA2", "glycan_count": 1, "glycosylation_sites": [], "id": "P0DJI9", "name": "Serum amyloid A-2", "organism": "Homo sapiens", "uniprot_id": "P0DJI9" }, { "function": "Crystallins are the dominant structural components of the vertebrate eye lens", "gene_name": "CRYBB2", "glycan_count": 0, "glycosylation_sites": [], "id": "P43320", "name": "Beta-crystallin B2", "organism": "Homo sapiens", "uniprot_id": "P43320" }, { "function": "Crystallins are the dominant structural components of the vertebrate eye lens", "gene_name": "CRYGS", "glycan_count": 0, "glycosylation_sites": [], "id": "A0A140CTX8", "name": "Gamma-crystallin S", "organism": "Homo sapiens", "uniprot_id": "A0A140CTX8" }, { "function": "Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES) and of RNAs. In the nucleus, in association with RANBP3, binds cooperatively to the NES on its target protein and to the GTPase RAN in its active GTP-bound form (Ran-GTP). Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Involved in U3 snoRNA transport from Cajal bodies to nucleoli. Binds to late precursor U3 snoRNA bearing a TMG cap", "gene_name": "XPO1", "glycan_count": 1, "glycosylation_sites": [], "id": "O14980", "name": "CRM1 (Exportin 1)", "organism": "Homo sapiens", "uniprot_id": "O14980" }, { "function": "Disrupts bidirectional nucleocytoplasmic transport by interacting with the host RAE1-NUP98 complex (PubMed:33360543, PubMed:33849972). Disrupts cell nuclear import complex formation by tethering karyopherin alpha 2 and karyopherin beta 1 to the membrane (PubMed:32979938). Retention of import factors at the ER/Golgi membrane leads to a loss of transport into the nucleus (By similarity). Prevents STAT1 nuclear translocation in response to interferon signaling, thus blocking the expression of interferon stimulated genes (ISGs) that display multiple antiviral activities (PubMed:33097660). Suppresses IFN-beta production possibly by blocking IRF3 nuclear translocation (PubMed:32979938). Might induce accumulation of host HNRNPA1 (PubMed:33360543)", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P0DTC6", "name": "SARS-CoV-2 ORF6 protein", "organism": "Severe acute respiratory syndrome coronavirus 2", "uniprot_id": "P0DTC6" }, { "function": "", "gene_name": "ORF10", "glycan_count": 0, "glycosylation_sites": [], "id": "A0A663DJA2", "name": "SARS-CoV-2 ORF10 protein", "organism": "Severe acute respiratory syndrome coronavirus 2", "uniprot_id": "A0A663DJA2" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01233-2", "name": "free beta-subunit human chorionic gonadotropin (free \u03b2-hCG)", "organism": "", "uniprot_id": "" }, { "function": "Essential bifunctional enzyme that catalyzes both the N-deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Has low deacetylase activity but high sulfotransferase activity (By similarity)", "gene_name": "NDST4", "glycan_count": 1, "glycosylation_sites": [ { "position": 226, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 341, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 391, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 657, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 793, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9H3R1", "name": "PDZK1IP1", "organism": "Homo sapiens", "uniprot_id": "Q9H3R1" }, { "function": "Involved in DNA replication and the cellular response to DNA damage. May participate in DNA replication factories and create a bridge between DNA replication and repair mediated by high molecular weight complexes. May play a role in illegitimate recombination and regulation of gene expression. May participate in mRNA processing. Binds, in vitro, to double-stranded DNA. Also shown to bind preferentially to curved DNA in vitro and in vivo (By similarity). Binds via its C-terminal domain to RNA in vitro", "gene_name": "KIN", "glycan_count": 0, "glycosylation_sites": [], "id": "O60870", "name": "PHEX", "organism": "Homo sapiens", "uniprot_id": "O60870" }, { "function": "Regulates the dendritic spine distribution of CTTN/cortactin in hippocampal neurons, and thus controls dendritic spinogenesis and dendritic spine maintenance. Associates with the striatin-interacting phosphatase and kinase (STRIPAK) core complex to regulate dendritic spine distribution of the STRIPAK complex in hippocampal neurons", "gene_name": "CTTNBP2", "glycan_count": 2, "glycosylation_sites": [], "id": "Q8WZ74", "name": "C1GALT1C1", "organism": "Homo sapiens", "uniprot_id": "Q8WZ74" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P05556/P18084", "name": "Integrin \u03b1v\u03b25", "organism": "", "uniprot_id": "" }, { "function": "Zinc ion transporter that mediates zinc efflux and plays a crucial role in intracellular zinc homeostasis (PubMed:25130899, PubMed:31697912, PubMed:36204728). Binds the divalent cations Zn(2+), Ni(2+), and to a minor extent Cu(2+) (By similarity). Is a functional modulator of P2X purinoceptors, including P2RX1, P2RX3, P2RX4 and P2RX7 (PubMed:32492420). Plays a role in central nervous system development and is required for myelination, and survival and proliferation of oligodendrocytes (PubMed:35455965)", "gene_name": "TMEM163", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UFG3", "name": "CD39", "organism": "Homo sapiens", "uniprot_id": "Q8TC26" }, { "function": "Catalyzes the deacetylation of N-acetylaspartic acid (NAA) to produce acetate and L-aspartate. NAA occurs in high concentration in brain and its hydrolysis NAA plays a significant part in the maintenance of intact white matter. In other tissues it acts as a scavenger of NAA from body fluids", "gene_name": "ASPA", "glycan_count": 0, "glycosylation_sites": [], "id": "P45381", "name": "CD73", "organism": "Homo sapiens", "uniprot_id": "P45381" }, { "function": "Possesses 3' to 5' helicase activity and exonuclease activity. Involved in neuronal development, specifically in the development of different sensory organs", "gene_name": "NAV2", "glycan_count": 18, "glycosylation_sites": [], "id": "Q8IVL1", "name": "NAV1", "organism": "Homo sapiens", "uniprot_id": "Q8IVL1" }, { "function": "Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis", "gene_name": "ODC1", "glycan_count": 0, "glycosylation_sites": [], "id": "P11926", "name": "ODC1 (Ornithine Decarboxylase 1)", "organism": "Homo sapiens", "uniprot_id": "P11926" }, { "function": "Serine/threonine kinase involved in cell cycle control and in RNA polymerase II-mediated RNA transcription (PubMed:9852112, PubMed:19136461, PubMed:26257281, PubMed:28768201). Cyclin-dependent kinases (CDKs) are activated by the binding to a cyclin and mediate the progression through the cell cycle. Each different complex controls a specific transition between 2 subsequent phases in the cell cycle. Required for both activation and complex formation of CDK1/cyclin-B during G2-M transition, and for activation of CDK2/cyclins during G1-S transition (but not complex formation). CDK7 is the catalytic subunit of the CDK-activating kinase (CAK) complex. Phosphorylates SPT5/SUPT5H, SF1/NR5A1, POLR2A, p53/TP53, CDK1, CDK2, CDK4, CDK6 and CDK11B/CDK11 (PubMed:9372954, PubMed:9840937, PubMed:19136461, PubMed:26257281, PubMed:28768201). Initiates transcription by RNA polymerase II by mediating phosphorylation of POLR2A at 'Ser-5' of the repetitive C-terminal domain (CTD) when POLR2A is in complex with DNA, promoting dissociation from DNA and initiation (PubMed:19136461, PubMed:26257281, PubMed:28768201). CAK activates the cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation, thus regulating cell cycle progression. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the CTD of POLR2A, allowing its escape from the promoter and elongation of the transcripts (PubMed:9852112). Its expression and activity are constant throughout the cell cycle. Upon DNA damage, triggers p53/TP53 activation by phosphorylation, but is inactivated in turn by p53/TP53; this feedback loop may lead to an arrest of the cell cycle and of the transcription, helping in cell recovery, or to apoptosis. Required for DNA-bound peptides-mediated transcription and cellular growth inhibition", "gene_name": "CDK7", "glycan_count": 1, "glycosylation_sites": [], "id": "P50613", "name": "CDK7", "organism": "Homo sapiens", "uniprot_id": "P50613" }, { "function": "Catalytic core component of RNA polymerase II (Pol II), a DNA-dependent RNA polymerase which synthesizes mRNA precursors and many functional non-coding RNAs using the four ribonucleoside triphosphates as substrates (By similarity) (PubMed:23748380, PubMed:27193682, PubMed:30190596, PubMed:9852112). Pol II-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol II pre-initiation complex (PIC) is recruited to DNA promoters, with focused-type promoters containing either the initiator (Inr) element, or the TATA-box found in cell-type specific genes and dispersed-type promoters that often contain hypomethylated CpG islands usually found in housekeeping genes. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Transcription termination involves the release of the RNA transcript and polymerase from the DNA (By similarity) (PubMed:23748380, PubMed:27193682, PubMed:28108474, PubMed:30190596, PubMed:9852112). Forms Pol II active center together with the second largest subunit POLR2B/RPB2. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR2A/RPB1 most likely contributing a Mg(2+)-coordinating DxDGD motif, and POLR2B/RPB2 participating in the coordination of a second Mg(2+) ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and template base. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate. The reversible pyrophosphorolysis can occur at high pyrophosphate concentrations (By similarity) (PubMed:30190596, PubMed:8381534, PubMed:9852112). Can proofread the nascent RNA transcript by means of a 3' -> 5' exonuclease activity. If a ribonucleotide is mis-incorporated, backtracks along the template DNA and cleaves the phosphodiester bond releasing the mis-incorporated 5'-ribonucleotide (By similarity) (PubMed:8381534). Through its unique C-terminal domain (CTD, 52 heptapeptide tandem repeats) serves as a platform for assembly of factors that regulate transcription initiation, elongation and termination. CTD phosphorylation on Ser-5 mediates Pol II promoter escape, whereas phosphorylation on Ser-2 is required for Pol II pause release during transcription elongation and further pre-mRNA processing. Additionally, the regulation of gene expression levels depends on the balance between methylation and acetylation levels of the CTD-lysines. Initiation or early elongation steps of transcription of growth-factor-induced immediate early genes are regulated by the acetylation status of the CTD. Methylation and dimethylation have a repressive effect on target genes expression. Cooperates with mRNA splicing machinery in co-transcriptional 5'-end capping and co-transcriptional splicing of pre-mRNA (By similarity) (PubMed:24207025, PubMed:26124092)", "gene_name": "POLR2A", "glycan_count": 2, "glycosylation_sites": [], "id": "P24928", "name": "RNA Pol II", "organism": "Homo sapiens", "uniprot_id": "P24928" }, { "function": "Membrane glycoproteins implicated in the pathologic deposition of cholesterol in arterial walls during atherogenesis. Two types of receptor subunits exist. These receptors mediate the endocytosis of a diverse group of macromolecules, including modified low density lipoproteins (LDL) (PubMed:2251254). Isoform III does not internalize acetylated LDL (PubMed:9548586)", "gene_name": "MSR1", "glycan_count": 10, "glycosylation_sites": [ { "position": 82, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 102, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 143, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 184, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 221, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 249, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 267, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P21757", "name": "SR-A (MSR1)", "organism": "Homo sapiens", "uniprot_id": "P21757" }, { "function": "Essential for the control of the cell cycle at the G2/M (mitosis) transition", "gene_name": "CCNB2", "glycan_count": 0, "glycosylation_sites": [], "id": "O95067", "name": "CCNB2", "organism": "Homo sapiens", "uniprot_id": "O95067" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P07550 (ADRB1)", "name": "Beta-adrenergic receptor", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02671, P02675, P02679", "name": "Fibrinogen", "organism": "", "uniprot_id": "" }, { "function": "Major acute phase reactant. Apolipoprotein of the HDL complex", "gene_name": "SAA1", "glycan_count": 0, "glycosylation_sites": [], "id": "P35541", "name": "Serum Amyloid A (SAA)", "organism": "Bos taurus", "uniprot_id": "P35541" }, { "function": "Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. The BORC complex is most probably associated with the cytosolic face of lysosomes, may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor", "gene_name": "BLOC1S1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q5R7L8", "name": "P-selectin (GMP-140)", "organism": "Pongo abelii", "uniprot_id": "Q5R7L8" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q14524 (SCN5A)", "name": "Sodium channel (Nav1.5)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q12809 (KCNH2)", "name": "Potassium channel (Kv11.1/hERG)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q13936 (CACNA1C)", "name": "Calcium channel (Cav1.2)", "organism": "", "uniprot_id": "" }, { "function": "Mainly functions as an acyl-CoA ligase catalyzing the ATP-dependent formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates (PubMed:15469937, PubMed:15699031). Can mediate the levels of long-chain fatty acids (LCFA) in the cell by facilitating their transport across membranes (PubMed:15699031)", "gene_name": "Slc27a3", "glycan_count": 0, "glycosylation_sites": [], "id": "O88561", "name": "Claudin-1", "organism": "Mus musculus", "uniprot_id": "O88561" }, { "function": "Key player in the regulation of energy balance and body weight control. Once released into the circulation, has central and peripheral effects by binding LEPR, found in many tissues, which results in the activation of several major signaling pathways (PubMed:11373681, PubMed:12594516, PubMed:15899045, PubMed:16825198, PubMed:20620997). In the hypothalamus, acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption by inducing anorexinogenic factors and suppressing orexigenic neuropeptides, also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, influences reproductive function, regulates pancreatic beta-cell function and insulin secretion, is pro-angiogenic for endothelial cell and affects innate and adaptive immunity (By similarity) (PubMed:10660043, PubMed:12594516, PubMed:25060689, PubMed:25383904, PubMed:8589726, PubMed:9732873). In the arcuate nucleus of the hypothalamus, activates by depolarization POMC neurons inducing FOS and SOCS3 expression to release anorexigenic peptides and inhibits by hyperpolarization NPY neurons inducing SOCS3 with a consequent reduction on release of orexigenic peptides (By similarity) (PubMed:11373681, PubMed:20620997). In addition to its known satiety inducing effect, has a modulatory role in nutrient absorption. In the intestine, reduces glucose absorption by enterocytes by activating PKC and leading to a sequential activation of p38, PI3K and ERK signaling pathways which exerts an inhibitory effect on glucose absorption. Acts as a growth factor on certain tissues, through the activation of different signaling pathways increases expression of genes involved in cell cycle regulation such as CCND1, via JAK2-STAT3 pathway, or VEGFA, via MAPK1/3 and PI3K-AKT1 pathways (By similarity) (PubMed:16825198, PubMed:20620997). May also play an apoptotic role via JAK2-STAT3 pathway and up-regulation of BIRC5 expression (By similarity). Pro-angiogenic, has mitogenic activity on vascular endothelial cells and plays a role in matrix remodeling by regulating the expression of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) (PubMed:16825198). In innate immunity, modulates the activity and function of neutrophils by increasing chemotaxis and the secretion of oxygen radicals. Increases phagocytosis by macrophages and enhances secretion of pro-inflammatory mediators. Increases cytotoxic ability of NK cells (Probable). Plays a pro-inflammatory role, in synergy with IL1B, by inducing NOS2 which promotes the production of IL6, IL8 and Prostaglandin E2, through a signaling pathway that involves JAK2, PI3K, MAP2K1/MEK1 and MAPK14/p38 (PubMed:15899045). In adaptive immunity, promotes the switch of memory T-cells towards T helper-1 cell immune responses (By similarity). Increases CD4(+)CD25(-) T cells proliferation and reduces autophagy during TCR (T cell receptor) stimulation, through MTOR signaling pathway activation and BCL2 up-regulation (PubMed:25060689)", "gene_name": "Lep", "glycan_count": 0, "glycosylation_sites": [], "id": "P41160", "name": "Leptin", "organism": "Mus musculus", "uniprot_id": "P41160" }, { "function": "Multifunctional and multicompartmental protein involved in inflammation and infection processes, ribosome biogenesis, protein synthesis in mitochondria, regulation of apoptosis, transcriptional regulation and pre-mRNA splicing (PubMed:10022843, PubMed:10479529, PubMed:10722602, PubMed:11086025, PubMed:11859136, PubMed:15243141, PubMed:16140380, PubMed:16177118, PubMed:17881511, PubMed:18676636, PubMed:19004836, PubMed:19164550, PubMed:20810993, PubMed:21536856, PubMed:21544310, PubMed:22700724, PubMed:28942965, PubMed:8662673, PubMed:8710908, PubMed:9461517). At the cell surface is thought to act as an endothelial receptor for plasma proteins of the complement and kallikrein-kinin cascades (PubMed:10479529, PubMed:11859136, PubMed:8662673, PubMed:8710908). Putative receptor for C1q; specifically binds to the globular 'heads' of C1q thus inhibiting C1; may perform the receptor function through a complex with C1qR/CD93 (PubMed:20810993, PubMed:8195709). In complex with cytokeratin-1/KRT1 is a high affinity receptor for kininogen-1/HMWK (PubMed:21544310). Can also bind other plasma proteins, such as coagulation factor XII leading to its autoactivation. May function to bind initially fluid kininogen-1 to the cell membrane. The secreted form may enhance both extrinsic and intrinsic coagulation pathways. It is postulated that the cell surface form requires docking with transmembrane proteins for downstream signaling which might be specific for a cell-type or response. By acting as C1q receptor is involved in chemotaxis of immature dendritic cells and neutrophils and is proposed to signal through CD209/DC-SIGN on immature dendritic cells, through integrin alpha-4/beta-1 during trophoblast invasion of the decidua, and through integrin beta-1 during endothelial cell adhesion and spreading (PubMed:16140380, PubMed:22700724, PubMed:9461517). Signaling involved in inhibition of innate immune response is implicating the PI3K-AKT/PKB pathway (PubMed:16177118). Required for protein synthesis in mitochondria (PubMed:28942965). In mitochondrial translation may be involved in formation of functional 55S mitoribosomes; the function seems to involve its RNA-binding activity (By similarity). Acts as a RNA modification reader, which specifically recognizes and binds mitochondrial RNAs modified by C5-methylcytosine (m5C) in response to stress, and promotes recruitment of the mitochondrial degradosome complex, leading to their degradation (PubMed:39019044). May be involved in the nucleolar ribosome maturation process; the function may involve the exchange of FBL for RRP1 in the association with pre-ribosome particles (By similarity). Involved in regulation of RNA splicing by inhibiting the RNA-binding capacity of SRSF1 and its phosphorylation (PubMed:10022843, PubMed:21536856). Is required for the nuclear translocation of splicing factor U2AF1L4 (By similarity). Involved in regulation of CDKN2A- and HRK-mediated apoptosis. Stabilizes mitochondrial CDKN2A isoform smARF (PubMed:17486078). May be involved in regulation of FOXC1 transcriptional activity and NFY/CCAAT-binding factor complex-mediated transcription (PubMed:15243141, PubMed:18676636). May play a role in antibacterial defense as it can bind to cell surface hyaluronan and inhibit Streptococcus pneumoniae hyaluronate lyase (PubMed:19004836). May be involved in modulation of the immune response; ligation by HCV core protein is resulting in suppression of interleukin-12 production in monocyte-derived dendritic cells (PubMed:11086025, PubMed:17881511). Involved in regulation of antiviral response by inhibiting RIGI- and IFIH1-mediated signaling pathways probably involving its association with MAVS after viral infection (PubMed:19164550). Acts as a regulator of DNA repair via homologous recombination by inhibiting the activity of MRE11: interacts with unphosphorylated MRE11 and RAD50 in absence of DNA damage, preventing formation and activity of the MRN complex. Following DNA damage, dissociates from phosphorylated MRE11, allowing formation of the MRN complex (PubMed:31353207)", "gene_name": "C1QBP", "glycan_count": 2, "glycosylation_sites": [], "id": "Q07021", "name": "C1qBP", "organism": "Homo sapiens", "uniprot_id": "Q07021" }, { "function": "G-protein coupled receptor for CRH (corticotropin-releasing factor), UCN (urocortin), UCN2 and UCN3. Has high affinity for UCN. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and down-stream effectors, such as adenylate cyclase. Promotes the activation of adenylate cyclase, leading to increased intracellular cAMP levels", "gene_name": "CRHR2", "glycan_count": 0, "glycosylation_sites": [ { "position": 13, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 41, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 74, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 86, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 94, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13324", "name": "Corticotropin-releasing factor receptor 2", "organism": "Homo sapiens", "uniprot_id": "Q13324" }, { "function": "G protein-coupled receptor which specificity is determined by its interaction with receptor-activity-modifying proteins (RAMPs) (PubMed:32296767, PubMed:33602864, PubMed:8626685). Together with RAMP1, form the receptor complex for calcitonin-gene-related peptides CALCA/CGRP1 and CALCB/CGRP2 (PubMed:33602864). Together with RAMP2 or RAMP3, function as receptor complexes for adrenomedullin (ADM and ADM2) (PubMed:32296767, PubMed:9620797). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors. Activates cAMP-dependent pathway (PubMed:32296767, PubMed:8626685)", "gene_name": "CALCRL", "glycan_count": 18, "glycosylation_sites": [ { "position": 66, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 118, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 123, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q16602", "name": "Calcitonin gene-related peptide type 1 receptor", "organism": "Homo sapiens", "uniprot_id": "Q16602" }, { "function": "NAD-dependent protein deacetylase (PubMed:12186850, PubMed:12374852, PubMed:16788062, PubMed:18680753, PubMed:18794531, PubMed:19535340, PubMed:23283301, PubMed:24121500, PubMed:24252090). Activates or deactivates mitochondrial target proteins by deacetylating key lysine residues (PubMed:12186850, PubMed:12374852, PubMed:16788062, PubMed:18680753, PubMed:18794531, PubMed:23283301, PubMed:24121500, PubMed:24252090, PubMed:38146092). Known targets include ACSS1, IDH, GDH, SOD2, PDHA1, LCAD, SDHA, MRPL12 and the ATP synthase subunit ATP5PO (PubMed:16788062, PubMed:18680753, PubMed:19535340, PubMed:24121500, PubMed:24252090, PubMed:38146092). Contributes to the regulation of the cellular energy metabolism (PubMed:24252090). Important for regulating tissue-specific ATP levels (PubMed:18794531). In response to metabolic stress, deacetylates transcription factor FOXO3 and recruits FOXO3 and mitochondrial RNA polymerase POLRMT to mtDNA to promote mtDNA transcription (PubMed:23283301). Acts as a regulator of ceramide metabolism by mediating deacetylation of ceramide synthases CERS1, CERS2 and CERS6, thereby increasing their activity and promoting mitochondrial ceramide accumulation (By similarity). Regulates hepatic lipogenesis (By similarity). Uses NAD(+) substrate imported by SLC25A47, triggering downstream activation of PRKAA1/AMPK-alpha signaling cascade that ultimately downregulates sterol regulatory element-binding protein (SREBP) transcriptional activities and ATP-consuming lipogenesis to restore cellular energy balance (By similarity). In addition to protein deacetylase activity, also acts as a protein-lysine deacylase by mediating delactylation of proteins, such as CCNE2 and 'Lys-16' of histone H4 (H4K16la) (PubMed:36896611, PubMed:37720100)", "gene_name": "SIRT3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NTG7", "name": "SIRT3", "organism": "Homo sapiens", "uniprot_id": "Q9NTG7" }, { "function": "E3 ubiquitin-protein ligase component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation (PubMed:17006537, PubMed:19136968, PubMed:20005846, PubMed:21455173, PubMed:21455180, PubMed:21455181, PubMed:22863777, PubMed:28189684, PubMed:28481331). LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways (PubMed:17006537, PubMed:19136968, PubMed:20005846, PubMed:21455173, PubMed:21455180, PubMed:21455181, PubMed:22863777, PubMed:28189684). Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation (PubMed:21455173, PubMed:28189684). LUBAC is recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex (PubMed:20005846, PubMed:27458237). The LUBAC complex is also involved in innate immunity by conjugating linear polyubiquitin chains at the surface of bacteria invading the cytosol to form the ubiquitin coat surrounding bacteria (PubMed:28481331, PubMed:34012115). LUBAC is not able to initiate formation of the bacterial ubiquitin coat, and can only promote formation of linear polyubiquitins on pre-existing ubiquitin (PubMed:28481331). Recruited to the surface of bacteria by RNF213, which initiates the bacterial ubiquitin coat (PubMed:34012115). The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation (PubMed:28481331, PubMed:34012115). Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis (PubMed:23708998). RNF31 is required for linear ubiquitination of BCL10, thereby promoting TCR-induced NF-kappa-B activation (PubMed:27777308). Binds polyubiquitin of different linkage types (PubMed:23708998)", "gene_name": "RNF31", "glycan_count": 0, "glycosylation_sites": [], "id": "Q96EP0", "name": "RNF31", "organism": "Homo sapiens", "uniprot_id": "Q96EP0" }, { "function": "Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (PubMed:10893423, PubMed:9497358). Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides (PubMed:10893423). Also has phospholipase activity, can therefore either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity) (PubMed:10893423, PubMed:26830860). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH (PubMed:10893423). Plays a role in cell protection against oxidative stress by detoxifying peroxides and in phospholipid homeostasis (PubMed:10893423). Exhibits acyl-CoA-dependent lysophospholipid acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (PubMed:26830860). Shows a clear preference for LPC as the lysophospholipid and for palmitoyl CoA as the fatty acyl substrate (PubMed:26830860)", "gene_name": "PRDX6", "glycan_count": 1, "glycosylation_sites": [], "id": "P30041", "name": "PRDX6", "organism": "Homo sapiens", "uniprot_id": "P30041" }, { "function": "Possesses tyrosine phosphatase activity. Plays a role in regulating the glomerular pressure/filtration rate relationship through an effect on podocyte structure and function (By similarity)", "gene_name": "PTPRO", "glycan_count": 6, "glycosylation_sites": [ { "position": 75, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 154, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 189, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 201, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 227, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 278, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 287, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 323, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 324, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 370, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 461, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 490, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 700, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 712, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 733, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q16827", "name": "PTPROt", "organism": "Homo sapiens", "uniprot_id": "Q16827" }, { "function": "", "gene_name": "amyS", "glycan_count": 0, "glycosylation_sites": [], "id": "P06278", "name": "Cyclodextrin glycosyltransferase", "organism": "Bacillus licheniformis", "uniprot_id": "P06278" }, { "function": "Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP3 is essential for sperm binding and zona matrix formation", "gene_name": "ZP3", "glycan_count": 30, "glycosylation_sites": [ { "position": 125, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 147, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 156, "type": "O-linked (GalNAc...) threonine" }, { "position": 162, "type": "O-linked (GalNAc...) threonine" }, { "position": 163, "type": "O-linked (GalNAc...) threonine" }, { "position": 272, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P21754", "name": "ZP3", "organism": "Homo sapiens", "uniprot_id": "P21754" }, { "function": "This is an intracellular thiol proteinase inhibitor. Has an important role in desmosome-mediated cell-cell adhesion in the lower levels of the epidermis", "gene_name": "CSTA", "glycan_count": 1, "glycosylation_sites": [], "id": "P01040", "name": "Cystatin A (CSTA)", "organism": "Homo sapiens", "uniprot_id": "P01040" }, { "function": "Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. When expressed in rat HTC4 hepatoma cells, is capable of mediating S1P-induced cell proliferation and suppression of apoptosis", "gene_name": "S1PR3", "glycan_count": 1, "glycosylation_sites": [ { "position": 15, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q99500", "name": "Sphingosine-1-phosphate receptor 3 (S1PR3)", "organism": "Homo sapiens", "uniprot_id": "Q99500" }, { "function": "Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of ADD1, BRCA2, CNN1, EZR, DPYSL2, EP300, MSN, MYL9/MLC2, NPM1, RDX, PPP1R12A and VIM. Phosphorylates SORL1 and IRF4. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Positively regulates the activation of p42/MAPK1-p44/MAPK3 and of p90RSK/RPS6KA1 during myogenic differentiation. Plays an important role in the timely initiation of centrosome duplication. Inhibits keratinocyte terminal differentiation. May regulate closure of the eyelids and ventral body wall through organization of actomyosin bundles. Plays a critical role in the regulation of spine and synaptic properties in the hippocampus. Plays an important role in generating the circadian rhythm of the aortic myofilament Ca(2+) sensitivity and vascular contractility by modulating the myosin light chain phosphorylation", "gene_name": "ROCK2", "glycan_count": 1, "glycosylation_sites": [], "id": "O75116", "name": "Rho-associated coiled-coil containing protein kinase 2 (ROCK2)", "organism": "Homo sapiens", "uniprot_id": "O75116" }, { "function": "Myosins are actin-based motor molecules with ATPase activity essential for muscle contraction", "gene_name": "MYH2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UKX2", "name": "Bone Morphogenetic Protein 6 (BMP-6)", "organism": "Homo sapiens", "uniprot_id": "Q9UKX2" }, { "function": "Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes (PubMed:15608617, PubMed:16166375, PubMed:20655466, PubMed:28216226, PubMed:9326950, PubMed:9326951, PubMed:9476899). In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo (PubMed:16166375, PubMed:20655466). Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection (PubMed:16166375). Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways (PubMed:16166375). Together with DCLRE1B/Apollo, plays a key role in telomeric loop (T loop) formation by generating 3' single-stranded overhang at the leading end telomeres: T loops have been proposed to protect chromosome ends from degradation and repair (PubMed:20655466). Required both to recruit DCLRE1B/Apollo to telomeres and activate the exonuclease activity of DCLRE1B/Apollo (PubMed:20655466, PubMed:28216226). Preferentially binds to positive supercoiled DNA (PubMed:15608617, PubMed:20655466). Together with DCLRE1B/Apollo, required to control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology (PubMed:20655466). Recruits TERF2IP/RAP1 to telomeres, thereby participating in to repressing homology-directed repair (HDR), which can affect telomere length (By similarity)", "gene_name": "TERF2", "glycan_count": 3, "glycosylation_sites": [], "id": "Q15554", "name": "Telomeric-repeat binding factor 2 (TRF2)", "organism": "Homo sapiens", "uniprot_id": "Q15554" }, { "function": "Acts both as a regulator of telomere function and as a transcription regulator. Involved in the regulation of telomere length and protection as a component of the shelterin complex (telosome). In contrast to other components of the shelterin complex, it is dispensible for telomere capping and does not participate in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair. Instead, it is required to negatively regulate telomere recombination and is essential for repressing homology-directed repair (HDR), which can affect telomere length. Does not bind DNA directly: recruited to telomeric double-stranded 5'-TTAGGG-3' repeats via its interaction with TERF2. Independently of its function in telomeres, also acts as a transcription regulator: recruited to extratelomeric 5'-TTAGGG-3' sites via its association with TERF2 or other factors, and regulates gene expression. When cytoplasmic, associates with the I-kappa-B-kinase (IKK) complex and acts as a regulator of the NF-kappa-B signaling by promoting IKK-mediated phosphorylation of RELA/p65, leading to activate expression of NF-kappa-B target genes", "gene_name": "TERF2IP", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NYB0", "name": "Repressor activator protein 1 (RAP1)", "organism": "Homo sapiens", "uniprot_id": "Q9NYB0" }, { "function": "Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. Active in progenitor and cancer cells. Inactive, or very low activity, in normal somatic cells. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres by acting as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. More active on substrates containing 2 or 3 telomeric repeats. Telomerase activity is regulated by a number of factors including telomerase complex-associated proteins, chaperones and polypeptide modifiers. Modulates Wnt signaling. Plays important roles in aging and antiapoptosis", "gene_name": "TERT", "glycan_count": 1, "glycosylation_sites": [], "id": "O14746", "name": "Telomerase", "organism": "Homo sapiens", "uniprot_id": "O14746" }, { "function": "Lipid transfer protein involved in autophagosome assembly (PubMed:28561066, PubMed:30952800, PubMed:31271352). Tethers the edge of the isolation membrane (IM) to the endoplasmic reticulum (ER) and mediates direct lipid transfer from ER to IM for IM expansion (PubMed:30952800, PubMed:31271352). Binds to the ER exit site (ERES), which is the membrane source for autophagosome formation, and extracts phospholipids from the membrane source and transfers them to ATG9 (ATG9A or ATG9B) to the IM for membrane expansion (PubMed:30952800, PubMed:31271352). Lipid transfer activity is enhanced by WIPI1 and WDR45/WIPI4, which promote ATG2A-association with phosphatidylinositol 3-monophosphate (PI3P)-containing membranes (PubMed:31271352). Also regulates lipid droplets morphology and distribution within the cell (PubMed:22219374, PubMed:28561066)", "gene_name": "ATG2A", "glycan_count": 1, "glycosylation_sites": [], "id": "Q2TAZ0", "name": "ATG2", "organism": "Homo sapiens", "uniprot_id": "Q2TAZ0" }, { "function": "Involved in the MEC1-mediated checkpoint response to DNA damage and replication arrest", "gene_name": "HUG1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6Q5K6", "name": "ATG32", "organism": "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "uniprot_id": "Q6Q5K6" }, { "function": "Involved in amino acid permease processing and required for the efficient translocation of structurally related amino acid permeases from the endoplasmic reticulum to the plasma membrane", "gene_name": "psh3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y876", "name": "Uric Acid Transporters (e.g., SLC22A12)", "organism": "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "uniprot_id": "Q9Y876" }, { "function": "RNA-binding protein that binds to AU-rich element (ARE) sequences of target mRNAs, including VEGF mRNA (PubMed:10710437). May also bind poly-A tracts via RRM 3 (By similarity). May be involved in neuronal differentiation and maintenance (By similarity). Plays a role in the stabilization of GAP43 mRNA and in spatial learning (By similarity)", "gene_name": "ELAVL3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q14576", "name": "Klebs von den Lungen-6 (KL-6)", "organism": "Homo sapiens", "uniprot_id": "Q14576" }, { "function": "Acts as a transcriptional regulator in adaptive response to low oxygen tension. Acts as a regulator of hypoxia-inducible gene expression (PubMed:11573933, PubMed:16126907, PubMed:19694616, PubMed:20416395, PubMed:21069422). Functions as an inhibitor of angiogenesis in hypoxic cells of the cornea. Plays a role in the development of the cardiorespiratory system. May also be involved in apoptosis (By similarity)", "gene_name": "HIF3A", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y2N7", "name": "HIF3A (Hypoxia-inducible factor 3 alpha)", "organism": "Homo sapiens", "uniprot_id": "Q9Y2N7" }, { "function": "Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Preferentially demethylates mono- and dimethylated H3 'Lys-9' residue, with a preference for dimethylated residue, while it has weak or no activity on trimethylated H3 'Lys-9'. Demethylation of Lys residue generates formaldehyde and succinate. Involved in hormone-dependent transcriptional activation, by participating in recruitment to androgen-receptor target genes, resulting in H3 'Lys-9' demethylation and transcriptional activation. Involved in spermatogenesis by regulating expression of target genes such as PRM1 and TNP1 which are required for packaging and condensation of sperm chromatin. Involved in obesity resistance through regulation of metabolic genes such as PPARA and UCP1", "gene_name": "KDM3A", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9Y4C1", "name": "KDM3A (Lysine demethylase 3A)", "organism": "Homo sapiens", "uniprot_id": "Q9Y4C1" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O00220/O14763", "name": "TRAIL Receptor (DR4/DR5)", "organism": "", "uniprot_id": "" }, { "function": "This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations and following phosphorylation by FAM20C, functions as a chaperone that inhibits aggregation of misfolded proteins (PubMed:32149426). At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts as a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP. Receptor for LGALS9; the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307)", "gene_name": "P4HB", "glycan_count": 2, "glycosylation_sites": [], "id": "P07237", "name": "Protein disulfide-isomerase (PDI)", "organism": "Homo sapiens", "uniprot_id": "P07237" }, { "function": "Cytokine secreted primarily by mast cells, T-cells, eosinophils, and basophils that plays a role in regulating antibody production, hematopoiesis and inflammation, and the development of effector T-cell responses (PubMed:3083412). Induces the expression of class II MHC molecules on resting B-cells (PubMed:3498301). Enhances both secretion and cell surface expression of IgE and IgG1 (PubMed:3498301). Also regulates the expression of the low affinity Fc receptor for IgE (CD23) on both lymphocytes and monocytes (By similarity). Positively regulates IL31RA expression in macrophages. Stimulates autophagy in dendritic cells by interfering with mTORC1 signaling and through the induction of RUFY4 (PubMed:26416964). In addition, plays a critical role in higher functions of the normal brain, such as memory and learning (PubMed:25772794, PubMed:28202615). Upon binding to IL4, IL4R receptor dimerizes either with the common IL2R gamma chain/IL2RG to produce the type 1 signaling complex, located mainly on hematopoietic cells, or with the IL13RA1 to produce the type 2 complex, which is also expressed on nonhematopoietic cells. Engagement of both types of receptors initiates JAK3 and to a lower extend JAK1 phosphorylation leading to activation of the signal transducer and activator of transcription 6/STAT6 (PubMed:25847241, PubMed:8624821)", "gene_name": "Il4", "glycan_count": 0, "glycosylation_sites": [ { "position": 61, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 91, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 117, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P07750", "name": "Interleukin-4 (IL-4)", "organism": "Mus musculus", "uniprot_id": "P07750" }, { "function": "Effector cytokine of innate and adaptive immune system involved in antimicrobial host defense and maintenance of tissue integrity (PubMed:18025225, PubMed:19144317, PubMed:26431948). Signals via IL17RA-IL17RC heterodimeric receptor complex, triggering homotypic interaction of IL17RA and IL17RC chains with TRAF3IP2 adapter. This leads to downstream TRAF6-mediated activation of NF-kappa-B and MAPkinase pathways ultimately resulting in transcriptional activation of cytokines, chemokines, antimicrobial peptides and matrix metalloproteinases, with potential strong immune inflammation (PubMed:16200068, PubMed:17911633, PubMed:19144317, PubMed:26431948). Plays an important role in connecting T cell-mediated adaptive immunity and acute inflammatory response to destroy extracellular bacteria and fungi. As a signature effector cytokine of T-helper 17 cells (Th17), primarily induces neutrophil activation and recruitment at infection and inflammatory sites (PubMed:18025225). In airway epithelium, mediates neutrophil chemotaxis via induction of CXCL1 and CXCL5 chemokines (PubMed:18025225, PubMed:27923703). In secondary lymphoid organs, contributes to germinal center formation by regulating the chemotactic response of B cells to CXCL12 and CXCL13, enhancing retention of B cells within the germinal centers, B cell somatic hypermutation rate and selection toward plasma cells (PubMed:18157131). Effector cytokine of a subset of gamma-delta T cells that functions as part of an inflammatory circuit downstream IL1B, TLR2 and IL23A-IL12B to promote neutrophil recruitment for efficient bacterial clearance (PubMed:17372004, PubMed:20364087, PubMed:28709803). Effector cytokine of innate immune cells including invariant natural killer cell (iNKT) and group 3 innate lymphoid cells that mediate initial neutrophilic inflammation (PubMed:17470641, PubMed:23255360). Involved in the maintenance of the integrity of epithelial barriers during homeostasis and pathogen infection. Upon acute injury, has a direct role in epithelial barrier formation by regulating OCLN localization and tight junction biogenesis (PubMed:26431948). As part of the mucosal immune response induced by commensal bacteria, enhances host's ability to resist pathogenic bacterial and fungal infections by promoting neutrophil recruitment and antimicrobial peptides release (PubMed:28709803). In synergy with IL17F, mediates the production of antimicrobial beta-defensins DEFB1, DEFB103A, and DEFB104A by mucosal epithelial cells, limiting the entry of microbes through the epithelial barriers (PubMed:19144317). Involved in antiviral host defense through various mechanisms (PubMed:21946434, PubMed:26735852, PubMed:27795421). Enhances immunity against West Nile virus by promoting T cell cytotoxicity (PubMed:27795421). May play a beneficial role in influenza A virus (H5N1) infection by enhancing B cell recruitment and immune response in the lung (PubMed:21946434). Contributes to influenza A virus (H1N1) clearance by driving the differentiation of B-1a B cells, providing for production of virus-specific IgM antibodies at first line of host defense (PubMed:26735852)", "gene_name": "Il17a", "glycan_count": 0, "glycosylation_sites": [ { "position": 71, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q62386", "name": "Interleukin-17 (IL-17)", "organism": "Mus musculus", "uniprot_id": "Q62386" }, { "function": "This is the major myelin protein from the central nervous system. It plays an important role in the formation or maintenance of the multilamellar structure of myelin", "gene_name": "Plp1", "glycan_count": 1, "glycosylation_sites": [], "id": "P60202", "name": "Proteolipid Protein (PLP)", "organism": "Mus musculus", "uniprot_id": "P60202" }, { "function": "G-protein coupled receptor for cannabinoids, including endocannabinoids (eCBs), such as N-arachidonoylethanolamide (also called anandamide or AEA) and 2-arachidonoylglycerol (2-AG) (PubMed:22388959, PubMed:9888857). Mediates many cannabinoid-induced effects, acting, among others, on food intake, memory loss, gastrointestinal motility, catalepsy, ambulatory activity, anxiety, chronic pain (PubMed:27828947, PubMed:9888857). Signaling typically involves reduction in cyclic AMP (PubMed:27828947, PubMed:8832654). In the hypothalamus, may have a dual effect on mitochondrial respiration depending upon the agonist dose and possibly upon the cell type. Increases respiration at low doses, while decreases respiration at high doses (PubMed:25707796, PubMed:27828947). At high doses, CNR1 signal transduction involves G-protein alpha-i protein activation and subsequent inhibition of mitochondrial soluble adenylate cyclase, decrease in cyclic AMP concentration, inhibition of protein kinase A (PKA)-dependent phosphorylation of specific subunits of the mitochondrial electron transport system, including NDUFS2 (PubMed:27828947). In the hypothalamus, inhibits leptin-induced reactive oxygen species (ROS) formation and mediates cannabinoid-induced increase in SREBF1 and FASN gene expression (PubMed:25869131). In response to cannabinoids, drives the release of orexigenic beta-endorphin, but not that of melanocyte-stimulating hormone alpha/alpha-MSH, from hypothalamic POMC neurons, hence promoting food intake (PubMed:25707796). In the hippocampus, regulates cellular respiration and energy production in response to cannabinoids. Involved in cannabinoid-dependent depolarization-induced suppression of inhibition (DSI), a process in which depolarization of CA1 postsynaptic pyramidal neurons mobilizes eCBs, which retrogradely activate presynaptic CB1 receptors, transiently decreasing GABAergic inhibitory neurotransmission (PubMed:22388959). Also reduces excitatory synaptic transmission (PubMed:27828947). In superior cervical ganglions and cerebral vascular smooth muscle cells, inhibits voltage-gated Ca(2+) channels in a constitutive, as well as agonist-dependent manner (By similarity). In cerebral vascular smooth muscle cells, cannabinoid-induced inhibition of voltage-gated Ca(2+) channels leads to vasodilation and decreased vascular tone (By similarity). Induces leptin production in adipocytes and reduces LRP2-mediated leptin clearance in the kidney, hence participating in hyperleptinemia (PubMed:22841573). In adipose tissue, CNR1 signaling leads to increased expression of SREBF1, ACACA and FASN genes (PubMed:15864349). In the liver, activation by endocannabinoids leads to increased de novo lipogenesis and reduced fatty acid catabolism, associated with increased expression of SREBF1/SREBP-1, GCK, ACACA, ACACB and FASN genes (PubMed:15864349, PubMed:21987372). May also affect de novo cholesterol synthesis and HDL-cholesteryl ether uptake (PubMed:21987372). Peripherally modulates energy metabolism. In high carbohydrate diet-induced obesity, may decrease the expression of mitochondrial dihydrolipoyl dehydrogenase/DLD in striated muscles, as well as that of selected glucose/ pyruvate metabolic enzymes, hence affecting energy expenditure through mitochondrial metabolism (PubMed:26671069). In response to cannabinoid anandamide, elicits a pro-inflammatory response in macrophages, which involves NLRP3 inflammasome activation and IL1B and IL18 secretion. In macrophages infiltrating pancreatic islets, this process may participate in the progression of type-2 diabetes and associated loss of pancreatic beta-cells (PubMed:23955712)", "gene_name": "Cnr1", "glycan_count": 2, "glycosylation_sites": [ { "position": 78, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 84, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P47746", "name": "Cannabinoid Receptor 1 (CB1)", "organism": "Mus musculus", "uniprot_id": "P47746" }, { "function": "IFN-induced antiviral host restriction factor which efficiently blocks the release of diverse mammalian enveloped viruses by directly tethering nascent virions to the membranes of infected cells. Acts as a direct physical tether, holding virions to the cell membrane and linking virions to each other. The tethered virions can be internalized by endocytosis and subsequently degraded or they can remain on the cell surface. In either case, their spread as cell-free virions is restricted. Its target viruses belong to diverse families, including retroviridae: human immunodeficiency virus type 1 (HIV-1), mouse mammary tumor virus (MMTV) and murine leukemia virus (MLV), filoviridae: ebola virus (EBOV), arenaviridae: lassa virus (LASV), and rhabdoviridae: vesicular stomatitis virus (VSV). Can inhibit cell surface proteolytic activity of MMP14 causing decreased activation of MMP15 which results in inhibition of cell growth and migration. Can stimulate signaling by LILRA4/ILT7 and consequently provide negative feedback to the production of IFN by plasmacytoid dendritic cells in response to viral infection. Plays a role in the organization of the subapical actin cytoskeleton in polarized epithelial cells", "gene_name": "Bst2", "glycan_count": 2, "glycosylation_sites": [ { "position": 70, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 94, "type": "N-linked (GlcNAc...) asparagine; atypical" }, { "position": 97, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8R2Q8", "name": "G protein-coupled receptor 141 (GPR141)", "organism": "Mus musculus", "uniprot_id": "Q8R2Q8" }, { "function": "", "gene_name": "FAH", "glycan_count": 1, "glycosylation_sites": [], "id": "P16930", "name": "FAH (Fumarylacetoacetate hydrolase)", "organism": "Homo sapiens", "uniprot_id": "P16930" }, { "function": "Catalyzes the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. It is the rate limiting component in the mammalian NAD biosynthesis pathway. The secreted form behaves both as a cytokine with immunomodulating properties and an adipokine with anti-diabetic properties, it has no enzymatic activity, partly because of lack of activation by ATP, which has a low level in extracellular space and plasma. Plays a role in the modulation of circadian clock function. NAMPT-dependent oscillatory production of NAD regulates oscillation of clock target gene expression by releasing the core clock component: CLOCK-BMAL1 heterodimer from NAD-dependent SIRT1-mediated suppression (By similarity)", "gene_name": "NAMPT", "glycan_count": 1, "glycosylation_sites": [], "id": "P43490", "name": "Visfatin (NAMPT)", "organism": "Homo sapiens", "uniprot_id": "P43490" }, { "function": "Lectin that specifically recognizes microbial carbohydrate chains in a calcium-dependent manner (PubMed:11313366, PubMed:26148048). Binds to microbial glycans that contain a terminal acyclic 1,2-diol moiety, including beta-linked D-galactofuranose (beta-Galf), D-phosphoglycerol-modified glycans, D-glycero-D-talo-oct-2-ulosonic acid (KO) and 3-deoxy-D-manno-oct-2-ulosonic acid (KDO) (PubMed:26148048). Binds to glycans from Gram-positive and Gram-negative bacteria, including K.pneumoniae, S.pneumoniae, Y.pestis, P.mirabilis and P.vulgaris (PubMed:26148048). Does not bind human glycans (PubMed:26148048). Probably plays a role in the defense system against microorganisms (Probable). May function as adipokine that has no effect on basal glucose uptake but enhances insulin-stimulated glucose uptake in adipocytes (PubMed:16531507). Increases AKT phosphorylation in the absence and presence of insulin (PubMed:16531507). May interact with lactoferrin/LTF and increase its uptake, and may thereby play a role in iron absorption (PubMed:11747454, PubMed:23921499)", "gene_name": "ITLN1", "glycan_count": 0, "glycosylation_sites": [ { "position": 163, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8WWA0", "name": "Omentin-1 (Intelectin-1)", "organism": "Homo sapiens", "uniprot_id": "Q8WWA0" }, { "function": "Bifunctional inositol kinase that acts in concert with the IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, exocytosis, insulin signaling and neutrophil activation. Phosphorylates inositol hexakisphosphate (InsP6) at position 1 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively, phosphorylates PP-InsP5 at position 1, produced by IP6Ks from InsP6, to produce (PP)2-InsP4. Activated when cells are exposed to hyperosmotic stress", "gene_name": "PPIP5K1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q6PFW1", "name": "Irisin", "organism": "Homo sapiens", "uniprot_id": "Q6PFW1" }, { "function": "Serine/threonine kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases (By similarity). Its targets include: protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), p70 ribosomal protein S6 kinase (RPS6KB1), p90 ribosomal protein S6 kinase (RPS6KA1, RPS6KA2 and RPS6KA3), cyclic AMP-dependent protein kinase (PRKACA), protein kinase C (PRKCD and PRKCZ), serum and glucocorticoid-inducible kinase (SGK1, SGK2 and SGK3), p21-activated kinase-1 (PAK1), TSSK3, protein kinase PKN (PKN1 and PKN2) (PubMed:11781095). Plays a central role in the transduction of signals from insulin by providing the activating phosphorylation to PKB/AKT1, thus propagating the signal to downstream targets controlling cell proliferation and survival, as well as glucose and amino acid uptake and storage (By similarity). Negatively regulates the TGF-beta-induced signaling by: modulating the association of SMAD3 and SMAD7 with TGF-beta receptor, phosphorylating SMAD2, SMAD3, SMAD4 and SMAD7, preventing the nuclear translocation of SMAD3 and SMAD4 and the translocation of SMAD7 from the nucleus to the cytoplasm in response to TGF-beta (By similarity). Activates PPARG transcriptional activity and promotes adipocyte differentiation (By similarity). Activates the NF-kappa-B pathway via phosphorylation of IKKB (By similarity). The tyrosine phosphorylated form is crucial for the regulation of focal adhesions by angiotensin II (By similarity). Controls proliferation, survival, and growth of developing pancreatic cells (By similarity). Participates in the regulation of Ca(2+) entry and Ca(2+)-activated K(+) channels of mast cells (By similarity). Essential for the motility of vascular endothelial cells (ECs) and is involved in the regulation of their chemotaxis (By similarity). Plays a critical role in cardiac homeostasis by serving as a dual effector for cell survival and beta-adrenergic response (By similarity). Plays an important role during thymocyte development by regulating the expression of key nutrient receptors on the surface of pre-T cells and mediating Notch-induced cell growth and proliferative responses (By similarity). Provides negative feedback inhibition to toll-like receptor-mediated NF-kappa-B activation in macrophages (By similarity)", "gene_name": "Pdpk1", "glycan_count": 0, "glycosylation_sites": [], "id": "O55173", "name": "Cyp8b1", "organism": "Rattus norvegicus", "uniprot_id": "O55173" }, { "function": "UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to facilitate their inactivation and excretion from the body (PubMed:8068691). Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds (PubMed:8068691). Involved in the glucuronidation of arachidonic acid (AA) and AA-derived eicosanoids including 15-HETE and 20-HETE (By similarity). Conjugates small planar phenolic molecules such as 4-nitrophenol, 1-naphthol, and 4-methylumbelliferone. The bulky phenol 4-hydroxybiphenyl, androgens and estrogens are not substrates. 2-hydroxybiphenyl is an excellent substrate (PubMed:8068691). Involved in the glucuronidation of the phytochemical ferulic acid at the phenolic or the carboxylic acid group (By similarity)", "gene_name": "Ugt1a6", "glycan_count": 1, "glycosylation_sites": [ { "position": 293, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 431, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q64435", "name": "Cyp27a1", "organism": "Mus musculus", "uniprot_id": "Q64435" }, { "function": "Destroys radicals which are normally produced within the cells and which are toxic to biological systems", "gene_name": "Sod1", "glycan_count": 2, "glycosylation_sites": [], "id": "P08228", "name": "Superoxide dismutase [Cu-Zn] (SOD1)", "organism": "Mus musculus", "uniprot_id": "P08228" }, { "function": "Catalyzes the reduction of hydroperoxides in a glutathione-dependent manner thus regulating cellular redox homeostasis (PubMed:10754271, PubMed:21420488, PubMed:36608588, PubMed:9126277, PubMed:9195979, PubMed:9712879). Can reduce small soluble hydroperoxides such as H2O2, cumene hydroperoxide and tert-butyl hydroperoxide, as well as several fatty acid-derived hydroperoxides (PubMed:10754271, PubMed:21420488, PubMed:36608588, PubMed:9126277, PubMed:9195979, PubMed:9712879). In platelets catalyzes the reduction of 12-hydroperoxyeicosatetraenoic acid, the primary product of the arachidonate 12-lipoxygenase pathway (PubMed:9195979)", "gene_name": "Gpx1", "glycan_count": 1, "glycosylation_sites": [], "id": "P11352", "name": "Glutathione peroxidase-1 (GPx1)", "organism": "Mus musculus", "uniprot_id": "P11352" }, { "function": "Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) generated by peroxisomal oxidases to water and oxygen, thereby protecting cells from the toxic effects of hydrogen peroxide. Promotes growth of cells including T-cells, B-cells, myeloid leukemia cells, melanoma cells, mastocytoma cells and normal and transformed fibroblast cells", "gene_name": "Cat", "glycan_count": 1, "glycosylation_sites": [], "id": "P24270", "name": "Catalase", "organism": "Mus musculus", "uniprot_id": "P24270" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P16070-variant", "name": "CD44v", "organism": "", "uniprot_id": "" }, { "function": "Catalyzes the ATP-dependent ligation of L-glutamate and L-cysteine and participates in the first and rate-limiting step in glutathione biosynthesis", "gene_name": "GCLC", "glycan_count": 0, "glycosylation_sites": [], "id": "P48506", "name": "GCL", "organism": "Homo sapiens", "uniprot_id": "P48506" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "fragment of Q9UMD9", "name": "Endostatin", "organism": "", "uniprot_id": "" }, { "function": "Bone marrow-derived monocyte and paracrine-acting protein that promotes cardiac myocyte survival and adaptive angiogenesis for cardiac protection and/or repair after myocardial infarction (MI). Stimulates endothelial cell proliferation through a MAPK1/3-, STAT3- and CCND1-mediated signaling pathway. Inhibits cardiac myocyte apoptosis in a PI3K/AKT-dependent signaling pathway (By similarity). Involved in endothelial cell proliferation and angiogenesis (PubMed:25581518)", "gene_name": "MYDGF", "glycan_count": 1, "glycosylation_sites": [], "id": "Q969H8", "name": "Microfibrillar-Associated Protein 4 (MFAP4)", "organism": "Homo sapiens", "uniprot_id": "Q969H8" }, { "function": "Chemoattractant for eosinophils and basophils (PubMed:10415065, PubMed:10488147). Acts as a ligand for C-C chemokine receptor CCR3 which triggers Ca(2+) mobilization in eosinophils (PubMed:10415065, PubMed:10488147, PubMed:11425309). Also acts as a ligand for CX3C chemokine receptor CX3CR1, inducing cell chemotaxis (PubMed:20974991)", "gene_name": "CCL26", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y258", "name": "Eotaxin-1 (CCL11)", "organism": "Homo sapiens", "uniprot_id": "Q9Y258" }, { "function": "Receptor tyrosine kinase involved in the development and the maturation of the central and peripheral nervous systems through regulation of proliferation, differentiation and survival of sympathetic and nervous neurons. High affinity receptor for NGF which is its primary ligand (PubMed:1281417, PubMed:15488758, PubMed:17196528, PubMed:1849459, PubMed:1850821, PubMed:22649032, PubMed:27445338, PubMed:8325889). Can also bind and be activated by NTF3/neurotrophin-3. However, NTF3 only supports axonal extension through NTRK1 but has no effect on neuron survival (By similarity). Upon dimeric NGF ligand-binding, undergoes homodimerization, autophosphorylation and activation (PubMed:1281417). Recruits, phosphorylates and/or activates several downstream effectors including SHC1, FRS2, SH2B1, SH2B2 and PLCG1 that regulate distinct overlapping signaling cascades driving cell survival and differentiation. Through SHC1 and FRS2 activates a GRB2-Ras-MAPK cascade that regulates cell differentiation and survival. Through PLCG1 controls NF-Kappa-B activation and the transcription of genes involved in cell survival. Through SHC1 and SH2B1 controls a Ras-PI3 kinase-AKT1 signaling cascade that is also regulating survival. In absence of ligand and activation, may promote cell death, making the survival of neurons dependent on trophic factors", "gene_name": "NTRK1", "glycan_count": 1, "glycosylation_sites": [ { "position": 67, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 95, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 121, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 188, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 202, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 253, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 262, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 281, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 318, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 323, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 338, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 358, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 401, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P04629", "name": "Tropomyosin receptor kinase A (TrkA)", "organism": "Homo sapiens", "uniprot_id": "P04629" }, { "function": "May play a role in RNA metabolism in both nuclei and mitochondria. In the nucleus binds to HNRPA1-associated poly(A) mRNAs and is part of nmRNP complexes at late stages of mRNA maturation which are possibly associated with nuclear mRNA export. Positively modulates nuclear export of mRNAs containing the EIF4E sensitivity element (4ESE) by binding simultaneously to both EIF4E and the 4ESE and acting as a platform for assembly for the RNA export complex (PubMed:19262567, PubMed:28325843). Also binds to exportin XPO1/CRM1 to engage the nuclear pore and traffic the bound mRNAs to the cytoplasm (PubMed:28325843). May bind mature mRNA in the nucleus outer membrane. In mitochondria binds to poly(A) mRNA. Plays a role in translation or stability of mitochondrially encoded cytochrome c oxidase (COX) subunits. May be involved in transcription regulation. Cooperates with PPARGC1A to regulate certain mitochondrially encoded genes and gluconeogenic genes and may regulate docking of PPARGC1A to transcription factors. Seems to be involved in the transcription regulation of the multidrug-related genes MDR1 and MVP. Part of a nuclear factor that binds to the invMED1 element of MDR1 and MVP gene promoters. Binds single-stranded DNA (By similarity). Required for maintaining mitochondrial potential (PubMed:23822101). Suppresses the initiation of basal levels of autophagy and mitophagy by sustaining BCL2 levels (PubMed:23822101)", "gene_name": "LRPPRC", "glycan_count": 2, "glycosylation_sites": [], "id": "P42704", "name": "LRPPRC", "organism": "Homo sapiens", "uniprot_id": "P42704" }, { "function": "Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2) (PubMed:9497357). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity)", "gene_name": "PRDX1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q06830", "name": "PRDX1", "organism": "Homo sapiens", "uniprot_id": "Q06830" }, { "function": "May function as a scaffold on which the coordinated assembly of proteins can occur. May play a role as an adapter that, via its PDZ domain, localizes LIM-binding proteins to actin filaments of both skeletal muscle and nonmuscle tissues. Involved in both of the two fundamental mechanisms of bone formation, direct bone formation (e.g. embryonic flat bones mandible and cranium), and endochondral bone formation (e.g. embryonic long bone development). Plays a role during fracture repair. Involved in BMP6 signaling pathway (By similarity)", "gene_name": "PDLIM7", "glycan_count": 4, "glycosylation_sites": [], "id": "Q9NR12", "name": "PDLIM1", "organism": "Homo sapiens", "uniprot_id": "Q9NR12" }, { "function": "F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (Probable). Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation (PubMed:15772161). Involved in tight junction assembly in epithelial cells probably through interaction with MICALL2. Links MICALL2 to the actin cytoskeleton and recruits it to the tight junctions (By similarity). May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA (PubMed:22351778). Association with IGSF8 regulates the immune synapse formation and is required for efficient T-cell activation (PubMed:22689882)", "gene_name": "ACTN4", "glycan_count": 2, "glycosylation_sites": [], "id": "O43707", "name": "ACTN4", "organism": "Homo sapiens", "uniprot_id": "O43707" }, { "function": "Essential acyltransferase that catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for synthesis and storage of intracellular triglycerides (PubMed:27184406). Probably plays a central role in cytosolic lipid accumulation. In liver, is primarily responsible for incorporating endogenously synthesized fatty acids into triglycerides (By similarity). Also functions as an acyl-CoA retinol acyltransferase (ARAT) (By similarity). Also able to use 1-monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG) (PubMed:28420705)", "gene_name": "DGAT2", "glycan_count": 6, "glycosylation_sites": [], "id": "Q96PD7", "name": "Interleukin-17F (IL-17F)", "organism": "Homo sapiens", "uniprot_id": "Q96PD7" }, { "function": "Glycinin is the major seed storage protein of soybean (PubMed:2485233). Glycinin basic peptides (GBPs), and, to a lower extent, glycinin exhibit antibacterial activity against Gram-negative and Gram-positive bacteria (e.g. L.monocytogenes, B.subtilis, E.coli and S.enteritidis) by forming pores and aggregating in transmembranes, leading to membrane permeability and, eventually, cell death (PubMed:22236762, PubMed:28590128, Ref.15)", "gene_name": "GY1", "glycan_count": 0, "glycosylation_sites": [], "id": "P04776", "name": "Apolipoprotein A1 (APOA1)", "organism": "Glycine max", "uniprot_id": "P04776" }, { "function": "May have a role in chylomicrons and VLDL secretion and catabolism. Required for efficient activation of lipoprotein lipase by ApoC-II; potent activator of LCAT. Apoa-IV is a major component of HDL and chylomicrons", "gene_name": "Apoa4", "glycan_count": 0, "glycosylation_sites": [], "id": "P02651", "name": "Apolipoprotein A2 (APOA2)", "organism": "Rattus norvegicus", "uniprot_id": "P02651" }, { "function": "Receptor for the hormone galanin, GALP and spexin-1. The activity of this receptor is mediated by G proteins that activate the phospholipase C/protein kinase C pathway (via G(q)) and that inhibit adenylyl cyclase (via G(i))", "gene_name": "Galr2", "glycan_count": 0, "glycosylation_sites": [ { "position": 2, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Z2B0", "name": "Phosphatidylserine synthase 1 (PTDSS1)", "organism": "Mus musculus", "uniprot_id": "O88854" }, { "function": "Catalyzes the conversion of (3S)-hydroxy-3-methylglutaryl-CoA (HMG-CoA) to mevalonic acid, the rate-limiting step in the synthesis of cholesterol and other isoprenoids, thus plays a critical role in cellular cholesterol homeostasis", "gene_name": "Hmgcr", "glycan_count": 1, "glycosylation_sites": [ { "position": 281, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q01237", "name": "3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR)", "organism": "Mus musculus", "uniprot_id": "Q01237" }, { "function": "Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) and in neurons (Ih) (PubMed:10962006, PubMed:11096117, PubMed:11459060, PubMed:11741901, PubMed:12034718, PubMed:12193608, PubMed:12968185, PubMed:17562314, PubMed:21347269, PubMed:21903816, PubMed:23103389). Can also transport ammonium in the distal nephron (By similarity). Involved in the initiation of neuropathic pain in sensory neurons (PubMed:21903816)", "gene_name": "Hcn2", "glycan_count": 0, "glycosylation_sites": [ { "position": 380, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O70506", "name": "3-hydroxy-3-methylglutaryl-CoA synthase 2 (HMGCS2)", "organism": "Mus musculus", "uniprot_id": "O88703" }, { "function": "Involved in the intramitochondrial synthesis of acylcarnitines from accumulated acyl-CoA metabolites. Reconverts acylcarnitines back into the respective acyl-CoA esters that can then undergo beta-oxidation, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion. Active with medium (C8-C12) and long-chain (C14-C18) acyl-CoA esters", "gene_name": "Cpt2", "glycan_count": 2, "glycosylation_sites": [], "id": "P52825", "name": "Carnitine palmitoyltransferase 2 (CPT2)", "organism": "Mus musculus", "uniprot_id": "P52825" }, { "function": "DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK3 is a negative regulator of JNK signaling in B-cells through interaction with INPP5D/SHIP1. May modulate ABL1 function", "gene_name": "Dok3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9QZK7", "name": "Acyl-CoA thioesterase 2 (ACOT2)", "organism": "Mus musculus", "uniprot_id": "Q9QZK7" }, { "function": "Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Within the 20S core complex, PSMB7 displays a trypsin-like activity", "gene_name": "Psmb7", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9JHW0", "name": "Acetyl-CoA acyltransferase 1b (ACAA1B)", "organism": "Rattus norvegicus", "uniprot_id": "Q9JHW0" }, { "function": "Bifunctional enzyme which catalyzes both the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation, and the conjugation of glutathione with a wide range of aryl halides and organic isothiocyanates. Also exhibits low glutathione-peroxidase activity", "gene_name": "Hpgds", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9JHF7", "name": "3-hydroxy-3-methylglutaryl-CoA lyase (HMGCL)", "organism": "Mus musculus", "uniprot_id": "Q9JHF7" }, { "function": "This is a receptor for GIP. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase", "gene_name": "GIPR", "glycan_count": 0, "glycosylation_sites": [ { "position": 62, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 77, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P48546", "name": "GIP receptor", "organism": "Homo sapiens", "uniprot_id": "P48546" }, { "function": "G-protein coupled receptor for glucagon that plays a central role in the regulation of blood glucose levels and glucose homeostasis. Regulates the rate of hepatic glucose production by promoting glycogen hydrolysis and gluconeogenesis. Plays an important role in mediating the responses to fasting. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Promotes activation of adenylate cyclase. Besides, plays a role in signaling via a phosphatidylinositol-calcium second messenger system", "gene_name": "GCGR", "glycan_count": 0, "glycosylation_sites": [ { "position": 46, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 59, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 74, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 78, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P47871", "name": "Glucagon receptor", "organism": "Homo sapiens", "uniprot_id": "P47871" }, { "function": "This gut peptide inhibits exocrine pancreatic secretion, has a vasoconstrictory action and inhibitis jejunal and colonic mobility", "gene_name": "PYY", "glycan_count": 0, "glycosylation_sites": [], "id": "P10082", "name": "Peptide YY", "organism": "Homo sapiens", "uniprot_id": "P10082" }, { "function": "ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2)", "gene_name": "ICAM5", "glycan_count": 5, "glycosylation_sites": [ { "position": 54, "type": "N-linked (GlcNAc...) (high mannose) asparagine" }, { "position": 74, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 137, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 195, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 214, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 303, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 316, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 371, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 397, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 583, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 646, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 764, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 795, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 796, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UMF0", "name": "ICAM5", "organism": "Homo sapiens", "uniprot_id": "Q9UMF0" }, { "function": "Catalyzes the deimination of arginine residues of proteins", "gene_name": "PADI2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y2J8", "name": "PAD2", "organism": "Homo sapiens", "uniprot_id": "Q9Y2J8" }, { "function": "Binds sialylated glycoproteins", "gene_name": "SIGLEC15", "glycan_count": 0, "glycosylation_sites": [ { "position": 172, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6ZMC9", "name": "Siglec-14", "organism": "Homo sapiens", "uniprot_id": "Q6ZMC9" }, { "function": "Required for ovarian folliculogenesis. Promotes primordial follicle development. Stimulates granulosa cell proliferation. Promotes cell transition from G0/G1 to S and G2/M phases, through an increase of CCND1 and CCNE1 expression, and RB1 phosphorylation. It regulates STAR expression and cAMP-dependent progesterone release in granulosa and thecal cells. Attenuates the suppressive effects of activin A on STAR expression and progesterone production by increasing the expression of inhibin B. It suppresses FST and FSTL3 production in granulosa-lutein cells", "gene_name": "GDF9", "glycan_count": 0, "glycosylation_sites": [ { "position": 106, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 163, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 236, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 255, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 268, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 338, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O60383", "name": "GDF9", "organism": "Homo sapiens", "uniprot_id": "O60383" }, { "function": "Required for maintaining the proliferative activity of embryonic cardiomyocytes by preventing premature activation of the negative cell cycle regulator CDKN1C/p57KIP and maintaining the required expression levels of cardiogenic factors such as MEF2C and NKX2-5. Acts as a ligand for ACVRL1/ALK1, BMPR1A/ALK3 and BMPR1B/ALK6, leading to activation of SMAD1, SMAD5 and SMAD8 transcription factors. Inhibits endothelial cell migration and growth. May reduce cell migration and cell matrix adhesion in breast cancer cell lines", "gene_name": "BMP10", "glycan_count": 0, "glycosylation_sites": [ { "position": 67, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 131, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O95393", "name": "BMP15", "organism": "Homo sapiens", "uniprot_id": "O95393" }, { "function": "Receptor for Wnt proteins. Component of the Wnt-Fzd-LRP5-LRP6 complex that triggers beta-catenin signaling through inducing aggregation of receptor-ligand complexes into ribosome-sized signalosomes. The beta-catenin canonical signaling pathway leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Coreceptor along with RYK of Wnt proteins, such as WNT1", "gene_name": "FZD8", "glycan_count": 1, "glycosylation_sites": [ { "position": 49, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 152, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 475, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9H461", "name": "Frizzled family receptor 7 (FZD7)", "organism": "Homo sapiens", "uniprot_id": "Q9H461" }, { "function": "Receptor for adenosine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase", "gene_name": "ADORA2B", "glycan_count": 0, "glycosylation_sites": [ { "position": 153, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 163, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P29275", "name": "A2B adenosine receptor (ADORA2B)", "organism": "Homo sapiens", "uniprot_id": "P29275" }, { "function": "Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred substrates. The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A. Also able to hydrolyze 5-phosphoribose 1-diphosphate", "gene_name": "NUDT10", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8NFP7", "name": "\u03b2-1,4-N-acetylglucosaminyltransferase 2 (POMGNT2)", "organism": "Homo sapiens", "uniprot_id": "Q8NFP7" }, { "function": "Endoglycosidase that cleaves heparan sulfate proteoglycans (HSPGs) into heparan sulfate side chains and core proteoglycans. Participates in extracellular matrix (ECM) degradation and remodeling. Selectively cleaves the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying either a 3-O-sulfo or a 6-O-sulfo group. Can also cleave the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying a 2-O-sulfo group, but not linkages between a glucuronic acid unit and a 2-O-sulfated iduronic acid moiety. It is essentially inactive at neutral pH but becomes active under acidic conditions such as during tumor invasion and in inflammatory processes. Facilitates cell migration associated with metastasis, wound healing and inflammation. Enhances shedding of syndecans, and increases endothelial invasion and angiogenesis in myelomas. Acts as a procoagulant by increasing the generation of activation factor X in the presence of tissue factor and activation factor VII. Increases cell adhesion to the extracellular matrix (ECM), independent of its enzymatic activity. Induces AKT1/PKB phosphorylation via lipid rafts increasing cell mobility and invasion. Heparin increases this AKT1/PKB activation. Regulates osteogenesis. Enhances angiogenesis through up-regulation of SRC-mediated activation of VEGF. Implicated in hair follicle inner root sheath differentiation and hair homeostasis", "gene_name": "HPSE", "glycan_count": 8, "glycosylation_sites": [ { "position": 162, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 178, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 200, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 217, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 238, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 459, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y251", "name": "Heparanase (HPSE)", "organism": "Homo sapiens", "uniprot_id": "Q9Y251" }, { "function": "Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER) (PubMed:10788476). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules (By similarity)", "gene_name": "SEC31A", "glycan_count": 3, "glycosylation_sites": [], "id": "O94979", "name": "SEC31A", "organism": "Homo sapiens", "uniprot_id": "O94979" }, { "function": "Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Covalently attached to the voltage-gated potassium channel KCNB1; this modulates the gating characteristics of KCNB1 (PubMed:19223394). Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development. Covalently attached to ZFHX3 (PubMed:24651376)", "gene_name": "SUMO1", "glycan_count": 2, "glycosylation_sites": [], "id": "P63165", "name": "Small ubiquitin-like modifier 1 (SUMO1)", "organism": "Homo sapiens", "uniprot_id": "P63165" }, { "function": "Growth factor of the TGF-beta superfamily that plays essential roles in many developmental processes, including cardiogenesis, neurogenesis, and osteogenesis (PubMed:18436533, PubMed:24362451, PubMed:31019025). Induces cartilage and bone formation (PubMed:3201241). Initiates the canonical BMP signaling cascade by associating with type I receptor BMPR1A and type II receptor BMPR2 (PubMed:15064755, PubMed:17295905, PubMed:18436533). Once all three components are bound together in a complex at the cell surface, BMPR2 phosphorylates and activates BMPR1A (PubMed:7791754). In turn, BMPR1A propagates signal by phosphorylating SMAD1/5/8 that travel to the nucleus and act as activators and repressors of transcription of target genes. Also acts to promote expression of HAMP, via the interaction with its receptor BMPR1A/ALK3 (PubMed:31800957). Can also signal through non-canonical pathways such as ERK/MAP kinase signaling cascade that regulates osteoblast differentiation (PubMed:16771708, PubMed:20851880). Also stimulates the differentiation of myoblasts into osteoblasts via the EIF2AK3-EIF2A-ATF4 pathway by stimulating EIF2A phosphorylation which leads to increased expression of ATF4 which plays a central role in osteoblast differentiation (PubMed:24362451). Acts as a positive regulator of odontoblast differentiation during mesenchymal tooth germ formation, expression is repressed during the bell stage by MSX1-mediated inhibition of CTNNB1 signaling (By similarity)", "gene_name": "BMP2", "glycan_count": 3, "glycosylation_sites": [ { "position": 135, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 163, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 164, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 200, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 338, "type": "N-linked (GlcNAc...) (high mannose) asparagine" } ], "id": "P12643", "name": "BMP2", "organism": "Homo sapiens", "uniprot_id": "P12643" }, { "function": "Growth factor of the TGF-beta superfamily that plays important role in various biological processes, including embryogenesis, hematopoiesis, neurogenesis and skeletal morphogenesis (PubMed:31208997). Initiates the canonical BMP signaling cascade by associating with type I receptor ACVR1 and type II receptor ACVR2A (PubMed:12667445, PubMed:9748228). Once all three components are bound together in a complex at the cell surface, ACVR2A phosphorylates and activates ACVR1. In turn, ACVR1 propagates signal by phosphorylating SMAD1/5/8 that travel to the nucleus and act as activators and repressors of transcription of target genes (PubMed:12478285). For specific functions such as growth cone collapse in developing spinal neurons and chemotaxis of monocytes, also uses BMPR2 as type II receptor (PubMed:31208997). Can also signal through non-canonical pathways such as P38 MAP kinase signaling cascade that promotes brown adipocyte differentiation through activation of target genes, including members of the SOX family of transcription factors (PubMed:27923061). Promotes the expression of HAMP, this is repressed by its interaction with ERFE (PubMed:30097509)", "gene_name": "BMP7", "glycan_count": 5, "glycosylation_sites": [ { "position": 187, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 302, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 321, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 372, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P18075", "name": "BMP7", "organism": "Homo sapiens", "uniprot_id": "P18075" }, { "function": "Plays an important role in the regulation of embryonic development, cell proliferation and cell differentiation. Required for normal branching morphogenesis. May play a role in wound healing", "gene_name": "FGF10", "glycan_count": 0, "glycosylation_sites": [ { "position": 51, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 196, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O15520", "name": "FGF10", "organism": "Homo sapiens", "uniprot_id": "O15520" }, { "function": "Calcium-binding protein. Binds one calcium ion per monomer (PubMed:17030513). Can promote differentiation of adipocytes (in vitro) (By similarity). Overexpression in preadipocytes increases their proliferation, enhances adipogenesis and reduces insulin-stimulated glucose uptake (By similarity)", "gene_name": "S100A16", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96FQ6", "name": "S100A16", "organism": "Homo sapiens", "uniprot_id": "Q96FQ6" }, { "function": "In vitro binds long double-stranded RNA (dsRNA) (500 and 700 base pairs), but not dsRNA shorter than 300 bp. Not involved in RNA autophagy, a process in which RNA is directly imported into lysosomes in an ATP-dependent manner, and degraded", "gene_name": "SIDT1", "glycan_count": 0, "glycosylation_sites": [ { "position": 57, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 67, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 83, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 136, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 282, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 471, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 567, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 764, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NXL6", "name": "SIDT1", "organism": "Homo sapiens", "uniprot_id": "Q9NXL6" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "fragment of P08571", "name": "Presepsin (sCD14-ST)", "organism": "", "uniprot_id": "" }, { "function": "Secreted ribonuclease that can either promote or restrict cell proliferation of target cells, depending on the context (PubMed:12051708, PubMed:1400510, PubMed:19332886, PubMed:20129916, PubMed:21855800, PubMed:23047679, PubMed:23843625, PubMed:2424496, PubMed:2459697, PubMed:2730651, PubMed:27518564, PubMed:28176817, PubMed:29100074, PubMed:29748193, PubMed:3122207, PubMed:32510170, PubMed:38718836, PubMed:8159680, PubMed:8570639, PubMed:8622921, PubMed:9578571). Endocytosed in target cells via its receptor PLXNB2 and translocates to the cytoplasm or nucleus (PubMed:29100074, PubMed:32510170). Under stress conditions, localizes to the cytoplasm and promotes the assembly of stress granules (SGs): specifically cleaves a subset of tRNAs within anticodon loops to produce tRNA-derived stress-induced fragments (tiRNAs), resulting in translation repression and inhibition of cell proliferation (PubMed:1400510, PubMed:19332886, PubMed:20129916, PubMed:21855800, PubMed:23047679, PubMed:27518564, PubMed:29100074, PubMed:29748193, PubMed:32510170, PubMed:38718836). tiRNas also prevent formation of apoptosome, thereby promoting cell survival (By similarity). Preferentially cleaves RNAs between a pyrimidine and an adenosine residue, suggesting that it cleaves the anticodon loop of tRNA(Ala) (32-UUAGCAU-38) after positions 33 and 36 (PubMed:3289612, PubMed:38718836). Cleaves a subset of tRNAs, including tRNA(Ala), tRNA(Glu), tRNA(Gly), tRNA(Lys), tRNA(Val), tRNA(His), tRNA(Asp) and tRNA(Sec) (PubMed:31582561). Under growth conditions and in differentiated cells, translocates to the nucleus and stimulates ribosomal RNA (rRNA) transcription, including that containing the initiation site sequences of 45S rRNA, thereby promoting cell growth and proliferation (PubMed:12051708, PubMed:15735021, PubMed:27518564, PubMed:29100074, PubMed:8127865). Angiogenin induces vascularization of normal and malignant tissues via its ability to promote rRNA transcription (PubMed:19354288, PubMed:4074709, PubMed:8448182). Involved in hematopoietic stem and progenitor cell (HSPC) growth and survival by promoting rRNA transcription in growth conditions and inhibiting translation in response to stress, respectively (PubMed:27518564). Mediates the crosstalk between myeloid and intestinal epithelial cells to protect the intestinal epithelial barrier integrity: secreted by myeloid cells and promotes intestinal epithelial cells proliferation and survival (PubMed:32510170). Also mediates osteoclast-endothelial cell crosstalk in growing bone: produced by osteoclasts and protects the neighboring vascular cells against senescence by promoting rRNA transcription (By similarity)", "gene_name": "ANG", "glycan_count": 1, "glycosylation_sites": [], "id": "P03950", "name": "Angiogenin (RNase 5)", "organism": "Homo sapiens", "uniprot_id": "P03950" }, { "function": "Cleaves preferentially after uridine bases (PubMed:3467790). Has antimicrobial activity against uropathogenic E.coli (UPEC) (PubMed:33818125). Probably contributes to urinary tract sterility (PubMed:33818125)", "gene_name": "RNASE4", "glycan_count": 0, "glycosylation_sites": [], "id": "P34096", "name": "RNase 4", "organism": "Homo sapiens", "uniprot_id": "P34096" }, { "function": "Transmembrane metalloprotease whose catalytic activity is critical for processing lamin A/LMNA on the inner nuclear membrane and clearing clogged translocons on the endoplasmic reticulum (PubMed:33293369, PubMed:33315887). Proteolytically removes the C-terminal three residues of farnesylated proteins (PubMed:33293369, PubMed:33315887). Also plays an antiviral role independently of its protease activity by restricting enveloped RNA and DNA viruses, including influenza A, Zika, Ebola, Sindbis, vesicular stomatitis, cowpox, and vaccinia (PubMed:28169297, PubMed:28246125). Mechanistically, controls IFITM antiviral pathway to hinder viruses from breaching the endosomal barrier by modulating membrane fluidity (PubMed:35283811)", "gene_name": "ZMPSTE24", "glycan_count": 1, "glycosylation_sites": [], "id": "O75844", "name": "ZMPSTE24", "organism": "Homo sapiens", "uniprot_id": "O75844" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P45973/P23179/Q13185", "name": "HP1 (Heterochromatin Protein 1)", "organism": "", "uniprot_id": "" }, { "function": "Histone methyltransferase. Methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones (PubMed:12123582). Binds to DNA (PubMed:12628190)", "gene_name": "DOT1L", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8TEK3", "name": "DOT1L", "organism": "Homo sapiens", "uniprot_id": "Q8TEK3" }, { "function": "Regulatory component of the cyclin D2-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition (PubMed:18827403, PubMed:8114739). Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase (PubMed:18827403, PubMed:8114739). Hypophosphorylates RB1 in early G(1) phase (PubMed:18827403, PubMed:8114739). Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals (PubMed:18827403, PubMed:8114739)", "gene_name": "CCND2", "glycan_count": 0, "glycosylation_sites": [], "id": "P30279", "name": "Cyclin D2", "organism": "Homo sapiens", "uniprot_id": "P30279" }, { "function": "Cytokine that binds to TNFRSF4. Co-stimulates T-cell proliferation and cytokine production", "gene_name": "TNFSF4", "glycan_count": 0, "glycosylation_sites": [ { "position": 90, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 114, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 152, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 157, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P23510", "name": "Tax-transcriptionally activated glycoprotein 1, 34 kD (TNFSF4/OX40L)", "organism": "Homo sapiens", "uniprot_id": "P23510" }, { "function": "Methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability (PubMed:12237300, PubMed:16497732, PubMed:19405910). Recruited to promoters upon gene activation together with histone acetyltransferases from EP300/P300 and p160 families, methylates histone H3 at 'Arg-17' (H3R17me), forming mainly asymmetric dimethylarginine (H3R17me2a), leading to activation of transcription via chromatin remodeling (PubMed:12237300, PubMed:16497732, PubMed:19405910). During nuclear hormone receptor activation and TCF7L2/TCF4 activation, acts synergically with EP300/P300 and either one of the p160 histone acetyltransferases NCOA1/SRC1, NCOA2/GRIP1 and NCOA3/ACTR or CTNNB1/beta-catenin to activate transcription (By similarity). During myogenic transcriptional activation, acts together with NCOA3/ACTR as a coactivator for MEF2C (By similarity). During monocyte inflammatory stimulation, acts together with EP300/P300 as a coactivator for NF-kappa-B (By similarity). Acts as a coactivator for PPARG, promotes adipocyte differentiation and the accumulation of brown fat tissue (By similarity). Plays a role in the regulation of pre-mRNA alternative splicing by methylation of splicing factors (By similarity). Also seems to be involved in p53/TP53 transcriptional activation (By similarity). Methylates EP300/P300, both at 'Arg-2142', which may loosen its interaction with NCOA2/GRIP1, and at 'Arg-580' and 'Arg-604' in the KIX domain, which impairs its interaction with CREB and inhibits CREB-dependent transcriptional activation (PubMed:15731352). Also methylates arginine residues in RNA-binding proteins PABPC1, ELAVL1 and ELAV4, which may affect their mRNA-stabilizing properties and the half-life of their target mRNAs (By similarity). Acts as a transcriptional coactivator of ACACA/acetyl-CoA carboxylase by enriching H3R17 methylation at its promoter, thereby positively regulating fatty acid synthesis (By similarity). Independently of its methyltransferase activity, involved in replication fork progression: promotes PARP1 recruitment to replication forks, leading to poly-ADP-ribosylation of chromatin at replication forks and reduced fork speed (PubMed:33412112)", "gene_name": "CARM1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q86X55", "name": "CARM1 (PRMT4)", "organism": "Homo sapiens", "uniprot_id": "Q86X55" }, { "function": "Carries out a dual function: signal transduction and activation of transcription. Mediates cellular responses to the cytokine KITLG/SCF and other growth factors. Mediates cellular responses to ERBB4. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Binds to the GAS element and activates PRL-induced transcription. Regulates the expression of milk proteins during lactation", "gene_name": "STAT5A", "glycan_count": 1, "glycosylation_sites": [], "id": "P42229", "name": "STAT5", "organism": "Homo sapiens", "uniprot_id": "P42229" }, { "function": "Involved in the fragmentation of the mitochondrial network and its perinuclear clustering (PubMed:12783892, PubMed:12861026, PubMed:14996942, PubMed:23283981). Plays a minor role in the recruitment and association of the fission mediator dynamin-related protein 1 (DNM1L) to the mitochondrial surface and mitochondrial fission (PubMed:12861026, PubMed:16118244, PubMed:23283981, PubMed:23530241, PubMed:24196833). May not be essential for the assembly of functional fission complexes and the subsequent membrane scission event (PubMed:23530241, PubMed:24196833). Also mediates peroxisomal fission (PubMed:16107562). May act when the products of fission are directed toward mitochondrial homeostasis, mitophagy, or apoptosis (PubMed:24196833). Can induce cytochrome c release from the mitochondrion to the cytosol, ultimately leading to apoptosis (PubMed:12783892)", "gene_name": "FIS1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y3D6", "name": "NAPB (NSF-attachment protein \u03b2)", "organism": "Homo sapiens", "uniprot_id": "Q9Y3D6" }, { "function": "Catalyzes the NAD-dependent oxidation of the highly active 17beta-hydroxysteroids, such as estradiol (E2), testosterone (T), and dihydrotestosterone (DHT), to their less active forms and thus regulates the biological potency of these steroids. Oxidizes estradiol to estrone, testosterone to androstenedione, and dihydrotestosterone to 5alpha-androstan-3,17-dione. Also has 20-alpha-HSD activity", "gene_name": "HSD17B2", "glycan_count": 0, "glycosylation_sites": [], "id": "P37059", "name": "HSD17B10 (17\u03b2-HSD)", "organism": "Homo sapiens", "uniprot_id": "P37059" }, { "function": "Induces apoptosis. Interacts with viral and cellular anti-apoptosis proteins. Can overcome the suppressors BCL-2 and BCL-XL, although high levels of BCL-XL expression will inhibit apoptosis. Inhibits apoptosis induced by BNIP3. Involved in mitochondrial quality control via its interaction with SPATA18/MIEAP: in response to mitochondrial damage, participates in mitochondrial protein catabolic process (also named MALM) leading to the degradation of damaged proteins inside mitochondria. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix. May function as a tumor suppressor", "gene_name": "BNIP3L", "glycan_count": 1, "glycosylation_sites": [], "id": "O60238", "name": "BNIP3L", "organism": "Homo sapiens", "uniprot_id": "O60238" }, { "function": "Hormone secreted by pancreatic cells that acts as a regulator of pancreatic and gastrointestinal functions probably by signaling through the G protein-coupled receptor NPY4R2", "gene_name": "PPY", "glycan_count": 0, "glycosylation_sites": [], "id": "P01298", "name": "Pancreatic Polypeptide (PP)", "organism": "Homo sapiens", "uniprot_id": "P01298" }, { "function": "Gastrin stimulates the stomach mucosa to produce and secrete hydrochloric acid and the pancreas to secrete its digestive enzymes. It also stimulates smooth muscle contraction and increases blood circulation and water secretion in the stomach and intestine", "gene_name": "GAST", "glycan_count": 1, "glycosylation_sites": [], "id": "P01350", "name": "Gastrin", "organism": "Homo sapiens", "uniprot_id": "P01350" }, { "function": "Inhibits the secretion of pituitary hormones, including that of growth hormone/somatotropin (GH1), PRL, ACTH, luteinizing hormone (LH) and TSH. Also impairs ghrelin- and GnRH-stimulated secretion of GH1 and LH; the inhibition of ghrelin-stimulated secretion of GH1 can be further increased by neuronostatin", "gene_name": "SST", "glycan_count": 0, "glycosylation_sites": [], "id": "P61278", "name": "Somatostatin", "organism": "Homo sapiens", "uniprot_id": "P61278" }, { "function": "VIP is a neuropeptide involved in a diverse array of physiological processes through activating the PACAP subfamily of class B1 G protein-coupled receptors: VIP receptor 1 (VPR1) and VIP receptor 2 (VPR2) (PubMed:1318039, PubMed:36385145, PubMed:8933357). Abundantly expressed throughout the CNS and peripheral nervous systems where they primarily exert neuroprotective and immune modulatory roles (PubMed:3456568). Also causes vasodilation, lowers arterial blood pressure, stimulates myocardial contractility, increases glycogenolysis and relaxes the smooth muscle of trachea, stomach and gall bladder (PubMed:15013843)", "gene_name": "VIP", "glycan_count": 0, "glycosylation_sites": [], "id": "P01282", "name": "Vasoactive Intestinal Peptide (VIP)", "organism": "Homo sapiens", "uniprot_id": "P01282" }, { "function": "F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein", "gene_name": "ACTN2", "glycan_count": 1, "glycosylation_sites": [], "id": "P35609", "name": "Actin-related protein 3 (ACTR3)", "organism": "Homo sapiens", "uniprot_id": "P35609" }, { "function": "S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methyluridine at position 1369 (Um1369) in the 16S mitochondrial large subunit ribosomal RNA (mtLSU rRNA), a universally conserved modification in the peptidyl transferase domain of the mtLSU rRNA (PubMed:25009282, PubMed:25074936, PubMed:35177605). This activity may require prior 2'-O-methylguanosine modification at position 1370 (Gm1370) by MRM3 (PubMed:35177605). Essential for late-stage assembly of mtLSU required for efficient translation of mitochondrial DNA encoded proteins; methyltransferase activity is not required for this function (PubMed:35177605). Essential for mitochondrial respiratory function (PubMed:35177605)", "gene_name": "MRM2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UI43", "name": "Cav3.1 (CACNA1G)", "organism": "Homo sapiens", "uniprot_id": "Q9UI43" }, { "function": "Intermediate conductance calcium-activated potassium channel that mediates the voltage-independent transmembrane transfer of potassium across the cell membrane through a constitutive interaction with calmodulin which binds the intracellular calcium allowing its opening (PubMed:10026195, PubMed:10961988, PubMed:11425865, PubMed:15831468, PubMed:17157250, PubMed:18796614, PubMed:26148990, PubMed:9326665, PubMed:9380751, PubMed:9407042). The current is characterized by a voltage-independent activation, an intracellular calcium concentration increase-dependent activation and a single-channel conductance of about 25 picosiemens (PubMed:9326665, PubMed:9380751, PubMed:9407042). Also presents an inwardly rectifying current, thus reducing its already small outward conductance of potassium ions, which is particularly the case when the membrane potential displays positive values, above + 20 mV (PubMed:9326665, PubMed:9380751, PubMed:9407042). Controls calcium influx during vascular contractility by being responsible of membrane hyperpolarization induced by vasoactive factors in proliferative vascular smooth muscle cell types (By similarity). Following calcium influx, the consecutive activation of KCNN4 channel leads to a hyperpolarization of the cell membrane potential and hence an increase of the electrical driving force for further calcium influx promoting sustained calcium entry in response to stimulation with chemotactic peptides (PubMed:26418693). Required for maximal calcium influx and proliferation during the reactivation of naive T-cells (PubMed:17157250, PubMed:18796614). Plays a role in the late stages of EGF-induced macropinocytosis through activation by PI(3)P (PubMed:24591580)", "gene_name": "KCNN4", "glycan_count": 1, "glycosylation_sites": [], "id": "O15554", "name": "KCa3.1 (KCNN4)", "organism": "Homo sapiens", "uniprot_id": "O15554" }, { "function": "Catalyzes the hydroxylation of dopamine to noradrenaline (also known as norepinephrine), and is thus vital for regulation of these neurotransmitters", "gene_name": "DBH", "glycan_count": 13, "glycosylation_sites": [ { "position": 64, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 184, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 344, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 566, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P09172", "name": "Dopamine beta-hydroxylase", "organism": "Homo sapiens", "uniprot_id": "P09172" }, { "function": "Key regulator of cell-cell adhesion that associates with and regulates the cell adhesion properties of both C-, E- and N-cadherins, being critical for their surface stability (PubMed:14610055, PubMed:20371349). Promotes localization and retention of DSG3 at cell-cell junctions, via its interaction with DSG3 (PubMed:18343367). Beside cell-cell adhesion, regulates gene transcription through several transcription factors including ZBTB33/Kaiso2 and GLIS2, and the activity of Rho family GTPases and downstream cytoskeletal dynamics (PubMed:10207085, PubMed:20371349). Implicated both in cell transformation by SRC and in ligand-induced receptor signaling through the EGF, PDGF, CSF-1 and ERBB2 receptors (PubMed:17344476)", "gene_name": "CTNND1", "glycan_count": 5, "glycosylation_sites": [], "id": "O60716", "name": "CTNND1 (delta-catenin)", "organism": "Homo sapiens", "uniprot_id": "O60716" }, { "function": "HMG-I/Y bind preferentially to the minor groove of A+T rich regions in double-stranded DNA. It is suggested that these proteins could function in nucleosome phasing and in the 3'-end processing of mRNA transcripts. They are also involved in the transcription regulation of genes containing, or in close proximity to A+T-rich regions", "gene_name": "HMGA1", "glycan_count": 1, "glycosylation_sites": [], "id": "P17096", "name": "HMGA1 (High mobility group protein A1)", "organism": "Homo sapiens", "uniprot_id": "P17096" }, { "function": "Orphan receptor that binds DNA as a monomer to hormone response elements (HRE) containing an extended core motif half-site sequence 5'-AAGGTCA-3' in which the 5' flanking nucleotides participate in determining receptor specificity (By similarity). May be required to pattern anterior brain differentiation. Involved in the regulation of retinal development and essential for vision. During retinogenesis, regulates PTEN-Cyclin D expression via binding to the promoter region of PTEN and suppressing its activity (By similarity). May be involved in retinoic acid receptor (RAR) regulation in retinal cells", "gene_name": "NR2E1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y466", "name": "RBFOX2 (RNA-binding protein fox-1 homolog 2)", "organism": "Homo sapiens", "uniprot_id": "Q9Y466" }, { "function": "Mediates pre-mRNA alternative splicing regulation. Acts either as activator or repressor of splicing on specific pre-mRNA targets. Inhibits cardiac troponin-T (TNNT2) pre-mRNA exon inclusion but induces insulin receptor (IR) pre-mRNA exon inclusion in muscle. Antagonizes the alternative splicing activity pattern of CELF proteins. Regulates the TNNT2 exon 5 skipping through competition with U2AF2. Inhibits the formation of the spliceosome A complex on intron 4 of TNNT2 pre-mRNA. Binds to the stem-loop structure within the polypyrimidine tract of TNNT2 intron 4 during spliceosome assembly. Binds to the 5'-YGCU(U/G)Y-3'consensus sequence. Binds to the IR RNA. Binds to expanded CUG repeat RNA, which folds into a hairpin structure containing GC base pairs and bulged, unpaired U residues. Together with RNA binding proteins RBPMS and RBFOX2, activates vascular smooth muscle cells alternative splicing events (PubMed:37548402). Regulates NCOR2 alternative splicing (By similarity)", "gene_name": "MBNL1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NR56", "name": "MBNL1 (Muscleblind-like protein 1)", "organism": "Homo sapiens", "uniprot_id": "Q9NR56" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Derived from APP (P05067)", "name": "A\u03b2 peptide (A\u03b240, A\u03b242)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Complex (Presenilin-1: P49768)", "name": "\u03b3-secretase", "organism": "", "uniprot_id": "" }, { "function": "Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links", "gene_name": "PLOD2", "glycan_count": 45, "glycosylation_sites": [ { "position": 63, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 209, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 297, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 365, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 522, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 696, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 725, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O00469", "name": "Lysyl hydroxylase 2 (LH2/PLOD2)", "organism": "Homo sapiens", "uniprot_id": "O00469" }, { "function": "SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. SOCS3 is involved in negative regulation of cytokines that signal through the JAK/STAT pathway. Inhibits cytokine signal transduction by binding to tyrosine kinase receptors including IL6ST/gp130, LIF, erythropoietin, insulin, IL12, GCSF and leptin receptors. Binding to JAK2 inhibits its kinase activity and regulates IL6 signaling. Suppresses fetal liver erythropoiesis. Regulates onset and maintenance of allergic responses mediated by T-helper type 2 cells (By similarity). Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:15601820)", "gene_name": "SOCS3", "glycan_count": 1, "glycosylation_sites": [], "id": "O14543", "name": "Suppressor of cytokine signaling 3 (SOCS3)", "organism": "Homo sapiens", "uniprot_id": "O14543" }, { "function": "Chemokine that acts as a ligand for both CX3CR1 and integrins ITGAV:ITGB3 and ITGA4:ITGB1 (PubMed:10187784, PubMed:18971423). The CX3CR1-CX3CL1 signaling exerts distinct functions in different tissue compartments, such as immune response, inflammation, cell adhesion and chemotaxis (PubMed:10187784, PubMed:10382755, PubMed:18971423, PubMed:9177350). Regulates leukocyte adhesion and migration processes at the endothelium (PubMed:10382755, PubMed:9177350). Can activate integrins in both a CX3CR1-dependent and CX3CR1-independent manner (By similarity). In the presence of CX3CR1, activates integrins by binding to the classical ligand-binding site (site 1) in integrins (By similarity). In the absence of CX3CR1, binds to a second site (site 2) in integrins which is distinct from site 1 and enhances the binding of other integrin ligands to site 1 (By similarity)", "gene_name": "Cx3cl1", "glycan_count": 2, "glycosylation_sites": [], "id": "O35188", "name": "Fractalkine/CX3CL1", "organism": "Mus musculus", "uniprot_id": "O35188" }, { "function": "Metalloaminopeptidase that catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro (PubMed:11106490, PubMed:18515364, PubMed:35165443). Contributes to the degradation of bradykinin (PubMed:11106490)", "gene_name": "XPNPEP1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NQW7", "name": "Anti-M\u00fcllerian hormone", "organism": "Homo sapiens", "uniprot_id": "Q9NQW7" }, { "function": "Ligand for the receptor-type protein-tyrosine kinase KIT. Plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. KITLG/SCF binding can activate several signaling pathways. Promotes phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and subsequent activation of the kinase AKT1. KITLG/SCF and KIT also transmit signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. KITLG/SCF and KIT promote activation of STAT family members STAT1, STAT3 and STAT5. KITLG/SCF and KIT promote activation of PLCG1, leading to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. KITLG/SCF acts synergistically with other cytokines, probably interleukins", "gene_name": "KITLG", "glycan_count": 3, "glycosylation_sites": [ { "position": 90, "type": "N-linked (GlcNAc...) asparagine; partial" }, { "position": 118, "type": "N-linked (GlcNAc...) asparagine; partial" }, { "position": 145, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 167, "type": "O-linked (GalNAc...) serine" }, { "position": 168, "type": "O-linked (GalNAc...) threonine" }, { "position": 180, "type": "O-linked (GalNAc...) threonine" }, { "position": 195, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P21583", "name": "KIT ligand (KITLG)", "organism": "Homo sapiens", "uniprot_id": "P21583" }, { "function": "Required for RNA-mediated gene silencing (RNAi) by the RNA-induced silencing complex (RISC). The 'minimal RISC' appears to include AGO2 bound to a short guide RNA such as a microRNA (miRNA) or short interfering RNA (siRNA). These guide RNAs direct RISC to complementary mRNAs that are targets for RISC-mediated gene silencing. The precise mechanism of gene silencing depends on the degree of complementarity between the miRNA or siRNA and its target. Binding of RISC to a perfectly complementary mRNA generally results in silencing due to endonucleolytic cleavage of the mRNA specifically by AGO2. Binding of RISC to a partially complementary mRNA results in silencing through inhibition of translation, and this is independent of endonuclease activity. May inhibit translation initiation by binding to the 7-methylguanosine cap, thereby preventing the recruitment of the translation initiation factor eIF4-E. May also inhibit translation initiation via interaction with EIF6, which itself binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit. The inhibition of translational initiation leads to the accumulation of the affected mRNA in cytoplasmic processing bodies (P-bodies), where mRNA degradation may subsequently occur. In some cases RISC-mediated translational repression is also observed for miRNAs that perfectly match the 3' untranslated region (3'-UTR). Can also up-regulate the translation of specific mRNAs under certain growth conditions. Binds to the AU element of the 3'-UTR of the TNF (TNF-alpha) mRNA and up-regulates translation under conditions of serum starvation. Also required for transcriptional gene silencing (TGS), in which short RNAs known as antigene RNAs or agRNAs direct the transcriptional repression of complementary promoter regions", "gene_name": "AGO2", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9UKV8", "name": "Glycoprotein 78 (GP78)", "organism": "Homo sapiens", "uniprot_id": "Q9UKV8" }, { "function": "Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity)", "gene_name": "TMOD3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NYL9", "name": "BAP31", "organism": "Homo sapiens", "uniprot_id": "Q9NYL9" }, { "function": "Mitochondrial chaperone that plays a key role in mitochondrial protein import, folding, and assembly. Plays an essential role in the protein quality control system, the correct folding of proteins, the re-folding of misfolded proteins, and the targeting of proteins for subsequent degradation. These processes are achieved through cycles of ATP binding, ATP hydrolysis, and ADP release, mediated by co-chaperones (PubMed:18632665, PubMed:25615450, PubMed:28848044, PubMed:30933555, PubMed:31177526). In mitochondria, it associates with the TIM (translocase of the inner membrane) protein complex to assist in the import and folding of mitochondrial proteins (By similarity). Plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis, interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU (PubMed:26702583). Regulates erythropoiesis via stabilization of ISC assembly (PubMed:21123823, PubMed:26702583). Regulates mitochondrial calcium-dependent apoptosis by coupling two calcium channels, ITPR1 and VDAC1, at the mitochondria-associated endoplasmic reticulum (ER) membrane to facilitate calcium transport from the ER lumen to the mitochondria intermembrane space, providing calcium for the downstream calcium channel MCU, which releases it into the mitochondrial matrix (By similarity). Although primarily located in the mitochondria, it is also found in other cellular compartments. In the cytosol, it associates with proteins involved in signaling, apoptosis, or senescence. It may play a role in cell cycle regulation via its interaction with and promotion of degradation of TP53 (PubMed:24625977, PubMed:26634371). May play a role in the control of cell proliferation and cellular aging (By similarity). Protects against reactive oxygen species (ROS) (By similarity). Extracellular HSPA9 plays a cytoprotective role by preventing cell lysis following immune attack by the membrane attack complex by disrupting formation of the complex (PubMed:16091382)", "gene_name": "HSPA9", "glycan_count": 3, "glycosylation_sites": [], "id": "P38646", "name": "Mortalin (GRP75)", "organism": "Homo sapiens", "uniprot_id": "P38646" }, { "function": "Catalyzes the phosphorylation of sphingosine to form sphingosine 1-phosphate (SPP), a lipid mediator with both intra- and extracellular functions. Also acts on D-erythro-sphingosine and to a lesser extent sphinganine, but not other lipids, such as D,L-threo-dihydrosphingosine, N,N-dimethylsphingosine, diacylglycerol, ceramide, or phosphatidylinositol (PubMed:11923095, PubMed:20577214, PubMed:23602659, PubMed:24929359, PubMed:29662056). In contrast to proapoptotic SPHK2, has a negative effect on intracellular ceramide levels, enhances cell growth and inhibits apoptosis (PubMed:16118219). Involved in the regulation of inflammatory response and neuroinflammation. Via the product sphingosine 1-phosphate, stimulates TRAF2 E3 ubiquitin ligase activity, and promotes activation of NF-kappa-B in response to TNF signaling leading to IL17 secretion (PubMed:20577214). In response to TNF and in parallel to NF-kappa-B activation, negatively regulates RANTES induction through p38 MAPK signaling pathway (PubMed:23935096). Involved in endocytic membrane trafficking induced by sphingosine, recruited to dilate endosomes, also plays a role on later stages of endosomal maturation and membrane fusion independently of its kinase activity (PubMed:24929359, PubMed:28049734). In Purkinje cells, seems to be also involved in the regulation of autophagosome-lysosome fusion upon VEGFA (PubMed:25417698)", "gene_name": "SPHK1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NYA1", "name": "Sphingosine kinase 1 (SphK1)", "organism": "Homo sapiens", "uniprot_id": "Q9NYA1" }, { "function": "Shelters ceramides and diacylglycerol lipids inside its START domain and mediates the intracellular trafficking of ceramides and diacylglycerol lipids in a non-vesicular manner", "gene_name": "CERT1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y5P4", "name": "Ceramide transport protein (CERT)", "organism": "Homo sapiens", "uniprot_id": "Q9Y5P4" }, { "function": "Part of the DNA-dependent RNA polymerase which catalyzes the transcription of viral DNA into RNA using the four ribonucleoside triphosphates as substrates. Responsible for the transcription of early, intermediate and late genes. DNA-dependent RNA polymerase associates with the early transcription factor (ETF), itself composed of D6 and A7, thereby allowing the early genes transcription. Late transcription, and probably also intermediate transcription, require newly synthesized RNA polymerase (By similarity)", "gene_name": "RPO132", "glycan_count": 0, "glycosylation_sites": [], "id": "P16716", "name": "Human cytomegalovirus glycoprotein H (gH)", "organism": "Sheeppox virus (strain KS-1)", "uniprot_id": "P16716" }, { "function": "Together with an NADPH cytochrome P450 the enzyme system catalyzes the terminal hydroxylation as the first step in the assimilation of alkanes and fatty acids. Preferentially hydroxylates hexadecane", "gene_name": "CYP52A6", "glycan_count": 0, "glycosylation_sites": [], "id": "P30608", "name": "PRPP synthetase (PRPS2)", "organism": "Candida tropicalis", "uniprot_id": "P30608" }, { "function": "Catalyzes two non-sequential steps in de novo AMP synthesis: converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, and thereby also contributes to de novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP) to AMP and fumarate", "gene_name": "ADSL", "glycan_count": 1, "glycosylation_sites": [], "id": "P30566", "name": "ADSL (Adenylosuccinate lyase)", "organism": "Homo sapiens", "uniprot_id": "P30566" }, { "function": "Bifunctional enzyme that catalyzes the last two steps of purine biosynthesis (PubMed:11948179, PubMed:14756554). Acts as a transformylase that incorporates a formyl group to the AMP analog AICAR (5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide) to produce the intermediate formyl-AICAR (FAICAR) (PubMed:10985775, PubMed:11948179, PubMed:9378707). Can use both 10-formyldihydrofolate and 10-formyltetrahydrofolate as the formyl donor in this reaction (PubMed:10985775). Also catalyzes the cyclization of FAICAR to inosine monophosphate (IMP) (PubMed:11948179, PubMed:14756554). Is able to convert thio-AICAR to 6-mercaptopurine ribonucleotide, an inhibitor of purine biosynthesis used in the treatment of human leukemias (PubMed:10985775). Promotes insulin receptor/INSR autophosphorylation and is involved in INSR internalization (PubMed:25687571)", "gene_name": "ATIC", "glycan_count": 2, "glycosylation_sites": [], "id": "P31939", "name": "ATIC (AICAR transformylase/IMP cyclohydrolase)", "organism": "Homo sapiens", "uniprot_id": "P31939" }, { "function": "Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors", "gene_name": "IMPDH1", "glycan_count": 1, "glycosylation_sites": [], "id": "P20839", "name": "IMPDH (Inosine monophosphate dehydrogenase)", "organism": "Homo sapiens", "uniprot_id": "P20839" }, { "function": "Trifunctional enzyme that catalyzes three distinct reactions as part of the 'de novo' inosine monophosphate biosynthetic pathway", "gene_name": "GART", "glycan_count": 1, "glycosylation_sites": [], "id": "P22102", "name": "PRPP amidotransferase (PPAT)", "organism": "Homo sapiens", "uniprot_id": "P22102" }, { "function": "Functions as a transcriptional repressor", "gene_name": "ZNF652", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y2D9", "name": "FGAMS", "organism": "Homo sapiens", "uniprot_id": "Q9Y2D9" }, { "function": "Sodium-dependent multivitamin transporter that mediates the electrogenic transport of pantothenate, biotin, lipoate and iodide (PubMed:10329687, PubMed:15561972, PubMed:19211916, PubMed:20980265, PubMed:21570947, PubMed:22015582, PubMed:25809983, PubMed:25971966, PubMed:27904971, PubMed:28052864, PubMed:31754459). Functions as a Na(+)-coupled substrate symporter where the stoichiometry of Na(+):substrate is 2:1, creating an electrochemical Na(+) gradient used as driving force for substrate uptake (PubMed:10329687, PubMed:20980265). Required for biotin and pantothenate uptake in the intestine across the brush border membrane (PubMed:19211916). Plays a role in the maintenance of intestinal mucosa integrity, by providing the gut mucosa with biotin (By similarity). Contributes to the luminal uptake of biotin and pantothenate into the brain across the blood-brain barrier (PubMed:25809983)", "gene_name": "SLC5A6", "glycan_count": 1, "glycosylation_sites": [ { "position": 138, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 489, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 498, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y289", "name": "Sodium-dependent multivitamin transporter (SMVT)", "organism": "Homo sapiens", "uniprot_id": "Q9Y289" }, { "function": "Mediates high affinity thiamine uptake, probably via a proton anti-port mechanism (PubMed:11731220, PubMed:33008889, PubMed:35512554, PubMed:35724964). Has no folate transport activity (PubMed:11731220). Mediates H(+)-dependent pyridoxine transport (PubMed:33008889, PubMed:35512554, PubMed:35724964, PubMed:36456177)", "gene_name": "SLC19A3", "glycan_count": 0, "glycosylation_sites": [ { "position": 45, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 166, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9BZV2", "name": "Thiamine transporter-2 (THTR2/SLC19A3)", "organism": "Homo sapiens", "uniprot_id": "Q9BZV2" }, { "function": "", "gene_name": "PSAP", "glycan_count": 0, "glycosylation_sites": [], "id": "P07602-3", "name": "Saposin C (SapC)", "organism": "Homo sapiens", "uniprot_id": "P07602-3" }, { "function": "", "gene_name": "PSAP", "glycan_count": 293, "glycosylation_sites": [], "id": "P07602-1", "name": "Saposin A", "organism": "Homo sapiens", "uniprot_id": "P07602-1" }, { "function": "", "gene_name": "PSAP", "glycan_count": 0, "glycosylation_sites": [], "id": "P07602-2", "name": "Saposin B", "organism": "Homo sapiens", "uniprot_id": "P07602-2" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P07602-4", "name": "Saposin D", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O15118/O15130", "name": "NPC1/NPC2", "organism": "", "uniprot_id": "" }, { "function": "Involved in many cell functions, including pre-mRNA splicing, the aryl hydrocarbon receptor (AHR) pathway, F-actin organization and protein ubiquitination. Plays a role in the dynamic organization of the actin skeleton as a stabilizer of actin filaments by association with F-actin through Kelch repeats (By similarity). Protects cells from cell death induced by actin destabilization (By similarity). Functions as modifier of the AHR/Aryl hydrocarbon receptor pathway increasing the concentration of AHR available to activate transcription (PubMed:16582008). In addition, functions as a negative regulator of BCR(KLHL20) E3 ubiquitin ligase complex to prevent ubiquitin-mediated proteolysis of PML and DAPK1, two tumor suppressors (PubMed:25619834). Inhibits pre-mRNA splicing (in vitro) (PubMed:9696811). May play a role in mRNA nuclear export (PubMed:30538201)", "gene_name": "IVNS1ABP", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y6Y0", "name": "Calpain-5", "organism": "Homo sapiens", "uniprot_id": "Q9Y6Y0" }, { "function": "Histone demethylase that specifically demethylates both mono- and dimethylated 'Lys-9' of histone H3. May act as a transcription regulator controlling hair biology (via targeting of collagens), neural activity, and cell cycle", "gene_name": "HR", "glycan_count": 0, "glycosylation_sites": [], "id": "O43593", "name": "Granzyme H", "organism": "Homo sapiens", "uniprot_id": "O43593" }, { "function": "May catalyze the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. Cleaves insulin A chain at '14-Tyr-|-Gln-15' and insulin B chain at '6-Leu-|-Cys-7', '16-Tyr-|-Leu-17', '25-Phe-|-Tyr-26' and '26-Tyr-|-Thr-27'. Could play a role in the activation of precursors to inflammatory cytokines", "gene_name": "KLK7", "glycan_count": 1, "glycosylation_sites": [ { "position": 246, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P49862", "name": "Granzyme K", "organism": "Homo sapiens", "uniprot_id": "P49862" }, { "function": "Since they lack a putative transactivation domain, the small Mafs behave as transcriptional repressors when they dimerize among themselves (PubMed:11154691). However, they seem to serve as transcriptional activators by dimerizing with other (usually larger) basic-zipper proteins, such as NFE2, NFE2L1 and NFE2L2, and recruiting them to specific DNA-binding sites (PubMed:11154691, PubMed:8932385, PubMed:9421508). Small Maf proteins heterodimerize with Fos and may act as competitive repressors of the NFE2L2 transcription factor (PubMed:11154691). Transcription factor, component of erythroid-specific transcription factor NFE2L2 (PubMed:11154691). Activates globin gene expression when associated with NFE2L2 (PubMed:11154691). May be involved in signal transduction of extracellular H(+) (By similarity)", "gene_name": "MAFG", "glycan_count": 1, "glycosylation_sites": [], "id": "O15525", "name": "Granzyme M", "organism": "Homo sapiens", "uniprot_id": "O15525" }, { "function": "Plays a role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex) (PubMed:28781166). The heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract of U6 snRNA (PubMed:10523320)", "gene_name": "LSM4", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y4Z0", "name": "LSM2", "organism": "Homo sapiens", "uniprot_id": "Q9Y4Z0" }, { "function": "Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (PubMed:11991638, PubMed:18984161, PubMed:19325628, PubMed:23333303, PubMed:25555158, PubMed:26912367, PubMed:28076346, PubMed:28502770, PubMed:28781166, PubMed:32494006). Component of both the pre-catalytic spliceosome B complex and activated spliceosome C complexes (PubMed:11991638, PubMed:28076346, PubMed:28502770, PubMed:28781166). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (PubMed:15146077). As part of the U7 snRNP it is involved in histone 3'-end processing (PubMed:12975319)", "gene_name": "SNRPF", "glycan_count": 1, "glycosylation_sites": [], "id": "P62306", "name": "LSM3", "organism": "Homo sapiens", "uniprot_id": "P62306" }, { "function": "Transcription activator that binds DNA elements with the consensus sequence 5'-CGGTAATTGG-3'. Binds DNA via its homeobox. Required for normal cell death of enteric neurons in the gastrointestinal tract. Required for normal development of the enteric nervous system, and for proper development of normal motility of the gastrointestinal tract (By similarity)", "gene_name": "TLX2", "glycan_count": 0, "glycosylation_sites": [], "id": "O43763", "name": "LSM5", "organism": "Homo sapiens", "uniprot_id": "O43763" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q60648 (mouse)", "name": "Serum amyloid A3 (SAA3)", "organism": "", "uniprot_id": "" }, { "function": "Major acute phase reactant", "gene_name": "SAA4", "glycan_count": 3, "glycosylation_sites": [ { "position": 94, "type": "N-linked (GlcNAc...) asparagine; partial" } ], "id": "P35542", "name": "Serum amyloid A4 (SAA4)", "organism": "Homo sapiens", "uniprot_id": "P35542" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P10155/P09923", "name": "Ro/SS-A (Ro52/Ro60)", "organism": "", "uniprot_id": "" }, { "function": "Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading", "gene_name": "HLA-DPB1", "glycan_count": 44, "glycosylation_sites": [ { "position": 48, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P04440", "name": "HLA-DPB1*05:01", "organism": "Homo sapiens", "uniprot_id": "P04440" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "see P-gp", "name": "Abcb1a/Abcb1b", "organism": "", "uniprot_id": "" }, { "function": "Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (PubMed:11422376, PubMed:1346131). The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable)", "gene_name": "HSPD1", "glycan_count": 6, "glycosylation_sites": [], "id": "P10809", "name": "Heat shock protein 60 (HSP60)", "organism": "Homo sapiens", "uniprot_id": "P10809" }, { "function": "The nonhelical tail domain is involved in promoting KRT5-KRT14 filaments to self-organize into large bundles and enhances the mechanical properties involved in resilience of keratin intermediate filaments in vitro", "gene_name": "KRT14", "glycan_count": 1, "glycosylation_sites": [], "id": "P02533", "name": "Keratin 14 (K14)", "organism": "Homo sapiens", "uniprot_id": "P02533" }, { "function": "Hormone involved in different processes, such as regulation of the pH of the duodenal content, food intake and water homeostasis (PubMed:25332973). Exerts its biological effects by binding to secretin receptor (SCTR), a G-protein coupled receptor expressed in the basolateral domain of several cells (PubMed:25332973, PubMed:33008599, PubMed:32811827). Acts as a key gastrointestinal hormone by regulating the pH of the duodenal content (By similarity). Secreted by S cells of the duodenum in the crypts of Lieberkuehn and regulates the pH of the duodenum by (1) inhibiting the secretion of gastric acid from the parietal cells of the stomach and (2) stimulating the production of bicarbonate (NaHCO(3)) from the ductal cells of the pancreas (By similarity). Production of bicarbonate is essential to neutralize the pH and ensure no damage is done to the small intestine by the gastric acid (By similarity). In addition to regulating the pH of the duodenal content, plays a central role in diet induced thermogenesis: acts as a non-sympathetic brown fat (BAT) activator mediating prandial thermogenesis, which consequentially induces satiation (Probable). Mechanistically, secretin released by the gut after a meal binds to secretin receptor (SCTR) in brown adipocytes, activating brown fat thermogenesis by stimulating lipolysis, which is sensed in the brain and promotes satiation (By similarity). Also able to stimulate lipolysis in white adipocytes (By similarity). Also plays an important role in cellular osmoregulation: released into the systemic circulation in response to hyperosmolality and acts at different levels in the hypothalamus, pituitary and kidney to regulate water homeostasis (By similarity). Also plays a role in the central nervous system, possibly by acting as a neuropeptide hormone: required for hippocampal synaptic function and neural progenitor cells maintenance (By similarity)", "gene_name": "SCT", "glycan_count": 0, "glycosylation_sites": [], "id": "P09683", "name": "Secretin", "organism": "Homo sapiens", "uniprot_id": "P09683" }, { "function": "This peptide hormone induces gall bladder contraction and the release of pancreatic enzymes in the gut. Its function in the brain is not clear. Binding to CCK-A receptors stimulates amylase release from the pancreas, binding to CCK-B receptors stimulates gastric acid secretion", "gene_name": "CCK", "glycan_count": 0, "glycosylation_sites": [ { "position": 31, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" } ], "id": "P06307", "name": "Cholecystokinin", "organism": "Homo sapiens", "uniprot_id": "P06307" }, { "function": "Participates in the primary piRNA biogenesis pathway and is required during spermatogenesis to repress transposable elements and prevent their mobilization, which is essential for the germline integrity. The piRNA metabolic process mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Required for the final steps of primary piRNA biogenesis by participating in the processing of 31-37 nt intermediates into mature piRNAs. May act in pi-bodies and piP-bodies by transferring piRNA precursors or intermediates to or between these granules", "gene_name": "TDRKH", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y2W6", "name": "Choline transporter (SLC5A7)", "organism": "Homo sapiens", "uniprot_id": "Q9Y2W6" }, { "function": "Lectin component of the HRD1 complex, which functions in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD) (PubMed:18264092, PubMed:18417469, PubMed:19084021, PubMed:19346256, PubMed:21172656, PubMed:24899641). Specifically recognizes and binds improperly folded glycoproteins as well as hyperglycosylated proteins, retain them in the ER, and transfers them to the ubiquitination machinery and promote their degradation (PubMed:18264092, PubMed:18417469, PubMed:19084021, PubMed:19346256, PubMed:21172656, PubMed:24899641). Possible targets include TRPV4 as well as hyperglycosylated HSP90B1 (PubMed:17932042)", "gene_name": "OS9", "glycan_count": 18, "glycosylation_sites": [ { "position": 177, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13438", "name": "Vitamin E transporter (TTPA)", "organism": "Homo sapiens", "uniprot_id": "Q13438" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "XP_018646423.1", "name": "Smserpin-p46", "organism": "", "uniprot_id": "" }, { "function": "Does not function as sodium/D-glucose symporter (PubMed:22301059). Generates D-glucose-induced depolarization in a pH-dependent manner, with activity in acidic conditions (pH 5) but not neutral conditions (PubMed:22301059)", "gene_name": "Slc5a4a", "glycan_count": 0, "glycosylation_sites": [ { "position": 248, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9ET37", "name": "SGLT-2 (Sodium-glucose cotransporter 2)", "organism": "Mus musculus", "uniprot_id": "Q9ET37" }, { "function": "Catalyzes the synthesis of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA) with pyridoxal 5'-phosphate as cofactor", "gene_name": "GAD1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q99259", "name": "GAD (Glutamic acid decarboxylase)", "organism": "Homo sapiens", "uniprot_id": "Q99259" }, { "function": "Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver", "gene_name": "Ins1", "glycan_count": 0, "glycosylation_sites": [], "id": "P01325", "name": "Insulin", "organism": "Mus musculus", "uniprot_id": "P01325" }, { "function": "Plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis. A counterregulatory hormone of insulin, raises plasma glucose levels in response to insulin-induced hypoglycemia. Plays an important role in initiating and maintaining hyperglycemic conditions in diabetes", "gene_name": "Gcg", "glycan_count": 0, "glycosylation_sites": [], "id": "P55095", "name": "Glucagon", "organism": "Mus musculus", "uniprot_id": "P55095" }, { "function": "Methyltransferase: Displays a capping enzyme activity. This function is necessary since all viral RNAs are synthesized in the cytoplasm, and host capping enzymes are restricted to the nucleus. The enzymatic reaction involves a covalent link between 7-methyl-GMP and the methyltransferase, whereas eukaryotic capping enzymes form a covalent complex only with GMP. Methyltransferase catalyzes transfer of a methyl group from S-adenosylmethionine to GTP and GDP to yield m(7)GTP or m(7)GDP. GDP is a better substrate than GTP. This enzyme also displays guanylyltransferase activity to form a covalent complex, methyltransferase-m(7)GMP, from which 7-methyl-GMP is transferred to the mRNA to create the cap structure", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P33424", "name": "NSP4 enterotoxin", "organism": "Hepatitis E virus genotype 1 (isolate Human/Pakistan/Sar-55)", "uniprot_id": "P33424" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02452 (COL1A1), P02462 (COL4A1)", "name": "Collagen (Type I/IV)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02788 (human)", "name": "Lactoferrin", "organism": "", "uniprot_id": "" }, { "function": "May play a role in the defense system against pathogens", "gene_name": "ITLN2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8WWU7", "name": "Intelectin 1 (ITLN1)", "organism": "Homo sapiens", "uniprot_id": "Q8WWU7" }, { "function": "Chemotactic for human polymorphonuclear leukocytes but does not induce chemokinesis or an oxidative burst", "gene_name": "Cxcl2", "glycan_count": 0, "glycosylation_sites": [], "id": "P10889", "name": "CXCL2 (Macrophage inflammatory protein-2\u03b1)", "organism": "Mus musculus", "uniprot_id": "P10889" }, { "function": "G-protein coupled receptor that binds to several ligands including 2-arachidonoyl lysophosphatidylinositol or lysophosphatidylglucoside with high affinity, leading to rapid and transient activation of numerous intracellular signaling pathways (PubMed:36142844, PubMed:36523570, PubMed:37544935). Induces the Ca(2+) release from intracellular stores via ERK, the heterotrimeric G protein GNA13 and RHOA leading to morphological changes including cell rounding and stress fiber formation (PubMed:36142844). In macrophages, acts downstream of lysophosphatidylglucoside to inhibit the translocation of the phospholipid-transporting ABCA1 to plasma membrane and subsequent cholesterol efflux leading to lipid accumulation and foam cell formation (PubMed:37544935)", "gene_name": "GPR55", "glycan_count": 0, "glycosylation_sites": [ { "position": 5, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 171, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y2T6", "name": "GPR55", "organism": "Homo sapiens", "uniprot_id": "Q9Y2T6" }, { "function": "Cytosolic phosphoenolpyruvate carboxykinase that catalyzes the reversible decarboxylation and phosphorylation of oxaloacetate (OAA) and acts as the rate-limiting enzyme in gluconeogenesis (PubMed:24863970, PubMed:26971250, PubMed:28216384, PubMed:30193097). Regulates cataplerosis and anaplerosis, the processes that control the levels of metabolic intermediates in the citric acid cycle (PubMed:24863970, PubMed:26971250, PubMed:28216384, PubMed:30193097). At low glucose levels, it catalyzes the cataplerotic conversion of oxaloacetate to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle (PubMed:30193097). At high glucose levels, it catalyzes the anaplerotic conversion of phosphoenolpyruvate to oxaloacetate (PubMed:30193097). Acts as a regulator of formation and maintenance of memory CD8(+) T-cells: up-regulated in these cells, where it generates phosphoenolpyruvate, via gluconeogenesis (By similarity). The resultant phosphoenolpyruvate flows to glycogen and pentose phosphate pathway, which is essential for memory CD8(+) T-cells homeostasis (By similarity). In addition to the phosphoenolpyruvate carboxykinase activity, also acts as a protein kinase when phosphorylated at Ser-90: phosphorylation at Ser-90 by AKT1 reduces the binding affinity to oxaloacetate and promotes an atypical serine protein kinase activity using GTP as donor (PubMed:32322062). The protein kinase activity regulates lipogenesis: upon phosphorylation at Ser-90, translocates to the endoplasmic reticulum and catalyzes phosphorylation of INSIG proteins (INSIG1 and INSIG2), thereby disrupting the interaction between INSIG proteins and SCAP and promoting nuclear translocation of SREBP proteins (SREBF1/SREBP1 or SREBF2/SREBP2) and subsequent transcription of downstream lipogenesis-related genes (PubMed:32322062)", "gene_name": "PCK1", "glycan_count": 1, "glycosylation_sites": [], "id": "P35558", "name": "PEPCK", "organism": "Homo sapiens", "uniprot_id": "P35558" }, { "function": "CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy", "gene_name": "Cntf", "glycan_count": 0, "glycosylation_sites": [], "id": "P51642", "name": "Ciliary neurotrophic factor receptor (Cntfr)", "organism": "Mus musculus", "uniprot_id": "P51642" }, { "function": "G-protein-coupled receptor for histamine, a biogenic amine that functions as an immune modulator and a neurotransmitter (PubMed:33828102, PubMed:8280179). Through the H1 receptor, histamine mediates the contraction of smooth muscles and increases capillary permeability due to contraction of terminal venules. Also mediates neurotransmission in the central nervous system and thereby regulates circadian rhythms, emotional and locomotor activities as well as cognitive functions (By similarity)", "gene_name": "HRH1", "glycan_count": 2, "glycosylation_sites": [ { "position": 5, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 18, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P35367", "name": "Histamine receptor H1 (Hrh1)", "organism": "Homo sapiens", "uniprot_id": "P35367" }, { "function": "Accessory protein that interacts with and modulates the function of G-protein coupled receptors including calcitonin gene-related peptide type 1 receptor (CALCRL) and calcitonin receptor (CALCR) (PubMed:33602864, PubMed:9620797, PubMed:35324283, PubMed:38603770). Required for the transport of CALCRL to the plasma membrane (PubMed:9620797). Together with CALCRL, form the receptor complex for the calcitonin gene-related peptides CGRP1/CALCA and CGRP2/CALCB (PubMed:33602864, PubMed:9620797). Together with CALCR, form the AMYR1 receptor complex for amylin/IAPP and CGRP1/CALCA (PubMed:35324283, PubMed:38603770)", "gene_name": "RAMP1", "glycan_count": 0, "glycosylation_sites": [], "id": "O60894", "name": "Receptor activity-modifying protein 3 (Ramp3)", "organism": "Homo sapiens", "uniprot_id": "O60894" }, { "function": "Involved in the initial immune cell clustering during inflammatory response and may regulate chemotactic activity of chemokines. May play a role in melanocortin signaling pathways that regulate energy homeostasis and hair color. Low-affinity receptor for agouti (By similarity). Has a critical role in normal myelination in the central nervous system (By similarity)", "gene_name": "ATRN", "glycan_count": 122, "glycosylation_sites": [ { "position": 213, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 237, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 242, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 253, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 264, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 300, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 325, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 362, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 383, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 416, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 428, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 575, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 623, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 731, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 863, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 914, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 923, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 986, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1043, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1054, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1073, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 1082, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1198, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1206, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1250, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1259, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O75882", "name": "Attractin (Atrn)", "organism": "Homo sapiens", "uniprot_id": "O75882" }, { "function": "Receptor for ADIPOQ, an essential hormone secreted by adipocytes that regulates glucose and lipid metabolism (PubMed:12802337, PubMed:25855295). Required for normal glucose and fat homeostasis and for maintaining a normal body weight. ADIPOQ-binding activates a signaling cascade that leads to increased AMPK activity, and ultimately to increased fatty acid oxidation, increased glucose uptake and decreased gluconeogenesis. Has high affinity for globular adiponectin and low affinity for full-length adiponectin (By similarity)", "gene_name": "ADIPOR1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q96A54", "name": "Adiponectin receptor protein 1 (Adipor1)", "organism": "Homo sapiens", "uniprot_id": "Q96A54" }, { "function": "Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of MET", "gene_name": "PTPN1", "glycan_count": 1, "glycosylation_sites": [], "id": "P18031", "name": "Protein tyrosine phosphatase non-receptor type 1 (Ptpn1)", "organism": "Homo sapiens", "uniprot_id": "P18031" }, { "function": "Membrane-associated protein that plays a role in the structural modulation of the actin cytoskeleton, chemotaxis, motility, cell adhesion, phagocytosis, and exocytosis through lipid sequestering and/or protein docking to membranes (PubMed:23704996, PubMed:36009319). Thus, exerts an influence on a plethora of physiological processes, such as embryonic development, tissue regeneration, neuronal plasticity, and inflammation. Sequesters phosphatidylinositol 4,5-bisphosphate (PIP2) at lipid rafts in the plasma membrane of quiescent cells, an action reversed by protein kinase C, ultimately inhibiting exocytosis (PubMed:23704996). During inflammation, promotes the migration and adhesion of inflammatory cells and the secretion of cytokines such as tumor necrosis factor (TNF), particularly in macrophages (PubMed:37949888). Plays an essential role in bacteria-induced intracellular reactive oxygen species (ROS) formation in the monocytic cell type. Participates in the regulation of neurite initiation and outgrowth by interacting with components of cellular machinery including CDC42 that regulates cell shape and process extension through modulation of the cytoskeleton (By similarity). Plays also a role in axon development by mediating docking and fusion of RAB10-positive vesicles with the plasma membrane (By similarity)", "gene_name": "MARCKS", "glycan_count": 1, "glycosylation_sites": [], "id": "P29966", "name": "MARCKS", "organism": "Homo sapiens", "uniprot_id": "P29966" }, { "function": "Ligand-activated transcription factor that enables cells to adapt to changing conditions by sensing compounds from the environment, diet, microbiome and cellular metabolism, and which plays important roles in development, immunity and cancer (PubMed:23275542, PubMed:30373764, PubMed:32818467, PubMed:7961644). Upon ligand binding, translocates into the nucleus, where it heterodimerizes with ARNT and induces transcription by binding to xenobiotic response elements (XRE) (PubMed:23275542, PubMed:30373764, PubMed:7961644). Regulates a variety of biological processes, including angiogenesis, hematopoiesis, drug and lipid metabolism, cell motility and immune modulation (PubMed:12213388). Xenobiotics can act as ligands: upon xenobiotic-binding, activates the expression of multiple phase I and II xenobiotic chemical metabolizing enzyme genes (such as the CYP1A1 gene) (PubMed:7961644, PubMed:33193710). Mediates biochemical and toxic effects of halogenated aromatic hydrocarbons (PubMed:34521881, PubMed:7961644). Next to xenobiotics, natural ligands derived from plants, microbiota, and endogenous metabolism are potent AHR agonists (PubMed:18076143). Tryptophan (Trp) derivatives constitute an important class of endogenous AHR ligands (PubMed:32818467, PubMed:32866000). Acts as a negative regulator of anti-tumor immunity: indoles and kynurenic acid generated by Trp catabolism act as ligand and activate AHR, thereby promoting AHR-driven cancer cell motility and suppressing adaptive immunity (PubMed:32818467). Regulates the circadian clock by inhibiting the basal and circadian expression of the core circadian component PER1 (PubMed:28602820). Inhibits PER1 by repressing the CLOCK-BMAL1 heterodimer mediated transcriptional activation of PER1 (PubMed:28602820). The heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription (PubMed:28602820)", "gene_name": "AHR", "glycan_count": 1, "glycosylation_sites": [], "id": "P35869", "name": "Aryl hydrocarbon receptor (AHR)", "organism": "Homo sapiens", "uniprot_id": "P35869" }, { "function": "Rubredoxin is a small nonheme, iron protein lacking acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions as an electron acceptor and may also stabilize the conformation of the molecule", "gene_name": "rub", "glycan_count": 0, "glycosylation_sites": [], "id": "P24297", "name": "Alanine Transaminase (ALT)", "organism": "Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)", "uniprot_id": "P24297" }, { "function": "Functions as a key mediator in apoptosis and inflammation (PubMed:11103777, PubMed:12646168, PubMed:15030775, PubMed:17349957, PubMed:17599095, PubMed:19158675, PubMed:19158676, PubMed:19234215, PubMed:19494289, PubMed:21487011, PubMed:24630722, PubMed:25847972, PubMed:30674671, PubMed:34678144, PubMed:36050480). Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner (PubMed:11103777, PubMed:12646168). Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3 (PubMed:14730312, PubMed:16964285). Involved in innate immune response by acting as an integral adapter in the assembly of various inflammasomes (NLRP1, NLRP2, NLRP3, NLRP6, AIM2 and probably IFI16) which recruit and activate caspase-1 leading to processing and secretion of pro-inflammatory cytokines (PubMed:15030775, PubMed:16982856, PubMed:17349957, PubMed:17599095, PubMed:19158675, PubMed:19158676, PubMed:19234215, PubMed:21487011, PubMed:23530044, PubMed:24630722, PubMed:25847972, PubMed:29440442, PubMed:30674671, PubMed:33980849, PubMed:34678144, PubMed:34706239). Caspase-1-dependent inflammation leads to macrophage pyroptosis, a form of cell death (PubMed:24630722). The function as activating adapter in different types of inflammasomes is mediated by the pyrin and CARD domains and their homotypic interactions (PubMed:14499617, PubMed:19234215, PubMed:24630722). Clustered PYCARD nucleates the formation of caspase-1 filaments through the interaction of their respective CARD domains, acting as a platform for of caspase-1 polymerization (PubMed:24630722). In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1 (PubMed:17349957). In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation (PubMed:16964285). May be involved in RIGI-triggered pro-inflammatory responses and inflammasome activation (PubMed:19915568). In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8 (PubMed:19158675, PubMed:19158676). In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form (PubMed:22732093). Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways (PubMed:12486103, PubMed:16585594). For regulation of NF-kappa-B activating and inhibiting functions have been reported (PubMed:12486103). Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK (PubMed:12486103, PubMed:16585594). Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing (PubMed:16585594). Modulates host resistance to DNA virus infection, probably by inducing the cleavage of and inactivating CGAS in presence of cytoplasmic double-stranded DNA (PubMed:28314590)", "gene_name": "PYCARD", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9ULZ3", "name": "ASC (PYCARD)", "organism": "Homo sapiens", "uniprot_id": "Q9ULZ3" }, { "function": "Controls the reversible conversion of biologically active glucocorticoids such as cortisone to cortisol, and 11-dehydrocorticosterone to corticosterone in the presence of NADP(H) (PubMed:10497248, PubMed:12460758, PubMed:14973125, PubMed:15152005, PubMed:15280030, PubMed:17593962, PubMed:21453287, PubMed:27927697, PubMed:30902677). Participates in the corticosteroid receptor-mediated anti-inflammatory response, as well as metabolic and homeostatic processes (PubMed:10497248, PubMed:12414862, PubMed:15152005, PubMed:21453287). Plays a role in the secretion of aqueous humor in the eye, maintaining a normotensive, intraocular environment (PubMed:11481269). Bidirectional in vitro, predominantly functions as a reductase in vivo, thereby increasing the concentration of active glucocorticoids (PubMed:10497248, PubMed:11481269, PubMed:12414862, PubMed:12460758). It has broad substrate specificity, besides glucocorticoids, it accepts other steroid and sterol substrates (PubMed:15095019, PubMed:15152005, PubMed:17593962, PubMed:21453287). Interconverts 7-oxo- and 7-hydroxy-neurosteroids such as 7-oxopregnenolone and 7beta-hydroxypregnenolone, 7-oxodehydroepiandrosterone (3beta-hydroxy-5-androstene-7,17-dione) and 7beta-hydroxydehydroepiandrosterone (3beta,7beta-dihydroxyandrost-5-en-17-one), among others (PubMed:17593962). Catalyzes the stereo-specific conversion of the major dietary oxysterol, 7-ketocholesterol (7-oxocholesterol), into the more polar 7-beta-hydroxycholesterol metabolite (PubMed:15095019, PubMed:15152005). 7-oxocholesterol is one of the most important oxysterols, it participates in several events such as induction of apoptosis, accumulation in atherosclerotic lesions, lipid peroxidation, and induction of foam cell formation (PubMed:15095019). Mediates the 7-oxo reduction of 7-oxolithocholate mainly to chenodeoxycholate, and to a lesser extent to ursodeoxycholate, both in its free form and when conjugated to glycine or taurine, providing a link between glucocorticoid activation and bile acid metabolism (PubMed:21453287). Catalyzes the synthesis of 7-beta-25-dihydroxycholesterol from 7-oxo-25-hydroxycholesterol in vitro, which acts as a ligand for the G-protein-coupled receptor (GPCR) Epstein-Barr virus-induced gene 2 (EBI2) and may thereby regulate immune cell migration (PubMed:30902677)", "gene_name": "HSD11B1", "glycan_count": 6, "glycosylation_sites": [ { "position": 123, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 162, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 207, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P28845", "name": "11\u03b2-hydroxysteroid dehydrogenase type 1 (11\u03b2-HSD-1)", "organism": "Homo sapiens", "uniprot_id": "P28845" }, { "function": "Glycogen synthase participates in the glycogen biosynthetic process along with glycogenin and glycogen branching enzyme. Extends the primer composed of a few glucose units formed by glycogenin by adding new glucose units to it. In this context, glycogen synthase transfers the glycosyl residue from UDP-Glc to the non-reducing end of alpha-1,4-glucan", "gene_name": "GYS1", "glycan_count": 1, "glycosylation_sites": [], "id": "P13807", "name": "Glycogen synthase (GS)", "organism": "Homo sapiens", "uniprot_id": "P13807" }, { "function": "Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway (PubMed:3086869). Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate (PubMed:3086869). Because of its role in metabolisms, is involved in sleep regulation (PubMed:3086869)", "gene_name": "Pfas", "glycan_count": 0, "glycosylation_sites": [], "id": "P35421", "name": "Phosphoenolpyruvate carboxykinase (PEPCK)", "organism": "Drosophila melanogaster", "uniprot_id": "P35421" }, { "function": "Component of the entry fusion complex (EFC), which consists of 11 proteins. During cell infection, this complex mediates entry of the virion core into the host cytoplasm by a two-step mechanism consisting of lipid mixing of the viral and cellular membranes and subsequent pore formation", "gene_name": "OPG099", "glycan_count": 0, "glycosylation_sites": [], "id": "P0DOU2", "name": "\u03b1-glucosidase", "organism": "Variola virus", "uniprot_id": "P0DOU2" }, { "function": "Cytosolic prostaglandin synthase that catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) (PubMed:10922363). Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes (PubMed:11274138, PubMed:12077419). Facilitates HIF alpha proteins hydroxylation via interaction with EGLN1/PHD2, leading to recruit EGLN1/PHD2 to the HSP90 pathway (PubMed:24711448)", "gene_name": "PTGES3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q15185", "name": "Prostaglandin E2 synthase", "organism": "Homo sapiens", "uniprot_id": "Q15185" }, { "function": "Catalyzes the three sequential steps of the methylation pathway for the biosynthesis of phosphatidylcholine, a critical and essential component for membrane structure (PubMed:12431977, PubMed:15927961). Uses S-adenosylmethionine (S-adenosyl-L-methionine, SAM or AdoMet) as the methyl group donor for the methylation of phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine, PE) to phosphatidylmonomethylethanolamine (1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine, PMME), PMME to phosphatidyldimethylethanolamine (1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine, PDME), and PDME to phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine, PC), producing S-adenosyl-L-homocysteine in each step (PubMed:12431977, PubMed:15927961). Responsible for approximately 30% of hepatic PC with the CDP-choline pathway accounting for the other 70% (Probable)", "gene_name": "PEMT", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UBM1", "name": "Phosphatidylethanolamine N-methyltransferase (PEMT)", "organism": "Homo sapiens", "uniprot_id": "Q9UBM1" }, { "function": "Highly specific for ethanolamine phosphorylation. May be a rate-controlling step in phosphatidylethanolamine biosynthesis", "gene_name": "ETNK1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9HBU6", "name": "STAMP2", "organism": "Homo sapiens", "uniprot_id": "Q9HBU6" }, { "function": "", "gene_name": "Qars1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8R1V9", "name": "F4/80", "organism": "Mus musculus", "uniprot_id": "Q8R1V9" }, { "function": "", "gene_name": "rpl16", "glycan_count": 0, "glycosylation_sites": [], "id": "P06384", "name": "Glucagon-like peptide-1 (GLP-1)", "organism": "Nicotiana tabacum", "uniprot_id": "P06384" }, { "function": "Sulfur-rich seed storage protein that remains undegraded at germination (PubMed:11406286). The uncleaved form exhibits some inhibitory activity against GH11 xylanase from T.longibrachiatum, more at pH 7 than at pH 5.3, but not against GH12 xyloglucan-specific endoglucanase (XEG) from A.aculeatus (PubMed:26741537). Binds to model phospholipid membranes containing dimyristoyl phosphatidylglycerol (DMPG), dioleoyl phosphatidic acid (DOPA) or mixture of dimyristoyl phosphatidylcholine and dimyristoyl phosphatidylglycerol (DMPC:DMPG), or mixture of dioleoyl phosphatidic acid and dioleoyl phosphatidylcholine (DOPC:DOPA) (PubMed:30312772)", "gene_name": "Cgamma", "glycan_count": 0, "glycosylation_sites": [ { "position": 131, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9FSH9", "name": "Miraculin", "organism": "Lupinus albus", "uniprot_id": "Q9FSH9" }, { "function": "Serine/threonine kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases (PubMed:10226025, PubMed:10480933, PubMed:10995762, PubMed:12167717, PubMed:14585963, PubMed:14604990, PubMed:16207722, PubMed:16251192, PubMed:17327236, PubMed:17371830, PubMed:18835241, PubMed:9094314, PubMed:9368760, PubMed:9445476, PubMed:9445477, PubMed:9707564, PubMed:9768361). Its targets include: protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), p70 ribosomal protein S6 kinase (RPS6KB1), p90 ribosomal protein S6 kinase (RPS6KA1, RPS6KA2 and RPS6KA3), cyclic AMP-dependent protein kinase (PRKACA), protein kinase C (PRKCD and PRKCZ), serum and glucocorticoid-inducible kinase (SGK1, SGK2 and SGK3), p21-activated kinase-1 (PAK1), TSSK3, protein kinase PKN (PKN1 and PKN2) (PubMed:10226025, PubMed:10480933, PubMed:10995762, PubMed:12167717, PubMed:14585963, PubMed:14604990, PubMed:16207722, PubMed:16251192, PubMed:17327236, PubMed:17371830, PubMed:18835241, PubMed:9094314, PubMed:9368760, PubMed:9445476, PubMed:9707564, PubMed:9768361). Plays a central role in the transduction of signals from insulin by providing the activating phosphorylation to PKB/AKT1, thus propagating the signal to downstream targets controlling cell proliferation and survival, as well as glucose and amino acid uptake and storage (PubMed:10226025, PubMed:12167717, PubMed:9094314). Negatively regulates the TGF-beta-induced signaling by: modulating the association of SMAD3 and SMAD7 with TGF-beta receptor, phosphorylating SMAD2, SMAD3, SMAD4 and SMAD7, preventing the nuclear translocation of SMAD3 and SMAD4 and the translocation of SMAD7 from the nucleus to the cytoplasm in response to TGF-beta (PubMed:17327236). Activates PPARG transcriptional activity and promotes adipocyte differentiation (By similarity). Activates the NF-kappa-B pathway via phosphorylation of IKKB (PubMed:16207722). The tyrosine phosphorylated form is crucial for the regulation of focal adhesions by angiotensin II (PubMed:14585963). Controls proliferation, survival, and growth of developing pancreatic cells (By similarity). Participates in the regulation of Ca(2+) entry and Ca(2+)-activated K(+) channels of mast cells (By similarity). Essential for the motility of vascular endothelial cells (ECs) and is involved in the regulation of their chemotaxis (PubMed:17371830). Plays a critical role in cardiac homeostasis by serving as a dual effector for cell survival and beta-adrenergic response (By similarity). Plays an important role during thymocyte development by regulating the expression of key nutrient receptors on the surface of pre-T cells and mediating Notch-induced cell growth and proliferative responses (By similarity). Provides negative feedback inhibition to toll-like receptor-mediated NF-kappa-B activation in macrophages (By similarity)", "gene_name": "PDPK1", "glycan_count": 1, "glycosylation_sites": [], "id": "O15530", "name": "PDK1 (3-phosphoinositide-dependent protein kinase-1)", "organism": "Homo sapiens", "uniprot_id": "O15530" }, { "function": "Structural component of specialized membrane microdomains known as tetraspanin-enriched microdomains (TERMs), which act as platforms for receptor clustering and signaling (PubMed:19497983). Participates thereby in diverse biological functions such as cell signal transduction, adhesion, migration and protein trafficking. Acts as a attenuator of EGF signaling, facilitating ligand-induced endocytosis of the receptor and its subsequent desensitization (PubMed:10985391, PubMed:35538033). Mechanistically, modulates ligand-induced ubiquitination and trafficking of EGFR via E3 ligase CBL phosphorylation by PKC (PubMed:23897813). Increases cell-matrix adhesion by regulating the membrane organization of integrin alpha4/ITA4 (PubMed:24623721, PubMed:8757325). Modulates adhesion and suppresses cell migration through other integrins such as the alpha6/ITGA6 and beta1/ITGB1 (PubMed:15557282, PubMed:17560548). Decreases cell-associated plasminogen activation by interfering with the interaction between urokinase-type plasminogen activator/PLAU and its receptor PLAUR (PubMed:15677461). Associates with CD4 or CD8 and delivers costimulatory signals for the TCR/CD3 pathway. Plays a role in TLR9 trafficking to acidified CpG-containing compartments by controlling interaction between TLR9 and VAMP3 and subsequent myddosome assembly (By similarity). Inhibits LPS-induced inflammatory response by preventing binding of LPS to TLR4 on the cell surface (PubMed:36945827). Plays a role in the activation of macrophages into anti-inflammatory phenotypes (By similarity). Independently of Toll-like receptor (TLR) signaling, is recruited to pathogen-containing phagosomes prior to fusion with lysosomes and thereby participates in antigen presentation (By similarity). Also acts to control angiogenesis and switch angiogenic milieu to quiescent state by binding and sequestering VEGFA and PDGFB to inhibit the signaling they trigger via their respective cell surface receptor (PubMed:34530889)", "gene_name": "CD82", "glycan_count": 13, "glycosylation_sites": [ { "position": 129, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 157, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 198, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P27701", "name": "CD82", "organism": "Homo sapiens", "uniprot_id": "P27701" }, { "function": "Membrane metallopeptidase that sheds many membrane-bound proteins. Exhibits a strong preference for acidic amino acids at the P1' position. Known substrates include: FGF19, VGFA, IL1B, IL18, procollagen I and III, E-cadherin, KLK7, gastrin, ADAM10, tenascin-C. The presence of several pro-inflammatory cytokine among substrates implicate MEP1B in inflammation. It is also involved in tissue remodeling due to its capability to degrade extracellular matrix components. Also cleaves the amyloid precursor protein/APP, thereby releasing neurotoxic amyloid beta peptides (PubMed:27180357)", "gene_name": "MEP1B", "glycan_count": 8, "glycosylation_sites": [ { "position": 218, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 254, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 370, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 421, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 436, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 445, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 547, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 592, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 593, "type": "O-linked (GalNAc...) serine" }, { "position": 594, "type": "O-linked (GalNAc...) threonine" }, { "position": 599, "type": "O-linked (GalNAc...) threonine" }, { "position": 603, "type": "O-linked (GalNAc...) serine" } ], "id": "Q16820", "name": "Meprin \u03b2", "organism": "Homo sapiens", "uniprot_id": "Q16820" }, { "function": "Has DNA hydrolytic activity. Is capable of both single- and double-stranded DNA cleavage, producing DNA fragments with 3'-OH ends (By similarity). Can cleave chromatin to nucleosomal units and cleaves nucleosomal and liposome-coated DNA (PubMed:10807908, PubMed:14646506, PubMed:27293190, PubMed:9070308, PubMed:9714828). Acts in internucleosomal DNA fragmentation (INDF) during apoptosis and necrosis (PubMed:23229555, PubMed:24312463). The role in apoptosis includes myogenic and neuronal differentiation, and BCR-mediated clonal deletion of self-reactive B cells (By similarity). Is active on chromatin in apoptotic cell-derived membrane-coated microparticles and thus suppresses anti-DNA autoimmunity (PubMed:27293190). Together with DNASE1, plays a key role in degrading neutrophil extracellular traps (NETs) (By similarity). NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (By similarity). Degradation of intravascular NETs by DNASE1 and DNASE1L3 is required to prevent formation of clots that obstruct blood vessels and cause organ damage following inflammation (By similarity)", "gene_name": "DNASE1L3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q13609", "name": "DNASE1L3", "organism": "Homo sapiens", "uniprot_id": "Q13609" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P17948/P35968", "name": "Vascular Endothelial Growth Factor Receptor (VEGFR-1/VEGFR-2)", "organism": "", "uniprot_id": "" }, { "function": "Growth factor that mediates its effects via EGFR, ERBB2 and ERBB4. Required for normal cardiac valve formation and normal heart function. Promotes smooth muscle cell proliferation. May be involved in macrophage-mediated cellular proliferation. It is mitogenic for fibroblasts, but not endothelial cells. It is able to bind EGF receptor/EGFR with higher affinity than EGF itself and is a far more potent mitogen for smooth muscle cells than EGF. Also acts as a diphtheria toxin receptor", "gene_name": "HBEGF", "glycan_count": 6, "glycosylation_sites": [ { "position": 37, "type": "O-linked (GalNAc...) threonine" }, { "position": 38, "type": "O-linked (GalNAc...) serine" }, { "position": 44, "type": "O-linked (GalNAc...) threonine" }, { "position": 47, "type": "O-linked (GalNAc...) threonine" }, { "position": 75, "type": "O-linked (GalNAc...) threonine" }, { "position": 85, "type": "O-linked (GalNAc...) threonine" } ], "id": "Q99075", "name": "Heparin-binding EGF-like growth factor (HB-EGF)", "organism": "Homo sapiens", "uniprot_id": "Q99075" }, { "function": "May act as a scaffolding protein within caveolar membranes. Interacts directly with G-protein alpha subunits and can functionally regulate their activity. Acts as an accessory protein in conjunction with CAV1 in targeting to lipid rafts and driving caveolae formation. The Ser-36 phosphorylated form has a role in modulating mitosis in endothelial cells. Positive regulator of cellular mitogenesis of the MAPK signaling pathway. Required for the insulin-stimulated nuclear translocation and activation of MAPK1 and STAT3, and the subsequent regulation of cell cycle progression (By similarity)", "gene_name": "CAV2", "glycan_count": 0, "glycosylation_sites": [], "id": "P51636", "name": "Caveolin-2", "organism": "Homo sapiens", "uniprot_id": "P51636" }, { "function": "Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. May be involved in the stability of secreted lipases", "gene_name": "sspA", "glycan_count": 0, "glycosylation_sites": [], "id": "P0C1U8", "name": "Coagulase (Staphylocoagulase)", "organism": "Staphylococcus aureus", "uniprot_id": "P0C1U8" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9I4S7", "name": "MexB efflux pump", "organism": "Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)", "uniprot_id": "Q9I4S7" }, { "function": "Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa. Acts as a key regulator of adaptive thermogenesis as part of the futile creatine cycle: localizes to the mitochondria of thermogenic fat cells and acts by mediating phosphorylation of creatine to initiate a futile cycle of creatine phosphorylation and dephosphorylation. During the futile creatine cycle, creatine and N-phosphocreatine are in a futile cycle, which dissipates the high energy charge of N-phosphocreatine as heat without performing any mechanical or chemical work", "gene_name": "Ckb", "glycan_count": 1, "glycosylation_sites": [], "id": "P07335", "name": "Creatine kinase (CK)", "organism": "Rattus norvegicus", "uniprot_id": "P07335" }, { "function": "E3 ubiquitin ligase that plays a crucial role in the activation of the IKBKE-dependent branch of the type I interferon signaling pathway (PubMed:24882218, PubMed:31694946). In concert with the ubiquitin-conjugating E2 enzyme UBE2K, synthesizes unanchored 'Lys-48'-linked polyubiquitin chains that promote the oligomerization and autophosphorylation of IKBKE leading to stimulation of an antiviral response (PubMed:24882218). Also ubiquitinates MYC and inhibits its transcription activation activity, maintaining the pluripotency of embryonic stem cells (By similarity). Promotes the association of unanchored 'Lys-48'-polyubiquitin chains with DHX16 leading to enhanced RIGI-mediated innate antiviral immune response (PubMed:35263596)", "gene_name": "TRIM6", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9C030", "name": "TRIM56", "organism": "Homo sapiens", "uniprot_id": "Q9C030" }, { "function": "Serine protease which possesses both gelatinolytic and caseinolytic activities. Shows a preference for Arg in the P1 position", "gene_name": "TMPRSS11E", "glycan_count": 0, "glycosylation_sites": [ { "position": 75, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 166, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 223, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UL52", "name": "Proadrenomedullin", "organism": "Homo sapiens", "uniprot_id": "Q9UL52" }, { "function": "", "gene_name": "UPRT", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96BW1", "name": "CTHRC1", "organism": "Homo sapiens", "uniprot_id": "Q96BW1" }, { "function": "Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols (PubMed:12732097, PubMed:18087047, PubMed:19013440, PubMed:19563777, PubMed:9565553). Displays strong enzymatic activity toward all-trans-retinal, 9-cis-retinal, and 13-cis-retinal (PubMed:12732097, PubMed:18087047). Plays a critical role in detoxifying dietary and lipid-derived unsaturated carbonyls, such as crotonaldehyde, 4-hydroxynonenal, trans-2-hexenal, trans-2,4-hexadienal and their glutathione-conjugates carbonyls (GS-carbonyls) (PubMed:19013440, PubMed:19563777). Displays no reductase activity towards glucose (PubMed:12732097)", "gene_name": "AKR1B10", "glycan_count": 1, "glycosylation_sites": [], "id": "O60218", "name": "AKR1B10", "organism": "Homo sapiens", "uniprot_id": "O60218" }, { "function": "Serine protease with trypsin- and chymotrypsin-like specificity (PubMed:29652924, PubMed:8194606). Also displays antibacterial activity against Gram-negative and Gram-positive bacteria independent of its protease activity (PubMed:2116408, PubMed:2117044). Prefers Phe and Tyr residues in the P1 position of substrates but also cleaves efficiently after Trp and Leu (PubMed:29652924). Shows a preference for negatively charged amino acids in the P2' position and for aliphatic amino acids both upstream and downstream of the cleavage site (PubMed:29652924). Required for recruitment and activation of platelets which is mediated by the F2RL3/PAR4 platelet receptor (PubMed:10702240, PubMed:3390156). Binds reversibly to and stimulates B cells and CD4(+) and CD8(+) T cells (PubMed:7842483, PubMed:9000539). Also binds reversibly to natural killer (NK) cells and enhances NK cell cytotoxicity through its protease activity (PubMed:9000539, PubMed:9536127). Cleaves complement C3 (PubMed:1861080). Cleaves vimentin (By similarity). Cleaves thrombin receptor F2R/PAR1 and acts as either an agonist or an inhibitor, depending on the F2R cleavage site (PubMed:10702240, PubMed:7744748). Cleavage of F2R at '41-Arg-|-Ser-42' results in receptor activation while cleavage at '55-Phe-|-Trp-56' results in inhibition of receptor activation (PubMed:7744748). Cleaves the synovial mucin-type protein PRG4/lubricin (PubMed:32144329). Cleaves and activates IL36G which promotes expression of chemokines CXCL1 and CXLC8 in keratinocytes (PubMed:30804664). Cleaves IL33 into mature forms which have greater activity than the unprocessed form (PubMed:22307629). Cleaves coagulation factor F8 to produce a partially activated form (PubMed:18217133). Also cleaves and activates coagulation factor F10 (PubMed:8920993). Cleaves leukocyte cell surface protein SPN/CD43 to release its extracellular domain and trigger its intramembrane proteolysis by gamma-secretase, releasing the CD43 cytoplasmic tail chain (CD43-ct) which translocates to the nucleus (PubMed:18586676). Cleaves CCL5/RANTES to produce RANTES(4-68) lacking the N-terminal three amino acids which exhibits reduced chemotactic and antiviral activities (PubMed:16963625). During apoptosis, cleaves SMARCA2/BRM to produce a 160 kDa cleavage product which localizes to the cytosol (PubMed:11259672). Cleaves myelin basic protein MBP in B cell lysosomes at '224-Phe-|-Lys-225' and '248-Phe-|-Ser-249', degrading the major immunogenic MBP epitope and preventing the activation of MBP-specific autoreactive T cells (PubMed:15100291). Cleaves annexin ANXA1 and antimicrobial peptide CAMP to produce peptides which act on neutrophil N-formyl peptide receptors to enhance the release of CXCL2 (PubMed:22879591). Acts as a ligand for the N-formyl peptide receptor FPR1, enhancing phagocyte chemotaxis (PubMed:15210802). Has antibacterial activity against the Gram-negative bacteria N.gonorrhoeae and P.aeruginosa (PubMed:1937776, PubMed:2116408). Likely to act against N.gonorrhoeae by interacting with N.gonorrhoeae penA/PBP2 (PubMed:2126324). Exhibits potent antimicrobial activity against the Gram-positive bacterium L.monocytogenes (PubMed:2117044). Has antibacterial activity against the Gram-positive bacterium S.aureus and degrades S.aureus biofilms, allowing polymorphonuclear leukocytes to penetrate the biofilm and phagocytose bacteria (PubMed:2117044, PubMed:32995850). Has antibacterial activity against M.tuberculosis (PubMed:15385470). Mediates CASP4 activation induced by the Td92 surface protein of the periodontal pathogen T.denticola, causing production and secretion of IL1A and leading to pyroptosis of gingival fibroblasts (PubMed:29077095). Induces platelet aggregation which is strongly potentiated in the presence of ELANE (PubMed:25211214, PubMed:9111081)", "gene_name": "CTSG", "glycan_count": 7, "glycosylation_sites": [ { "position": 71, "type": "N-linked (GlcNAc...) (complex) asparagine; alternate" }, { "position": 71, "type": "N-linked (GlcNAc...) (paucimannose) asparagine; alternate" } ], "id": "P08311", "name": "Cathepsin G", "organism": "Homo sapiens", "uniprot_id": "P08311" }, { "function": "This is a neutrophil granule-derived antibacterial and monocyte- and fibroblast-specific chemotactic glycoprotein. Binds heparin. The cytotoxic action is limited to many species of Gram-negative bacteria; this specificity may be explained by a strong affinity of the very basic N-terminal half for the negatively charged lipopolysaccharides that are unique to the Gram-negative bacterial outer envelope. It may play a role in mediating recruitment of monocytes in the second wave of inflammation. Has antibacterial activity against the Gram-negative bacterium P.aeruginosa, this activity is inhibited by LPS from P.aeruginosa. Acting alone, it does not have antimicrobial activity against the Gram-negative bacteria A.actinomycetemcomitans ATCC 29532, A.actinomycetemcomitans NCTC 9709, A.actinomycetemcomitans FDC-Y4, H.aphrophilus ATCC 13252, E.corrodens ATCC 23834, C.sputigena ATCC 33123, Capnocytophaga sp ATCC 33124, Capnocytophaga sp ATCC 27872 or E.coli ML-35. Has antibacterial activity against C.sputigena ATCC 33123 when acting synergistically with either elastase or cathepsin G", "gene_name": "AZU1", "glycan_count": 28, "glycosylation_sites": [ { "position": 126, "type": "N-linked (GlcNAc...) asparagine; partial" }, { "position": 140, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 171, "type": "N-linked (GlcNAc...) asparagine; partial" } ], "id": "P20160", "name": "Azurocidin", "organism": "Homo sapiens", "uniprot_id": "P20160" }, { "function": "Alkaline phosphatase that can hydrolyze various phosphate compounds", "gene_name": "ALPI", "glycan_count": 33, "glycosylation_sites": [ { "position": 141, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 268, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 429, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P09923", "name": "Alkaline phosphatase (ALP)", "organism": "Homo sapiens", "uniprot_id": "P09923" }, { "function": "Could be a 3Fe-4S cluster-containing protein", "gene_name": "fixX", "glycan_count": 0, "glycosylation_sites": [], "id": "P53658", "name": "Alanine aminotransferase (ALT)", "organism": "Azotobacter vinelandii", "uniprot_id": "P53658" }, { "function": "Receptor for TNFSF11/RANKL/TRANCE/OPGL; essential for RANKL-mediated osteoclastogenesis (PubMed:9878548). Its interaction with EEIG1 promotes osteoclastogenesis via facilitating the transcription of NFATC1 and activation of PLCG2 (By similarity). Involved in the regulation of interactions between T-cells and dendritic cells (By similarity)", "gene_name": "TNFRSF11A", "glycan_count": 1, "glycosylation_sites": [ { "position": 105, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 174, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y6Q6", "name": "OX40L (CD252, TNFSF4, GP34)", "organism": "Homo sapiens", "uniprot_id": "Q9Y6Q6" }, { "function": "Binds to transferrin receptor (TFR) and reduces its affinity for iron-loaded transferrin", "gene_name": "HFE", "glycan_count": 4, "glycosylation_sites": [ { "position": 110, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 130, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 234, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q30201", "name": "HFE", "organism": "Homo sapiens", "uniprot_id": "Q30201" }, { "function": "Mediates cellular uptake of transferrin-bound iron in a non-iron dependent manner. May be involved in iron metabolism, hepatocyte function and erythrocyte differentiation", "gene_name": "TFR2", "glycan_count": 0, "glycosylation_sites": [ { "position": 240, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 339, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 540, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 754, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UP52", "name": "Transferrin receptor 2 (TFR2)", "organism": "Homo sapiens", "uniprot_id": "Q9UP52" }, { "function": "Acts as a bone morphogenetic protein (BMP) coreceptor (PubMed:18976966). Through enhancement of BMP signaling regulates hepcidin (HAMP) expression and regulates iron homeostasis (PubMed:18976966)", "gene_name": "HJV", "glycan_count": 1, "glycosylation_sites": [ { "position": 118, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 213, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 372, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6ZVN8", "name": "Hemojuvelin (HJV)", "organism": "Homo sapiens", "uniprot_id": "Q6ZVN8" }, { "function": "Potent circulating inhibitor of angiogenesis. Signals through the type I activin receptor ACVRL1 but not other Alks. Signaling through SMAD1 in endothelial cells requires TGF-beta coreceptor endoglin/ENG", "gene_name": "GDF2", "glycan_count": 1, "glycosylation_sites": [ { "position": 71, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 136, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UK05", "name": "Bone morphogenetic protein 6 (BMP6)", "organism": "Homo sapiens", "uniprot_id": "Q9UK05" }, { "function": "Component of the primary cilium that controls cilium formation and length (PubMed:31712586). May function within retrograde intraflagellar transport (IFT)-associated pathways to remove signaling proteins from primary cilia (PubMed:31712586). Also involved in neuronal vesicle biogenesis and neurotransmitter vesicular function (PubMed:33230203)", "gene_name": "ERICH3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q5RHP9", "name": "Fibulin 3 (EFEMP1)", "organism": "Homo sapiens", "uniprot_id": "Q5RHP9" }, { "function": "Cleaves C-terminal arginine or lysine residues from biologically active peptides such as kinins or anaphylatoxins in the circulation thereby regulating their activities. Down-regulates fibrinolysis by removing C-terminal lysine residues from fibrin that has already been partially degraded by plasmin", "gene_name": "CPB2", "glycan_count": 40, "glycosylation_sites": [ { "position": 44, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 73, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 85, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 108, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 241, "type": "N-linked (GlcNAc...) asparagine; partial" } ], "id": "Q96IY4", "name": "Thrombin-activatable fibrinolysis inhibitor (TAFI)", "organism": "Homo sapiens", "uniprot_id": "Q96IY4" }, { "function": "Seems to act as an adapter protein between membrane proteins and the actin cytoskeleton (PubMed:10339567). In collaboration with CBLC, modulates the rate of RET turnover and may act as regulatory checkpoint that limits the potency of GDNF on neuronal survival. Controls CBLC function, converting it from an inhibitor to a promoter of RET degradation (By similarity). May play a role in receptor clustering and cytoskeletal polarity in the junction between T-cell and antigen-presenting cell (By similarity). May anchor the podocyte slit diaphragm to the actin cytoskeleton in renal glomerolus. Also required for cytokinesis (PubMed:15800069). Plays a role in epithelial cell junctions formation (PubMed:22891260)", "gene_name": "CD2AP", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y5K6", "name": "CD2-associated protein (CD2AP)", "organism": "Homo sapiens", "uniprot_id": "Q9Y5K6" }, { "function": "Catalytic subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:8463241). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment (PubMed:32001091). In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation (PubMed:28296633). May play a role in neurite development and synaptic connectivity (PubMed:29668857)", "gene_name": "ATP6V1A", "glycan_count": 1, "glycosylation_sites": [], "id": "P38606", "name": "V-ATPase subunit ATP6V1A", "organism": "Homo sapiens", "uniprot_id": "P38606" }, { "function": "Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components", "gene_name": "LAMC3", "glycan_count": 17, "glycosylation_sites": [ { "position": 87, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 119, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 295, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 328, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 631, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 837, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 980, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1185, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y6N6", "name": "Synaptopodin", "organism": "Homo sapiens", "uniprot_id": "Q9Y6N6" }, { "function": "Serine/threonine-protein kinase involved in different processes such as membrane blebbing and apoptotic bodies formation DNA damage response and MAPK14/p38 MAPK stress-activated MAPK cascade. Phosphorylates itself, MBP, activated MAPK8, MAP2K3, MAP2K6 and tubulins. Activates the MAPK14/p38 MAPK signaling pathway through the specific activation and phosphorylation of the upstream MAP2K3 and MAP2K6 kinases. In response to DNA damage, involved in the G2/M transition DNA damage checkpoint by activating the p38/MAPK14 stress-activated MAPK cascade, probably by mediating phosphorylation of upstream MAP2K3 and MAP2K6 kinases. Isoform 1, but not isoform 2, plays a role in apoptotic morphological changes, including cell contraction, membrane blebbing and apoptotic bodies formation. This function, which requires the activation of MAPK8/JNK and nuclear localization of C-terminally truncated isoform 1, may be linked to the mitochondrial CASP9-associated death pathway. Isoform 1 binds to microtubules and affects their organization and stability independently of its kinase activity. Prevents MAP3K7-mediated activation of CHUK, and thus NF-kappa-B activation, but not that of MAPK8/JNK. May play a role in the osmotic stress-MAPK8 pathway. Isoform 2, but not isoform 1, is required for PCDH8 endocytosis. Following homophilic interactions between PCDH8 extracellular domains, isoform 2 phosphorylates and activates MAPK14/p38 MAPK which in turn phosphorylates isoform 2. This process leads to PCDH8 endocytosis and CDH2 cointernalization. Both isoforms are involved in MAPK14 phosphorylation", "gene_name": "TAOK2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UL54", "name": "TAO Kinase 1", "organism": "Homo sapiens", "uniprot_id": "Q9UL54" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P36334 (hCoV-OC43), P0DTC2 (SARS-CoV-2)", "name": "Spike glycoprotein (S)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03468 (Influenza A)", "name": "Neuraminidase (NA)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03423 (RSV)", "name": "G glycoprotein", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "YK3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9M5I1", "name": "BanLec", "organism": "Oryza sativa subsp. japonica", "uniprot_id": "Q9M5I1" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6Y2C5", "name": "Griffithsin", "organism": "Hepacivirus hominis", "uniprot_id": "Q6Y2C5" }, { "function": "G protein-coupled receptor that is activated by a major product of dietary fiber digestion, the short chain fatty acids (SCFAs), and that plays a role in the regulation of whole-body energy homeostasis and in intestinal immunity. In omnivorous mammals, the short chain fatty acids acetate, propionate and butyrate are produced primarily by the gut microbiome that metabolizes dietary fibers. SCFAs serve as a source of energy but also act as signaling molecules. That G protein-coupled receptor is probably coupled to the pertussis toxin-sensitive, G(i/o)-alpha family of G proteins but also to the Gq family (PubMed:12496283, PubMed:12711604, PubMed:23589301). Its activation results in the formation of inositol 1,4,5-trisphosphate, the mobilization of intracellular calcium, the phosphorylation of the MAPK3/ERK1 and MAPK1/ERK2 kinases and the inhibition of intracellular cAMP accumulation. May play a role in glucose homeostasis by regulating the secretion of GLP-1, in response to short-chain fatty acids accumulating in the intestine. May also regulate the production of LEP/Leptin, a hormone acting on the central nervous system to inhibit food intake. Finally, may also regulate whole-body energy homeostasis through adipogenesis regulating both differentiation and lipid storage of adipocytes. In parallel to its role in energy homeostasis, may also mediate the activation of the inflammatory and immune responses by SCFA in the intestine, regulating the rapid production of chemokines and cytokines. May also play a role in the resolution of the inflammatory response and control chemotaxis in neutrophils. In addition to SCFAs, may also be activated by the extracellular lectin FCN1 in a process leading to activation of monocytes and inducing the secretion of interleukin-8/IL-8 in response to the presence of microbes (PubMed:21037097). Among SCFAs, the fatty acids containing less than 6 carbons, the most potent activators are probably acetate, propionate and butyrate (PubMed:12496283, PubMed:12711604). Exhibits a SCFA-independent constitutive G protein-coupled receptor activity (PubMed:23066016)", "gene_name": "FFAR2", "glycan_count": 0, "glycosylation_sites": [ { "position": 151, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 167, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O15552", "name": "GPR43 (FFAR2)", "organism": "Homo sapiens", "uniprot_id": "O15552" }, { "function": "G protein-coupled receptor that is activated by a major product of dietary fiber digestion, the short chain fatty acids (SCFAs), and that plays a role in the regulation of whole-body energy homeostasis and in intestinal immunity. In omnivorous mammals, the short chain fatty acids acetate, propionate and butyrate are produced primarily by the gut microbiome that metabolizes dietary fibers. SCFAs serve as a source of energy but also act as signaling molecules. That G protein-coupled receptor is probably coupled to the pertussis toxin-sensitive, G(i/o)-alpha family of G proteins. Its activation results in the formation of inositol 1,4,5-trisphosphate, the mobilization of intracellular calcium, the phosphorylation of the MAPK3/ERK1 and MAPK1/ERK2 kinases and the inhibition of intracellular cAMP accumulation (PubMed:12711604). Activated by SCFAs and by beta-hydroxybutyrate, a ketone body produced by the liver upon starvation, it inhibits N-type calcium channels and modulates the activity of sympathetic neurons through a signaling cascade involving the beta and gamma subunits of its coupled G protein, phospholipase C and MAP kinases. Thereby, it may regulate energy expenditure through the control of the sympathetic nervous system that controls for instance heart rate. Upon activation by SCFAs accumulating in the intestine, it may also signal to the brain via neural circuits which in turn would regulate intestinal gluconeogenesis. May also control the production of hormones involved in whole-body energy homeostasis. May for instance, regulate blood pressure through renin secretion. May also regulate secretion of the PYY peptide by enteroendocrine cells and control gut motility, intestinal transit rate, and the harvesting of energy from SCFAs produced by gut microbiota. May also indirectly regulate the production of LEP/Leptin, a hormone acting on the CNS to inhibit food intake, in response to the presence of short-chain fatty acids in the intestine. Finally, may also play a role in glucose homeostasis. Besides its role in energy homeostasis, may play a role in intestinal immunity. May mediate the activation of the inflammatory and immune response by SCFAs in the gut, regulating the rapid production of chemokines and cytokines by intestinal epithelial cells. Among SCFAs, the fatty acids containing less than 6 carbons, the most potent activators are probably propionate, butyrate and pentanoate while acetate is a poor activator (PubMed:12496283, PubMed:12711604)", "gene_name": "FFAR3", "glycan_count": 0, "glycosylation_sites": [ { "position": 166, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O14843", "name": "GPR41 (FFAR3)", "organism": "Homo sapiens", "uniprot_id": "O14843" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q13547/Q92769", "name": "HDAC1/2", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Derived from APP", "name": "Amyloid-beta (A\u03b2)", "organism": "", "uniprot_id": "" }, { "function": "Catalyzes the translocation of specific phospholipids from the cytoplasmic to the extracellular/lumenal leaflet of membrane coupled to the hydrolysis of ATP (PubMed:24097981). Transports preferentially phosphatidylserine over phosphatidylcholine (PubMed:24097981). Plays a role in lipid homeostasis and macrophage-mediated phagocytosis (PubMed:12917409, PubMed:12925201, PubMed:14570867, PubMed:14592415). Binds APOA1 and may function in apolipoprotein-mediated phospholipid efflux from cells (PubMed:12917409, PubMed:14570867, PubMed:14592415). May also mediate cholesterol efflux (PubMed:14570867). May regulate cellular ceramide homeostasis during keratinocyte differentiation (PubMed:12925201). Involved in lipid raft organization and CD1D localization on thymocytes and antigen-presenting cells, which plays an important role in natural killer T-cell development and activation (By similarity). Plays a role in phagocytosis of apoptotic cells by macrophages (By similarity). Macrophage phagocytosis is stimulated by APOA1 or APOA2, probably by stabilization of ABCA7 (By similarity). Also involved in phagocytic clearance of amyloid-beta by microglia cells and macrophages (By similarity). Further limits amyloid-beta production by playing a role in the regulation of amyloid-beta A4 precursor protein (APP) endocytosis and/or processing (PubMed:26260791). Amyloid-beta is the main component of amyloid plaques found in the brains of Alzheimer patients (PubMed:26260791)", "gene_name": "ABCA7", "glycan_count": 5, "glycosylation_sites": [ { "position": 312, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8IZY2", "name": "ABCA7", "organism": "Homo sapiens", "uniprot_id": "Q8IZY2" }, { "function": "A beta chain of antigen-presenting major histocompatibility complex class II (MHCII) molecule. In complex with the alpha chain HLA-DRA, displays antigenic peptides on professional antigen presenting cells (APCs) for recognition by alpha-beta T cell receptor (TCR) on HLA-DRB1-restricted CD4-positive T cells. This guides antigen-specific T-helper effector functions, both antibody-mediated immune response and macrophage activation, to ultimately eliminate the infectious agents and transformed cells (PubMed:15265931, PubMed:16148104, PubMed:22327072, PubMed:27591323, PubMed:29884618, PubMed:31495665, PubMed:8642306). Typically presents extracellular peptide antigens of 10 to 30 amino acids that arise from proteolysis of endocytosed antigens in lysosomes (PubMed:8145819). In the tumor microenvironment, presents antigenic peptides that are primarily generated in tumor-resident APCs likely via phagocytosis of apoptotic tumor cells or macropinocytosis of secreted tumor proteins (PubMed:31495665). Presents peptides derived from intracellular proteins that are trapped in autolysosomes after macroautophagy, a mechanism especially relevant for T cell selection in the thymus and central immune tolerance (PubMed:17182262, PubMed:23783831). The selection of the immunodominant epitopes follows two processing modes: 'bind first, cut/trim later' for pathogen-derived antigenic peptides and 'cut first, bind later' for autoantigens/self-peptides (PubMed:25413013). The anchor residue at position 1 of the peptide N-terminus, usually a large hydrophobic residue, is essential for high affinity interaction with MHCII molecules (PubMed:8145819)", "gene_name": "HLA-DRB1", "glycan_count": 56, "glycosylation_sites": [ { "position": 48, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01911", "name": "HLA-DRB1*15", "organism": "Homo sapiens", "uniprot_id": "P01911" }, { "function": "Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading", "gene_name": "HLA-DQB1", "glycan_count": 0, "glycosylation_sites": [ { "position": 51, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01920", "name": "HLA-DQB1*06:02", "organism": "Homo sapiens", "uniprot_id": "P01920" }, { "function": "Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading", "gene_name": "HLA-DQA2", "glycan_count": 0, "glycosylation_sites": [ { "position": 104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 144, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01906", "name": "HLA-DQA1*01:02", "organism": "Homo sapiens", "uniprot_id": "P01906" }, { "function": "Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CXCL11 and CXCL12/SDF1 (PubMed:16107333, PubMed:19255243, PubMed:19380869, PubMed:20161793, PubMed:22300987). Chemokine binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalization and activation of MAPK signaling pathway (PubMed:16940167, PubMed:18653785, PubMed:20018651). Required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness (PubMed:16940167, PubMed:18653785). In glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis. Promotes cell growth and survival (PubMed:16940167, PubMed:20388803). Not involved in cell migration, adhesion or proliferation of normal hematopoietic progenitors but activated by CXCL11 in malignant hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration (PubMed:17804806, PubMed:18653785, PubMed:19641136, PubMed:20887389). Plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12 (PubMed:18653785). Required for heart valve development (PubMed:17804806). Regulates axon guidance in the oculomotor system through the regulation of CXCL12 levels (PubMed:31211835)", "gene_name": "ACKR3", "glycan_count": 1, "glycosylation_sites": [ { "position": 13, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 22, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 39, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P25106", "name": "ACKR3", "organism": "Homo sapiens", "uniprot_id": "P25106" }, { "function": "Plays a role in the apoptotic process and has a pro-apoptotic activity", "gene_name": "IFI27L2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H2X8", "name": "LEFTY2", "organism": "Homo sapiens", "uniprot_id": "Q9H2X8" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P05444", "name": "REG1A", "organism": "Fuscovulum blasticum", "uniprot_id": "P05444" }, { "function": "Transcriptional activator", "gene_name": "FOXC2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q99958", "name": "FOXC2", "organism": "Homo sapiens", "uniprot_id": "Q99958" }, { "function": "Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone", "gene_name": "NDUFA10", "glycan_count": 1, "glycosylation_sites": [], "id": "O95299", "name": "CCNA1", "organism": "Homo sapiens", "uniprot_id": "O95299" }, { "function": "Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane", "gene_name": "SPRR1A", "glycan_count": 1, "glycosylation_sites": [], "id": "P35321", "name": "SPRR2B", "organism": "Homo sapiens", "uniprot_id": "P35321" }, { "function": "Lectin that plays a role in innate immunity, apoptosis and embryogenesis (PubMed:21258343, PubMed:23954398, PubMed:25912189). Calcium-dependent lectin that binds self and non-self glycoproteins presenting high mannose oligosaccharides with at least one terminal alpha-1,2-linked mannose epitope (PubMed:25912189). Primarily recognizes the terminal disaccharide of the glycan (PubMed:25912189). Also recognizes a subset of fucosylated glycans and lipopolysaccharides (PubMed:17179669, PubMed:25912189). Plays a role in innate immunity through its ability to bind non-self sugars presented by microorganisms and to activate the complement through the recruitment of MAPS1 (PubMed:20956340, PubMed:25912189). Also plays a role in apoptosis through its ability to bind in a calcium-independent manner the DNA present at the surface of apoptotic cells and to activate the complement in response to this binding (Probable). Finally, plays a role in development, probably serving as a guidance cue during the migration of neural crest cells and other cell types during embryogenesis (PubMed:21258343, PubMed:28301481)", "gene_name": "COLEC11", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9BWP8", "name": "Collectin 11", "organism": "Homo sapiens", "uniprot_id": "Q9BWP8" }, { "function": "Self-ligand receptor of the signaling lymphocytic activation molecule (SLAM) family. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. Can mediate natural killer (NK) cell cytotoxicity dependent on SH2D1A and SH2D1B (By similarity). Increases proliferative responses of activated T-cells and SH2D1A/SAP does not seem be required for this process. Homophilic interactions enhance interferon gamma/IFNG secretion in lymphocytes and induce platelet stimulation via a SH2D1A-dependent pathway. May serve as a marker for hematopoietic progenitor cells (PubMed:11564780, PubMed:12115647, PubMed:12928397, PubMed:12962726, PubMed:16037392) Required for a prolonged T-cell:B-cell contact, optimal T follicular helper function, and germinal center formation. In germinal centers involved in maintaining B-cell tolerance and in preventing autoimmunity (By similarity). In mast cells negatively regulates high affinity immunoglobulin epsilon receptor signaling; independent of SH2D1A and SH2D1B but implicating FES and PTPN6/SHP-1 (PubMed:22068234). In macrophages enhances LPS-induced MAPK phosphorylation and NF-kappaB activation and modulates LPS-induced cytokine secretion; involving ITSM 2 (By similarity). Positively regulates macroautophagy in primary dendritic cells via stabilization of IRF8; inhibits TRIM21-mediated proteasomal degradation of IRF8 (PubMed:29434592)", "gene_name": "CD84", "glycan_count": 0, "glycosylation_sites": [ { "position": 150, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UIB8", "name": "SLAMF1 (CD150)", "organism": "Homo sapiens", "uniprot_id": "Q9UIB8" }, { "function": "Self-ligand receptor of the signaling lymphocytic activation molecule (SLAM) family. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. Can mediate natural killer (NK) cell cytotoxicity dependent on SH2D1A and SH2D1B (By similarity). Increases proliferative responses of activated T-cells and SH2D1A/SAP does not seem be required for this process. Homophilic interactions enhance interferon gamma/IFNG secretion in lymphocytes and induce platelet stimulation via a SH2D1A-dependent pathway. May serve as a marker for hematopoietic progenitor cells (PubMed:11564780, PubMed:12115647, PubMed:12928397, PubMed:12962726, PubMed:16037392) Required for a prolonged T-cell:B-cell contact, optimal T follicular helper function, and germinal center formation. In germinal centers involved in maintaining B-cell tolerance and in preventing autoimmunity (By similarity). In mast cells negatively regulates high affinity immunoglobulin epsilon receptor signaling; independent of SH2D1A and SH2D1B but implicating FES and PTPN6/SHP-1 (PubMed:22068234). In macrophages enhances LPS-induced MAPK phosphorylation and NF-kappaB activation and modulates LPS-induced cytokine secretion; involving ITSM 2 (By similarity). Positively regulates macroautophagy in primary dendritic cells via stabilization of IRF8; inhibits TRIM21-mediated proteasomal degradation of IRF8 (PubMed:29434592)", "gene_name": "CD84", "glycan_count": 0, "glycosylation_sites": [ { "position": 150, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UIB6", "name": "SLAMF5 (CD84)", "organism": "Homo sapiens", "uniprot_id": "Q9UIB8" }, { "function": "Interferon (IFN)-inducible GTPase that plays important roles in innate immunity against a diverse range of bacterial, viral and protozoan pathogens (By similarity). Hydrolyzes GTP, but in contrast to other family members, does not produce GMP (PubMed:20180847). Following infection, recruited to the pathogen-containing vacuoles or vacuole-escaped bacteria and acts as a positive regulator of inflammasome assembly by promoting the release of inflammasome ligands from bacteria (By similarity). Acts by promoting lysis of pathogen-containing vacuoles, releasing pathogens into the cytosol (By similarity). Following pathogen release in the cytosol, promotes recruitment of proteins that mediate bacterial cytolysis: this liberates ligands that are detected by inflammasomes, such as lipopolysaccharide (LPS) that activates the non-canonical CASP4/CASP11 inflammasome or double-stranded DNA (dsDNA) that activates the AIM2 inflammasome (By similarity). As an activator of NLRP3 inflammasome assembly: promotes selective NLRP3 inflammasome assembly in response to microbial and soluble, but not crystalline, agents (PubMed:22461501). Independently of its GTPase activity, acts as an inhibitor of various viruses infectivity, such as HIV-1, Zika and influenza A viruses, by inhibiting FURIN-mediated maturation of viral envelope proteins (PubMed:26996307, PubMed:31091448)", "gene_name": "GBP5", "glycan_count": 2, "glycosylation_sites": [], "id": "Q96PP8", "name": "GBP5", "organism": "Homo sapiens", "uniprot_id": "Q96PP8" }, { "function": "May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3", "gene_name": "MMP12", "glycan_count": 0, "glycosylation_sites": [ { "position": 20, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 285, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P39900", "name": "MMP12", "organism": "Homo sapiens", "uniprot_id": "P39900" }, { "function": "Interferon-inducible antiviral protein which plays a major role in the cell antiviral state induced by type I and type II interferon (PubMed:31812350). Catalyzes the conversion of cytidine triphosphate (CTP) to 3'-deoxy-3',4'-didehydro-CTP (ddhCTP) via a SAM-dependent radical mechanism (PubMed:29925952, PubMed:30872404). In turn, ddhCTP acts as a chain terminator for the RNA-dependent RNA polymerases from multiple viruses and directly inhibits viral replication (PubMed:29925952). Therefore, inhibits a wide range of DNA and RNA viruses, including human cytomegalovirus (HCMV), hepatitis C virus (HCV), west Nile virus (WNV), dengue virus, sindbis virus, influenza A virus, sendai virus, vesicular stomatitis virus (VSV), zika virus, and human immunodeficiency virus (HIV-1) (PubMed:29925952, PubMed:30587778, PubMed:30934824, PubMed:31921110). Also promotes TLR7 and TLR9-dependent production of IFN-beta production in plasmacytoid dendritic cells (pDCs) by facilitating 'Lys-63'-linked ubiquitination of IRAK1 by TRAF6 (PubMed:30872404). Plays a role in CD4+ T-cells activation and differentiation. Facilitates T-cell receptor (TCR)-mediated GATA3 activation and optimal T-helper 2 (Th2) cytokine production by modulating NFKB1 and JUNB activities. Can inhibit secretion of soluble proteins", "gene_name": "RSAD2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8WXG1", "name": "RSAD2 (Viperin)", "organism": "Homo sapiens", "uniprot_id": "Q8WXG1" }, { "function": "5'->3' exonuclease that hydrolyzes the phosphodiester bond of single-stranded DNA (ssDNA) and RNA molecules to form nucleoside 3'-monophosphates and 5'-end 5'-hydroxy deoxyribonucleotide/ribonucleotide fragments (PubMed:30111894, PubMed:30312375, PubMed:34620855, PubMed:37225734, PubMed:37994783, PubMed:38537643, PubMed:38697119). Partially redundant with PLD4, can cleave all four nucleotides displaying higher efficiency for ssDNA and RNA fragments initiated with uridine and guanosine residues and lower efficiency for cytidine-initiated substrates (PubMed:30111894, PubMed:30312375, PubMed:34620855, PubMed:37225734, PubMed:37994783, PubMed:38537643, PubMed:38697119). As a result, it does not always degrade polynucleotides to the single nucleotide level, it can stall at specific sites sparing certain fragments from exonucleolytic degradation (PubMed:30111894, PubMed:30312375, PubMed:34620855, PubMed:37225734, PubMed:37994783, PubMed:38537643, PubMed:38697119). Processes self and pathogenic ssDNA and RNA molecules that reach the endolysosomal compartment via phagocytosis or autophagy and may serve as 'danger' signals for recognition by innate immune receptors such as toll-like receptors (TLRs) (PubMed:34620855, PubMed:37225734, PubMed:38697119). Degrades mitochondrial CpG-rich ssDNA fragments to prevent TLR9 activation and autoinflammatory response, but it can cleave viral RNA to generate ligands for TLR7 activation and initiate antiviral immune responses (PubMed:34620855, PubMed:37225734, PubMed:38697119). In plasmacytoid dendritic cells, it cooperates with endonuclease RNASET2 to release 2',3'-cyclic guanosine monophosphate (2',3'-cGMP), a potent stimulatory ligand for TLR7 (PubMed:34620855, PubMed:37225734, PubMed:38697119). Produces 2',3'-cGMPs and cytidine-rich RNA fragments that occupy TLR7 ligand-binding pockets and trigger a signaling-competent state (PubMed:34620855, PubMed:37225734, PubMed:38697119). Can exert polynucleotide phosphatase activity toward 5'-phosphorylated ssDNA substrates although at a slow rate (PubMed:38537643). Transphosphatidylase that catalyzes the exchange with R to S stereo-inversion of the glycerol moiety between (S,R)-lysophosphatidylglycerol (LPG) and monoacylglycerol (MAG) substrates to yield (S,S)-bis(monoacylglycero)phosphate (BMP) (PubMed:39423811). Can synthesize a variety of (S,S)-BMPs representing the main phospholipid constituent of lysosomal intralumenal vesicle (ILV) membranes that bind acid hydrolases for lipid degradation (PubMed:39423811). Regulates the homeostasis and interorganellar communication of the endolysosomal system with an overall impact on cellular removal of dysfunctional organelles via autophagy as well as proper protein and lipid turnover (PubMed:28128235, PubMed:29368044, PubMed:37225734). May play a role in myotube formation in response to ER stress (PubMed:22428023)", "gene_name": "PLD3", "glycan_count": 40, "glycosylation_sites": [ { "position": 97, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 132, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 236, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 284, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 387, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8IV08", "name": "PLD3", "organism": "Homo sapiens", "uniprot_id": "Q8IV08" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9QX05/Q7TSC7", "name": "GR-1 (Ly6G/Ly6C)", "organism": "", "uniprot_id": "" }, { "function": "Possible taste receptor", "gene_name": "Or13a27", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Z1T9", "name": "NK1.1 (Klrb1c)", "organism": "Mus musculus", "uniprot_id": "Q9Z1T9" }, { "function": "", "gene_name": "Ighg2b", "glycan_count": 6, "glycosylation_sites": [ { "position": 104, "type": "O-linked (GalNAc...) threonine" }, { "position": 185, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01867", "name": "TCR\u03b2", "organism": "Mus musculus", "uniprot_id": "P01867" }, { "function": "Promotes renal phosphate excretion and inhibits intestinal phosphate absorption (PubMed:14962809, PubMed:19005008). Promotes bone mineralization by osteoblasts and cartilage mineralization by chondrocytes (PubMed:18162525, PubMed:19998030, PubMed:22766095). Regulates the mineralization of the extracellular matrix of the craniofacial complex, such as teeth, bone and cartilage (By similarity). Promotes dental pulp stem cell proliferation and differentiation (PubMed:22341070)", "gene_name": "MEPE", "glycan_count": 1, "glycosylation_sites": [ { "position": 256, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 477, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 478, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NQ76", "name": "Matrix extracellular phosphoglycoprotein (MEPE)", "organism": "Homo sapiens", "uniprot_id": "Q9NQ76" }, { "function": "Involved in endochondral bone formation as negative regulator of bone mineralization. Stimulates the proliferation of endothelial cells and promotes angiogenesis. Inhibits MMP9 proteolytic activity", "gene_name": "ECM1", "glycan_count": 48, "glycosylation_sites": [ { "position": 354, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 444, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 530, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q16610", "name": "ECM1", "organism": "Homo sapiens", "uniprot_id": "Q16610" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04578-2", "name": "HIV-1 gp41", "organism": "", "uniprot_id": "" }, { "function": "Tetanus toxin acts by inhibiting neurotransmitter release. It binds to peripheral neuronal synapses, is internalized and moves by retrograde transport up the axon into the spinal cord where it can move between postsynaptic and presynaptic neurons. It inhibits neurotransmitter release by acting as a zinc endopeptidase that catalyzes the hydrolysis of the '76-Gln-|-Phe-77' bond of synaptobrevin-2", "gene_name": "tetX", "glycan_count": 0, "glycosylation_sites": [], "id": "P04958", "name": "Tetanus toxoid", "organism": "Clostridium tetani (strain Massachusetts / E88)", "uniprot_id": "P04958" }, { "function": "Has chemotactic activity for neutrophils. May play a role in inflammation and exerts its effects on endothelial cells in an autocrine fashion. In vitro, the processed forms GRO-alpha(4-73), GRO-alpha(5-73) and GRO-alpha(6-73) show a 30-fold higher chemotactic activity", "gene_name": "CXCL1", "glycan_count": 0, "glycosylation_sites": [], "id": "P09341", "name": "CXCL1", "organism": "Homo sapiens", "uniprot_id": "P09341" }, { "function": "Monokine with inflammatory and chemokinetic properties. Binds to CCR5. One of the major HIV-suppressive factors produced by CD8+ T-cells. Recombinant MIP-1-beta induces a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV). The processed form MIP-1-beta(3-69) retains the abilities to induce down-modulation of surface expression of the chemokine receptor CCR5 and to inhibit the CCR5-mediated entry of HIV-1 in T-cells. MIP-1-beta(3-69) is also a ligand for CCR1 and CCR2 isoform B", "gene_name": "CCL4", "glycan_count": 0, "glycosylation_sites": [], "id": "P13236", "name": "CCL4", "organism": "Homo sapiens", "uniprot_id": "P13236" }, { "function": "Catalyzes the oxygenation of arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate) to 5-hydroperoxyeicosatetraenoate (5-HPETE) followed by the dehydration to 5,6- epoxyeicosatetraenoate (Leukotriene A4/LTA4), the first two steps in the biosynthesis of leukotrienes, which are potent mediators of inflammation (PubMed:19022417, PubMed:21233389, PubMed:22516296, PubMed:23246375, PubMed:24282679, PubMed:24893149, PubMed:31664810, PubMed:8615788, PubMed:8631361). Also catalyzes the oxygenation of arachidonate into 8-hydroperoxyicosatetraenoate (8-HPETE) and 12-hydroperoxyicosatetraenoate (12-HPETE) (PubMed:23246375). Displays lipoxin synthase activity being able to convert (15S)-HETE into a conjugate tetraene (PubMed:31664810). Although arachidonate is the preferred substrate, this enzyme can also metabolize oxidized fatty acids derived from arachidonate such as (15S)-HETE, eicosapentaenoate (EPA) such as (18R)- and (18S)-HEPE or docosahexaenoate (DHA) which lead to the formation of specialized pro-resolving mediators (SPM) lipoxin and resolvins E and D respectively, therefore it participates in anti-inflammatory responses (PubMed:17114001, PubMed:21206090, PubMed:31664810, PubMed:32404334, PubMed:8615788). Oxidation of DHA directly inhibits endothelial cell proliferation and sprouting angiogenesis via peroxisome proliferator-activated receptor gamma (PPARgamma) (By similarity). It does not catalyze the oxygenation of linoleic acid and does not convert (5S)-HETE to lipoxin isomers (PubMed:31664810). In addition to inflammatory processes, it participates in dendritic cell migration, wound healing through an antioxidant mechanism based on heme oxygenase-1 (HO-1) regulation expression, monocyte adhesion to the endothelium via ITGAM expression on monocytes (By similarity). Moreover, it helps establish an adaptive humoral immunity by regulating primary resting B cells and follicular helper T cells and participates in the CD40-induced production of reactive oxygen species (ROS) after CD40 ligation in B cells through interaction with PIK3R1 that bridges ALOX5 with CD40 (PubMed:21200133). May also play a role in glucose homeostasis, regulation of insulin secretion and palmitic acid-induced insulin resistance via AMPK (By similarity). Can regulate bone mineralization and fat cell differentiation increases in induced pluripotent stem cells (By similarity)", "gene_name": "ALOX5", "glycan_count": 0, "glycosylation_sites": [], "id": "P09917", "name": "5-lipoxygenase (5-LO)", "organism": "Homo sapiens", "uniprot_id": "P09917" }, { "function": "Belongs to an adhesion system, which plays a role in the organization of homotypic, interneuronal and heterotypic cell-cell adherens junctions (AJs). May connect the nectin-afadin and E-cadherin-catenin system through alpha-actinin and may be involved in organization of the actin cytoskeleton at AJs through afadin and alpha-actinin (By similarity). Involved in cell movement: localizes at the leading edge of moving cells in response to PDGF and is required for the formation of the leading edge and the promotion of cell movement, possibly via activation of Rac signaling (By similarity). Acts as a centrosome maturation factor, probably by maintaining the integrity of the pericentriolar material and proper microtubule nucleation at mitotic spindle poles. The function seems to implicate at least in part WRAP73; the SSX2IP:WRAP73 complex is proposed to act as regulator of spindle anchoring at the mitotic centrosome (PubMed:23816619, PubMed:26545777). Involved in ciliogenesis (PubMed:24356449). It is required for targeted recruitment of the BBSome, CEP290, RAB8, and SSTR3 to the cilia (PubMed:24356449)", "gene_name": "SSX2IP", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y2D8", "name": "ACAD9", "organism": "Homo sapiens", "uniprot_id": "Q9Y2D8" }, { "function": "Dynamin-related GTPase that is essential for normal mitochondrial morphology by mediating fusion of the mitochondrial inner membranes, regulating cristae morphology and maintaining respiratory chain function (PubMed:16778770, PubMed:17709429, PubMed:20185555, PubMed:24616225, PubMed:28628083, PubMed:28746876, PubMed:31922487, PubMed:32228866, PubMed:32567732, PubMed:33130824, PubMed:33237841, PubMed:37612504, PubMed:37612506). Exists in two forms: the transmembrane, long form (Dynamin-like GTPase OPA1, long form; L-OPA1), which is tethered to the inner mitochondrial membrane, and the short soluble form (Dynamin-like GTPase OPA1, short form; S-OPA1), which results from proteolytic cleavage and localizes in the intermembrane space (PubMed:31922487, PubMed:32228866, PubMed:33237841, PubMed:37612504, PubMed:37612506). Both forms (L-OPA1 and S-OPA1) cooperate to catalyze the fusion of the mitochondrial inner membrane (PubMed:31922487, PubMed:37612504, PubMed:37612506). The equilibrium between L-OPA1 and S-OPA1 is essential: excess levels of S-OPA1, produced by cleavage by OMA1 following loss of mitochondrial membrane potential, lead to an impaired equilibrium between L-OPA1 and S-OPA1, inhibiting mitochondrial fusion (PubMed:20038677, PubMed:31922487). The balance between L-OPA1 and S-OPA1 also influences cristae shape and morphology (By similarity). Involved in remodeling cristae and the release of cytochrome c during apoptosis (By similarity). Proteolytic processing by PARL in response to intrinsic apoptotic signals may lead to disassembly of OPA1 oligomers and release of the caspase activator cytochrome C (CYCS) into the mitochondrial intermembrane space (By similarity). Acts as a regulator of T-helper Th17 cells, which are characterized by cells with fused mitochondria with tight cristae, by mediating mitochondrial membrane remodeling: OPA1 is required for interleukin-17 (IL-17) production (By similarity). Its role in mitochondrial morphology is required for mitochondrial genome maintenance (PubMed:18158317, PubMed:20974897)", "gene_name": "OPA1", "glycan_count": 1, "glycosylation_sites": [], "id": "O60313", "name": "OPA1", "organism": "Homo sapiens", "uniprot_id": "O60313" }, { "function": "DNA- and RNA-binding protein involved in various processes, such as translational repression, RNA stabilization, mRNA splicing, DNA repair and transcription regulation. Predominantly acts as a RNA-binding protein: binds preferentially to the 5'-[CU]CUGCG-3' RNA motif and specifically recognizes mRNA transcripts modified by C5-methylcytosine (m5C). Promotes mRNA stabilization: acts by binding to m5C-containing mRNAs and recruiting the mRNA stability maintainer ELAVL1, thereby preventing mRNA decay. Component of the CRD-mediated complex that promotes MYC mRNA stability (By similarity). Contributes to the regulation of translation by modulating the interaction between the mRNA and eukaryotic initiation factors (By similarity). Plays a key role in RNA composition of extracellular exosomes by defining the sorting of small non-coding RNAs, such as tRNAs, Y RNAs, Vault RNAs and miRNAs. Probably sorts RNAs in exosomes by recognizing and binding C5-methylcytosine (m5C)-containing RNAs. Acts as a key effector of epidermal progenitors by preventing epidermal progenitor senescence: acts by regulating the translation of a senescence-associated subset of cytokine mRNAs, possibly by binding to m5C-containing mRNAs. Also involved in pre-mRNA alternative splicing regulation: binds to splice sites in pre-mRNA and regulates splice site selection. Binds to TSC22D1 transcripts, thereby inhibiting their translation and negatively regulating TGF-beta-mediated transcription of COL1A2 (By similarity). Also able to bind DNA: regulates transcription of the multidrug resistance gene MDR1 is enhanced in presence of the APEX1 acetylated form at 'Lys-6' and 'Lys-7'. Binds to promoters that contain a Y-box (5'-CTGATTGGCCAA-3'), such as MDR1 and HLA class II genes. Promotes separation of DNA strands that contain mismatches or are modified by cisplatin. Has endonucleolytic activity and can introduce nicks or breaks into double-stranded DNA, suggesting a role in DNA repair. The secreted form acts as an extracellular mitogen and stimulates cell migration and proliferation (By similarity)", "gene_name": "YBX1", "glycan_count": 0, "glycosylation_sites": [], "id": "P67808", "name": "MT-TL1", "organism": "Bos taurus", "uniprot_id": "P67808" }, { "function": "Subunit a, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (Probable). ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel (PubMed:37244256). These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk (PubMed:37244256). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (Probable). With the subunit c (ATP5MC1), forms the proton-conducting channel in the F(0) domain, that contains two crucial half-channels (inlet and outlet) that facilitate proton movement from the mitochondrial intermembrane space (IMS) into the matrix (PubMed:37244256). Protons are taken up via the inlet half-channel and released through the outlet half-channel, following a Grotthuss mechanism (PubMed:37244256)", "gene_name": "MT-ATP6", "glycan_count": 1, "glycosylation_sites": [], "id": "P00846", "name": "MT-ATP6", "organism": "Homo sapiens", "uniprot_id": "P00846" }, { "function": "Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone", "gene_name": "NDUFS4", "glycan_count": 1, "glycosylation_sites": [], "id": "O43181", "name": "NDUFS4", "organism": "Homo sapiens", "uniprot_id": "O43181" }, { "function": "Required for the assembly of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) (PubMed:20858599, PubMed:25678554). Involved in mid-late stages of complex I assembly (PubMed:25678554)", "gene_name": "FOXRED1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96CU9", "name": "NDUFAF6", "organism": "Homo sapiens", "uniprot_id": "Q96CU9" }, { "function": "Phosphorylates thymidine, deoxycytidine, and deoxyuridine in the mitochondrial matrix (PubMed:11687801, PubMed:9989599). In non-replicating cells, where cytosolic dNTP synthesis is down-regulated, mtDNA synthesis depends solely on TK2 and DGUOK (PubMed:9989599). Widely used as target of antiviral and chemotherapeutic agents (PubMed:9989599)", "gene_name": "TK2", "glycan_count": 0, "glycosylation_sites": [], "id": "O00142", "name": "Thymidine kinase 2", "organism": "Homo sapiens", "uniprot_id": "O00142" }, { "function": "Catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis (fatty acid synthesis type II). Fatty acid chain elongation in mitochondria uses acyl carrier protein (ACP) as an acyl group carrier, but the enzyme accepts both ACP and CoA thioesters as substrates in vitro. Displays a preference for medium-chain over short- and long-chain substrates (PubMed:12654921, PubMed:18479707, PubMed:27817865). May provide the octanoyl chain used for lipoic acid biosynthesis, regulating protein lipoylation and mitochondrial respiratory activity particularly in Purkinje cells (By similarity). Involved in iron homeostasis; affecting Fe-S cluster assembly and ceramide metabolism (PubMed:37653044). Required for proper morphology and bioenergetic functions of mitochondria (PubMed:37653044). Required for maintenance of neurons (By similarity)", "gene_name": "MECR", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9BV79", "name": "MECR", "organism": "Homo sapiens", "uniprot_id": "Q9BV79" }, { "function": "Plays a role in the normal development of the peripheral and central nervous system (PubMed:11062474, PubMed:11159947, PubMed:16022285). Required for the correct localization of aurora kinase AURKA and the microtubule minus end-binding protein NUMA1 as well as a subset of AURKA targets which ensures proper spindle formation and timely chromosome alignment (PubMed:26246606)", "gene_name": "AAAS", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NRG9", "name": "AASDHPPT", "organism": "Homo sapiens", "uniprot_id": "Q9NRG9" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P23674", "name": "Cardiac troponin I (cTnI)", "organism": "", "uniprot_id": "" }, { "function": "Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Inhibition of pyruvate dehydrogenase decreases glucose utilization and increases fat metabolism in response to prolonged fasting and starvation. Plays an important role in maintaining normal blood glucose levels under starvation, and is involved in the insulin signaling cascade. Via its regulation of pyruvate dehydrogenase activity, plays an important role in maintaining normal blood pH and in preventing the accumulation of ketone bodies under starvation. In the fed state, mediates cellular responses to glucose levels and to a high-fat diet. Regulates both fatty acid oxidation and de novo fatty acid biosynthesis. Plays a role in the generation of reactive oxygen species. Protects detached epithelial cells against anoikis. Plays a role in cell proliferation via its role in regulating carbohydrate and fatty acid metabolism", "gene_name": "PDK4", "glycan_count": 0, "glycosylation_sites": [], "id": "Q16654", "name": "Pyruvate dehydrogenase kinase 4 (PDK4)", "organism": "Homo sapiens", "uniprot_id": "Q16654" }, { "function": "Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. In vitro it binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. It may modulate muscle contraction or may play a more structural role", "gene_name": "MYBPC3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q14896", "name": "Myosin-binding protein C (MYBPC3)", "organism": "Homo sapiens", "uniprot_id": "Q14896" }, { "function": "Major secreted protease of mast cells with suspected roles in vasoactive peptide generation, extracellular matrix degradation, and regulation of gland secretion", "gene_name": "CMA1", "glycan_count": 4, "glycosylation_sites": [ { "position": 80, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 103, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P23946", "name": "Chymase", "organism": "Homo sapiens", "uniprot_id": "P23946" }, { "function": "Acts as a receptor for L-lactate and mediates its anti-lipolytic effect through a G(i)-protein-mediated pathway", "gene_name": "HCAR1", "glycan_count": 0, "glycosylation_sites": [ { "position": 3, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9BXC0", "name": "Follistatin like 3 (FSTL3)", "organism": "Homo sapiens", "uniprot_id": "Q9BXC0" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P08476 (INHBA, a subunit)", "name": "Activin", "organism": "", "uniprot_id": "" }, { "function": "Histone methyltransferase. Preferentially dimethylates 'Lys-4' and 'Lys-27' of histone H3 forming H3K4me2 and H3K27me2. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation, while 'Lys-27' is a mark for transcriptional repression", "gene_name": "NSD3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9BYU8", "name": "Follistatin like 3 (FSTL3)", "organism": "Homo sapiens", "uniprot_id": "Q9BZ95" }, { "function": "Tyrosine-protein kinase that acts as a cell-surface receptor for the cytokine KITLG/SCF and plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. In response to KITLG/SCF binding, KIT can activate several signaling pathways. Phosphorylates PIK3R1, PLCG1, SH2B2/APS and CBL. Activates the AKT1 signaling pathway by phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase. Activated KIT also transmits signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3, STAT5A and STAT5B. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. KIT signaling is modulated by protein phosphatases, and by rapid internalization and degradation of the receptor. Activated KIT promotes phosphorylation of the protein phosphatases PTPN6/SHP-1 and PTPRU, and of the transcription factors STAT1, STAT3, STAT5A and STAT5B. Promotes phosphorylation of PIK3R1, CBL, CRK (isoform Crk-II), LYN, MAPK1/ERK2 and/or MAPK3/ERK1, PLCG1, SRC and SHC1", "gene_name": "KIT", "glycan_count": 26, "glycosylation_sites": [ { "position": 130, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 145, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 283, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 293, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 300, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 320, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 352, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 367, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 463, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 486, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P10721", "name": "KIT", "organism": "Homo sapiens", "uniprot_id": "P10721" }, { "function": "Involved in the activation of Ras protein signal transduction (PubMed:22821884). Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (PubMed:12740440, PubMed:14500341, PubMed:9020151)", "gene_name": "HRAS", "glycan_count": 1, "glycosylation_sites": [ { "position": 35, "type": "(Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL" } ], "id": "P01112", "name": "HRAS", "organism": "Homo sapiens", "uniprot_id": "P01112" }, { "function": "Ras proteins bind GDP/GTP and possess intrinsic GTPase activity", "gene_name": "NRAS", "glycan_count": 1, "glycosylation_sites": [ { "position": 35, "type": "(Microbial infection) O-linked (Glc) threonine; by P.sordellii toxin TcsL" } ], "id": "P01111", "name": "NRAS", "organism": "Homo sapiens", "uniprot_id": "P01111" }, { "function": "Plays a role in the inhibition of the host innate and adaptive immune responses. Possesses five immunoglobulin-binding domains that capture both the fragment crystallizable region (Fc region) and the Fab region (part of Ig that identifies antigen) of immunoglobulins (PubMed:10805799, PubMed:2938951, PubMed:4163007). In turn, Staphylococcus aureus is protected from phagocytic killing via inhibition of Ig Fc region. In addition, the host elicited B-cell response is prevented due to a decrease of antibody-secreting cell proliferation that enter the bone marrow, thereby decreasing long-term antibody production. Inhibits osteogenesis by preventing osteoblast proliferation and expression of alkaline phosphatase, type I collagen, osteopontin and osteocalcin. Acts directly as a pro-inflammatory factor in the lung through its ability to bind and activate tumor necrosis factor alpha receptor 1/TNFRSF1A (By similarity)", "gene_name": "spa", "glycan_count": 0, "glycosylation_sites": [], "id": "P02976", "name": "Streptococcal M protein", "organism": "Staphylococcus aureus (strain NCTC 8325 / PS 47)", "uniprot_id": "P02976" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q99ZP0", "name": "Streptococcal C5a peptidase", "organism": "Streptococcus pyogenes serotype M1", "uniprot_id": "Q99ZP0" }, { "function": "Type I interferon-stimulated gene (ISG) that plays a critical role in antiviral and antibacterial activity (PubMed:34722780). During bacterial infection, promotes macrophage differentiation and facilitates inflammatory cytokine secretion (PubMed:34722780). Plays a role in the control of respiratory syncytial virus/RSV infection, reducing the ability of the virus to replicate (PubMed:32611756). Exhibits a low antiviral activity against hepatitis C virus (PubMed:21478870). Also acts as a feedback regulator of IFN responses by negatively regulating IKBKB and IKBKE kinase activities through interaction with FKBP5 (PubMed:31434731)", "gene_name": "IFI44L", "glycan_count": 1, "glycosylation_sites": [], "id": "Q53G44", "name": "IFI27", "organism": "Homo sapiens", "uniprot_id": "Q53G44" }, { "function": "Regulatory subunit of the IKK core complex which phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor (PubMed:14695475, PubMed:20724660, PubMed:21518757, PubMed:9751060). Its binding to scaffolding polyubiquitin plays a key role in IKK activation by multiple signaling receptor pathways (PubMed:16547522, PubMed:18287044, PubMed:19033441, PubMed:19185524, PubMed:21606507, PubMed:27777308, PubMed:33567255). Can recognize and bind both 'Lys-63'-linked and linear polyubiquitin upon cell stimulation, with a much higher affinity for linear polyubiquitin (PubMed:16547522, PubMed:18287044, PubMed:19033441, PubMed:19185524, PubMed:21606507, PubMed:27777308). Could be implicated in NF-kappa-B-mediated protection from cytokine toxicity. Essential for viral activation of IRF3 (PubMed:19854139). Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination (PubMed:20724660)", "gene_name": "IKBKG", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y6K9", "name": "IKBKG (NEMO)", "organism": "Homo sapiens", "uniprot_id": "Q9Y6K9" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P08519 (apo(a))", "name": "Lipoprotein(a) [Lp(a)]", "organism": "", "uniprot_id": "" }, { "function": "Transcription factor that binds to the DNA sequence 5'-CCAACC-3'. Regulates directly PME5, UND and GLOX1 (PubMed:21673079). Essential for tapetum development in anthers and microsporogenesis (PubMed:12848824, PubMed:21673079). Regulates the timing of tapetal programmed cell death (PCD) which is critical for pollen development. May act through the activation of UND, encoding an A1 aspartic protease (PubMed:21673079). Required for anther development by regulating tapetum development, callose dissolution and exine formation. Acts upstream of A6 and FAR2/MS2, two genes required for pollen exine formation (PubMed:17727613). Negatively regulates trichome endoreduplication and trichome branching (PubMed:12848824)", "gene_name": "MYB80", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9XHV0", "name": "CYP2B6", "organism": "Arabidopsis thaliana", "uniprot_id": "Q9XHV0" }, { "function": "", "gene_name": "10A19I.15", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9XHV1", "name": "CYP2D6", "organism": "Oryza sativa subsp. japonica", "uniprot_id": "Q9XHV1" }, { "function": "", "gene_name": "10A19I.14", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9XHV2", "name": "CYP1A2", "organism": "Oryza sativa subsp. japonica", "uniprot_id": "Q9XHV2" }, { "function": "", "gene_name": "10A19I.13", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9XHV3", "name": "GSTZ1", "organism": "Oryza sativa subsp. japonica", "uniprot_id": "Q9XHV3" }, { "function": "Involved in synthesis of starch. Catalyzes the synthesis of ADP-glucose, a molecule that serves as an activated glycosyl donor for alpha-1,4-glucan synthesis. Essential for starch synthesis in leaf chloroplasts", "gene_name": "AGPL3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9XHV4", "name": "HSP90B1", "organism": "Oryza sativa subsp. japonica", "uniprot_id": "Q688T8" }, { "function": "", "gene_name": "10A19I.11", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9XHV5", "name": "HSPA8", "organism": "Oryza sativa subsp. japonica", "uniprot_id": "Q9XHV5" }, { "function": "", "gene_name": "10A19I.10", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9XHV6", "name": "GLUD1", "organism": "Oryza sativa subsp. japonica", "uniprot_id": "Q9XHV6" }, { "function": "", "gene_name": "10A19I.9", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9XHV7", "name": "CD163", "organism": "Oryza sativa subsp. japonica", "uniprot_id": "Q9XHV7" }, { "function": "", "gene_name": "10A19I.8", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9XHV8", "name": "PEX14", "organism": "Oryza sativa subsp. japonica", "uniprot_id": "Q9XHV8" }, { "function": "", "gene_name": "10A19I.7", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9XHV9", "name": "F5", "organism": "Oryza sativa subsp. japonica", "uniprot_id": "Q9XHV9" }, { "function": "SNARE promoting movement of transport vesicles to target membranes. Targets endosomes to the trans-Golgi network, and may therefore function in retrograde trafficking. Together with SNARE STX12, promotes movement of vesicles from endosomes to the cell membrane, and may therefore function in the endocytic recycling pathway", "gene_name": "STX6", "glycan_count": 1, "glycosylation_sites": [], "id": "O43752", "name": "Syntaxin-6 (STX6)", "organism": "Homo sapiens", "uniprot_id": "O43752" }, { "function": "GTPase component of the eRF1-eRF3-GTP ternary complex, a ternary complex that mediates translation termination in response to the termination codons UAA, UAG and UGA (PubMed:34413231, PubMed:7556078). SUP35/eRF3 mediates SUP45/eRF1 delivery to stop codons: The eRF1-eRF3-GTP complex binds to a stop codon in the ribosomal A-site (PubMed:34413231, PubMed:7556078). GTP hydrolysis by SUP35/eRF3 induces a conformational change that leads to its dissociation, permitting SUP45/eRF1 to accommodate fully in the A-site (PubMed:34413231, PubMed:7556078). Recruited by polyadenylate-binding protein PAB1 to poly(A)-tails of mRNAs (PubMed:12923185, PubMed:15337765). Interaction with PAB1 is also required for regulation of normal mRNA decay through translation termination-coupled poly(A) shortening (PubMed:12923185, PubMed:15337765)", "gene_name": "SUP35", "glycan_count": 1, "glycosylation_sites": [], "id": "P05453", "name": "Sup35p", "organism": "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "uniprot_id": "P05453" }, { "function": "A beta chain of antigen-presenting major histocompatibility complex class II (MHCII) molecule. In complex with the alpha chain HLA-DRA, displays antigenic peptides on professional antigen presenting cells (APCs) for recognition by alpha-beta T cell receptor (TCR) on HLA-DRB1-restricted CD4-positive T cells. This guides antigen-specific T-helper effector functions, both antibody-mediated immune response and macrophage activation, to ultimately eliminate the infectious agents and transformed cells (PubMed:15265931, PubMed:16148104, PubMed:22327072, PubMed:27591323, PubMed:29884618, PubMed:31495665, PubMed:8642306). Typically presents extracellular peptide antigens of 10 to 30 amino acids that arise from proteolysis of endocytosed antigens in lysosomes (PubMed:8145819). In the tumor microenvironment, presents antigenic peptides that are primarily generated in tumor-resident APCs likely via phagocytosis of apoptotic tumor cells or macropinocytosis of secreted tumor proteins (PubMed:31495665). Presents peptides derived from intracellular proteins that are trapped in autolysosomes after macroautophagy, a mechanism especially relevant for T cell selection in the thymus and central immune tolerance (PubMed:17182262, PubMed:23783831). The selection of the immunodominant epitopes follows two processing modes: 'bind first, cut/trim later' for pathogen-derived antigenic peptides and 'cut first, bind later' for autoantigens/self-peptides (PubMed:25413013). The anchor residue at position 1 of the peptide N-terminus, usually a large hydrophobic residue, is essential for high affinity interaction with MHCII molecules (PubMed:8145819)", "gene_name": "HLA-DRB1", "glycan_count": 0, "glycosylation_sites": [ { "position": 48, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P04229", "name": "HLA-DR", "organism": "Homo sapiens", "uniprot_id": "P01911" }, { "function": "Ubiquitin-protein ligase which is a core component of several complexes mainly involved pre-mRNA splicing and DNA repair. Required for pre-mRNA splicing as component of the spliceosome (PubMed:28076346, PubMed:28502770, PubMed:29301961, PubMed:29360106, PubMed:30705154). Core component of the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome and participates in its assembly, its remodeling and is required for its activity. During assembly of the spliceosome, mediates 'Lys-63'-linked polyubiquitination of the U4 spliceosomal protein PRPF3. Ubiquitination of PRPF3 allows its recognition by the U5 component PRPF8 and stabilizes the U4/U5/U6 tri-snRNP spliceosomal complex (PubMed:20595234). Recruited to RNA polymerase II C-terminal domain (CTD) and the pre-mRNA, it may also couple the transcriptional and spliceosomal machineries (PubMed:21536736). The XAB2 complex, which contains PRPF19, is also involved in pre-mRNA splicing, transcription and transcription-coupled repair (PubMed:17981804). Beside its role in pre-mRNA splicing PRPF19, as part of the PRP19-CDC5L complex, plays a role in the DNA damage response/DDR. It is recruited to the sites of DNA damage by the RPA complex where PRPF19 directly ubiquitinates RPA1 and RPA2. 'Lys-63'-linked polyubiquitination of the RPA complex allows the recruitment of the ATR-ATRIP complex and the activation of ATR, a master regulator of the DNA damage response (PubMed:24332808). May also play a role in DNA double-strand break (DSB) repair by recruiting the repair factor SETMAR to altered DNA (PubMed:18263876). As part of the PSO4 complex may also be involved in the DNA interstrand cross-links/ICLs repair process (PubMed:16223718). In addition, may also mediate 'Lys-48'-linked polyubiquitination of substrates and play a role in proteasomal degradation (PubMed:11435423). May play a role in the biogenesis of lipid droplets (By similarity). May play a role in neural differentiation possibly through its function as part of the spliceosome (By similarity)", "gene_name": "PRPF19", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9UMS4", "name": "Lutheran/basal cell adhesion molecule (Lu/BCAM)", "organism": "Homo sapiens", "uniprot_id": "Q9UMS4" }, { "function": "As a component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), it is required in ciliogenesis and ciliary protein trafficking (PubMed:27932497, PubMed:29220510). Involved in cilia formation during neuronal patterning. Acts as a negative regulator of Shh signaling. Required to recruit TULP3 to primary cilia (By similarity)", "gene_name": "IFT122", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9HBG5", "name": "Intercellular adhesion molecule 4 (ICAM4)", "organism": "Homo sapiens", "uniprot_id": "Q9HBG6" }, { "function": "Gamma chains make up the fetal hemoglobin F, in combination with alpha chains", "gene_name": "HBG1", "glycan_count": 1, "glycosylation_sites": [], "id": "P69891", "name": "Hemoglobin F (HbF)", "organism": "Homo sapiens", "uniprot_id": "P69891" }, { "function": "Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. Involved in DNA double-strand break repair and UV-damage excision repair", "gene_name": "ACTR5", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H9F9", "name": "BCL11A", "organism": "Homo sapiens", "uniprot_id": "Q9H9F9" }, { "function": "The zeta chain is an alpha-type chain of mammalian embryonic hemoglobin", "gene_name": "HBZ", "glycan_count": 0, "glycosylation_sites": [], "id": "P02008", "name": "Zeta globin", "organism": "Homo sapiens", "uniprot_id": "P02008" }, { "function": "Orphan receptor. May play a role in brain function", "gene_name": "GPR45", "glycan_count": 0, "glycosylation_sites": [ { "position": 4, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 17, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 20, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y5Y3", "name": "KLF1", "organism": "Homo sapiens", "uniprot_id": "Q9Y5Y3" }, { "function": "Polycomb group (PcG) protein. Component of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' and 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Also recognizes 'Lys-26' trimethylated histone H1 with the effect of inhibiting PRC2 complex methyltransferase activity on nucleosomal histone H3 'Lys-27', whereas H3 'Lys-27' recognition has the opposite effect, enabling the propagation of this repressive mark. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1 and CDKN2A", "gene_name": "EED", "glycan_count": 1, "glycosylation_sites": [], "id": "O75530", "name": "Embryonic Ectoderm Development (EED)", "organism": "Homo sapiens", "uniprot_id": "O75530" }, { "function": "Ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase activities. Involved in immune and inflammatory responses signaled by cytokines, such as TNF-alpha and IL-1 beta, or pathogens via Toll-like receptors (TLRs) through terminating NF-kappa-B activity. Essential component of a ubiquitin-editing protein complex, comprising also RNF11, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. In cooperation with TAX1BP1 promotes disassembly of E2-E3 ubiquitin protein ligase complexes in IL-1R and TNFR-1 pathways; affected are at least E3 ligases TRAF6, TRAF2 and BIRC2, and E2 ubiquitin-conjugating enzymes UBE2N and UBE2D3. In cooperation with TAX1BP1 promotes ubiquitination of UBE2N and proteasomal degradation of UBE2N and UBE2D3. Upon TNF stimulation, deubiquitinates 'Lys-63'-polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Deubiquitinates TRAF6 probably acting on 'Lys-63'-linked polyubiquitin. Upon T-cell receptor (TCR)-mediated T-cell activation, deubiquitinates 'Lys-63'-polyubiquitin chains on MALT1 thereby mediating disassociation of the CBM (CARD11:BCL10:MALT1) and IKK complexes and preventing sustained IKK activation. Deubiquitinates NEMO/IKBKG; the function is facilitated by TNIP1 and leads to inhibition of NF-kappa-B activation. Upon stimulation by bacterial peptidoglycans, probably deubiquitinates RIPK2. Can also inhibit I-kappa-B-kinase (IKK) through a non-catalytic mechanism which involves polyubiquitin; polyubiquitin promotes association with IKBKG and prevents IKK MAP3K7-mediated phosphorylation. Targets TRAF2 for lysosomal degradation. In vitro able to deubiquitinate 'Lys-11'-, 'Lys-48'- and 'Lys-63' polyubiquitin chains. Inhibitor of programmed cell death. Has a role in the function of the lymphoid system. Required for LPS-induced production of pro-inflammatory cytokines and IFN beta in LPS-tolerized macrophages", "gene_name": "TNFAIP3", "glycan_count": 1, "glycosylation_sites": [], "id": "P21580", "name": "TNFAIP3", "organism": "Homo sapiens", "uniprot_id": "P21580" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P49994", "name": "RRM2", "organism": "", "uniprot_id": "P49994" }, { "function": "Transcription factor involved in the regulation of cell survival, proliferation, and differentiation. Transactivates the expression of the CLU gene", "gene_name": "MYBL2", "glycan_count": 1, "glycosylation_sites": [], "id": "P10244", "name": "MYBL2", "organism": "Homo sapiens", "uniprot_id": "P10244" }, { "function": "Shared cell surface receptor required for the activation of five class 2 cytokines: IL10, IL22, IL26, IL28, and IFNL1. The IFNLR1/IL10RB dimer is a receptor for the cytokine ligands IFNL2 and IFNL3 and mediates their antiviral activity. The ligand/receptor complex stimulate the activation of the JAK/STAT signaling pathway leading to the expression of IFN-stimulated genes (ISG), which contribute to the antiviral state", "gene_name": "IL10RB", "glycan_count": 1, "glycosylation_sites": [ { "position": 49, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 68, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 102, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 161, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q08334", "name": "IL-10RB", "organism": "Homo sapiens", "uniprot_id": "Q08334" }, { "function": "Heterotetrameric enzyme that catalyzes the condensation of farnesyl diphosphate (FPP), which acts as a primer, and isopentenyl diphosphate (IPP) to produce prenyl diphosphates of varying chain lengths and participates in the determination of the side chain of ubiquinone (PubMed:16262699). Supplies nona and decaprenyl diphosphate, the precursors for the side chain of the isoprenoid quinones ubiquinone-9 (Q9)and ubiquinone-10 (Q10) respectively (PubMed:16262699). The enzyme adds isopentenyl diphosphate molecules sequentially to farnesyl diphosphate with trans stereochemistry (PubMed:16262699)", "gene_name": "PDSS1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y2W5", "name": "Neuronal Pentraxin Receptor", "organism": "Homo sapiens", "uniprot_id": "Q5T2R2" }, { "function": "May be involved in formation of stretch-resistant cell-cell adhesion complexes", "gene_name": "CTNNA3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UI47", "name": "CTNNA1 (Catenin alpha-1)", "organism": "Homo sapiens", "uniprot_id": "Q9UI47" }, { "function": "Catalyzes the first step in the biosynthesis of chondroitin sulfate and dermatan sulfate proteoglycans, such as DCN. Transfers D-xylose from UDP-D-xylose to specific serine residues of the core protein (PubMed:15461586, PubMed:17189265, PubMed:23982343, PubMed:24581741). Required for normal embryonic and postnatal skeleton development, especially of the long bones (PubMed:23982343, PubMed:24581741). Required for normal maturation of chondrocytes during bone development, and normal onset of ossification (By similarity)", "gene_name": "XYLT1", "glycan_count": 2, "glycosylation_sites": [ { "position": 226, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 421, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 777, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q86Y38", "name": "XYLT1", "organism": "Homo sapiens", "uniprot_id": "Q86Y38" }, { "function": "Plays a critical role in homologous recombination repair (HRR) through its ability to recruit BRCA2 and RAD51 to DNA breaks (PubMed:16793542, PubMed:19369211, PubMed:19423707, PubMed:22941656, PubMed:24141787, PubMed:28319063). Strongly stimulates the DNA strand-invasion activity of RAD51, stabilizes the nucleoprotein filament against a disruptive BRC3-BRC4 polypeptide and helps RAD51 to overcome the suppressive effect of replication protein A (RPA) (PubMed:20871615). Functionally cooperates with RAD51AP1 in promoting of D-loop formation by RAD51 (PubMed:20871616). Serves as the molecular scaffold in the formation of the BRCA1-PALB2-BRCA2 complex which is essential for homologous recombination (PubMed:19369211). Via its WD repeats is proposed to scaffold a HR complex containing RAD51C and BRCA2 which is thought to play a role in HR-mediated DNA repair (PubMed:24141787). Essential partner of BRCA2 that promotes the localization and stability of BRCA2 (PubMed:16793542). Also enables its recombinational repair and checkpoint functions of BRCA2 (PubMed:16793542). May act by promoting stable association of BRCA2 with nuclear structures, allowing BRCA2 to escape the effects of proteasome-mediated degradation (PubMed:16793542). Binds DNA with high affinity for D loop, which comprises single-stranded, double-stranded and branched DNA structures (PubMed:20871616). May play a role in the extension step after strand invasion at replication-dependent DNA double-strand breaks; together with BRCA2 is involved in both POLH localization at collapsed replication forks and DNA polymerization activity (PubMed:24485656)", "gene_name": "PALB2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q86YC2", "name": "PALB2", "organism": "Homo sapiens", "uniprot_id": "Q86YC2" }, { "function": "Required in engulfing to control the phagocytosis of apoptotic cell corpses (PubMed:10707082, PubMed:20126385). Required in embryonic development for the correct positioning and orientation of the mitotic spindles and division planes in blastomere cells (PubMed:20126385). Involved in hypodermal cell fusion, together with pak-1 and cdc-42, leading to embryonic body elongation, which involves dramatic cytoskeletal reorganization (PubMed:8824291). ced-2 and ced-5 function to activate ced-10 in a GTPase signaling pathway that controls the polarized extension of cell surfaces (PubMed:10707082). Plays a redundant role with mig-2 in dorsal axonal guidance in ventral cord commissural motoneurons and in P neuroblast migration. May regulate these 2 processes by activating pak-1 and/or max-2 (PubMed:17050621). Plays a role, probably via mig-10, in orientating axonal growth of HSN and AVM neurons in response to guidance cues such as slt-1. Regulates mig-10 asymmetric distribution in HSN neurons (PubMed:18499456). During the dorso-ventral axonal guidance and outgrowth of VD neurons, required together with mig-2 to inhibit growth cone filopodial protrusion mediated by netrin guidance cue unc-6 and its receptors unc-5 and unc-40 (PubMed:25371370, PubMed:30045855). Specifically, regulates growth cone filopodial protrusion polarity, and thus migration, by promoting F-actin polarization and, together with mig-2, by restricting plus-end microtubule accumulation in the growth cone (PubMed:30045855). Plays a role in protecting dopaminergic neurons from oxidative stress-induced degeneration (PubMed:29346382). During gonad morphogenesis, plays a role in distal tip cell (DTC)-mediated guidance of gonad elongation, probably by activating max-2 (PubMed:19023419, PubMed:19797046). Furthermore, plays a role in distal tip cell polarity and migration by negatively regulating the unc-6/Netrin receptor unc-5 (PubMed:26292279). May be involved in signal transduction during cell migration (PubMed:10707082). May be involved in the positioning of ray 1, the most anterior ray sensilium, in the male tail (PubMed:24004945)", "gene_name": "ced-10", "glycan_count": 0, "glycosylation_sites": [], "id": "Q03206", "name": "Non-structural protein 1 (NS1)", "organism": "Caenorhabditis elegans", "uniprot_id": "Q03206" }, { "function": "Associates with IL12RB1 to form the interleukin-23 receptor. Binds IL23 and mediates T-cells, NK cells and possibly certain macrophage/myeloid cells stimulation probably through activation of the Jak-Stat signaling cascade. IL23 functions in innate and adaptive immunity and may participate in acute response to infection in peripheral tissues. IL23 may be responsible for autoimmune inflammatory diseases and be important for tumorigenesis", "gene_name": "IL23R", "glycan_count": 0, "glycosylation_sites": [ { "position": 29, "type": "N-linked (GlcNAc...) asparagine; partial" }, { "position": 47, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 81, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 141, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 180, "type": "N-linked (GlcNAc...) (high mannose) asparagine" }, { "position": 232, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 262, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 273, "type": "N-linked (GlcNAc...) asparagine; partial" } ], "id": "Q5VWK5", "name": "Interleukin-23 receptor (IL-23R)", "organism": "Homo sapiens", "uniprot_id": "Q5VWK5" }, { "function": "May be involved in the fusion of the spermatozoa with the oocyte during fertilization", "gene_name": "Cd46", "glycan_count": 0, "glycosylation_sites": [ { "position": 181, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 205, "type": "O-linked (GalNAc...) threonine" }, { "position": 301, "type": "O-linked (GalNAc...) threonine" }, { "position": 304, "type": "O-linked (GalNAc...) threonine" }, { "position": 310, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 312, "type": "O-linked (GalNAc...) threonine" } ], "id": "Q9R0R9", "name": "C1galt1", "organism": "Mus musculus", "uniprot_id": "O88174" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P15391 (mouse)", "name": "CD19", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P42082 (mouse)", "name": "CD86", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P33681 (mouse)", "name": "CD80", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9WU72 (mouse)", "name": "Baff (TNFSF13B)", "organism": "", "uniprot_id": "" }, { "function": "G-protein coupled receptor for 5-hydroxytryptamine (serotonin) (PubMed:1330647, PubMed:18703043, PubMed:19057895, PubMed:21645528, PubMed:22300836, PubMed:35084960, PubMed:38552625). Also functions as a receptor for various drugs and psychoactive substances, including mescaline, psilocybin, 1-(2,5-dimethoxy-4-iodophenyl)-2-aminopropane (DOI) and lysergic acid diethylamide (LSD) (PubMed:28129538, PubMed:35084960). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors (PubMed:28129538, PubMed:35084960). HTR2A is coupled to G(q)/G(11) G alpha proteins and activates phospholipase C-beta, releasing diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) second messengers that modulate the activity of phosphatidylinositol 3-kinase and promote the release of Ca(2+) ions from intracellular stores, respectively (PubMed:18703043, PubMed:28129538, PubMed:35084960). Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways (PubMed:28129538, PubMed:35084960). Affects neural activity, perception, cognition and mood (PubMed:18297054). Plays a role in the regulation of behavior, including responses to anxiogenic situations and psychoactive substances. Plays a role in intestinal smooth muscle contraction, and may play a role in arterial vasoconstriction (By similarity)", "gene_name": "HTR2A", "glycan_count": 0, "glycosylation_sites": [ { "position": 8, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 38, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 44, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 51, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 54, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P28223", "name": "5-HT2A receptor", "organism": "Homo sapiens", "uniprot_id": "P28223" }, { "function": "Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells", "gene_name": "nef", "glycan_count": 0, "glycosylation_sites": [], "id": "P03407", "name": "Nef", "organism": "Human immunodeficiency virus type 1 group M subtype B (isolate ARV2/SF2)", "uniprot_id": "P03407" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P05067 (APP)", "name": "A\u03b2 (Amyloid-beta)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "various subunits", "name": "GABA-A receptor", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P40933/P40933", "name": "IL-15/IL-15R\u03b1", "organism": "", "uniprot_id": "" }, { "function": "Part of the TCR-CD3 complex present on T-lymphocyte cell surface that plays an essential role in adaptive immune response. When antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transmitted across the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3 chains contain immunoreceptor tyrosine-based activation motifs (ITAMs) in their cytoplasmic domain. Upon TCR engagement, these motifs become phosphorylated by Src family protein tyrosine kinases LCK and FYN, resulting in the activation of downstream signaling pathways (PubMed:1384049, PubMed:1385158, PubMed:2470098, PubMed:7509083). CD3Z ITAMs phosphorylation creates multiple docking sites for the protein kinase ZAP70 leading to ZAP70 phosphorylation and its conversion into a catalytically active enzyme (PubMed:7509083). Plays an important role in intrathymic T-cell differentiation. Additionally, participates in the activity-dependent synapse formation of retinal ganglion cells (RGCs) in both the retina and dorsal lateral geniculate nucleus (dLGN) (By similarity)", "gene_name": "CD247", "glycan_count": 0, "glycosylation_sites": [], "id": "P20963", "name": "CD3\u03b6", "organism": "Homo sapiens", "uniprot_id": "P20963" }, { "function": "Modulates negatively TGFB1 signaling in keratinocytes", "gene_name": "CD109", "glycan_count": 107, "glycosylation_sites": [ { "position": 68, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 118, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 247, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 279, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 365, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 419, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 513, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 645, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1086, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1355, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6YHK3", "name": "CD109", "organism": "Homo sapiens", "uniprot_id": "Q6YHK3" }, { "function": "Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag-Pol, or to Gag-Pol binding host factors. Interaction with HECT ubiquitin ligases probably link the viral protein to the host ESCRT pathway and facilitates release", "gene_name": "pol", "glycan_count": 0, "glycosylation_sites": [], "id": "P03356", "name": "HTLV-1 envelope glycoprotein (Env)", "organism": "AKV murine leukemia virus", "uniprot_id": "P03356" }, { "function": "E3 ubiquitin-protein ligase that functions in the antephase checkpoint by actively delaying passage into mitosis in response to microtubule poisons. Acts in early prophase before chromosome condensation, when the centrosome move apart from each other along the periphery of the nucleus. Probably involved in signaling the presence of mitotic stress caused by microtubule poisons by mediating the 'Lys-48'-linked ubiquitination of target proteins, leading to their degradation by the proteasome. Promotes the ubiquitination and subsequent degradation of AURKA and PLK1. Probably acts as a tumor suppressor, possibly by mediating the polyubiquitination of HDAC1, leading to its degradation. May also promote the formation of 'Lys-63'-linked polyubiquitin chains and functions with the specific ubiquitin-conjugating UBC13-MMS2 (UBE2N-UBE2V2) heterodimer. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation, but are rather involved in signaling cellular stress", "gene_name": "CHFR", "glycan_count": 0, "glycosylation_sites": [], "id": "Q96EP1", "name": "CHFR", "organism": "Homo sapiens", "uniprot_id": "Q96EP1" }, { "function": "May be involved in the regulation of p53-dependent G2 arrest of the cell cycle. Seems to induce cell cycle arrest by inhibiting CDK1 activity and nuclear translocation of the CDC2 cyclin B1 complex (By similarity)", "gene_name": "RPRM", "glycan_count": 1, "glycosylation_sites": [ { "position": 7, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 18, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NS64", "name": "REPRIMO", "organism": "Homo sapiens", "uniprot_id": "Q9NS64" }, { "function": "Plays an important role in the regulation of cell proliferation and cell differentiation. Required for normal regulation of the hair growth cycle. Functions as an inhibitor of hair elongation by promoting progression from anagen, the growth phase of the hair follicle, into catagen the apoptosis-induced regression phase (By similarity)", "gene_name": "FGF5", "glycan_count": 1, "glycosylation_sites": [ { "position": 110, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P12034", "name": "FGF5", "organism": "Homo sapiens", "uniprot_id": "P12034" }, { "function": "In T-cells, functions as a regulator of p38 MAPKs by inhibiting p88 phosphorylation and activity (By similarity). Might affect PCNA interaction with some CDK (cell division protein kinase) complexes; stimulates DNA excision repair in vitro and inhibits entry of cells into S phase", "gene_name": "GADD45A", "glycan_count": 0, "glycosylation_sites": [], "id": "P24522", "name": "GADD45\u03b1", "organism": "Homo sapiens", "uniprot_id": "P24522" }, { "function": "Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3') and activates the promoters of the genes for some small nuclear RNAs (snRNA) and of genes such as those for histone H2B and immunoglobulins. Modulates transcription transactivation by NR3C1, AR and PGR", "gene_name": "POU2F1", "glycan_count": 2, "glycosylation_sites": [], "id": "P14859", "name": "OCT1", "organism": "Homo sapiens", "uniprot_id": "P14859" }, { "function": "Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types. SFRP1 decreases intracellular beta-catenin levels (By similarity). Has antiproliferative effects on vascular cells, in vitro and in vivo, and can induce, in vivo, an angiogenic response. In vascular cell cycle, delays the G1 phase and entry into the S phase (By similarity). In kidney development, inhibits tubule formation and bud growth in metanephroi (By similarity). Inhibits WNT1/WNT4-mediated TCF-dependent transcription", "gene_name": "SFRP1", "glycan_count": 3, "glycosylation_sites": [ { "position": 173, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8N474", "name": "SFRP1", "organism": "Homo sapiens", "uniprot_id": "Q8N474" }, { "function": "Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate (PubMed:14506254, PubMed:15265858, PubMed:26690923, PubMed:7521911). Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion (PubMed:14506254). Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport (PubMed:14506254). Essential for the rapid removal of released glutamate from the synaptic cleft, and for terminating the postsynaptic action of glutamate (By similarity)", "gene_name": "SLC1A2", "glycan_count": 0, "glycosylation_sites": [ { "position": 206, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 216, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P43004", "name": "GLT-1 (EAAT2)", "organism": "Homo sapiens", "uniprot_id": "P43004" }, { "function": "Involved in spermatogenesis and sperm function. Plays a role in regulation of cell growth. Binds to double-stranded DNA and RNA. Binds most efficiently to poly(I:C) RNA than to poly(dI:dC) DNA. Binds also to single-stranded poly(G) RNA. Binds non-specifically to the mRNA PRM1 3'-UTR and adenovirus VA RNA (By similarity)", "gene_name": "STRBP", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H7V1", "name": "ZDHHC9", "organism": "Homo sapiens", "uniprot_id": "Q96SI9" }, { "function": "Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates and therefore functions in several unrelated biological processes (Probable). Through the palmitoylation of ABCA1 regulates the localization of the transporter to the plasma membrane and thereby regulates its function in cholesterol and phospholipid efflux (Probable). Could also pamitoylate the D(2) dopamine receptor DRD2 and regulate its stability and localization to the plasma membrane (Probable). Could also play a role in glutamatergic transmission (By similarity)", "gene_name": "ZDHHC8", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9ULC8", "name": "ZDHHC8", "organism": "Homo sapiens", "uniprot_id": "Q9ULC8" }, { "function": "Mitochondrial carbonic anhydrase that catalyzes the reversible conversion of carbon dioxide to bicarbonate/HCO3", "gene_name": "CA5B", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y2D0", "name": "ZDHHC2", "organism": "Homo sapiens", "uniprot_id": "Q9Y2D0" }, { "function": "May regulate AMPA receptor content at nascent synapses, and have a role in postsynaptic development and maturation", "gene_name": "SYNDIG1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H7V2", "name": "ZDHHC15", "organism": "Homo sapiens", "uniprot_id": "Q9H7V2" }, { "function": "Involved in the negative regulation of lymphocyte motility. It mediates the migration-inhibitory effects of IL6. Serves as a positive regulator of the RhoA signaling pathway. Enhancement of RhoA activation results in inhibition of lymphocyte and lymphoma cell motility by activation of its downstream effector ROCK. Is a regulator of B-cell receptor signaling, that acts through SYK kinase activation", "gene_name": "GCSAM", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8N6F7", "name": "TMEM88", "organism": "Homo sapiens", "uniprot_id": "Q8N6F7" }, { "function": "In neurons, involved in the transport of late endosomes/lysosomes (PubMed:25066864). May be involved in dendrite morphogenesis and maintenance by regulating lysosomal trafficking (PubMed:25066864). May act as a molecular brake for retrograde transport of late endosomes/lysosomes, possibly via its interaction with MAP6 (By similarity). In motoneurons, may mediate the axonal transport of lysosomes and axonal sorting at the initial segment (By similarity). It remains unclear whether TMEM106B affects the transport of moving lysosomes in the anterograde or retrograde direction in neurites and whether it is important in the sorting of lysosomes in axons or in dendrites (By similarity). In neurons, may also play a role in the regulation of lysosomal size and responsiveness to stress (PubMed:25066864). Required for proper lysosomal acidification (By similarity)", "gene_name": "TMEM106B", "glycan_count": 29, "glycosylation_sites": [ { "position": 145, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 151, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 164, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 183, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 256, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NUM4", "name": "TMEM106B", "organism": "Homo sapiens", "uniprot_id": "Q9NUM4" }, { "function": "Required for ciliary structure and function. Part of the tectonic-like complex which is required for tissue-specific ciliogenesis and may regulate ciliary membrane composition (By similarity). Involved in centrosome migration to the apical cell surface during early ciliogenesis. Involved in the regulation of cilia length and appropriate number through the control of centrosome duplication. Is a key regulator of stereociliary bundle orientation (By similarity). Required for epithelial cell branching morphology. Essential for endoplasmic reticulum-associated degradation (ERAD) of surfactant protein C (SFTPC). Involved in the negative regulation of canonical Wnt signaling, and activation of the non-canonical cascade stimulated by WNT5A (PubMed:26035863). In non-canonical Wnt signaling, it may act as ROR2 coreceptor (By similarity)", "gene_name": "TMEM67", "glycan_count": 2, "glycosylation_sites": [ { "position": 141, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 179, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 242, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 318, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q5HYA8", "name": "TMEM67 (Meckelin)", "organism": "Homo sapiens", "uniprot_id": "Q5HYA8" }, { "function": "Inhibitor of bone morphogenetic protein (BMP) function, it may regulate BMP responsiveness of osteoblasts and chondrocytes", "gene_name": "BMPER", "glycan_count": 1, "glycosylation_sites": [ { "position": 116, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 247, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 255, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 318, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 441, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8N8U9", "name": "TMEM63C", "organism": "Homo sapiens", "uniprot_id": "Q8N8U9" }, { "function": "Phospholipid scramblase that promotes phosphatidylserine exposure on apoptotic cell surface (PubMed:23845944, PubMed:25231987). Phosphatidylserine is a specific marker only present at the surface of apoptotic cells and acts as a specific signal for engulfment (PubMed:23845944). Required for the clearance of apoptotic cells, such as engulfment of apoptotic germ cells by Sertoli cells, clearance of senescent neutrophils or regulation of bipolar cell numbers in the retina (By similarity). Has no effect on calcium-induced exposure of phosphatidylserine (PubMed:23845944). Promotes myoblast differentiation and survival (PubMed:28881496)", "gene_name": "XKR8", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H6D3", "name": "TMEM22", "organism": "Homo sapiens", "uniprot_id": "Q9H6D3" }, { "function": "Acts as a selective Mg(2+) transporter", "gene_name": "NIPA2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8N8Q9", "name": "TMEM174", "organism": "Homo sapiens", "uniprot_id": "Q8N8Q9" }, { "function": "", "gene_name": "C1orf52", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8N6N3", "name": "ZFYVE19 (ANCHR)", "organism": "Homo sapiens", "uniprot_id": "Q8N6N3" }, { "function": "Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their disassembly, possibly in combination with membrane fission. Redistributes the ESCRT-III components to the cytoplasm for further rounds of MVB sorting. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. It is required for proper accomplishment of various processes including the regulation of endosome size, primary cilium organization, mitotic spindle organization, chromosome segregation, and nuclear envelope sealing and spindle disassembly during anaphase (PubMed:33186545). Involved in cytokinesis: retained at the midbody by ZFYVE19/ANCHR and CHMP4C until abscission checkpoint signaling is terminated at late cytokinesis. It is then released following dephosphorylation of CHMP4C, leading to abscission (PubMed:24814515). VPS4A/B are required for the exosomal release of SDCBP, CD63 and syndecan (PubMed:22660413). Critical for normal erythroblast cytokinesis and correct erythropoiesis (PubMed:33186543)", "gene_name": "VPS4A", "glycan_count": 3, "glycosylation_sites": [], "id": "Q9UN37", "name": "VPS4", "organism": "Homo sapiens", "uniprot_id": "Q9UN37" }, { "function": "Ligand-gated anion channel that allows the movement of anions across cell membranes when activated by calcium (Ca2+) (PubMed:11904445, PubMed:12907679, PubMed:18179881, PubMed:18400985, PubMed:19853238, PubMed:21330666, PubMed:26200502, PubMed:26720466, PubMed:35789156). Allows the movement of chloride and hydrogencarbonate (PubMed:11904445, PubMed:12907679, PubMed:18179881, PubMed:18400985, PubMed:19853238, PubMed:21330666, PubMed:26200502, PubMed:26720466, PubMed:35789156). Found in a partially open conformation leading to significantly smaller chloride movement (PubMed:35789156). Upon F2R/PAR-1 activation, the sequestered calcium is released into the cytosol of astrocytes, leading to the (Ca2+)-dependent release of L-glutamate into the synaptic cleft that targets the neuronal postsynaptic GRIN2A/NMDAR receptor resulting in the synaptic plasticity regulation (By similarity). Upon activation of the norepinephrine-alpha-1 adrenergic receptor signaling pathway, transports as well D-serine than L-glutamate in a (Ca2+)-dependent manner, leading to activation of adjacent NMDAR receptors and therefore regulates the heterosynaptic long-term depression and metaplasticity during initial memory acquisition (By similarity). Releases the 4-aminobutanoate neurotransmitter in a (Ca2+)-dependent manner, and participates in its tonic release from cerebellar glial cells (By similarity)", "gene_name": "BEST1", "glycan_count": 0, "glycosylation_sites": [], "id": "O76090", "name": "Bestrophin-1", "organism": "Homo sapiens", "uniprot_id": "O76090" }, { "function": "E3 ubiquitin ligase that plays important roles in DNA methylation, histone modifications, cell cycle and DNA repair (PubMed:15178429, PubMed:23404503, PubMed:27743347, PubMed:29506131). Acts as a specific reader for 5-hydroxymethylcytosine (5hmC) and thereby recruits various substrates to these sites to ubiquitinate them (PubMed:24813944, PubMed:27129234). This activity also allows the maintenance of 5mC levels at specific genomic loci and regulates neuron-related gene expression (By similarity). Participates in cell cycle regulation by ubiquitinating cyclins CCND1 and CCNE1 and thereby inducing G1 arrest (PubMed:15178429, PubMed:15361834, PubMed:21952639). Also ubiquitinates PCNP leading to its degradation by the proteasome (PubMed:12176013, PubMed:14741369). Plays an active role in DNA damage repair by ubiquitinating p21/CDKN1A leading to its proteasomal degradation (PubMed:29923055). Also promotes DNA repair by acting as an interstrand cross-links (ICLs) sensor. Mechanistically, cooperates with UHRF1 to ensure recruitment of FANCD2 to ICLs, leading to FANCD2 monoubiquitination and subsequent activation (PubMed:30335751). Contributes to UV-induced DNA damage response by physically interacting with ATR in response to irradiation, thereby promoting ATR activation (PubMed:33848395)", "gene_name": "UHRF2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96PU4", "name": "Nephrin", "organism": "Homo sapiens", "uniprot_id": "Q96PU4" }, { "function": "Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments. May be involved in targeting of the catalytic subunit of protein phosphatase 1 during brain development. Activates PI3K and concomitantly recruits the WAVE1 complex to the close vicinity of PI3K and regulates neuronal morphogenesis (By similarity)", "gene_name": "MYO16", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y6X6", "name": "MYO1B", "organism": "Homo sapiens", "uniprot_id": "Q9Y6X6" }, { "function": "After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane", "gene_name": "CHRND", "glycan_count": 3, "glycosylation_sites": [ { "position": 97, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 164, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q07001", "name": "Acetylcholine Receptor (AChR)", "organism": "Homo sapiens", "uniprot_id": "Q07001" }, { "function": "Functions as a guanine nucleotide exchange factor for RAC1. May play a role in semaphorin signaling. Plays a role in the assembly and disassembly of dendritic filopodia, the formation of dendritic spines, regulation of dendrite length and ultimately the formation of synapses (By similarity)", "gene_name": "FARP1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y4F1", "name": "Low-density lipoprotein receptor-related protein 4 (LRP4)", "organism": "Homo sapiens", "uniprot_id": "Q9Y4F1" }, { "function": "Catalytic component of multiple cullin-5-RING E3 ubiquitin-protein ligase complexes (ECS complexes), which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:21980433, PubMed:33268465, PubMed:38418882, PubMed:38574733, PubMed:35512830). It is thereby involved in various biological processes, such as cell cycle progression, signal transduction and transcription (PubMed:21980433, PubMed:33268465, PubMed:38418882, PubMed:38574733). The functional specificity of the E3 ubiquitin-protein ligase ECS complexes depend on the variable SOCS box-containing substrate recognition component (PubMed:21980433, PubMed:33268465). Within ECS complexes, RNF7/RBX2 recruits the E2 ubiquitination enzyme to the complex via its RING-type and brings it into close proximity to the substrate (PubMed:34518685). Catalytic subunit of various SOCS-containing ECS complexes, such as the ECS(SOCS7) complex, that regulate reelin signaling by mediating ubiquitination and degradation of DAB1 (By similarity). The ECS(SOCS2) complex mediates the ubiquitination and subsequent proteasomal degradation of phosphorylated EPOR and GHR (PubMed:21980433, PubMed:25505247). Promotes ubiquitination and degradation of NF1, thereby regulating Ras protein signal transduction (By similarity). As part of the ECS(ASB9) complex, catalyzes ubiquitination and degradation of CKB (PubMed:33268465). The ECS(SPSB3) complex catalyzes ubiquitination of nuclear CGAS (PubMed:38418882). As part of the ECS(RAB40C) complex, mediates ANKRD28 ubiquitination and degradation, thereby inhibiting protein phosphatase 6 (PP6) complex activity and focal adhesion assembly during cell migration (PubMed:35512830). As part of some ECS complex, catalyzes 'Lys-11'-linked ubiquitination and degradation of BTRC (PubMed:27910872). ECS complexes and ARIH2 collaborate in tandem to mediate ubiquitination of target proteins; ARIH2 mediating addition of the first ubiquitin on CRLs targets (PubMed:34518685, PubMed:38418882). Specifically catalyzes the neddylation of CUL5 via its interaction with UBE2F (PubMed:19250909). Does not catalyze neddylation of other cullins (CUL1, CUL2, CUL3, CUL4A or CUL4B) (PubMed:19250909). May play a role in protecting cells from apoptosis induced by redox agents (PubMed:10082581)", "gene_name": "RNF7", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UBF6", "name": "UFM1 (Ubiquitin-fold modifier 1)", "organism": "Homo sapiens", "uniprot_id": "Q9UBF6" }, { "function": "Thiol-dependent isopeptidase that specifically mediate the processing of UFM1 precursors as well as the deconjugation of UFM1 from target proteins (PubMed:35525273, PubMed:35926457). Mainly responsible for the maturation of the UFM1 precursor, a prerequisite for conjugation reactions (PubMed:35525273, PubMed:35926457)", "gene_name": "UFSP1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6NVU6", "name": "UFL1 (UFM1-specific ligase 1)", "organism": "Homo sapiens", "uniprot_id": "Q6NVU6" }, { "function": "Transcriptional activator that recognizes and binds to the DNA sequence 5'-[AG]TAAA[TC]A-3' and regulates different processes, such as apoptosis and autophagy (PubMed:10102273, PubMed:16751106, PubMed:21329882, PubMed:30513302). Acts as a positive regulator of autophagy in skeletal muscle: in starved cells, enters the nucleus following dephosphorylation and binds the promoters of autophagy genes, such as GABARAP1L, MAP1LC3B and ATG12, thereby activating their expression, resulting in proteolysis of skeletal muscle proteins (By similarity). Triggers apoptosis in the absence of survival factors, including neuronal cell death upon oxidative stress (PubMed:10102273, PubMed:16751106). Participates in post-transcriptional regulation of MYC: following phosphorylation by MAPKAPK5, promotes induction of miR-34b and miR-34c expression, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent its translation (PubMed:21329882). In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription (PubMed:23283301). In response to metabolic stress, translocates into the mitochondria where it promotes mtDNA transcription. Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). Also acts as a key regulator of regulatory T-cells (Treg) differentiation by activating expression of FOXP3 (PubMed:30513302)", "gene_name": "FOXO3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9BZ04", "name": "UBA5 (UFM1-activating enzyme 5)", "organism": "Homo sapiens", "uniprot_id": "O43524" }, { "function": "Sulfotransferase that catalyzes the transfer of sulfate to the position 2 of uronyl residues in glycosaminoglycan chains (PubMed:10187838, PubMed:17227754). Has mainly activity toward iduronyl residues in dermatan sulfate, and weaker activity toward glucuronyl residues of chondroitin sulfate (PubMed:10187838). Has little to no activity toward desulfated N-resulfated heparin or N-sulfoheparosan (PubMed:10187838, PubMed:17227754)", "gene_name": "UST", "glycan_count": 10, "glycosylation_sites": [ { "position": 84, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 140, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 155, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 173, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 319, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y2C2", "name": "ANGPTL3", "organism": "Homo sapiens", "uniprot_id": "Q9Y2C2" }, { "function": "Nuclease involved in DNA non-homologous end joining (NHEJ); required for double-strand break repair and V(D)J recombination (PubMed:11336668, PubMed:11955432, PubMed:12055248, PubMed:14744996, PubMed:15071507, PubMed:15574326, PubMed:15936993). Required for V(D)J recombination, the process by which exons encoding the antigen-binding domains of immunoglobulins and T-cell receptor proteins are assembled from individual V, (D), and J gene segments (PubMed:11336668, PubMed:11955432, PubMed:14744996). V(D)J recombination is initiated by the lymphoid specific RAG endonuclease complex, which generates site specific DNA double strand breaks (DSBs) (PubMed:11336668, PubMed:11955432, PubMed:14744996). These DSBs present two types of DNA end structures: hairpin sealed coding ends and phosphorylated blunt signal ends (PubMed:11336668, PubMed:11955432, PubMed:14744996). These ends are independently repaired by the non homologous end joining (NHEJ) pathway to form coding and signal joints respectively (PubMed:11336668, PubMed:11955432, PubMed:14744996). This protein exhibits single-strand specific 5'-3' exonuclease activity in isolation and acquires endonucleolytic activity on 5' and 3' hairpins and overhangs when in a complex with PRKDC (PubMed:11955432, PubMed:15071507, PubMed:15574326, PubMed:15936993). The latter activity is required specifically for the resolution of closed hairpins prior to the formation of the coding joint (PubMed:11955432). Also required for the repair of complex DSBs induced by ionizing radiation, which require substantial end-processing prior to religation by NHEJ (PubMed:15456891, PubMed:15468306, PubMed:15574327, PubMed:15811628)", "gene_name": "DCLRE1C", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96SD1", "name": "Artemis (DCLRE1C)", "organism": "Homo sapiens", "uniprot_id": "Q96SD1" }, { "function": "Template-independent DNA polymerase which catalyzes the random addition of deoxynucleoside 5'-triphosphate to the 3'-end of a DNA initiator. One of the in vivo functions of this enzyme is the addition of nucleotides at the junction (N region) of rearranged Ig heavy chain and T-cell receptor gene segments during the maturation of B- and T-cells", "gene_name": "DNTT", "glycan_count": 1, "glycosylation_sites": [], "id": "P04053", "name": "TdT (Terminal deoxynucleotidyl transferase)", "organism": "Homo sapiens", "uniprot_id": "P04053" }, { "function": "Transcriptional regulator which displays a remarkable functional diversity in the regulation of cellular responses (PubMed:15226432, PubMed:15509808, PubMed:17516545, PubMed:17942705, PubMed:18497060, PubMed:19404407, PubMed:19851330, PubMed:22367195, PubMed:32385160). Regulates transcription of IFN and IFN-inducible genes, host response to viral and bacterial infections, regulation of many genes expressed during hematopoiesis, inflammation, immune responses and cell proliferation and differentiation, regulation of the cell cycle and induction of growth arrest and programmed cell death following DNA damage (PubMed:15226432, PubMed:15509808, PubMed:17516545, PubMed:17942705, PubMed:18497060, PubMed:19404407, PubMed:19851330, PubMed:22367195). Stimulates both innate and acquired immune responses through the activation of specific target genes and can act as a transcriptional activator and repressor regulating target genes by binding to an interferon-stimulated response element (ISRE) in their promoters (PubMed:15226432, PubMed:15509808, PubMed:17516545, PubMed:17942705, PubMed:18497060, PubMed:19404407, PubMed:19851330, PubMed:21389130, PubMed:22367195). Has an essentail role in IFNG-dependent immunity to mycobacteria (PubMed:36736301). Competes with the transcriptional repressor ZBED2 for binding to a common consensus sequence in gene promoters (PubMed:32385160). Its target genes for transcriptional activation activity include: genes involved in anti-viral response, such as IFN-alpha/beta, RIGI, TNFSF10/TRAIL, ZBP1, OAS1/2, PIAS1/GBP, EIF2AK2/PKR and RSAD2/viperin; antibacterial response, such as GBP2, GBP5 and NOS2/INOS; anti-proliferative response, such as p53/TP53, LOX and CDKN1A; apoptosis, such as BBC3/PUMA, CASP1, CASP7 and CASP8; immune response, such as IL7, IL12A/B and IL15, PTGS2/COX2 and CYBB; DNA damage responses and DNA repair, such as POLQ/POLH; MHC class I expression, such as TAP1, PSMB9/LMP2, PSME1/PA28A, PSME2/PA28B and B2M and MHC class II expression, such as CIITA; metabolic enzymes, such as ACOD1/IRG1 (PubMed:15226432, PubMed:15509808, PubMed:17516545, PubMed:17942705, PubMed:18497060, PubMed:19404407, PubMed:19851330, PubMed:22367195). Represses genes involved in anti-proliferative response, such as BIRC5/survivin, CCNB1, CCNE1, CDK1, CDK2 and CDK4 and in immune response, such as FOXP3, IL4, ANXA2 and TLR4 (PubMed:18641303, PubMed:22200613). Stimulates p53/TP53-dependent transcription through enhanced recruitment of EP300 leading to increased acetylation of p53/TP53 (PubMed:15509808, PubMed:18084608). Plays an important role in immune response directly affecting NK maturation and activity, macrophage production of IL12, Th1 development and maturation of CD8+ T-cells (PubMed:11244049, PubMed:11846971, PubMed:11846974, PubMed:16932750). Also implicated in the differentiation and maturation of dendritic cells and in the suppression of regulatory T (Treg) cells development (PubMed:11244049, PubMed:11846971, PubMed:11846974, PubMed:16932750). Acts as a tumor suppressor and plays a role not only in antagonism of tumor cell growth but also in stimulating an immune response against tumor cells (PubMed:20049431)", "gene_name": "IRF1", "glycan_count": 0, "glycosylation_sites": [], "id": "P10914", "name": "IRF1", "organism": "Homo sapiens", "uniprot_id": "P10914" }, { "function": "Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoA for both synthesis of cellular lipids, and degradation via beta-oxidation (PubMed:21242590, PubMed:22633490, PubMed:24269233). Preferentially activates arachidonate and eicosapentaenoate as substrates (PubMed:21242590). Preferentially activates 8,9-EET > 14,15-EET > 5,6-EET > 11,12-EET. Modulates glucose-stimulated insulin secretion by regulating the levels of unesterified EETs (By similarity). Modulates prostaglandin E2 secretion (PubMed:21242590)", "gene_name": "ACSL4", "glycan_count": 1, "glycosylation_sites": [], "id": "O60488", "name": "ACSL4", "organism": "Homo sapiens", "uniprot_id": "O60488" }, { "function": "Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (PubMed:17182577, PubMed:19032234, PubMed:2176490). Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity (PubMed:16408020, PubMed:17606900). Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity (PubMed:11118054, PubMed:9108029)", "gene_name": "TXN", "glycan_count": 1, "glycosylation_sites": [], "id": "P10599", "name": "TXN", "organism": "Homo sapiens", "uniprot_id": "P10599" }, { "function": "", "gene_name": "SBSN", "glycan_count": 2, "glycosylation_sites": [], "id": "Q6UWP8", "name": "Suprabasin (SBSN)", "organism": "Homo sapiens", "uniprot_id": "Q6UWP8" }, { "function": "Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Inhibits androgen receptor (AR) and HTT aggregation and binding of G-actin is essential for its inhibition of AR", "gene_name": "PFN1", "glycan_count": 3, "glycosylation_sites": [], "id": "P07737", "name": "Profilin-1 (PFN1)", "organism": "Homo sapiens", "uniprot_id": "P07737" }, { "function": "Binds to the C-terminal propeptide of type I procollagen and enhances procollagen C-proteinase activity", "gene_name": "PCOLCE", "glycan_count": 2, "glycosylation_sites": [ { "position": 29, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 431, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q15113", "name": "Procollagen C-endopeptidase enhancer 1 (PCOLCE)", "organism": "Homo sapiens", "uniprot_id": "Q15113" }, { "function": "Receptor with an affinity for galactose and fucose. Could be involved in endocytosis (By similarity)", "gene_name": "CLEC4F", "glycan_count": 0, "glycosylation_sites": [ { "position": 79, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 113, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 207, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 230, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 244, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 312, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 385, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 399, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8N1N0", "name": "WAP four-disulfide core domain protein 3 (WFDC3)", "organism": "Homo sapiens", "uniprot_id": "Q8N1N0" }, { "function": "A component of desmosome cell-cell junctions which are required for positive regulation of cellular adhesion (PubMed:38395410). Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. Required for proliferation and viability of embryonic stem cells in the blastocyst, thereby crucial for progression of post-implantation embryonic development (By similarity). Maintains pluripotency by regulating epithelial to mesenchymal transition/mesenchymal to epithelial transition (EMT/MET) via interacting with and sequestering CTNNB1 to sites of cell-cell contact, thereby reducing translocation of CTNNB1 to the nucleus and subsequent transcription of CTNNB1/TCF-target genes (PubMed:29910125). Promotes pluripotency and the multi-lineage differentiation potential of hematopoietic stem cells (PubMed:27338829). Plays a role in endothelial cell sprouting and elongation via mediating the junctional-association of cortical actin fibers and CDH5 (PubMed:27338829). Plays a role in limiting inflammatory infiltration and the apoptotic response to injury in kidney tubular epithelial cells, potentially via its role in maintaining cell-cell adhesion and the epithelial barrier (PubMed:38395410)", "gene_name": "DSG2", "glycan_count": 86, "glycosylation_sites": [ { "position": 112, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 182, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 309, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 462, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 514, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q14126", "name": "Desmoglein-2 (DSG2)", "organism": "Homo sapiens", "uniprot_id": "Q14126" }, { "function": "Required for synaptic transmission regulation (PubMed:33539324). It probably controls the recruitement of voltage-gated calcium channels to the presynaptic membrane, and modulates neurotransmitter release", "gene_name": "TSPOAP1", "glycan_count": 0, "glycosylation_sites": [], "id": "O95153", "name": "ATPase copper-transporting \u03b2 protein (ATP7B)", "organism": "Homo sapiens", "uniprot_id": "O95153" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P21447 (mouse)", "name": "Abcb1b (P-glycoprotein/MDR1)", "organism": "", "uniprot_id": "" }, { "function": "Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus", "gene_name": "FABP4", "glycan_count": 0, "glycosylation_sites": [], "id": "P15090", "name": "Adipocyte fatty acid-binding protein", "organism": "Homo sapiens", "uniprot_id": "P15090" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P05109/P06702 (S100A8/S100A9)", "name": "Calprotectin", "organism": "", "uniprot_id": "" }, { "function": "Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Plays an important role in wound healing. Induces macrophage recruitment, increased interstitial pressure, and blood vessel maturation during angiogenesis. Can initiate events that lead to a mesangial proliferative glomerulonephritis, including influx of monocytes and macrophages and production of extracellular matrix (By similarity)", "gene_name": "PDGFD", "glycan_count": 4, "glycosylation_sites": [ { "position": 276, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9GZP0", "name": "Platelet-derived growth factor-D (PDGF-D)", "organism": "Homo sapiens", "uniprot_id": "Q9GZP0" }, { "function": "Actin-binding protein (PubMed:16636079, PubMed:17294403, PubMed:28493397). Plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28 (PubMed:17294403). Modulates the cell surface expression of IL2RA/CD25 and CD69 (PubMed:17294403)", "gene_name": "LCP1", "glycan_count": 1, "glycosylation_sites": [], "id": "P13796", "name": "LCP1 (lymphocyte cytosolic protein 1)", "organism": "Homo sapiens", "uniprot_id": "P13796" }, { "function": "Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. PB-cadherins may have a role in the morphological organization of pituitary gland and brain tissues (By similarity)", "gene_name": "CDH22", "glycan_count": 1, "glycosylation_sites": [ { "position": 162, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 466, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 612, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UJ99", "name": "SGCE (Sarcoglycan epsilon)", "organism": "Homo sapiens", "uniprot_id": "Q9UJ99" }, { "function": "May be involved in neuronal differentiation", "gene_name": "AATK", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6ZMQ8", "name": "OLFML3 (Olfactomedin-like protein 3)", "organism": "Homo sapiens", "uniprot_id": "Q6ZMQ8" }, { "function": "Catalyzes the hydrolytic deamination of enamine/imine intermediates that form during the course of normal metabolism. May facilitate the release of ammonia from these potentially toxic reactive metabolites, reducing their impact on cellular components. It may act on enamine/imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases including L-threonine dehydratase", "gene_name": "RIDA", "glycan_count": 0, "glycosylation_sites": [], "id": "P52758", "name": "HRSP12 (Heat-responsive protein 12)", "organism": "Homo sapiens", "uniprot_id": "P52758" }, { "function": "Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways (PubMed:21189250). Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif (PubMed:35343654). Binding generally results in the modulation of the activity of the binding partner (By similarity). Positively regulates phosphorylated protein HSF1 nuclear export to the cytoplasm (PubMed:12917326). Plays a positive role in the antiviral signaling pathway upstream of TBK1 via interaction with RIGI (PubMed:37555661). Mechanistically, directs RIGI redistribution from the cytosol to mitochondrial associated membranes where it mediates MAVS-dependent innate immune signaling during viral infection (PubMed:22607805). Plays a role in proliferation inhibition and cell cycle arrest by exporting HNRNPC from the nucleus to the cytoplasm to be degraded by ubiquitination (PubMed:37599448)", "gene_name": "YWHAE", "glycan_count": 16, "glycosylation_sites": [], "id": "P62258", "name": "YWHAE (14-3-3 protein epsilon)", "organism": "Homo sapiens", "uniprot_id": "P62258" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Z0J7 (mouse)", "name": "CD169 (Siglec-1)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01574 (mouse)", "name": "Interferon alpha (IFN\u03b1)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q61830 (mouse)", "name": "CD206 (mannose receptor)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q64287 (mouse)", "name": "IFNAR1 (Interferon alpha/beta receptor 1)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02763 (human)", "name": "Alpha-1-acid glycoprotein (AGP)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9QUN7 (mouse)", "name": "CD163", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q07011 (mouse)", "name": "CD68", "organism": "", "uniprot_id": "" }, { "function": "Involved in the regulation of homocysteine metabolism. Converts homocysteine to methionine using S-methylmethionine (SMM) as a methyl donor", "gene_name": "BHMT2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H2M3", "name": "Prolargin", "organism": "Homo sapiens", "uniprot_id": "Q9H2M3" }, { "function": "Membrane-bound component of the endocytic receptor formed by AMN and CUBN (PubMed:14576052, PubMed:29402915, PubMed:30523278). Required for normal CUBN glycosylation and trafficking to the cell surface (PubMed:14576052, PubMed:29402915). The complex formed by AMN and CUBN is required for efficient absorption of vitamin B12 (PubMed:12590260, PubMed:14576052, PubMed:26040326). Required for normal CUBN-mediated protein transport in the kidney (Probable)", "gene_name": "AMN", "glycan_count": 0, "glycosylation_sites": [ { "position": 35, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9BXJ7", "name": "CRTAC1", "organism": "Homo sapiens", "uniprot_id": "Q9BXJ7" }, { "function": "Function as phospholipase selective for phosphatidylcholine (PubMed:25936805, PubMed:8530346, PubMed:9582313). Implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. May be involved in the regulation of perinuclear intravesicular membrane traffic (By similarity)", "gene_name": "PLD1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q13393", "name": "Phospholipase D1", "organism": "Homo sapiens", "uniprot_id": "Q13393" }, { "function": "Catalyzes the final step of de novo phosphatidylcholine (PC) synthesis, i.e. the transfer of choline phosphate from CDP-choline to the free hydroxyl of a diacylglycerol (DAG), producing a PC. It thereby plays a central role in the formation and maintenance of vesicular membranes", "gene_name": "CHPT1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8WUD6", "name": "Cholinephosphotransferase 1", "organism": "Homo sapiens", "uniprot_id": "Q8WUD6" }, { "function": "Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids with implications in host antimicrobial defense, inflammatory response and tissue regeneration (PubMed:10455175, PubMed:10681567, PubMed:2925633). Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines (PubMed:10455175, PubMed:10681567). Contributes to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Displays bactericidal activity against Gram-positive bacteria by directly hydrolyzing phospholipids of the bacterial membrane (PubMed:10358193, PubMed:11694541). Upon sterile inflammation, targets membrane phospholipids of extracellular mitochondria released from activated platelets, generating free unsaturated fatty acids such as arachidonate that is used by neighboring leukocytes to synthesize inflammatory eicosanoids such as leukotrienes. Simultaneously, by compromising mitochondrial membrane integrity, promotes the release in circulation of potent damage-associated molecular pattern molecules that activate the innate immune response (PubMed:25082876). Plays a stem cell regulator role in the intestinal crypt. Within intracellular compartment mediates Paneth cell differentiation and its stem cell supporting functions by inhibiting Wnt signaling pathway in intestinal stem cell (ICS). Secreted in the intestinal lumen upon inflammation, acts in an autocrine way and promotes prostaglandin E2 synthesis that stimulates Wnt signaling pathway in ICS cells and tissue regeneration (By similarity). May play a role in the biosynthesis of N-acyl ethanolamines that regulate energy metabolism and inflammation. Hydrolyzes N-acyl phosphatidylethanolamines to N-acyl lysophosphatidylethanolamines, which are further cleaved by a lysophospholipase D to release N-acyl ethanolamines (PubMed:14998370). Independent of its catalytic activity, acts as a ligand for integrins (PubMed:18635536, PubMed:25398877). Binds to and activates integrins ITGAV:ITGB3, ITGA4:ITGB1 and ITGA5:ITGB1 (PubMed:18635536, PubMed:25398877). Binds to a site (site 2) which is distinct from the classical ligand-binding site (site 1) and induces integrin conformational changes and enhanced ligand binding to site 1 (PubMed:25398877). Induces cell proliferation in an integrin-dependent manner (PubMed:18635536)", "gene_name": "PLA2G2A", "glycan_count": 1, "glycosylation_sites": [], "id": "P14555", "name": "Phospholipase A2 group IIA", "organism": "Homo sapiens", "uniprot_id": "P14555" }, { "function": "Involved in bone homeostasis. Acts as a negative regulator of RANKL-induced osteoclast precursor differentiation from bone marrow precursors (By similarity)", "gene_name": "LRRC17", "glycan_count": 2, "glycosylation_sites": [], "id": "Q8N6Y2", "name": "Oncoprotein-induced transcript 3 protein (OIT3)", "organism": "Homo sapiens", "uniprot_id": "Q8N6Y2" }, { "function": "Mediates the post-translational oxidative deamination of lysine residues on target proteins leading to the formation of deaminated lysine (allysine) (PubMed:27735137). Acts as a transcription corepressor and specifically mediates deamination of trimethylated 'Lys-4' of histone H3 (H3K4me3), a specific tag for epigenetic transcriptional activation (PubMed:27735137). Shows no activity against histone H3 when it is trimethylated on 'Lys-9' (H3K9me3) or 'Lys-27' (H3K27me3) or when 'Lys-4' is monomethylated (H3K4me1) or dimethylated (H3K4me2) (PubMed:27735137). Also mediates deamination of methylated TAF10, a member of the transcription factor IID (TFIID) complex, which induces release of TAF10 from promoters, leading to inhibition of TFIID-dependent transcription (PubMed:25959397). LOXL2-mediated deamination of TAF10 results in transcriptional repression of genes required for embryonic stem cell pluripotency including POU5F1/OCT4, NANOG, KLF4 and SOX2 (By similarity). Involved in epithelial to mesenchymal transition (EMT) via interaction with SNAI1 and participates in repression of E-cadherin CDH1, probably by mediating deamination of histone H3 (PubMed:16096638, PubMed:24414204, PubMed:27735137). During EMT, involved with SNAI1 in negatively regulating pericentromeric heterochromatin transcription (PubMed:24239292). SNAI1 recruits LOXL2 to pericentromeric regions to oxidize histone H3 and repress transcription which leads to release of heterochromatin component CBX5/HP1A, enabling chromatin reorganization and acquisition of mesenchymal traits (PubMed:24239292). Interacts with the endoplasmic reticulum protein HSPA5 which activates the IRE1-XBP1 pathway of the unfolded protein response, leading to expression of several transcription factors involved in EMT and subsequent EMT induction (PubMed:28332555). Involved in E-cadherin repression following hypoxia, a hallmark of EMT believed to amplify tumor aggressiveness, suggesting that it may play a role in tumor progression (PubMed:20026874). When secreted into the extracellular matrix, promotes cross-linking of extracellular matrix proteins by mediating oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin (PubMed:20306300). Acts as a regulator of sprouting angiogenesis, probably via collagen IV scaffolding (PubMed:21835952). Acts as a regulator of chondrocyte differentiation, probably by regulating expression of factors that control chondrocyte differentiation (By similarity)", "gene_name": "LOXL2", "glycan_count": 17, "glycosylation_sites": [ { "position": 288, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 455, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 644, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "Q9Y4K0", "name": "Lysyl oxidase like protein 1 (LOXL1)", "organism": "Homo sapiens", "uniprot_id": "Q9Y4K0" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02452 (human)", "name": "Collagen type I", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P42574/P55210", "name": "Caspase 3/7", "organism": "", "uniprot_id": "" }, { "function": "GTP hydrolase that promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis", "gene_name": "tuf", "glycan_count": 0, "glycosylation_sites": [], "id": "P69952", "name": "UreA", "organism": "Streptococcus pyogenes serotype M1", "uniprot_id": "P69952" }, { "function": "Potent pro-inflammatory cytokine. Initially discovered as the major endogenous pyrogen, induces prostaglandin synthesis, neutrophil influx and activation, T-cell activation and cytokine production, B-cell activation and antibody production, and fibroblast proliferation and collagen production. Promotes Th17 differentiation of T-cells. Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T-helper 1 (Th1) cells. Plays a role in angiogenesis by inducing VEGF production synergistically with TNF and IL6. Involved in transduction of inflammation downstream of pyroptosis: its mature form is specifically released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore", "gene_name": "Il1b", "glycan_count": 0, "glycosylation_sites": [], "id": "P10749", "name": "Interleukin-1 beta (IL-1\u03b2)", "organism": "Mus musculus", "uniprot_id": "P10749" }, { "function": "Precursor of the transcription factor form (Processed sterol regulatory element-binding protein 1), which is embedded in the endoplasmic reticulum membrane (PubMed:11782483, PubMed:12855691, PubMed:19244231). Low sterol concentrations promote processing of this form, releasing the transcription factor form that translocates into the nucleus and activates transcription of genes involved in cholesterol biosynthesis and lipid homeostasis (PubMed:11782483, PubMed:12855691, PubMed:16100574, PubMed:19244231)", "gene_name": "Srebf1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9WTN3", "name": "Sterol Regulatory Element-Binding Protein 1 (SREBP1)", "organism": "Mus musculus", "uniprot_id": "Q9WTN3" }, { "function": "Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis. ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated pro-inflammatory responses. Plays a role in the regulation of cardiovascular circadian rhythms by regulating the transcription of BMAL1 in the blood vessels (PubMed:19041764)", "gene_name": "Pparg", "glycan_count": 0, "glycosylation_sites": [ { "position": 84, "type": "O-linked (GlcNAc) threonine" } ], "id": "P37238", "name": "Peroxisome Proliferator-Activated Receptor Gamma (PPAR\u03b3)", "organism": "Mus musculus", "uniprot_id": "P37238" }, { "function": "Protein, which is both involved in DNA repair and protein ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box) complexes, respectively (PubMed:12107171, PubMed:26431207, PubMed:28790135). Core component of the UV-DDB complex (UV-damaged DNA-binding protein complex), a complex that recognizes UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair (PubMed:12107171). The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches (By similarity). Also functions as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). The functional specificity of the DCX E3 ubiquitin-protein ligase complex is determined by the variable substrate recognition component recruited by DDB1 (By similarity). DCX(DDB2) (also known as DDB1-CUL4-ROC1, CUL4-DDB-ROC1 and CUL4-DDB-RBX1) may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage (By similarity). The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair (By similarity). DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER (By similarity). DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of TP53 in response to radiation-induced DNA damage and during DNA replication (By similarity). DCX(ERCC8) (the CSA complex) plays a role in transcription-coupled repair (TCR) (By similarity). The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1 (PubMed:26431207). DDB1-mediated CRY1 degradation promotes FOXO1 protein stability and FOXO1-mediated gluconeogenesis in the liver (PubMed:28790135). By acting on TET dioxygenses, essential for oocyte maintenance at the primordial follicle stage, hence essential for female fertility (PubMed:24357321). Maternal factor required for proper zygotic genome activation and genome reprogramming (PubMed:24357321)", "gene_name": "Ddb1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q3U1J4", "name": "Fatty Acid Synthase (FASN)", "organism": "Mus musculus", "uniprot_id": "Q3U1J4" }, { "function": "Voltage-gated chloride channel involved in high-concentration salt taste sensation (PubMed:34429071). Depolarization induced by high NaCl concentration may trigger the activation of TMC4-mediated chloride influx into taste bud cells, helping the return to resting potential (PubMed:34429071). Also allows permeation of organic anions including gluconate, but their current amplitudes at positive potentials are less than that of chloride (PubMed:34429071). Involved in pH and temperature-dependent modulation of salty taste (By similarity)", "gene_name": "Tmc4", "glycan_count": 0, "glycosylation_sites": [ { "position": 691, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8R1X9", "name": "Acetyl-CoA Carboxylase (ACC)", "organism": "Mus musculus", "uniprot_id": "Q7TQ65" }, { "function": "Plays a role in cell adhesion, and in cohesion of the endothelial monolayer at intercellular junctions in vascular tissue. Its expression may allow melanoma cells to interact with cellular elements of the vascular system, thereby enhancing hematogeneous tumor spread. Could be an adhesion molecule active in neural crest cells during embryonic development. Acts as a surface receptor that triggers tyrosine phosphorylation of FYN and PTK2/FAK1, and a transient increase in the intracellular calcium concentration (By similarity)", "gene_name": "Mcam", "glycan_count": 4, "glycosylation_sites": [ { "position": 58, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 510, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8R2Y2", "name": "F4/80 (EMR1)", "organism": "Mus musculus", "uniprot_id": "Q8R2Y2" }, { "function": "Mediates the endocytosis of glycoproteins by macrophages. Binds both sulfated and non-sulfated polysaccharide chains. Acts as phagocytic receptor for bacteria, fungi and other pathogens", "gene_name": "Mrc1", "glycan_count": 2, "glycosylation_sites": [ { "position": 104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 344, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 529, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 926, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 930, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1159, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1204, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q61830", "name": "CD206 (Mannose Receptor, MRC1)", "organism": "Mus musculus", "uniprot_id": "Q61830" }, { "function": "Calcium-dependent cell-adhesion protein. Mediates functions in neuroprogenitor cell proliferation and differentiation. In the heart, has a critical role for proper morphogenesis of the mitral valve, acting in the regulation of cell migration involved in valve formation (PubMed:26258302)", "gene_name": "DCHS1", "glycan_count": 16, "glycosylation_sites": [ { "position": 217, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 256, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 402, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 584, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1249, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1521, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1718, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1996, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2361, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2428, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2569, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2761, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2792, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2862, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q96JQ0", "name": "MS4A4A", "organism": "Homo sapiens", "uniprot_id": "Q96JQ0" }, { "function": "Force generating protein of respiratory cilia. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP", "gene_name": "DNAH11", "glycan_count": 12, "glycosylation_sites": [], "id": "Q96DT5", "name": "HE4 (Human Epididymis Protein 4)", "organism": "Homo sapiens", "uniprot_id": "Q96DT5" }, { "function": "Dipeptidase that catalyzes the hydrolysis of dipeptides with a prolyl (Xaa-Pro) or hydroxyprolyl residue in the C-terminal position (PubMed:17081196, PubMed:35165443). The preferred dipeptide substrate is Gly-Pro, but other Xaa-Pro dipeptides, such as Ala-Pro, Met-Pro, Phe-Pro, Val-Pro and Leu-Pro, can be cleaved (PubMed:17081196). Plays an important role in collagen metabolism because the high level of iminoacids in collagen (PubMed:2925654)", "gene_name": "PEPD", "glycan_count": 1, "glycosylation_sites": [], "id": "P12955", "name": "Prolidase (PEPD)", "organism": "Homo sapiens", "uniprot_id": "P12955" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P13674/P54868", "name": "Prolyl 4-hydroxylase (P4HA1/P4HA2)", "organism": "", "uniprot_id": "" }, { "function": "Involved in DNA damage response and double-strand break (DSB) repair. Component of the BRCA1-A complex, acting as a central scaffold protein that assembles the various components of the complex and mediates the recruitment of BRCA1. The BRCA1-A complex specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesion sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at DSBs. This complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX", "gene_name": "ABRAXAS1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H9N4", "name": "Hydroxyproline dehydrogenase 2 (PRODH2/OH-POX)", "organism": "Homo sapiens", "uniprot_id": "Q6UWZ7" }, { "function": "Catalyzes the conversion of sulfated steroid precursors, such as dehydroepiandrosterone sulfate (DHEA-S) and estrone sulfate to the free steroid", "gene_name": "STS", "glycan_count": 10, "glycosylation_sites": [ { "position": 47, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 259, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08842", "name": "Alkaline phosphatase (ALP)", "organism": "Homo sapiens", "uniprot_id": "P08842" }, { "function": "Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia", "gene_name": "glnII", "glycan_count": 0, "glycosylation_sites": [], "id": "P19432", "name": "Gamma-glutamyl transferase (GGT)", "organism": "Streptomyces viridochromogenes", "uniprot_id": "P19432" }, { "function": "Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway", "gene_name": "HPRT1", "glycan_count": 1, "glycosylation_sites": [], "id": "P00492", "name": "Hypoxanthine-guanine phosphoribosyltransferase (HGPRT)", "organism": "Homo sapiens", "uniprot_id": "P00492" }, { "function": "Plays an important role in the regulation of embryonic development, cell proliferation and cell differentiation. Required for normal branching morphogenesis. Growth factor active on keratinocytes. Possible major paracrine effector of normal epithelial cell proliferation", "gene_name": "FGF7", "glycan_count": 1, "glycosylation_sites": [ { "position": 45, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P21781", "name": "Keratinocyte Growth Factor-2 (KGF-2) / Fibroblast Growth Factor-10 (FGF-10)", "organism": "Homo sapiens", "uniprot_id": "P21781" }, { "function": "", "gene_name": "BTN2A1", "glycan_count": 5, "glycosylation_sites": [ { "position": 46, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 114, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 120, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q7KYR7", "name": "BTN3A3", "organism": "Homo sapiens", "uniprot_id": "Q7KYR7" }, { "function": "ABC transporter associated with antigen processing. In complex with TAP2 mediates unidirectional translocation of peptide antigens from cytosol to endoplasmic reticulum (ER) for loading onto MHC class I (MHCI) molecules (PubMed:25377891, PubMed:25656091). Uses the chemical energy of ATP to export peptides against the concentration gradient (PubMed:25377891). During the transport cycle alternates between 'inward-facing' state with peptide binding site facing the cytosol to 'outward-facing' state with peptide binding site facing the ER lumen. Peptide antigen binding to ATP-loaded TAP1-TAP2 induces a switch to hydrolysis-competent 'outward-facing' conformation ready for peptide loading onto nascent MHCI molecules. Subsequently ATP hydrolysis resets the transporter to the 'inward facing' state for a new cycle (PubMed:11274390, PubMed:25377891, PubMed:25656091). Typically transports intracellular peptide antigens of 8 to 13 amino acids that arise from cytosolic proteolysis via IFNG-induced immunoproteasome. Binds peptides with free N- and C-termini, the first three and the C-terminal residues being critical. Preferentially selects peptides having a highly hydrophobic residue at position 3 and hydrophobic or charged residues at the C-terminal anchor. Proline at position 2 has the most destabilizing effect (PubMed:11274390, PubMed:7500034, PubMed:9256420). As a component of the peptide loading complex (PLC), acts as a molecular scaffold essential for peptide-MHCI assembly and antigen presentation (PubMed:1538751, PubMed:25377891, PubMed:26611325)", "gene_name": "TAP1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q03518", "name": "TAP2", "organism": "Homo sapiens", "uniprot_id": "Q03518" }, { "function": "Serine protease inhibitor with activity toward thrombin, trypsin, and urokinase. Promotes neurite extension by inhibiting thrombin. Binds heparin", "gene_name": "SERPINE2", "glycan_count": 12, "glycosylation_sites": [ { "position": 118, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 159, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P07093", "name": "SERPINE2", "organism": "Homo sapiens", "uniprot_id": "P07093" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "LAMA1: P25391, LAMB1: P07942, LAMC1: P11047", "name": "Laminin-111", "organism": "", "uniprot_id": "" }, { "function": "Myosins are actin-based motor molecules with ATPase activity essential for muscle contraction. Forms regular bipolar thick filaments that, together with actin thin filaments, constitute the fundamental contractile unit of skeletal and cardiac muscle", "gene_name": "MYH7", "glycan_count": 1, "glycosylation_sites": [], "id": "P12883", "name": "Myosin Heavy Chain 7 (MYH7)", "organism": "Homo sapiens", "uniprot_id": "P12883" }, { "function": "Muscle contraction", "gene_name": "MYH6", "glycan_count": 1, "glycosylation_sites": [], "id": "P13533", "name": "Myosin Heavy Chain 6 (MYH6)", "organism": "Homo sapiens", "uniprot_id": "P13533" }, { "function": "DNA-binding transcriptional activator. Recognizes and binds to the consensus octamer binding site 5'-ATAATTAA-3' in promoter of target genes. Plays a fundamental role in the gene regulatory network essential for retinal ganglion cell (RGC) differentiation. Cooperates with the transcription factor POU4F2 to achieve maximal levels of expression of RGC target genes and RGC fate specification in the developing retina. Involved in the specification of motor neurons in cooperation with LHX3 and LDB1 (By similarity). Binds to insulin gene enhancer sequences (By similarity). Essential for heart development. Marker of one progenitor cell population that give rise to the outflow tract, right ventricle, a subset of left ventricular cells, and a large number of atrial cells as well, its function is required for these progenitors to contribute to the heart. Controls the expression of FGF and BMP growth factors in this cell population and is required for proliferation and survival of cells within pharyngeal foregut endoderm and adjacent splanchnic mesoderm as well as for migration of cardiac progenitors into the heart (By similarity)", "gene_name": "ISL1", "glycan_count": 1, "glycosylation_sites": [], "id": "P61371", "name": "ISL1", "organism": "Homo sapiens", "uniprot_id": "P61371" }, { "function": "Protein phosphatase involved in the inactivation of MAP kinases. Has a specificity for the MAPK11/MAPK12/MAPK13/MAPK14 subfamily. It preferably dephosphorylates p38", "gene_name": "DUSP10", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y6W6", "name": "SVIL", "organism": "Homo sapiens", "uniprot_id": "Q9Y6W6" }, { "function": "Acts as an inhibitor of BTK tyrosine kinase activity, thereby playing a role in B-cell development. Down-regulates BTK kinase activity, leading to interference with BTK-mediated calcium mobilization and NF-kappa-B-driven transcription", "gene_name": "IBTK", "glycan_count": 3, "glycosylation_sites": [], "id": "Q9P2D0", "name": "NTM", "organism": "Homo sapiens", "uniprot_id": "Q9P2D0" }, { "function": "IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors", "gene_name": "IGFBP4", "glycan_count": 2, "glycosylation_sites": [ { "position": 125, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P22692", "name": "IGFBP-4", "organism": "Homo sapiens", "uniprot_id": "P22692" }, { "function": "Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. Represses the transcriptional activity of MYC", "gene_name": "PFDN5", "glycan_count": 1, "glycosylation_sites": [], "id": "Q99471", "name": "Prohibitin 1 (PHB1)", "organism": "Homo sapiens", "uniprot_id": "Q99471" }, { "function": "Metalloprotease that is part of the quality control system in the inner membrane of mitochondria (PubMed:20038677, PubMed:25605331, PubMed:32132706, PubMed:32132707). Activated in response to various mitochondrial stress, leading to the proteolytic cleavage of target proteins, such as OPA1, UQCC3 and DELE1 (PubMed:20038677, PubMed:25275009, PubMed:32132706, PubMed:32132707). Involved in the fusion of the mitochondrial inner membranes by mediating cleavage of OPA1 at S1 position, generating the soluble OPA1 (S-OPA1), which cooperates with the membrane form (L-OPA1) to coordinate the fusion of mitochondrial inner membranes (PubMed:31922487). Following stress conditions that induce loss of mitochondrial membrane potential, mediates cleavage of OPA1, leading to excess production of soluble OPA1 (S-OPA1) and negative regulation of mitochondrial fusion (PubMed:20038677, PubMed:25275009). Involved in mitochondrial safeguard in response to transient mitochondrial membrane depolarization (flickering) by catalyzing cleavage of OPA1, leading to excess production of S-OPA1, preventing mitochondrial hyperfusion (By similarity). Also acts as a regulator of apoptosis: upon BAK and BAX aggregation, mediates cleavage of OPA1, leading to the remodeling of mitochondrial cristae and allowing the release of cytochrome c from mitochondrial cristae (PubMed:25275009). In depolarized mitochondria, may also act as a backup protease for PINK1 by mediating PINK1 cleavage and promoting its subsequent degradation by the proteasome (PubMed:30733118). May also cleave UQCC3 in response to mitochondrial depolarization (PubMed:25605331). Also acts as an activator of the integrated stress response (ISR): in response to mitochondrial stress, mediates cleavage of DELE1 to generate the processed form of DELE1 (S-DELE1), which translocates to the cytosol and activates EIF2AK1/HRI to trigger the ISR (PubMed:32132706, PubMed:32132707). Its role in mitochondrial quality control is essential for regulating lipid metabolism as well as to maintain body temperature and energy expenditure under cold-stress conditions (By similarity). Binds cardiolipin, possibly regulating its protein turnover (By similarity). Required for the stability of the respiratory supercomplexes (By similarity)", "gene_name": "OMA1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q96E52", "name": "OMA1", "organism": "Homo sapiens", "uniprot_id": "Q96E52" }, { "function": "Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing (PubMed:29507755). Required for accumulation of METTL3 and METTL14 to nuclear speckle (PubMed:24316715, PubMed:24407421, PubMed:24981863). Acts as a mRNA splicing regulator (PubMed:12444081). Regulates G2/M cell-cycle transition by binding to the 3' UTR of CCNA2, which enhances its stability (PubMed:17088532). Impairs WT1 DNA-binding ability and inhibits expression of WT1 target genes (PubMed:17095724)", "gene_name": "WTAP", "glycan_count": 1, "glycosylation_sites": [], "id": "Q15007", "name": "WTAP", "organism": "Homo sapiens", "uniprot_id": "Q15007" }, { "function": "Dioxygenase that specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes (PubMed:23177736, PubMed:24489119, PubMed:24616105, PubMed:24778178, PubMed:34048572, PubMed:36944332, PubMed:37257451, PubMed:37369679). Demethylates RNA by oxidative demethylation, which requires molecular oxygen, alpha-ketoglutarate and iron (PubMed:21264265, PubMed:23177736, PubMed:24489119, PubMed:24616105, PubMed:24778178). Demethylation of m6A mRNA affects mRNA processing, translation and export (PubMed:23177736, PubMed:34048572, PubMed:36944332, PubMed:37257451). Can also demethylate N(6)-methyladenosine in single-stranded DNA (in vitro) (PubMed:24616105). Required for the late meiotic and haploid phases of spermatogenesis by mediating m6A demethylation in spermatocytes and round spermatids: m6A demethylation of target transcripts is required for correct splicing and the production of longer 3'-UTR mRNAs in male germ cells (By similarity). Involved in paraspeckle assembly, a nuclear membraneless organelle, by undergoing liquid-liquid phase separation (PubMed:37369679, PubMed:37474102). Paraspeckle assembly is coupled with m6A demethylation of RNAs, such as NEAT1 non-coding RNA (PubMed:37474102). Also acts as a negative regulator of T-cell development: inhibits gamma-delta T-cell proliferation via demethylation of JAG1 and NOTCH2 transcripts (By similarity). Inhibits regulatory T-cell (Treg) recruitment by mediating demethylation and destabilization of CCL28 mRNAs (By similarity)", "gene_name": "ALKBH5", "glycan_count": 1, "glycosylation_sites": [], "id": "Q6P6C2", "name": "ALKBH5", "organism": "Homo sapiens", "uniprot_id": "Q6P6C2" }, { "function": "Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, and regulates their stability (PubMed:24284625, PubMed:26046440, PubMed:26318451, PubMed:32492408). M6A is a modification present at internal sites of mRNAs and some non-coding RNAs and plays a role in mRNA stability and processing (PubMed:22575960, PubMed:24284625, PubMed:25412658, PubMed:25412661, PubMed:32492408). Acts as a regulator of mRNA stability by promoting degradation of m6A-containing mRNAs via interaction with the CCR4-NOT and ribonuclease P/MRP complexes, depending on the context (PubMed:24284625, PubMed:26046440, PubMed:27558897, PubMed:30930054, PubMed:32492408). The YTHDF paralogs (YTHDF1, YTHDF2 and YTHDF3) share m6A-containing mRNAs targets and act redundantly to mediate mRNA degradation and cellular differentiation (PubMed:28106072, PubMed:32492408). M6A-containing mRNAs containing a binding site for RIDA/HRSP12 (5'-GGUUC-3') are preferentially degraded by endoribonucleolytic cleavage: cooperative binding of RIDA/HRSP12 and YTHDF2 to transcripts leads to recruitment of the ribonuclease P/MRP complex (PubMed:30930054). Other m6A-containing mRNAs undergo deadenylation via direct interaction between YTHDF2 and CNOT1, leading to recruitment of the CCR4-NOT and subsequent deadenylation of m6A-containing mRNAs (PubMed:27558897). Required maternally to regulate oocyte maturation: probably acts by binding to m6A-containing mRNAs, thereby regulating maternal transcript dosage during oocyte maturation, which is essential for the competence of oocytes to sustain early zygotic development (By similarity). Also required during spermatogenesis: regulates spermagonial adhesion by promoting degradation of m6A-containing transcripts coding for matrix metallopeptidases (By similarity). Also involved in hematopoietic stem cells specification by binding to m6A-containing mRNAs, leading to promote their degradation (PubMed:30065315). Also acts as a regulator of neural development by promoting m6A-dependent degradation of neural development-related mRNA targets (By similarity). Inhibits neural specification of induced pluripotent stem cells by binding to methylated neural-specific mRNAs and promoting their degradation, thereby restraining neural differentiation (PubMed:32169943). Regulates circadian regulation of hepatic lipid metabolism: acts by promoting m6A-dependent degradation of PPARA transcripts (PubMed:30428350). Regulates the innate immune response to infection by inhibiting the type I interferon response: acts by binding to m6A-containing IFNB transcripts and promoting their degradation (PubMed:30559377). May also act as a promoter of cap-independent mRNA translation following heat shock stress: upon stress, relocalizes to the nucleus and specifically binds mRNAs with some m6A methylation mark at their 5'-UTR, protecting demethylation of mRNAs by FTO, thereby promoting cap-independent mRNA translation (PubMed:26458103). Regulates mitotic entry by promoting the phase-specific m6A-dependent degradation of WEE1 transcripts (PubMed:32267835). Promotes formation of phase-separated membraneless compartments, such as P-bodies or stress granules, by undergoing liquid-liquid phase separation upon binding to mRNAs containing multiple m6A-modified residues: polymethylated mRNAs act as a multivalent scaffold for the binding of YTHDF proteins, juxtaposing their disordered regions and thereby leading to phase separation (PubMed:31292544, PubMed:31388144, PubMed:31642031, PubMed:32451507). The resulting mRNA-YTHDF complexes then partition into different endogenous phase-separated membraneless compartments, such as P-bodies, stress granules or neuronal RNA granules (PubMed:31292544). May also recognize and bind RNAs modified by C5-methylcytosine (m5C) and act as a regulator of rRNA processing (PubMed:31815440)", "gene_name": "YTHDF2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y5A9", "name": "YTHDF2", "organism": "Homo sapiens", "uniprot_id": "Q9Y5A9" }, { "function": "Heterogeneous nuclear ribonucleoprotein (hnRNP) that associates with nascent pre-mRNAs, packaging them into hnRNP particles. The hnRNP particle arrangement on nascent hnRNA is non-random and sequence-dependent and serves to condense and stabilize the transcripts and minimize tangling and knotting. Packaging plays a role in various processes such as transcription, pre-mRNA processing, RNA nuclear export, subcellular location, mRNA translation and stability of mature mRNAs (PubMed:19099192). Forms hnRNP particles with at least 20 other different hnRNP and heterogeneous nuclear RNA in the nucleus. Involved in transport of specific mRNAs to the cytoplasm in oligodendrocytes and neurons: acts by specifically recognizing and binding the A2RE (21 nucleotide hnRNP A2 response element) or the A2RE11 (derivative 11 nucleotide oligonucleotide) sequence motifs present on some mRNAs, and promotes their transport to the cytoplasm (PubMed:10567417). Specifically binds single-stranded telomeric DNA sequences, protecting telomeric DNA repeat against endonuclease digestion (By similarity). Also binds other RNA molecules, such as primary miRNA (pri-miRNAs): acts as a nuclear 'reader' of the N6-methyladenosine (m6A) mark by specifically recognizing and binding a subset of nuclear m6A-containing pri-miRNAs. Binding to m6A-containing pri-miRNAs promotes pri-miRNA processing by enhancing binding of DGCR8 to pri-miRNA transcripts (PubMed:26321680). Involved in miRNA sorting into exosomes following sumoylation, possibly by binding (m6A)-containing pre-miRNAs (PubMed:24356509). Acts as a regulator of efficiency of mRNA splicing, possibly by binding to m6A-containing pre-mRNAs (PubMed:26321680). Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (PubMed:20010808). Also plays a role in the activation of the innate immune response (PubMed:31320558). Mechanistically, senses the presence of viral DNA in the nucleus, homodimerizes and is demethylated by JMJD6 (PubMed:31320558). In turn, translocates to the cytoplasm where it activates the TBK1-IRF3 pathway, leading to interferon alpha/beta production (PubMed:31320558)", "gene_name": "HNRNPA2B1", "glycan_count": 2, "glycosylation_sites": [], "id": "P22626", "name": "HNRNPA2B1", "organism": "Homo sapiens", "uniprot_id": "P22626" }, { "function": "The METTL3-METTL14 heterodimer forms a N6-methyltransferase complex that methylates adenosine residues at the N(6) position of some mRNAs and regulates the circadian clock, differentiation of embryonic stem cells and cortical neurogenesis (PubMed:24316715, PubMed:24407421, PubMed:25719671, PubMed:27281194, PubMed:27373337, PubMed:29348140). In the heterodimer formed with METTL3, METTL14 constitutes the RNA-binding scaffold that recognizes the substrate rather than the catalytic core (PubMed:27281194, PubMed:27373337, PubMed:27627798, PubMed:29348140). N6-methyladenosine (m6A), which takes place at the 5'-[AG]GAC-3' consensus sites of some mRNAs, plays a role in mRNA stability and processing (PubMed:24316715, PubMed:24407421, PubMed:25719671). M6A acts as a key regulator of mRNA stability by promoting mRNA destabilization and degradation (By similarity). In embryonic stem cells (ESCs), m6A methylation of mRNAs encoding key naive pluripotency-promoting transcripts results in transcript destabilization (By similarity). M6A regulates spermatogonial differentiation and meiosis and is essential for male fertility and spermatogenesis (By similarity). M6A also regulates cortical neurogenesis: m6A methylation of transcripts related to transcription factors, neural stem cells, the cell cycle and neuronal differentiation during brain development promotes their destabilization and decay, promoting differentiation of radial glial cells (By similarity)", "gene_name": "METTL14", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9HCE5", "name": "METTL14", "organism": "Homo sapiens", "uniprot_id": "Q9HCE5" }, { "function": "Receptor for the MIP-3-beta chemokine. Probable mediator of EBV effects on B-lymphocytes or of normal lymphocyte functions", "gene_name": "CCR7", "glycan_count": 0, "glycosylation_sites": [ { "position": 36, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P32248", "name": "CCR7", "organism": "Homo sapiens", "uniprot_id": "P32248" }, { "function": "Cytokine that induces the release of T-cell-attracting chemokines from monocytes and, in particular, enhances the maturation of CD11c(+) dendritic cells. Can induce allergic inflammation by directly activating mast cells", "gene_name": "TSLP", "glycan_count": 0, "glycosylation_sites": [ { "position": 64, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 119, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q969D9", "name": "TSLP", "organism": "Homo sapiens", "uniprot_id": "Q969D9" }, { "function": "Precursor of a pore-forming protein that acts as a downstream mediator of granzyme-mediated cell death (PubMed:32299851). This form constitutes the precursor of the pore-forming protein: upon cleavage, the released N-terminal moiety (Gasdermin-B, N-terminal) binds to membranes and forms pores, triggering pyroptosis (PubMed:32299851). Also acts as a regulator of epithelial cell repair independently of programmed cell death: translocates to the plasma membrane and promotes epithelial maintenance and repair by regulating PTK2/FAK-mediated phosphorylation of PDGFA (PubMed:35021065)", "gene_name": "GSDMB", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8TAX9", "name": "GSDMB", "organism": "Homo sapiens", "uniprot_id": "Q8TAX9" }, { "function": "Maintains low levels of EIF2S1 phosphorylation in unstressed cells by promoting its dephosphorylation by PP1", "gene_name": "PPP1R15B", "glycan_count": 1, "glycosylation_sites": [], "id": "Q5SWA1", "name": "PPP1R11", "organism": "Homo sapiens", "uniprot_id": "Q5SWA1" }, { "function": "Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans", "gene_name": "GLB1", "glycan_count": 82, "glycosylation_sites": [ { "position": 26, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 247, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 464, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 498, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 542, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 545, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 555, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P16278", "name": "GLB1", "organism": "Homo sapiens", "uniprot_id": "P16278" }, { "function": "Glycosyltransferase that catalyzes the transfer of GlcNAc from UDP-GlcNAc to the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans through a beta1-4 linkage and participates in the production of tri- and tetra-antennary N-linked sugar chains (PubMed:10372966, PubMed:17006639). Prefers complex-type N-glycans over hybrid-types (PubMed:17006639). Has lower affinities for donors or acceptors than MGAT4A, suggesting that, under physiological conditions, it is not the main contributor in N-glycan biosynthesis (PubMed:17006639)", "gene_name": "MGAT4B", "glycan_count": 3, "glycosylation_sites": [ { "position": 87, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 103, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UQ53", "name": "LAMP3", "organism": "Homo sapiens", "uniprot_id": "Q9UQ53" }, { "function": "Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Ladsin exerts cell-scattering activity toward a wide variety of cells, including epithelial, endothelial, and fibroblastic cells", "gene_name": "LAMC2", "glycan_count": 7, "glycosylation_sites": [ { "position": 342, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 362, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 803, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 805, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 942, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1033, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13753", "name": "LAMC2", "organism": "Homo sapiens", "uniprot_id": "Q13753" }, { "function": "Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping protein. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments. Plays a role in actin-based mobility of Listeria monocytogenes in host cells. Regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation", "gene_name": "VASP", "glycan_count": 2, "glycosylation_sites": [], "id": "P50552", "name": "VASP", "organism": "Homo sapiens", "uniprot_id": "P50552" }, { "function": "G-protein coupled receptor for endogenous cannabinoids (eCBs), including N-arachidonoylethanolamide (also called anandamide or AEA) and 2-arachidonoylglycerol (2-AG), as well as phytocannabinoids, such as delta(9)-tetrahydrocannabinol (THC) (PubMed:15620723, PubMed:27768894, PubMed:27851727). Mediates many cannabinoid-induced effects, acting, among others, on food intake, memory loss, gastrointestinal motility, catalepsy, ambulatory activity, anxiety, chronic pain. Signaling typically involves reduction in cyclic AMP (PubMed:1718258, PubMed:21895628, PubMed:27768894). In the hypothalamus, may have a dual effect on mitochondrial respiration depending upon the agonist dose and possibly upon the cell type. Increases respiration at low doses, while decreases respiration at high doses. At high doses, CNR1 signal transduction involves G-protein alpha-i protein activation and subsequent inhibition of mitochondrial soluble adenylate cyclase, decrease in cyclic AMP concentration, inhibition of protein kinase A (PKA)-dependent phosphorylation of specific subunits of the mitochondrial electron transport system, including NDUFS2. In the hypothalamus, inhibits leptin-induced reactive oxygen species (ROS) formation and mediates cannabinoid-induced increase in SREBF1 and FASN gene expression. In response to cannabinoids, drives the release of orexigenic beta-endorphin, but not that of melanocyte-stimulating hormone alpha/alpha-MSH, from hypothalamic POMC neurons, hence promoting food intake. In the hippocampus, regulates cellular respiration and energy production in response to cannabinoids. Involved in cannabinoid-dependent depolarization-induced suppression of inhibition (DSI), a process in which depolarization of CA1 postsynaptic pyramidal neurons mobilizes eCBs, which retrogradely activate presynaptic CB1 receptors, transiently decreasing GABAergic inhibitory neurotransmission. Also reduces excitatory synaptic transmission (By similarity). In superior cervical ganglions and cerebral vascular smooth muscle cells, inhibits voltage-gated Ca(2+) channels in a constitutive, as well as agonist-dependent manner (PubMed:17895407). In cerebral vascular smooth muscle cells, cannabinoid-induced inhibition of voltage-gated Ca(2+) channels leads to vasodilation and decreased vascular tone (By similarity). Induces leptin production in adipocytes and reduces LRP2-mediated leptin clearance in the kidney, hence participating in hyperleptinemia. In adipose tissue, CNR1 signaling leads to increased expression of SREBF1, ACACA and FASN genes (By similarity). In the liver, activation by endocannabinoids leads to increased de novo lipogenesis and reduced fatty acid catabolism, associated with increased expression of SREBF1/SREBP-1, GCK, ACACA, ACACB and FASN genes. May also affect de novo cholesterol synthesis and HDL-cholesteryl ether uptake. Peripherally modulates energy metabolism (By similarity). In high carbohydrate diet-induced obesity, may decrease the expression of mitochondrial dihydrolipoyl dehydrogenase/DLD in striated muscles, as well as that of selected glucose/ pyruvate metabolic enzymes, hence affecting energy expenditure through mitochondrial metabolism (By similarity). In response to cannabinoid anandamide, elicits a pro-inflammatory response in macrophages, which involves NLRP3 inflammasome activation and IL1B and IL18 secretion (By similarity). In macrophages infiltrating pancreatic islets, this process may participate in the progression of type-2 diabetes and associated loss of pancreatic beta-cells (PubMed:23955712)", "gene_name": "CNR1", "glycan_count": 0, "glycosylation_sites": [ { "position": 77, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 83, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P21554", "name": "Cannabinoid Type 1 Receptor (CB1R)", "organism": "Homo sapiens", "uniprot_id": "P21554" }, { "function": "Cyclic nucleotide phosphodiesterase with specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes (PubMed:1315035, PubMed:25961942, PubMed:8155697, PubMed:8695850). Also has activity toward cUMP (PubMed:27975297). Independently of its catalytic activity it is part of an E2/17beta-estradiol-induced pro-apoptotic signaling pathway. E2 stabilizes the PDE3A/SLFN12 complex in the cytosol, promoting the dephosphorylation of SLFN12 and activating its pro-apoptotic ribosomal RNA/rRNA ribonuclease activity. This apoptotic pathway might be relevant in tissues with high concentration of E2 and be for instance involved in placenta remodeling (PubMed:31420216, PubMed:34707099)", "gene_name": "PDE3A", "glycan_count": 1, "glycosylation_sites": [], "id": "Q14432", "name": "Glucagon-like Peptide-1 Receptor (GLP-1R)", "organism": "Homo sapiens", "uniprot_id": "Q14432" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8RGR9", "name": "IL-17", "organism": "Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355)", "uniprot_id": "Q8RGR9" }, { "function": "Stimulatory receptor expressed in activated or antigen-experienced T-cells that plays an important role in the immune response (PubMed:11343123). Upon binding to its ligand ICOSL expressed on antigen presenting cells (APCs), delivers costimulatory signals that enhances all basic T-cell responses to a foreign antigen, namely proliferation, secretion of lymphokines including IL10, up-regulation of molecules that mediate cell-cell interaction, and effective help for antibody secretion by B-cells (PubMed:10657606). Also acts as a costimulatory receptor critical for the differentiation of T follicular regulatory cells upon immune challenges such as viral infection (PubMed:36754569). Mechanistically, potentiates TCR-induced calcium flux by augmenting PLCG1 activation and actin remodeling (PubMed:27693916). In addition, activates PI3K signaling pathways independently of calcium flux (PubMed:19915142, PubMed:27693916). Essential both for efficient interaction between T and B-cells and for normal antibody responses to T-cell dependent antigens. Prevents the apoptosis of pre-activated T-cells. Plays a critical role in CD40-mediated class switching of immunoglobin isotypes (PubMed:11343122)", "gene_name": "Icos", "glycan_count": 0, "glycosylation_sites": [ { "position": 23, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 89, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 123, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9WVS0", "name": "T-bet", "organism": "Mus musculus", "uniprot_id": "Q9WVS0" }, { "function": "Transcriptional regulator which is important for the differentiation and maintenance of meso-diencephalic dopaminergic (mdDA) neurons during development. In addition to its importance during development, it also has roles in the long-term survival and maintenance of the mdDA neurons. Activates NR4A2/NURR1-mediated transcription of genes such as SLC6A3, SLC18A2, TH and DRD2 which are essential for development of mdDA neurons. Acts by decreasing the interaction of NR4A2/NURR1 with the corepressor NCOR2/SMRT which acts through histone deacetylases (HDACs) to keep promoters of NR4A2/NURR1 target genes in a repressed deacetylated state. Essential for the normal lens development and differentiation. Plays a critical role in the maintenance of mitotic activity of lens epithelial cells, fiber cell differentiation and in the control of the temporal and spatial activation of fiber cell-specific crystallins. Positively regulates FOXE3 expression and negatively regulates PROX1 in the anterior lens epithelium, preventing activation of CDKN1B/P27Kip1 and CDKN1C/P57Kip2 and thus maintains lens epithelial cells in cell cycle", "gene_name": "Pitx3", "glycan_count": 0, "glycosylation_sites": [], "id": "O35160", "name": "ABCC3", "organism": "Mus musculus", "uniprot_id": "O35160" }, { "function": "Plays a role in neurofilament network integrity. May be involved in modulating axonal architecture during development and in the adult. In vitro, increases the susceptibility of neurofilament-H to calcium-dependent proteases. May also function in modulating the keratin network in skin. Activates the MAPK and Elk-1 signal transduction pathway (By similarity)", "gene_name": "Sncg", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9Z0F7", "name": "CYP7A1", "organism": "Mus musculus", "uniprot_id": "Q9Z0F7" }, { "function": "P450 monooxygenase that plays a major role in cholesterol homeostasis in the brain. Primarily catalyzes the hydroxylation (with S stereochemistry) at C-24 of cholesterol side chain, triggering cholesterol diffusion out of neurons and its further degradation (PubMed:10377398, PubMed:14640697, PubMed:18621681, PubMed:25017465). By promoting constant cholesterol elimination in neurons, may activate the mevalonate pathway and coordinate the synthesis of new cholesterol and nonsterol isoprenoids involved in synaptic activity and learning (By similarity). Further hydroxylates cholesterol derivatives and hormone steroids on both the ring and side chain of these molecules, converting them into active oxysterols involved in lipid signaling and biosynthesis (PubMed:12077124, PubMed:14640697, PubMed:28190002). Acts as an epoxidase converting cholesta-5,24-dien-3beta-ol/desmosterol into (24S),25-epoxycholesterol, an abundant lipid ligand of nuclear NR1H2 and NR1H3 receptors shown to promote neurogenesis in developing brain (PubMed:25017465). May also catalyze the oxidative metabolism of xenobiotics, such as clotrimazole (PubMed:20667828)", "gene_name": "CYP46A1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y6A2", "name": "CYP7B1", "organism": "Homo sapiens", "uniprot_id": "Q9Y6A2" }, { "function": "UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to facilitate their inactivation and excretion from the body (PubMed:15231852, PubMed:21422672). Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds (PubMed:15231852, PubMed:21422672). Involved in the glucuronidation of arachidonic acid (AA) and AA-derived eicosanoids including 15-HETE and 20-HETE (PubMed:15231852). Conjugates small planar phenolic molecules such as 4-nitrophenol, 1-naphthol, and 4-methylumbelliferone. The bulky phenol 4-hydroxybiphenyl, androgens and estrogens are not substrates. 2-hydroxybiphenyl is an excellent substrate (By similarity). Involved in the glucuronidation of the phytochemical ferulic acid at the phenolic or the carboxylic acid group (PubMed:21422672)", "gene_name": "UGT1A6", "glycan_count": 2, "glycosylation_sites": [ { "position": 294, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 346, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P19224", "name": "UGT1A6", "organism": "Homo sapiens", "uniprot_id": "P19224" }, { "function": "Involved in pre-mRNA splicing process (PubMed:11991638, PubMed:12084575, PubMed:28076346, PubMed:28502770). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable)", "gene_name": "CRNKL1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9BZJ0", "name": "NKG2D", "organism": "Homo sapiens", "uniprot_id": "Q9BZJ0" }, { "function": "V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268)", "gene_name": "IGKV2-30", "glycan_count": 0, "glycosylation_sites": [], "id": "P06310", "name": "SPINK1", "organism": "Homo sapiens", "uniprot_id": "P06310" }, { "function": "Multi-functional cell surface receptor regulating cell adhesion in many diverse developmental processes, including neural tube and mammary gland formation, myogenesis and angiogenesis. Receptor for members of the BMP, netrin, and repulsive guidance molecule (RGM) families. Netrin-Neogenin interactions result in a chemoattractive axon guidance response and cell-cell adhesion, the interaction between NEO1/Neogenin and RGMa and RGMb induces a chemorepulsive response", "gene_name": "NEO1", "glycan_count": 28, "glycosylation_sites": [ { "position": 73, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 210, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 326, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 470, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 489, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 639, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 715, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 909, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q92859", "name": "ENTP6 (Ectonucleotide Pyrophosphatase/Phosphodiesterase Family Member 6)", "organism": "Homo sapiens", "uniprot_id": "Q92859" }, { "function": "Involved in cell branching and adhesion mediated by BCAR1-CRK-RAPGEF1 signaling and activation of RAP1", "gene_name": "CRK", "glycan_count": 2, "glycosylation_sites": [], "id": "P46108", "name": "CRK (Adapter molecule crk)", "organism": "Homo sapiens", "uniprot_id": "P46108" }, { "function": "Catalyzes the oxidative deamination of primary and some secondary amine such as neurotransmitters, with concomitant reduction of oxygen to hydrogen peroxide and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues (PubMed:18391214, PubMed:20493079, PubMed:24169519, PubMed:8316221). Preferentially oxidizes serotonin (PubMed:20493079, PubMed:24169519). Also catalyzes the oxidative deamination of kynuramine to 3-(2-aminophenyl)-3-oxopropanal that can spontaneously condense to 4-hydroxyquinoline (By similarity)", "gene_name": "MAOA", "glycan_count": 1, "glycosylation_sites": [], "id": "P21397", "name": "Monoamine oxidase A (MAOA)", "organism": "Homo sapiens", "uniprot_id": "P21397" }, { "function": "Transcription factor regulating the expression of cell cycle genes essential for DNA replication and mitosis (PubMed:19160488, PubMed:20360045). Plays a role in the control of cell proliferation (PubMed:19160488). Also plays a role in DNA break repair, participating in the DNA damage checkpoint response (PubMed:17101782). Promotes transcription of PHB2 (PubMed:33754036)", "gene_name": "FOXM1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q08050", "name": "CD36", "organism": "Homo sapiens", "uniprot_id": "Q08050" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q02750/Q9Y6R4", "name": "MEK1/2", "organism": "", "uniprot_id": "" }, { "function": "Synaptic adhesion molecule required for the formation of target-specific synapses. Required for formation of target-specific synapses at hippocampal mossy fiber synapses. Required for formation of mossy fiber filopodia, the synaptic structures connecting dentate granule and GABA neurons. Probably acts as a homophilic adhesion molecule that promotes trans-cellular interactions and stabilize mossy fiber filipodia contact and subsequent synapse formation. Required for the coalescence of vomeronasal sensory neuron axons. May be involved in the hematopoietic supportive capacity of stroma cells; the secreted extracellular domain is directly responsible for supporting hematopoietic stem cells", "gene_name": "KIRREL3", "glycan_count": 0, "glycosylation_sites": [ { "position": 167, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 253, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 324, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 498, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8IZU9", "name": "HEG1", "organism": "Homo sapiens", "uniprot_id": "Q8IZU9" }, { "function": "Catalyzes the production of spermine from spermidine and decarboxylated S-adenosylmethionine (dcSAM)", "gene_name": "SMS", "glycan_count": 1, "glycosylation_sites": [], "id": "P52788", "name": "SMS", "organism": "Homo sapiens", "uniprot_id": "P52788" }, { "function": "Transcriptional activator. Binds the consensus sequence 5'-DHWATTGAYTWWD-3' on a variety of gene promoters such as those of HNF3B and TTR. Important for liver genes transcription", "gene_name": "ONECUT1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UBC0", "name": "MYO1B", "organism": "Homo sapiens", "uniprot_id": "Q9UBC0" }, { "function": "Major constituent of messenger ribonucleoprotein particles (mRNPs). Involved in the regulation of the stability and/or translation of germ cell mRNAs. Binds to Y-box consensus promoter element. Binds to full-length mRNA with high affinity in a sequence-independent manner. Binds to short RNA sequences containing the consensus site 5'-UCCAUCA-3' with low affinity and limited sequence specificity. Its binding with maternal mRNAs is necessary for its cytoplasmic retention. May mark specific mRNAs (those transcribed from Y-box promoters) in the nucleus for cytoplasmic storage, thereby linking transcription and mRNA storage/translational delay (By similarity)", "gene_name": "YBX2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y2T7", "name": "YBX2", "organism": "Homo sapiens", "uniprot_id": "Q9Y2T7" }, { "function": "Acts as a transcriptional transactivator of TCEA1 elongation activity (By similarity). Acts as a transcriptional transactivator of ELL and ELL2 elongation activities. Potent inducer of apoptosis in prostatic and non-prostatic cell lines. Inhibits prostate tumor growth in vivo", "gene_name": "EAF2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q96CJ1", "name": "ERRFI1", "organism": "Homo sapiens", "uniprot_id": "Q96CJ1" }, { "function": "Plays a key role in the control of the eukaryotic cell cycle by modulating the centrosome cycle as well as mitotic onset; promotes G2-M transition via association with multiple interphase cyclins (PubMed:16407259, PubMed:16933150, PubMed:17459720, PubMed:18356527, PubMed:19509060, PubMed:19917720, PubMed:20171170, PubMed:20935635, PubMed:20937773, PubMed:21063390, PubMed:2188730, PubMed:23355470, PubMed:2344612, PubMed:23601106, PubMed:23602554, PubMed:25556658, PubMed:26829474, PubMed:27814491, PubMed:30139873, PubMed:30704899). Phosphorylates PARVA/actopaxin, APC, AMPH, APC, BARD1, Bcl-xL/BCL2L1, BRCA2, CALD1, CASP8, CDC7, CDC20, CDC25A, CDC25C, CC2D1A, CENPA, CSNK2 proteins/CKII, FZR1/CDH1, CDK7, CEBPB, CHAMP1, DMD/dystrophin, EEF1 proteins/EF-1, EZH2, KIF11/EG5, EGFR, FANCG, FOS, GFAP, GOLGA2/GM130, GRASP1, UBE2A/hHR6A, HIST1H1 proteins/histone H1, HMGA1, HIVEP3/KRC, KAT5, LMNA, LMNB, LBR, MKI67, LATS1, MAP1B, MAP4, MARCKS, MCM2, MCM4, MKLP1, MLST8, MYB, NEFH, NFIC, NPC/nuclear pore complex, PITPNM1/NIR2, NPM1, NCL, NUCKS1, NPM1/numatrin, ORC1, PRKAR2A, EEF1E1/p18, EIF3F/p47, p53/TP53, NONO/p54NRB, PAPOLA, PLEC/plectin, RB1, TPPP, UL40/R2, RAB4A, RAP1GAP, RBBP8/CtIP, RCC1, RPS6KB1/S6K1, KHDRBS1/SAM68, ESPL1, SKI, BIRC5/survivin, STIP1, TEX14, beta-tubulins, MAPT/TAU, NEDD1, VIM/vimentin, TK1, FOXO1, RUNX1/AML1, SAMHD1, SIRT2, CGAS and RUNX2 (PubMed:16407259, PubMed:16933150, PubMed:17459720, PubMed:18356527, PubMed:19202191, PubMed:19509060, PubMed:19917720, PubMed:20171170, PubMed:20935635, PubMed:20937773, PubMed:21063390, PubMed:2188730, PubMed:23355470, PubMed:2344612, PubMed:23601106, PubMed:23602554, PubMed:25012651, PubMed:25556658, PubMed:26829474, PubMed:27814491, PubMed:30704899, PubMed:32351706, PubMed:34741373). CDK1/CDC2-cyclin-B controls pronuclear union in interphase fertilized eggs (PubMed:18480403, PubMed:20360007). Essential for early stages of embryonic development (PubMed:18480403, PubMed:20360007). During G2 and early mitosis, CDC25A/B/C-mediated dephosphorylation activates CDK1/cyclin complexes which phosphorylate several substrates that trigger at least centrosome separation, Golgi dynamics, nuclear envelope breakdown and chromosome condensation (PubMed:18480403, PubMed:20360007, PubMed:2188730, PubMed:2344612, PubMed:30139873). Once chromosomes are condensed and aligned at the metaphase plate, CDK1 activity is switched off by WEE1- and PKMYT1-mediated phosphorylation to allow sister chromatid separation, chromosome decondensation, reformation of the nuclear envelope and cytokinesis (PubMed:18480403, PubMed:20360007). Phosphorylates KRT5 during prometaphase and metaphase (By similarity). Inactivated by PKR/EIF2AK2- and WEE1-mediated phosphorylation upon DNA damage to stop cell cycle and genome replication at the G2 checkpoint thus facilitating DNA repair (PubMed:20360007). Reactivated after successful DNA repair through WIP1-dependent signaling leading to CDC25A/B/C-mediated dephosphorylation and restoring cell cycle progression (PubMed:20395957). Catalyzes lamin (LMNA, LMNB1 and LMNB2) phosphorylation at the onset of mitosis, promoting nuclear envelope breakdown (PubMed:2188730, PubMed:2344612, PubMed:37788673). In proliferating cells, CDK1-mediated FOXO1 phosphorylation at the G2-M phase represses FOXO1 interaction with 14-3-3 proteins and thereby promotes FOXO1 nuclear accumulation and transcription factor activity, leading to cell death of postmitotic neurons (PubMed:18356527). The phosphorylation of beta-tubulins regulates microtubule dynamics during mitosis (PubMed:16371510). NEDD1 phosphorylation promotes PLK1-mediated NEDD1 phosphorylation and subsequent targeting of the gamma-tubulin ring complex (gTuRC) to the centrosome, an important step for spindle formation (PubMed:19509060). In addition, CC2D1A phosphorylation regulates CC2D1A spindle pole localization and association with SCC1/RAD21 and centriole cohesion during mitosis (PubMed:20171170). The phosphorylation of Bcl-xL/BCL2L1 after prolongated G2 arrest upon DNA damage triggers apoptosis (PubMed:19917720). In contrast, CASP8 phosphorylation during mitosis prevents its activation by proteolysis and subsequent apoptosis (PubMed:20937773). This phosphorylation occurs in cancer cell lines, as well as in primary breast tissues and lymphocytes (PubMed:20937773). EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing (PubMed:20935635). CALD1 phosphorylation promotes Schwann cell migration during peripheral nerve regeneration (By similarity). CDK1-cyclin-B complex phosphorylates NCKAP5L and mediates its dissociation from centrosomes during mitosis (PubMed:26549230). Regulates the amplitude of the cyclic expression of the core clock gene BMAL1 by phosphorylating its transcriptional repressor NR1D1, and this phosphorylation is necessary for SCF(FBXW7)-mediated ubiquitination and proteasomal degradation of NR1D1 (PubMed:27238018). Phosphorylates EML3 at 'Thr-881' which is essential for its interaction with HAUS augmin-like complex and TUBG1 (PubMed:30723163). Phosphorylates CGAS during mitosis, leading to its inhibition, thereby preventing CGAS activation by self DNA during mitosis (PubMed:32351706). Phosphorylates SKA3 on multiple sites during mitosis which promotes SKA3 binding to the NDC80 complex and anchoring of the SKA complex to kinetochores, to enable stable attachment of mitotic spindle microtubules to kinetochores (PubMed:28479321, PubMed:31804178, PubMed:32491969)", "gene_name": "CDK1", "glycan_count": 1, "glycosylation_sites": [], "id": "P06493", "name": "CDK1", "organism": "Homo sapiens", "uniprot_id": "P06493" }, { "function": "Non-selective ion channel permeable to monovalent and divalent cations, including Na(+), K(+), and Ca(2+), with higher permeability for Ca(2+). Activated by multiple factors, such as temperature, voltage, pressure, and changes in osmolality. Activated by cool temperatures (<23-28 degrees Celsius) and by chemical ligands evoking a sensation of coolness, such as menthol and icilin therefore plays a central role in the detection of environmental cold temperatures (PubMed:15306801, PubMed:15852009, PubMed:16174775, PubMed:25559186, PubMed:37857704). TRPM8 is a voltage-dependent channel; its activation by cold or chemical ligands shifts its voltage thresholds towards physiological membrane potentials, leading to the opening of the channel (PubMed:15306801). In addition to its critical role in temperature sensing, regulates basal tear secretion by sensing evaporation-induced cooling and changes in osmolality (By similarity). May plays a role in prostate cancer cell migration (PubMed:16174775, PubMed:25559186)", "gene_name": "TRPM8", "glycan_count": 1, "glycosylation_sites": [ { "position": 934, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "Q7Z2W7", "name": "TRPM8", "organism": "Homo sapiens", "uniprot_id": "Q7Z2W7" }, { "function": "Catalyzes the oxidative deamination of primary amines to the corresponding aldehydes with the concomitant production of hydrogen peroxide and ammonia (PubMed:19588076, PubMed:24304424, PubMed:9653080). Has a preference for the primary monoamines methylamine and benzylamine (PubMed:19588076, PubMed:9653080). Could also act on 2-phenylethylamine but much less efficiently (PubMed:19588076). At endothelial cells surface can also function as a cell adhesion protein that participates in lymphocyte extravasation and recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin-independent fashion (PubMed:9254657, PubMed:9653080)", "gene_name": "AOC3", "glycan_count": 47, "glycosylation_sites": [ { "position": 43, "type": "O-linked (GalNAc...) serine" }, { "position": 137, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 212, "type": "O-linked (GalNAc...) threonine" }, { "position": 232, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 294, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 592, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 618, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 666, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 679, "type": "O-linked (GlcNAc) threonine" } ], "id": "Q16853", "name": "Vascular adhesion protein-1 (VAP-1)", "organism": "Homo sapiens", "uniprot_id": "Q16853" }, { "function": "Binds to the Fc region of immunoglobulins alpha. Mediates several functions including cytokine production", "gene_name": "FCAR", "glycan_count": 1, "glycosylation_sites": [ { "position": 65, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 79, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 141, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 177, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 186, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P24071", "name": "Fc\u03b1RI (CD89)", "organism": "Homo sapiens", "uniprot_id": "P24071" }, { "function": "Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including TULP1 or GAS6. Regulates many physiological processes including cell survival, migration and differentiation. Ligand binding at the cell surface induces dimerization and autophosphorylation of TYRO3 on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with PIK3R1 and thereby enhances PI3-kinase activity. Activates the AKT survival pathway, including nuclear translocation of NF-kappa-B and up-regulation of transcription of NF-kappa-B-regulated genes. TYRO3 signaling plays a role in various processes such as neuron protection from excitotoxic injury, platelet aggregation and cytoskeleton reorganization. Also plays an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response by activating STAT1, which selectively induces production of suppressors of cytokine signaling SOCS1 and SOCS3", "gene_name": "TYRO3", "glycan_count": 13, "glycosylation_sites": [ { "position": 63, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 191, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 230, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 240, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 293, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 366, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 380, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q06418", "name": "TYRO3", "organism": "Homo sapiens", "uniprot_id": "Q06418" }, { "function": "Probable chaperone required for the generation of 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins. Probably acts as a specific molecular chaperone assisting the folding/stability of core 1 beta-3-galactosyltransferase (C1GALT1)", "gene_name": "C1GALT1C1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q96EU7", "name": "C1GALT1C1", "organism": "Homo sapiens", "uniprot_id": "Q96EU7" }, { "function": "Functions in post-Golgi recycling pathways. Acts as a recycling carrier to the cell surface", "gene_name": "SCAMP1", "glycan_count": 2, "glycosylation_sites": [], "id": "O15126", "name": "SCAMP1", "organism": "Homo sapiens", "uniprot_id": "O15126" }, { "function": "Substrate-binding subunit of the Rab geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab proteins and presents the substrate peptide to the catalytic component B composed of RABGGTA and RABGGTB, and remains bound to it after the geranylgeranyl transfer reaction. The component A is thought to be regenerated by transferring its prenylated Rab back to the donor membrane. Besides, a pre-formed complex consisting of CHM and the Rab GGTase dimer (RGGT or component B) can bind to and prenylate Rab proteins; this alternative pathway is proposed to be the predominant pathway for Rab protein geranylgeranylation", "gene_name": "CHM", "glycan_count": 1, "glycosylation_sites": [], "id": "P24386", "name": "CHM", "organism": "Homo sapiens", "uniprot_id": "P24386" }, { "function": "Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Required for the stability of the SWI/SNF chromatin remodeling complex SWI/SNF-B (PBAF). Acts as a negative regulator of cell proliferation", "gene_name": "PBRM1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q86U86", "name": "PBRM1", "organism": "Homo sapiens", "uniprot_id": "Q86U86" }, { "function": "Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36'. May also recognize and bind to some phosphorylated proteins and promote their ubiquitination and degradation. Required to maintain the heterochromatic state. Associates with centromeres and represses transcription of small non-coding RNAs that are encoded by the clusters of satellite repeats at the centromere. Required to sustain centromeric integrity and genomic stability, particularly during mitosis. Regulates circadian gene expression by repressing the transcriptional activator activity of CLOCK-BMAL1 heterodimer and RORA in a catalytically-independent manner (PubMed:26037310)", "gene_name": "KDM2A", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y2K7", "name": "BRD1", "organism": "Homo sapiens", "uniprot_id": "Q9Y2K7" }, { "function": "Implicated in nucleolar organization, ribosome biogenesis, protein synthesis and cytoplasmic dsRNA sensing (By similarity) (PubMed:21930779, PubMed:23871209, PubMed:26100019). Stimulates RNA polymerase I transcription of the 47S precursor rRNA. Associates with ribosomal DNA (rDNA) loci where it is involved in POLR1A recruitment (PubMed:21930779). In the cytoplasm, promotes elongation-competent 80S ribosome assembly at the late stage of mRNA translation initiation (PubMed:26100019). Senses cytosolic dsRNA mediating NLRP3 inflammasome formation in macrophages and type I interferon production in myeloid dendritic cells (PubMed:23871209). Required for NLRP3 activation induced by viral dsRNA and bacterial RNA (PubMed:23871209). In dendritic cells, required for induction of type I interferon production induced by cytoplasmic dsRNA via the activation of MAPK and NF-kappa-B signaling pathways (By similarity)", "gene_name": "DHX33", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H6R0", "name": "PAK1IP1", "organism": "Homo sapiens", "uniprot_id": "Q9H6R0" }, { "function": "Key functional receptor for CCL2 but can also bind CCL7, and CCL12 (PubMed:23408426, PubMed:38157855, PubMed:8048929, PubMed:8146186). Also transduces signaling mediated by CCL13 (PubMed:38157855). Its binding with CCL2 on monocytes and macrophages mediates chemotaxis and migration induction through the activation of the PI3K cascade, the small G protein Rac and lamellipodium protrusion (PubMed:38157855). Also acts as a receptor for the beta-defensin DEFB106A/DEFB106B (PubMed:23938203). Regulates the expression of T-cell inflammatory cytokines and T-cell differentiation, promoting the differentiation of T-cells into T-helper 17 cells (Th17) during inflammation (By similarity). Facilitates the export of mature thymocytes by enhancing directional movement of thymocytes to sphingosine-1-phosphate stimulation and up-regulation of S1P1R expression; signals through the JAK-STAT pathway to regulate FOXO1 activity leading to an increased expression of S1P1R (By similarity). Plays an important role in mediating peripheral nerve injury-induced neuropathic pain (By similarity). Increases NMDA-mediated synaptic transmission in both dopamine D1 and D2 receptor-containing neurons, which may be caused by MAPK/ERK-dependent phosphorylation of GRIN2B/NMDAR2B (By similarity). Mediates the recruitment of macrophages and monocytes to the injury site following brain injury (By similarity)", "gene_name": "CCR2", "glycan_count": 0, "glycosylation_sites": [ { "position": 14, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P41597", "name": "C-C chemokine receptor type 2 (CCR2)", "organism": "Homo sapiens", "uniprot_id": "P41597" }, { "function": "Envelope glycoprotein that forms spikes at the surface of virion envelope. Essential for the initial attachment to heparan sulfate moieties of the host cell surface proteoglycans. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell. Following initial binding to its host receptors, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May be involved in the fusion between the virion envelope and the outer nuclear membrane during virion egress", "gene_name": "gB", "glycan_count": 0, "glycosylation_sites": [ { "position": 76, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 163, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 290, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 329, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 348, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 395, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 436, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 563, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 629, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P03188", "name": "EBV Viral Capsid Antigen (VCA)", "organism": "Epstein-Barr virus (strain B95-8)", "uniprot_id": "P03188" }, { "function": "Lipoprotein-associated calcium-independent phospholipase A2 involved in phospholipid catabolism during inflammatory and oxidative stress response (PubMed:10066756, PubMed:18434304). At the lipid-aqueous interface, hydrolyzes the ester bond of fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) (PubMed:10066756, PubMed:18434304). Specifically targets phospholipids with a short-chain fatty acyl group at sn-2 position. Can hydrolyze phospholipids with long fatty acyl chains, only if they carry oxidized functional groups (By similarity). Hydrolyzes and inactivates platelet-activating factor (PAF, 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine), a potent pro-inflammatory signaling lipid that acts through PTAFR on various innate immune cells (PubMed:10066756, PubMed:18434304). Hydrolyzes oxidatively truncated phospholipids carrying an aldehyde group at omega position, preventing their accumulation in lipoprotein particles and uncontrolled pro-inflammatory effects (By similarity). As part of high-density lipoprotein (HDL) particles, can hydrolyze phospholipids having long-chain fatty acyl hydroperoxides at sn-2 position and protect against potential accumulation of these oxylipins in the vascular wall (By similarity). Catalyzes the release from membrane phospholipids of F2-isoprostanes, lipid biomarkers of cellular oxidative damage (By similarity)", "gene_name": "Pla2g7", "glycan_count": 1, "glycosylation_sites": [ { "position": 59, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 75, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 199, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q60963", "name": "Bax", "organism": "Mus musculus", "uniprot_id": "Q60963" }, { "function": "Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively (PubMed:19903941). Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate (PubMed:19903941). Modulates the organization and assembly of the cytoskeleton (By similarity). Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules (By similarity). Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes (PubMed:23071094). Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation (PubMed:23071094). Also plays a role in innate immunity by promoting TNF-induced NF-kappa-B activation and type I interferon production, via interaction with TRAF2 and TRAF3, respectively (By similarity). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity)", "gene_name": "Gapdh", "glycan_count": 1, "glycosylation_sites": [], "id": "P16858", "name": "GAPDH", "organism": "Mus musculus", "uniprot_id": "P16858" }, { "function": "Lipid transferase specifically expressed in white adipose tissue, which promotes unilocular lipid droplet formation by mediating lipid droplet fusion (PubMed:18334488, PubMed:19843876, PubMed:20049731, PubMed:23399566, PubMed:30361435). Lipid droplet fusion promotes their enlargement, restricting lipolysis and favoring lipid storage (PubMed:18334488, PubMed:19843876, PubMed:20049731, PubMed:23399566). Localizes on the lipid droplet surface, at focal contact sites between lipid droplets, and mediates atypical lipid droplet fusion by undergoing liquid-liquid phase separation (LLPS) and promoting directional net neutral lipid transfer from the smaller to larger lipid droplets (PubMed:18334488, PubMed:19843876, PubMed:20049731, PubMed:23399566). The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair (PubMed:18334488, PubMed:19843876, PubMed:20049731, PubMed:23399566). Its role in neutral lipid transfer and lipid droplet enlargement is activated by the interaction with PLIN1 (PubMed:23399566). May also act as a CEBPB coactivator in the white adipose tissue to control the expression of a subset of CEBPB downstream target genes, including SOCS1, SOCS3, TGFB1, TGFBR1, ID2 and XDH (By similarity). When overexpressed in preadipocytes, induces apoptosis or increases cell susceptibility to apoptosis induced by serum deprivation or TGFB treatment (PubMed:12429024)", "gene_name": "CIDEC", "glycan_count": 0, "glycosylation_sites": [], "id": "Q96AQ7", "name": "CIDEC", "organism": "Homo sapiens", "uniprot_id": "Q96AQ7" }, { "function": "Lipase with broad substrate specificity, catalyzing the hydrolysis of triacylglycerols (TAGs), diacylglycerols (DAGs), monoacylglycerols (MAGs), cholesteryl esters and retinyl esters (PubMed:15716583, PubMed:15955102, PubMed:19800417, PubMed:8812477). Shows a preferential hydrolysis of DAGs over TAGs and MAGs and preferentially hydrolyzes the fatty acid (FA) esters at the sn-3 position of the glycerol backbone in DAGs (PubMed:19800417). Preferentially hydrolyzes FA esters at the sn-1 and sn-2 positions of the glycerol backbone in TAGs (By similarity). Catalyzes the hydrolysis of 2-arachidonoylglycerol, an endocannabinoid and of 2-acetyl monoalkylglycerol ether, the penultimate precursor of the pathway for de novo synthesis of platelet-activating factor (By similarity). In adipose tissue and heart, it primarily hydrolyzes stored triglycerides to free fatty acids, while in steroidogenic tissues, it principally converts cholesteryl esters to free cholesterol for steroid hormone production (By similarity)", "gene_name": "LIPE", "glycan_count": 0, "glycosylation_sites": [], "id": "Q05469", "name": "Hormone-sensitive lipase (LIPE)", "organism": "Homo sapiens", "uniprot_id": "Q05469" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P05556/P02511", "name": "\u03b1v\u03b23 Integrin", "organism": "", "uniprot_id": "" }, { "function": "Receptor for TNFSF13B/BLyS/BAFF and TNFSF13/APRIL. Promotes B-cell survival and plays a role in the regulation of humoral immunity. Activates NF-kappa-B and JNK", "gene_name": "TNFRSF17", "glycan_count": 13, "glycosylation_sites": [], "id": "Q02223", "name": "BCMA (B-cell maturation antigen)", "organism": "Homo sapiens", "uniprot_id": "Q02223" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NZD0-2", "name": "Claudin 18.2", "organism": "", "uniprot_id": "" }, { "function": "Required for Ca(2+) flux in immune cells and plays a role in T-cell proliferation and in T-cell and neutrophil migration (By similarity). Involved in endoplasmic reticulum-associated degradation (ERAD) of soluble glycosylated proteins (PubMed:22016385). Required for palmitoylation and cell surface expression of CD36 and involved in macrophage uptake of low-density lipoprotein and in foam cell formation (By similarity). Together with ZDHHC6, required for palmitoylation of ITPR1 in immune cells, leading to regulate ITPR1 stability and function (PubMed:25368151). Plays a role in protection of cells from ER stress-induced apoptosis (PubMed:20692228). Protects cells from oxidative stress when overexpressed in cardiomyocytes (PubMed:16962588)", "gene_name": "SELENOK", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y6D0", "name": "SGLT2 (Sodium-glucose co-transporter 2)", "organism": "Homo sapiens", "uniprot_id": "Q9Y6D0" }, { "function": "Part of the TCR-CD3 complex present on T-lymphocyte cell surface that plays an essential role in adaptive immune response. When antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transmitted across the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3 chains contain immunoreceptor tyrosine-based activation motifs (ITAMs) in their cytoplasmic domain. Upon TCR engagement, these motifs become phosphorylated by Src family protein tyrosine kinases LCK and FYN, resulting in the activation of downstream signaling pathways (PubMed:2470098). In addition to this role of signal transduction in T-cell activation, CD3G plays an essential role in the dynamic regulation of TCR expression at the cell surface (PubMed:8187769). Indeed, constitutive TCR cycling is dependent on the di-leucine-based (diL) receptor-sorting motif present in CD3G", "gene_name": "CD3G", "glycan_count": 0, "glycosylation_sites": [ { "position": 52, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 92, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P09693", "name": "CD3G", "organism": "Homo sapiens", "uniprot_id": "P09693" }, { "function": "Receptor for class I MHC antigens. Recognizes a broad spectrum of HLA-A, HLA-B, HLA-C, HLA-G and HLA-F alleles (PubMed:11169396, PubMed:12853576, PubMed:16455647, PubMed:20448110, PubMed:27859042). Involved in the down-regulation of the immune response and the development of tolerance. Recognizes HLA-G in complex with B2M/beta-2 microglobulin and a nonamer self-peptide (peptide-bound HLA-G-B2M) triggering differentiation of type 1 regulatory T cells and myeloid-derived suppressor cells, both of which actively maintain maternal-fetal tolerance (PubMed:16455647, PubMed:20448110, PubMed:27859042). Competes with CD8A for binding to class I MHC antigens. Inhibits FCGR1A-mediated phosphorylation of cellular proteins and mobilization of intracellular calcium ions (PubMed:11875462, PubMed:12853576, PubMed:9548455, PubMed:9842885)", "gene_name": "LILRB2", "glycan_count": 0, "glycosylation_sites": [ { "position": 280, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 301, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 340, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8N423", "name": "LILRB4", "organism": "Homo sapiens", "uniprot_id": "Q8N423" }, { "function": "Structural component of specialized membrane microdomains known as tetraspanin-enriched microdomains (TERMs), which act as platforms for receptor clustering and signaling. Participates thereby in diverse biological functions such as cell signal transduction, adhesion, migration and protein trafficking (PubMed:30066932, PubMed:30291375). Regulates neuronal differentiation in response to NGF by facilitating NGF-mediated activation of NTRK1/TRKA receptor tyrosine kinase and subsequent downstream signaling pathways (By similarity). Plays a role in the inhibition of TNFalpha-induced apoptosis. Mechanistically, inhibits the NF-kappa-B signaling pathway by blocking phosphorylation of CHUK (PubMed:30291375). Also promotes the stability of the thiamine transporter 1/SLC19A2 in intestinal epithelial cells leading to an increase of thiamine uptake process (PubMed:21836059)", "gene_name": "TSPAN1", "glycan_count": 74, "glycosylation_sites": [ { "position": 141, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 154, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 178, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 184, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O60635", "name": "TSPAN2", "organism": "Homo sapiens", "uniprot_id": "O60635" }, { "function": "Adapter protein which associates with tyrosine-phosphorylated growth factor receptors, such as KDR and PDGFRB, or their cellular substrates. Maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. Plays a role in the DNA damage response, not in the detection of the damage by ATM/ATR, but for efficient activation of downstream effectors, such as that of CHEK2. Plays a role in ELK1-dependent transcriptional activation in response to activated Ras signaling. Modulates the activation of EIF2AK2/PKR by dsRNA. May play a role in cell adhesion and migration through interaction with ephrin receptors", "gene_name": "NCK1", "glycan_count": 0, "glycosylation_sites": [], "id": "P16333", "name": "POU2F2", "organism": "Homo sapiens", "uniprot_id": "P16333" }, { "function": "Serine-threonine kinase which is a key regulator of TNF-mediated apoptosis, necroptosis and inflammatory pathways (PubMed:17703191, PubMed:24144979, PubMed:31827280, PubMed:31827281, PubMed:32657447, PubMed:35831301). Exhibits kinase activity-dependent functions that regulate cell death and kinase-independent scaffold functions regulating inflammatory signaling and cell survival (PubMed:11101870, PubMed:19524512, PubMed:19524513, PubMed:29440439, PubMed:30988283). Has kinase-independent scaffold functions: upon binding of TNF to TNFR1, RIPK1 is recruited to the TNF-R1 signaling complex (TNF-RSC also known as complex I) where it acts as a scaffold protein promoting cell survival, in part, by activating the canonical NF-kappa-B pathway (By similarity). Kinase activity is essential to regulate necroptosis and apoptosis, two parallel forms of cell death: upon activation of its protein kinase activity, regulates assembly of two death-inducing complexes, namely complex IIa (RIPK1-FADD-CASP8), which drives apoptosis, and the complex IIb (RIPK1-RIPK3-MLKL), which drives necroptosis (By similarity). RIPK1 is required to limit CASP8-dependent TNFR1-induced apoptosis (By similarity). In normal conditions, RIPK1 acts as an inhibitor of RIPK3-dependent necroptosis, a process mediated by RIPK3 component of complex IIb, which catalyzes phosphorylation of MLKL upon induction by ZBP1 (PubMed:19524512, PubMed:19524513, PubMed:29440439, PubMed:30988283). Inhibits RIPK3-mediated necroptosis via FADD-mediated recruitment of CASP8, which cleaves RIPK1 and limits TNF-induced necroptosis (PubMed:19524512, PubMed:19524513, PubMed:29440439, PubMed:30988283). Required to inhibit apoptosis and necroptosis during embryonic development: acts by preventing the interaction of TRADD with FADD thereby limiting aberrant activation of CASP8 (By similarity). In addition to apoptosis and necroptosis, also involved in inflammatory response by promoting transcriptional production of pro-inflammatory cytokines, such as interleukin-6 (IL6) (PubMed:31827280, PubMed:31827281). Phosphorylates RIPK3: RIPK1 and RIPK3 undergo reciprocal auto- and trans-phosphorylation (PubMed:19524513). Phosphorylates DAB2IP at 'Ser-728' in a TNF-alpha-dependent manner, and thereby activates the MAP3K5-JNK apoptotic cascade (PubMed:15310755, PubMed:17389591). Required for ZBP1-induced NF-kappa-B activation in response to DNA damage (By similarity)", "gene_name": "RIPK1", "glycan_count": 1, "glycosylation_sites": [ { "position": 603, "type": "(Microbial infection) N-beta-linked (GlcNAc) arginine" } ], "id": "Q13546", "name": "Receptor-interacting serine/threonine kinase 1 (RIPK1)", "organism": "Homo sapiens", "uniprot_id": "Q13546" }, { "function": "A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins (PubMed:10681376, PubMed:11555828, PubMed:12865317, PubMed:19965576, PubMed:9435160). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase) (PubMed:10681376, PubMed:11555828, PubMed:12865317, PubMed:19965576, PubMed:9435160). Catalyzes the hydroxylation of carbon-hydrogen bonds (PubMed:11555828, PubMed:12865317). Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2 (PubMed:11555828, PubMed:12865317). Metabolizes cholesterol toward 25-hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis (PubMed:21576599). May act as a major enzyme for all-trans retinoic acid biosynthesis in the liver. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid (PubMed:10681376). Primarily catalyzes stereoselective epoxidation of the last double bond of polyunsaturated fatty acids (PUFA), displaying a strong preference for the (R,S) stereoisomer (PubMed:19965576). Catalyzes bisallylic hydroxylation and omega-1 hydroxylation of PUFA (PubMed:9435160). May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent) (PubMed:21068195). Plays a role in the oxidative metabolism of xenobiotics. Catalyzes the N-hydroxylation of heterocyclic amines and the O-deethylation of phenacetin (PubMed:14725854). Metabolizes caffeine via N3-demethylation (Probable)", "gene_name": "CYP1A2", "glycan_count": 0, "glycosylation_sites": [ { "position": 69, "type": "O-linked (GlcNAc) serine" } ], "id": "P05177", "name": "Cytochrome P450 1A2 (CYP1A2)", "organism": "Homo sapiens", "uniprot_id": "P05177" }, { "function": "A cytochrome P450 monooxygenase involved in the metabolism of endocannabinoids and steroids (PubMed:12865317, PubMed:21289075). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the epoxidation of double bonds of arachidonoylethanolamide (anandamide) to 8,9-, 11,12-, and 14,15-epoxyeicosatrienoic acid ethanolamides (EpETrE-EAs), potentially modulating endocannabinoid system signaling (PubMed:21289075). Hydroxylates steroid hormones, including testosterone at C-16 and estrogens at C-2 (PubMed:12865317, PubMed:21289075). Plays a role in the oxidative metabolism of xenobiotics, including plant lipids and drugs (PubMed:11695850, PubMed:22909231). Acts as a 1,4-cineole 2-exo-monooxygenase (PubMed:11695850)", "gene_name": "CYP2B6", "glycan_count": 0, "glycosylation_sites": [], "id": "P20813", "name": "Cytochrome P450 2B6 (CYP2B6)", "organism": "Homo sapiens", "uniprot_id": "P20813" }, { "function": "A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids and steroids (PubMed:12865317, PubMed:15766564, PubMed:19965576, PubMed:21576599, PubMed:7574697, PubMed:9435160, PubMed:9866708). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase) (PubMed:12865317, PubMed:15766564, PubMed:19965576, PubMed:21576599, PubMed:7574697, PubMed:9435160, PubMed:9866708). Catalyzes the epoxidation of double bonds of polyunsaturated fatty acids (PUFA) (PubMed:15766564, PubMed:19965576, PubMed:7574697, PubMed:9866708). Catalyzes the hydroxylation of carbon-hydrogen bonds. Metabolizes cholesterol toward 25-hydroxycholesterol, a physiological regulator of cellular cholesterol homeostasis (PubMed:21576599). Exhibits low catalytic activity for the formation of catechol estrogens from 17beta-estradiol (E2) and estrone (E1), namely 2-hydroxy E1 and E2 (PubMed:12865317). Catalyzes bisallylic hydroxylation and hydroxylation with double-bond migration of polyunsaturated fatty acids (PUFA) (PubMed:9435160, PubMed:9866708). Also metabolizes plant monoterpenes such as limonene. Oxygenates (R)- and (S)-limonene to produce carveol and perillyl alcohol (PubMed:11950794). Contributes to the wide pharmacokinetics variability of the metabolism of drugs such as S-warfarin, diclofenac, phenytoin, tolbutamide and losartan (PubMed:25994031)", "gene_name": "CYP2C9", "glycan_count": 0, "glycosylation_sites": [], "id": "P11712", "name": "Cytochrome P450 2C9 (CYP2C9)", "organism": "Homo sapiens", "uniprot_id": "P11712" }, { "function": "A cytochrome P450 monooxygenase involved in primary bile acid biosynthesis. Catalyzes the 12alpha-hydroxylation of 7alpha-hydroxy-4-cholesten-3-one, an intermediate metabolite in cholic acid biosynthesis (PubMed:10051404). Controls biliary balance of cholic acid and chenodeoxycholic acid, ultimately regulating the intestinal absorption of dietary lipids (By similarity). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH--hemoprotein reductase) (By similarity)", "gene_name": "CYP8B1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UNU6", "name": "Cytochrome P450 7A1 (CYP7A1)", "organism": "Homo sapiens", "uniprot_id": "Q9UNU6" }, { "function": "GFAP, a class-III intermediate filament, is a cell-specific marker that, during the development of the central nervous system, distinguishes astrocytes from other glial cells", "gene_name": "Gfap", "glycan_count": 1, "glycosylation_sites": [], "id": "P47819", "name": "Glial fibrillary acidic protein (GFAP)", "organism": "Rattus norvegicus", "uniprot_id": "P47819" }, { "function": "Calcium-permeable, non-selective cation channel with an outward rectification. Seems to be regulated, at least in part, by IGF1, PDGF and neuropeptide head activator. May transduce physical stimuli in mast cells. Activated by temperatures higher than 52 degrees Celsius; is not activated by vanilloids and acidic pH", "gene_name": "TRPV2", "glycan_count": 0, "glycosylation_sites": [ { "position": 570, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y5S1", "name": "y+LAT1 (SLC7A7)", "organism": "Homo sapiens", "uniprot_id": "Q9Y5S1" }, { "function": "Serine/threonine protein kinase which activates checkpoint signaling upon double strand breaks (DSBs), apoptosis and genotoxic stresses such as ionizing ultraviolet A light (UVA), thereby acting as a DNA damage sensor (PubMed:10550055, PubMed:10839545, PubMed:10910365, PubMed:12556884, PubMed:14871926, PubMed:15064416, PubMed:15448695, PubMed:15456891, PubMed:15790808, PubMed:15916964, PubMed:17923702, PubMed:21757780, PubMed:24534091, PubMed:35076389, PubMed:9733514). Recognizes the substrate consensus sequence [ST]-Q (PubMed:10550055, PubMed:10839545, PubMed:10910365, PubMed:12556884, PubMed:14871926, PubMed:15448695, PubMed:15456891, PubMed:15916964, PubMed:17923702, PubMed:24534091, PubMed:9733514). Phosphorylates 'Ser-139' of histone variant H2AX at double strand breaks (DSBs), thereby regulating DNA damage response mechanism (By similarity). Also plays a role in pre-B cell allelic exclusion, a process leading to expression of a single immunoglobulin heavy chain allele to enforce clonality and monospecific recognition by the B-cell antigen receptor (BCR) expressed on individual B-lymphocytes. After the introduction of DNA breaks by the RAG complex on one immunoglobulin allele, acts by mediating a repositioning of the second allele to pericentromeric heterochromatin, preventing accessibility to the RAG complex and recombination of the second allele. Also involved in signal transduction and cell cycle control. May function as a tumor suppressor. Necessary for activation of ABL1 and SAPK. Phosphorylates DYRK2, CHEK2, p53/TP53, FBXW7, FANCD2, NFKBIA, BRCA1, CREBBP/CBP, RBBP8/CTIP, FBXO46, MRE11, nibrin (NBN), RAD50, RAD17, PELI1, TERF1, UFL1, RAD9, UBQLN4 and DCLRE1C (PubMed:10550055, PubMed:10766245, PubMed:10802669, PubMed:10839545, PubMed:10910365, PubMed:10973490, PubMed:11375976, PubMed:12086603, PubMed:15456891, PubMed:19965871, PubMed:21757780, PubMed:24534091, PubMed:26240375, PubMed:26774286, PubMed:30171069, PubMed:30612738, PubMed:30886146, PubMed:30952868, PubMed:38128537, PubMed:9733515, PubMed:9843217). May play a role in vesicle and/or protein transport. Could play a role in T-cell development, gonad and neurological function. Plays a role in replication-dependent histone mRNA degradation. Binds DNA ends. Phosphorylation of DYRK2 in nucleus in response to genotoxic stress prevents its MDM2-mediated ubiquitination and subsequent proteasome degradation (PubMed:19965871). Phosphorylates ATF2 which stimulates its function in DNA damage response (PubMed:15916964). Phosphorylates ERCC6 which is essential for its chromatin remodeling activity at DNA double-strand breaks (PubMed:29203878). Phosphorylates TTC5/STRAP at 'Ser-203' in the cytoplasm in response to DNA damage, which promotes TTC5/STRAP nuclear localization (PubMed:15448695). Also involved in pexophagy by mediating phosphorylation of PEX5: translocated to peroxisomes in response to reactive oxygen species (ROS), and catalyzes phosphorylation of PEX5, promoting PEX5 ubiquitination and induction of pexophagy (PubMed:26344566)", "gene_name": "ATM", "glycan_count": 2, "glycosylation_sites": [], "id": "Q13315", "name": "ATM", "organism": "Homo sapiens", "uniprot_id": "Q13315" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9U3Q0 (C. elegans)", "name": "FLR-2", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9U3P9 (C. elegans)", "name": "FSHR-1", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9U3N0 (C. elegans)", "name": "TIR-1/SARM1", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9U3P7 (C. elegans)", "name": "MOD-1", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9U3P8 (C. elegans)", "name": "METR-1", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9U3Q1 (C. elegans)", "name": "FLR-4", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9U3Q2 (C. elegans)", "name": "TPH-1", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9U3P6 (C. elegans)", "name": "PMK-1", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9U3P5 (C. elegans)", "name": "SEK-1", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9U3P4 (C. elegans)", "name": "NSY-1", "organism": "", "uniprot_id": "" }, { "function": "Involved in complement regulation. The dimerized forms have avidity for tissue-bound complement fragments and efficiently compete with the physiological complement inhibitor CFH. Can associate with lipoproteins and may play a role in lipid metabolism", "gene_name": "CFHR1", "glycan_count": 36, "glycosylation_sites": [ { "position": 126, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 194, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q03591", "name": "CFHR1", "organism": "Homo sapiens", "uniprot_id": "Q03591" }, { "function": "Involved in complement regulation. Can associate with lipoproteins and may play a role in lipid metabolism", "gene_name": "CFHR4", "glycan_count": 16, "glycosylation_sites": [ { "position": 127, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 186, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 206, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 374, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 433, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 453, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 557, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q92496", "name": "CFHR4", "organism": "Homo sapiens", "uniprot_id": "Q92496" }, { "function": "Monokine with inflammatory and chemokinetic properties. Binds to CCR1, CCR4 and CCR5. One of the major HIV-suppressive factors produced by CD8+ T-cells. Recombinant MIP-1-alpha induces a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV)", "gene_name": "CCL3", "glycan_count": 0, "glycosylation_sites": [], "id": "P10147", "name": "CCL3", "organism": "Homo sapiens", "uniprot_id": "P10147" }, { "function": "Transcriptional activator, essential for early embryonic development and survival of embryonic stem cells (ESCs) (By similarity). Supports cell growth and survival during early development by transcriptionally activating the expression of the translation initiation factor EIF3B, to sustain global translation (By similarity). Activates the transcription of FLNC (PubMed:36440963)", "gene_name": "PRDM10", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9NQV6", "name": "PEBP4", "organism": "Homo sapiens", "uniprot_id": "Q9NQV6" }, { "function": "Plasma membrane-associated small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses. Involved in epithelial cell polarization processes. Regulates the bipolar attachment of spindle microtubules to kinetochores before chromosome congression in metaphase (PubMed:15642749). Regulates cell migration (PubMed:17038317, PubMed:22843693). In neurons, plays a role in the extension and maintenance of the formation of filopodia, thin and actin-rich surface projections (PubMed:14978216). Required for DOCK10-mediated spine formation in Purkinje cells and hippocampal neurons. In podocytes, facilitates filopodia and podosomes formation upon DOCK11-activation (PubMed:33523862). Upon activation by CaMKII, modulates dendritic spine structural plasticity by relaying CaMKII transient activation to synapse-specific, long-term signaling (By similarity). Also plays a role in phagocytosis through organization of the F-actin cytoskeleton associated with forming phagocytic cups (PubMed:26465210). Upon activation by PLEKHG4B, involved in actin cytoskeletal remodeling during epithelial cell-cell junction formation (PubMed:33310911)", "gene_name": "CDC42", "glycan_count": 1, "glycosylation_sites": [ { "position": 32, "type": "(Microbial infection) O-linked (GlcNAc) tyrosine; by Photorhabdus PAU_02230; alternate" }, { "position": 35, "type": "(Microbial infection) O-alpha-linked (GlcNAc) threonine; by C.novyi toxin TcdA; alternate" }, { "position": 35, "type": "(Microbial infection) O-linked (Glc) threonine; by C.difficile toxins TcdA and TcdB; alternate" } ], "id": "P60953", "name": "CDC42", "organism": "Homo sapiens", "uniprot_id": "P60953" }, { "function": "Dephosphorylates specifically the 5' and 2'(3')-phosphates of uracil and thymine deoxyribonucleotides, and so protects mitochondrial DNA replication from excess dTTP. Has only marginal activity towards dIMP and dGMP", "gene_name": "NT5M", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NPB1", "name": "GPR183", "organism": "Homo sapiens", "uniprot_id": "Q9NPB1" }, { "function": "G protein-coupled receptor (GPCR) that plays a role in diverse physiological processes particularly within the immune and nervous systems (PubMed:21732409, PubMed:26195725). Becomes active when triggered by various endogenous ligands including endocannabinoid N-arachidonyl glycine (NAGly), delta-9-tetrahydrocannabinol or resolvin D2/RvD2 derived from the omega-3 fatty acid docosahexaenoic acid (DHA) (PubMed:16844083, PubMed:24762058, PubMed:26195725, PubMed:27572937). Upon RvD2 binding, facilitates the resolution of inflammation, aiding in tissue repair and homeostasis. Mechanistically, RvD2 ligation initiates Galphas protein coupling, activation of cAMP-PKA signaling pathway and phosphorylation of STAT3, leading to RvD2-stimulated macrophage phagocytosis (PubMed:27994074). Mediates NAGly-induced process of reorganization of actin filaments and induction of acrosomal exocytosis (PubMed:27572937). Activation by N-arachidonoyl glycine (NAGly) can also induce apoptosis in macrophages (By similarity). Plays a role in homeostasis of CD8+ subsets of intraepithelial lymphocytes (IELs) (CD8alphaalpha and CD8alphabeta IELs) in small intestine by supporting preferential migration of CD8alphaalpha T-cells to intraepithelial compartment over lamina propria compartment, and by mediating their reconstitution into small intestine after bone marrow transplant (By similarity). Also participates in hypotensive responses, mediating reduction in intraocular and blood pressure (By similarity)", "gene_name": "GPR18", "glycan_count": 0, "glycosylation_sites": [ { "position": 14, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q14330", "name": "GPR18", "organism": "Homo sapiens", "uniprot_id": "Q14330" }, { "function": "Calcium-binding enzyme that initiates starch digestion in the oral cavity (PubMed:12527308). Catalyzes the hydrolysis of internal (1->4)-alpha-D-glucosidic bonds, yielding a mixture of maltose, isomaltose, small amounts of glucose as well as small linear and branched oligosaccharides called dextrins (PubMed:12527308)", "gene_name": "AMY1A", "glycan_count": 0, "glycosylation_sites": [ { "position": 427, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 476, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P0DUB6", "name": "\u03b1-glucosidase", "organism": "Homo sapiens", "uniprot_id": "P0DUB6" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02794 (FTH1), P02792 (FTL)", "name": "Ferritin", "organism": "", "uniprot_id": "" }, { "function": "Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. Binds cooperatively to specific DNA consensus sequences that are separated from XerD binding sites by a short central region, forming the heterotetrameric XerC-XerD complex that recombines DNA substrates. The complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. In the complex XerC specifically exchanges the top DNA strands", "gene_name": "xerC", "glycan_count": 0, "glycosylation_sites": [], "id": "P55888", "name": "Sult1e1", "organism": "Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)", "uniprot_id": "P55888" }, { "function": "Nuclear receptor that binds DNA as a monomer to ROR response elements (RORE) containing a single core motif half-site 5'-AGGTCA-3' preceded by a short A-T-rich sequence. Key regulator of embryonic development, cellular differentiation, immunity, circadian rhythm as well as lipid, steroid, xenobiotics and glucose metabolism. Considered to have intrinsic transcriptional activity, have some natural ligands like oxysterols that act as agonists (25-hydroxycholesterol) or inverse agonists (7-oxygenated sterols), enhancing or repressing the transcriptional activity, respectively. Recruits distinct combinations of cofactors to target genes regulatory regions to modulate their transcriptional expression, depending on the tissue, time and promoter contexts. Regulates genes involved in photoreceptor development including OPN1SW, OPN1SM and ARR3 and skeletal muscle development with MYOD1. Required for proper cerebellum development (PubMed:29656859). Regulates SHH gene expression, among others, to induce granule cells proliferation as well as expression of genes involved in calcium-mediated signal transduction. Regulates the circadian expression of several clock genes, including CLOCK, BMAL1, NPAS2 and CRY1. Competes with NR1D1 for binding to their shared DNA response element on some clock genes such as BMAL1, CRY1 and NR1D1 itself, resulting in NR1D1-mediated repression or RORA-mediated activation of clock genes expression, leading to the circadian pattern of clock genes expression. Therefore influences the period length and stability of the clock. Regulates genes involved in lipid metabolism such as apolipoproteins APOA1, APOA5, APOC3 and PPARG. In liver, has specific and redundant functions with RORC as positive or negative modulator of expression of genes encoding phase I and phase II proteins involved in the metabolism of lipids, steroids and xenobiotics, such as CYP7B1 and SULT2A1. Induces a rhythmic expression of some of these genes. In addition, interplays functionally with NR1H2 and NR1H3 for the regulation of genes involved in cholesterol metabolism. Also involved in the regulation of hepatic glucose metabolism through the modulation of G6PC1 and PCK1. In adipose tissue, plays a role as negative regulator of adipocyte differentiation, probably acting through dual mechanisms. May suppress CEBPB-dependent adipogenesis through direct interaction and PPARG-dependent adipogenesis through competition for DNA-binding. Downstream of IL6 and TGFB and synergistically with RORC isoform 2, is implicated in the lineage specification of uncommitted CD4(+) T-helper (T(H)) cells into T(H)17 cells, antagonizing the T(H)1 program. Probably regulates IL17 and IL17F expression on T(H) by binding to the essential enhancer conserved non-coding sequence 2 (CNS2) in the IL17-IL17F locus. Involved in hypoxia signaling by interacting with and activating the transcriptional activity of HIF1A. May inhibit cell growth in response to cellular stress. May exert an anti-inflammatory role by inducing CHUK expression and inhibiting NF-kappa-B signaling", "gene_name": "RORA", "glycan_count": 1, "glycosylation_sites": [], "id": "P35398", "name": "Retinoic Acid Receptor-Related Orphan Receptor Alpha (ROR\u03b1)", "organism": "Homo sapiens", "uniprot_id": "P35398" }, { "function": "May be involved in BMP2-induced transcription", "gene_name": "ZBTB24", "glycan_count": 0, "glycosylation_sites": [], "id": "O43167", "name": "Per3", "organism": "Homo sapiens", "uniprot_id": "O43167" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UJM6", "name": "REVERB\u03b1 (NR1D1)", "organism": "", "uniprot_id": "Q9UJM6" }, { "function": "Interferon-induced ISG15-specific protease that plays a crucial role for maintaining a proper balance of ISG15-conjugated proteins in cells (PubMed:11788588). Regulates protein ISGylation by efficiently cleaving ISG15 conjugates linked via isopeptide bonds. Regulates T-cell activation and T-helper 17 (Th17) cell differentiation by deubiquitinating TAK1, likely to keep TAK1-TAB complexes in steady conditions (PubMed:23825189). In turn, restricts activation of NF-kappa-B, NFAT, and JNK as well as expression of IL2 in T-cells after TCR activation (PubMed:23825189). Acts as a molecular adapter with USP20 to promote innate antiviral response through deubiquitinating STING1 (PubMed:27801882). Involved also in the negative regulation of the inflammatory response triggered by type I interferon (PubMed:27325888, PubMed:28165510). Upon recruitment by STAT2 to the type I interferon receptor subunit IFNAR2 interferes with the assembly of the ternary interferon-IFNAR1-IFNAR2 complex and acts as a negative regulator of the type I interferon signaling pathway (PubMed:28165510)", "gene_name": "USP18", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UMW8", "name": "UbD (Ubiquitin D)", "organism": "Homo sapiens", "uniprot_id": "Q9UMW8" }, { "function": "Plays a role with ILK in promoting the cell adhesion and spreading of leukocytes", "gene_name": "PARVG", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NSG1", "name": "B4GALT3", "organism": "Homo sapiens", "uniprot_id": "Q9HBI0" }, { "function": "DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates", "gene_name": "rpoC", "glycan_count": 0, "glycosylation_sites": [], "id": "P0A8T7", "name": "Murein hydrolase activator NlpD", "organism": "Escherichia coli (strain K12)", "uniprot_id": "P0A8T7" }, { "function": "Plays a role in the inhibition of the host innate and adaptive immune responses. Possesses five immunoglobulin-binding domains that capture both the fragment crystallizable region (Fc region) and the Fab region (part of Ig that identifies antigen) of immunoglobulins (By similarity). In turn, Staphylococcus aureus is protected from phagocytic killing via inhibition of Ig Fc region. In addition, the host elicited B-cell response is prevented due to a decrease of antibody-secreting cell proliferation that enter the bone marrow, thereby decreasing long-term antibody production. Inhibits osteogenesis by preventing osteoblast proliferation and expression of alkaline phosphatase, type I collagen, osteopontin and osteocalcin. Acts directly as a pro-inflammatory factor in the lung through its ability to bind and activate tumor necrosis factor alpha receptor 1/TNFRSF1A (By similarity)", "gene_name": "spa", "glycan_count": 0, "glycosylation_sites": [], "id": "P38507", "name": "Protein A", "organism": "Staphylococcus aureus", "uniprot_id": "P38507" }, { "function": "Serine/threonine-protein phosphatase component of macronutrients metabolism. Forms a functional kinase and phosphatase pair with BCKDK, serving as a metabolic regulatory node that coordinates branched-chain amino acids (BCAAs) with glucose and lipid metabolism via two distinct phosphoprotein targets: mitochondrial BCKDHA subunit of the branched-chain alpha-ketoacid dehydrogenase (BCKDH) complex and cytosolic ACLY, a lipogenic enzyme of Krebs cycle (PubMed:17336929, PubMed:17374715, PubMed:19411760, PubMed:22291014, PubMed:22589535, PubMed:23086801, PubMed:29779826). At high levels of branched-chain ketoacids, dephosphorylates and activates mitochondrial BCKDH complex, a multisubunit complex consisting of three multimeric components each involved in different steps of BCAA catabolism: E1 composed of BCKDHA and BCKDHB, E2 core composed of DBT monomers, and E3 composed of DLD monomers. Tightly associates with the E2 component of BCKDH complex and dephosphorylates BCKDHA on Ser-337 (PubMed:17336929, PubMed:17374715, PubMed:19411760, PubMed:22291014, PubMed:22589535, PubMed:23086801, PubMed:29779826). Regulates the reversible phosphorylation of ACLY in response to changes in cellular carbohydrate abundance such as occurs during fasting to feeding metabolic transition. At fasting state, appears to dephosphorylate ACLY on Ser-455 and inactivate it. Refeeding stimulates MLXIPL/ChREBP transcription factor, leading to increased BCKDK to PPM1K expression ratio, phosphorylation and activation of ACLY that ultimately results in the generation of malonyl-CoA and oxaloacetate immediate substrates of de novo lipogenesis and gluconeogenesis, respectively (PubMed:29779826). Recognizes phosphosites having SxS or RxxS motifs and strictly depends on Mn(2+) ions for the phosphatase activity (PubMed:29779826). Regulates Ca(2+)-induced opening of mitochondrial transition pore and apoptotic cell death (PubMed:17374715)", "gene_name": "PPM1K", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8N3J5", "name": "PPM1K", "organism": "Homo sapiens", "uniprot_id": "Q8N3J5" }, { "function": "Bidirectional proton-coupled monocarboxylate transporter (PubMed:12946269, PubMed:32946811, PubMed:33333023). Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, acetate and the ketone bodies acetoacetate and beta-hydroxybutyrate, and thus contributes to the maintenance of intracellular pH (PubMed:12946269, PubMed:33333023). The transport direction is determined by the proton motive force and the concentration gradient of the substrate monocarboxylate. MCT1 is a major lactate exporter (By similarity). Plays a role in cellular responses to a high-fat diet by modulating the cellular levels of lactate and pyruvate that contribute to the regulation of central metabolic pathways and insulin secretion, with concomitant effects on plasma insulin levels and blood glucose homeostasis (By similarity). Facilitates the protonated monocarboxylate form of succinate export, that its transient protonation upon muscle cell acidification in exercising muscle and ischemic heart (PubMed:32946811). Functions via alternate outward- and inward-open conformation states. Protonation and deprotonation of 309-Asp is essential for the conformational transition (PubMed:33333023)", "gene_name": "SLC16A1", "glycan_count": 1, "glycosylation_sites": [], "id": "P53985", "name": "MCT1 (SLC16A1)", "organism": "Homo sapiens", "uniprot_id": "P53985" }, { "function": "NADPH oxidase that catalyzes predominantly the reduction of oxygen to H2O2 (PubMed:14966267, PubMed:15356101, PubMed:15927447, PubMed:21343298, PubMed:25062272). Can also catalyze to a smaller extent, the reduction of oxygen to superoxide (PubMed:10869423, PubMed:11032835, PubMed:15155719, PubMed:15572675, PubMed:15927447, PubMed:16019190, PubMed:16179589, PubMed:16230378, PubMed:16324151, PubMed:25062272). May function as an oxygen sensor regulating the KCNK3/TASK-1 potassium channel and HIF1A activity (PubMed:16019190). May regulate insulin signaling cascade (PubMed:14966267). May play a role in apoptosis, bone resorption and lipolysaccharide-mediated activation of NFKB (PubMed:15356101, PubMed:15572675). May produce superoxide in the nucleus and play a role in regulating gene expression upon cell stimulation (PubMed:16324151). Promotes ferroptosis, reactive oxygen species production and reduced glutathione (GSH) levels by activating NLRP3 inflammasome activation and cytokine release (PubMed:39909992)", "gene_name": "NOX4", "glycan_count": 0, "glycosylation_sites": [ { "position": 133, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 230, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NPH5", "name": "NOX4 (NADPH oxidase 4)", "organism": "Homo sapiens", "uniprot_id": "Q9NPH5" }, { "function": "Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication (PubMed:10675335, PubMed:12717439, PubMed:17050006, PubMed:17704056, PubMed:18625225, PubMed:28992046). The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase (PubMed:10675335, PubMed:12717439, PubMed:17704056). E2F1 binds preferentially RB1 in a cell-cycle dependent manner (PubMed:10675335, PubMed:12717439, PubMed:17704056). It can mediate both cell proliferation and TP53/p53-dependent apoptosis (PubMed:8170954). Blocks adipocyte differentiation by binding to specific promoters repressing CEBPA binding to its target gene promoters (PubMed:20176812). Directly activates transcription of PEG10 (PubMed:17050006, PubMed:18625225, PubMed:28992046). Positively regulates transcription of RRP1B (PubMed:20040599)", "gene_name": "E2F1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q01094", "name": "E2F1", "organism": "Homo sapiens", "uniprot_id": "Q01094" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P19429 (Troponin I)", "name": "Troponin", "organism": "", "uniprot_id": "" }, { "function": "Precursor of non-enzymatic components of the classical, alternative, lectin and GZMK complement pathways, which consist in a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system", "gene_name": "C3", "glycan_count": 2, "glycosylation_sites": [ { "position": 939, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1617, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01027", "name": "Complement C3", "organism": "Mus musculus", "uniprot_id": "P01027" }, { "function": "Probable neurotoxin", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P0C2S8", "name": "Complement C4", "organism": "Phoneutria nigriventer", "uniprot_id": "P0C2S8" }, { "function": "Transcriptional coactivator for CREB1 which activates transcription through both consensus and variant cAMP response element (CRE) sites. Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated and acts independently of CREB1 'Ser-133' phosphorylation. Enhances the interaction of CREB1 with TAF4. Regulates the expression of specific CREB-activated genes such as the steroidogenic gene, StAR. Potent coactivator of PGC1alpha and inducer of mitochondrial biogenesis in muscle cells. In the hippocampus, involved in late-phase long-term potentiation (L-LTP) maintenance at the Schaffer collateral-CA1 synapses. May be required for dendritic growth of developing cortical neurons (By similarity). In concert with SIK1, regulates the light-induced entrainment of the circadian clock. In response to light stimulus, coactivates the CREB-mediated transcription of PER1 which plays an important role in the photic entrainment of the circadian clock", "gene_name": "CRTC1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q6UUV9", "name": "Epithelial splicing regulatory protein 1 (ESRP1)", "organism": "Homo sapiens", "uniprot_id": "Q6UUV9" }, { "function": "A cytochrome P450 monooxygenase involved in the metabolism of steroid hormones and vitamins (PubMed:10681376, PubMed:11093772, PubMed:12865317, PubMed:2732228). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds (PubMed:10681376, PubMed:11093772, PubMed:12865317, PubMed:2732228). Exhibits high catalytic activity for the formation of catechol estrogens from 17beta-estradiol (E2) and estrone (E1), namely 2-hydroxy E1 and E2 (PubMed:12865317). Catalyzes 6beta-hydroxylation of the steroid hormones testosterone, progesterone, and androstenedione (PubMed:2732228). Catalyzes the oxidative conversion of all-trans-retinol to all-trans-retinal, a rate-limiting step for the biosynthesis of all-trans-retinoic acid (atRA) (PubMed:10681376). Further metabolizes all trans-retinoic acid (atRA) to 4-hydroxyretinoate and may play a role in hepatic atRA clearance (PubMed:11093772). Also involved in the oxidative metabolism of xenobiotics, including calcium channel blocking drug nifedipine and immunosuppressive drug cyclosporine (PubMed:2732228)", "gene_name": "CYP3A5", "glycan_count": 1, "glycosylation_sites": [], "id": "P20815", "name": "Cytochrome P450 3A5 (CYP3A5)", "organism": "Homo sapiens", "uniprot_id": "P20815" }, { "function": "Involved in the initial and rate-limiting step of peroxisomal beta-oxidation of straight-chain saturated and unsaturated very-long-chain fatty acids (PubMed:15060085, PubMed:17458872, PubMed:17603022, PubMed:32169171, PubMed:33234382, PubMed:7876265). Catalyzes the desaturation of fatty acyl-CoAs such as palmitoyl-CoA (hexadecanoyl-CoA) to 2-trans-enoyl-CoAs ((2E)-enoyl-CoAs) such as (2E)-hexadecenoyl-CoA, and donates electrons directly to molecular oxygen (O(2)), thereby producing hydrogen peroxide (H(2)O(2)) (PubMed:17458872, PubMed:17603022, PubMed:7876265)", "gene_name": "ACOX1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q15067", "name": "Acyl-CoA oxidase 1 (ACOX1)", "organism": "Homo sapiens", "uniprot_id": "Q15067" }, { "function": "", "gene_name": "Nrxn2", "glycan_count": 0, "glycosylation_sites": [], "id": "O88723", "name": "Claudin5", "organism": "Mus musculus", "uniprot_id": "O88723" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q61537", "name": "E-selectin", "organism": "Mus musculus", "uniprot_id": "Q61536" }, { "function": "Core component of the complement C1 complex, a multiprotein complex that initiates the classical pathway of the complement system, a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system. The classical complement pathway is initiated by the C1Q subcomplex of the C1 complex, which specifically binds IgG or IgM immunoglobulins complexed with antigens, forming antigen-antibody complexes on the surface of pathogens: C1QA, together with C1QB and C1QC, specifically recognizes and binds the Fc regions of IgG or IgM via its C1q domain. Immunoglobulin-binding activates the proenzyme C1R, which cleaves C1S, initiating the proteolytic cascade of the complement system. The C1Q subcomplex is activated by a hexamer of IgG complexed with antigens, while it is activated by a pentameric IgM. The C1Q subcomplex also recognizes and binds phosphatidylserine exposed on the surface of cells undergoing programmed cell death, possibly promoting activation of the complement system", "gene_name": "C1qc", "glycan_count": 1, "glycosylation_sites": [ { "position": 76, "type": "O-linked (Gal...) hydroxylysine" } ], "id": "Q02105", "name": "VCAM-1", "organism": "Mus musculus", "uniprot_id": "Q02105" }, { "function": "Endothelins are endothelium-derived vasoconstrictor peptides (By similarity). Probable ligand for G-protein coupled receptors EDNRA and EDNRB which activates PTK2B, BCAR1, BCAR3 and, GTPases RAP1 and RHOA cascade in glomerular mesangial cells (By similarity). Also binds the DEAR/FBXW7-AS1 receptor (PubMed:16293765). Promotes mesenteric arterial wall remodeling via activation of ROCK signaling and subsequent colocalization of NFATC3 with F-actin filaments (PubMed:20495147, PubMed:21525433). NFATC3 then translocates to the nucleus where it subsequently promotes the transcription of the smooth muscle hypertrophy and differentiation marker ACTA2 (PubMed:20495147)", "gene_name": "Edn1", "glycan_count": 0, "glycosylation_sites": [], "id": "P22387", "name": "Endothelin-1", "organism": "Mus musculus", "uniprot_id": "P22387" }, { "function": "", "gene_name": "U38", "glycan_count": 0, "glycosylation_sites": [], "id": "P28857", "name": "PDGFR\u03b2", "organism": "Human herpesvirus 6A (strain Uganda-1102)", "uniprot_id": "P28857" }, { "function": "Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration (By similarity). Could play a role in bone osteoclastic resorption (PubMed:8132709). Cleaves KiSS1 at a Gly-|-Leu bond (By similarity). Cleaves NINJ1 to generate the Secreted ninjurin-1 form (PubMed:23142597, PubMed:32883094). Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide (By similarity)", "gene_name": "Mmp9", "glycan_count": 1, "glycosylation_sites": [ { "position": 39, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 120, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 127, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P41245", "name": "MMP9", "organism": "Mus musculus", "uniprot_id": "P41245" }, { "function": "Component of chylomicrons, very low-density lipoproteins (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) in plasma. Plays an important role in lipoprotein metabolism as an activator of lipoprotein lipase. Both proapolipoprotein C-II and apolipoprotein C-II can activate lipoprotein lipase. In normolipidemic individuals, it is mainly distributed in the HDL, whereas in hypertriglyceridemic individuals, predominantly found in the VLDL and LDL", "gene_name": "APOC2", "glycan_count": 4, "glycosylation_sites": [], "id": "P02655", "name": "APOC2", "organism": "Homo sapiens", "uniprot_id": "P02655" }, { "function": "May play a scavenger role by digesting biologically active peptidoglycan (PGN) into biologically inactive fragments. Has no direct bacteriolytic activity", "gene_name": "PGLYRP2", "glycan_count": 57, "glycosylation_sites": [ { "position": 77, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 367, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 485, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q96PD5", "name": "PGLYRP2", "organism": "Homo sapiens", "uniprot_id": "Q96PD5" }, { "function": "Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline", "gene_name": "BHMT", "glycan_count": 1, "glycosylation_sites": [], "id": "Q93088", "name": "Enteropeptidase (EP)", "organism": "Homo sapiens", "uniprot_id": "Q93088" }, { "function": "", "gene_name": "CTRB1", "glycan_count": 0, "glycosylation_sites": [], "id": "P17538", "name": "Chymotrypsinogen", "organism": "Homo sapiens", "uniprot_id": "P17538" }, { "function": "A cytochrome P450 monooxygenase involved in the metabolism of polyunsaturated fatty acids (PUFA) in the cardiovascular system (PubMed:19965576, PubMed:8631948). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase) (PubMed:19965576, PubMed:8631948). Catalyzes the epoxidation of double bonds of PUFA (PubMed:19965576, PubMed:8631948). Converts arachidonic acid to four regioisomeric epoxyeicosatrienoic acids (EpETrE), likely playing a major role in the epoxidation of endogenous cardiac arachidonic acid pools (PubMed:8631948). In endothelial cells, participates in eicosanoids metabolism by converting hydroperoxide species into hydroxy epoxy metabolites. In combination with 15-lipoxygenase metabolizes arachidonic acid and converts hydroperoxyicosatetraenoates (HpETEs) into hydroxy epoxy eicosatrienoates (HEETs), which are precursors of vasodilatory trihydroxyicosatrienoic acids (THETAs). This hydroperoxide isomerase activity is NADPH- and O2-independent (PubMed:19737933). Catalyzes the monooxygenation of a various xenobiotics, such as danazol, amiodarone, terfenadine, astemizole, thioridazine, tamoxifen, cyclosporin A and nabumetone (PubMed:19923256). Catalyzes hydroxylation of the anthelmintics albendazole and fenbendazole (PubMed:23959307). Catalyzes the sulfoxidation of fenbedazole (PubMed:19923256)", "gene_name": "CYP2J2", "glycan_count": 0, "glycosylation_sites": [], "id": "P51589", "name": "CYP2J2", "organism": "Homo sapiens", "uniprot_id": "P51589" }, { "function": "Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Preferentially hydrolyzes the basic residues Arg and Lys", "gene_name": "ERAP2", "glycan_count": 46, "glycosylation_sites": [ { "position": 85, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 119, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 219, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 405, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 650, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6P179", "name": "ERAP2 (Endoplasmic Reticulum Aminopeptidase 2)", "organism": "Homo sapiens", "uniprot_id": "Q6P179" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "various (e.g., P01892 for HLA-A)", "name": "HLA class I molecules", "organism": "", "uniprot_id": "" }, { "function": "Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney", "gene_name": "ERAP1", "glycan_count": 34, "glycosylation_sites": [ { "position": 70, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 154, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 414, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 760, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 901, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NZ08", "name": "ERAP1 (Endoplasmic Reticulum Aminopeptidase 1)", "organism": "Homo sapiens", "uniprot_id": "Q9NZ08" }, { "function": "Neurotrophic factor that regulates central nervous development and function", "gene_name": "FGF20", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NP95", "name": "Aquaporin-9 (AQP9)", "organism": "Homo sapiens", "uniprot_id": "Q9NP95" }, { "function": "Transcriptional activator which regulates endothelin-1 gene expression in endothelial cells. Binds to the consensus sequence 5'-AGATAG-3'", "gene_name": "GATA2", "glycan_count": 1, "glycosylation_sites": [], "id": "P23769", "name": "GATA-2", "organism": "Homo sapiens", "uniprot_id": "P23769" }, { "function": "Acts as a NAD-dependent protein lipoamidase, biotinylase, deacetylase and ADP-ribosyl transferase (PubMed:16959573, PubMed:17715127, PubMed:24052263, PubMed:25525879). Catalyzes more efficiently removal of lipoyl- and biotinyl- than acetyl-lysine modifications (PubMed:24052263, PubMed:25525879). Inhibits the pyruvate dehydrogenase complex (PDH) activity via the enzymatic hydrolysis of the lipoamide cofactor from the E2 component, DLAT, in a phosphorylation-independent manner (PubMed:25525879). Catalyzes the transfer of ADP-ribosyl groups onto target proteins, including mitochondrial GLUD1, inhibiting GLUD1 enzyme activity (PubMed:16959573, PubMed:17715127). Acts as a negative regulator of mitochondrial glutamine metabolism by mediating mono ADP-ribosylation of GLUD1: expressed in response to DNA damage and negatively regulates anaplerosis by inhibiting GLUD1, leading to block metabolism of glutamine into tricarboxylic acid cycle and promoting cell cycle arrest (PubMed:16959573, PubMed:17715127). In response to mTORC1 signal, SIRT4 expression is repressed, promoting anaplerosis and cell proliferation (PubMed:23663782). Acts as a tumor suppressor (PubMed:23562301, PubMed:23663782). Also acts as a NAD-dependent protein deacetylase: mediates deacetylation of 'Lys-471' of MLYCD, inhibiting its activity, thereby acting as a regulator of lipid homeostasis (By similarity). Does not seem to deacetylate PC (PubMed:23438705). Controls fatty acid oxidation by inhibiting PPARA transcriptional activation (PubMed:24043310). Impairs SIRT1-PPARA interaction probably through the regulation of NAD(+) levels (PubMed:24043310). Down-regulates insulin secretion (PubMed:17715127)", "gene_name": "SIRT4", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y6E7", "name": "Sirtuin 4", "organism": "Homo sapiens", "uniprot_id": "Q9Y6E7" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6V1C2", "name": "FAT/CD36", "organism": "", "uniprot_id": "" }, { "function": "Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER) (PubMed:34020957). As part of the SRP complex, associates with the SRP receptor (SR) component SRPRA to target secretory proteins to the endoplasmic reticulum membrane (PubMed:34020957). Binds to the signal sequence of presecretory proteins when they emerge from the ribosomes (PubMed:34020957). Displays basal GTPase activity, and stimulates reciprocal GTPase activation of the SR subunit SRPRA (PubMed:28972538, PubMed:34020957). Forms a guanosine 5'-triphosphate (GTP)-dependent complex with the SR subunit SRPRA (PubMed:34020957). SR compaction and GTPase mediated rearrangement of SR drive SRP-mediated cotranslational protein translocation into the ER (PubMed:34020957). Requires the presence of SRP9/SRP14 and/or SRP19 to stably interact with RNA (By similarity). Plays a role in proliferation and differentiation of granulocytic cells, neutrophils migration capacity and exocrine pancreas development (PubMed:28972538, PubMed:29914977)", "gene_name": "SRP54", "glycan_count": 3, "glycosylation_sites": [], "id": "P61011", "name": "Signal Recognition Particle 54 kDa subunit (SRP54)", "organism": "Homo sapiens", "uniprot_id": "P61011" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "not applicable (therapeutic Fc fragment)", "name": "Fc fragment of IgG1 (efgartigimod)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "complex", "name": "Membrane Attack Complex (MAC)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "not applicable (autoantibody)", "name": "Anti-SRP antibody", "organism": "", "uniprot_id": "" }, { "function": "May play an integral structural role in elastic-fiber architectural organization and/or assembly", "gene_name": "LTBP2", "glycan_count": 41, "glycosylation_sites": [ { "position": 181, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 343, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 421, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 616, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 811, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1170, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1309, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1430, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1568, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q14767", "name": "LTBP1", "organism": "Homo sapiens", "uniprot_id": "Q14767" }, { "function": "Chemotactic factor that attracts monocytes, lymphocytes, basophils and eosinophils, but not neutrophils. Signals through CCR2B and CCR3 receptors. Plays a role in the accumulation of leukocytes at both sides of allergic and non-allergic inflammation. May be involved in the recruitment of monocytes into the arterial wall during the disease process of atherosclerosis. May play a role in the monocyte attraction in tissues chronically exposed to exogenous pathogens", "gene_name": "CCL13", "glycan_count": 0, "glycosylation_sites": [], "id": "Q99616", "name": "Heparin-binding protein", "organism": "Homo sapiens", "uniprot_id": "Q99616" }, { "function": "Regulator of actin cytoskeleton dynamics underlying cell motility and adhesion. Functions as a component of the WAVE complex, which activates actin nucleating machinery Arp2/3 to drive lamellipodia formation (PubMed:21107423). Acts as a regulator and substrate of nonreceptor tyrosine kinases ABL1 and ABL2 involved in processes linked to cell growth and differentiation. Positively regulates ABL1-mediated phosphorylation of ENAH, which is required for proper polymerization of nucleated actin filaments at the leading edge (PubMed:10498863, PubMed:7590236, PubMed:8649853). Contributes to the regulation of actin assembly at the tips of neuron projections. In particular, controls dendritic spine morphogenesis and may promote dendritic spine specification toward large mushroom-type spines known as repositories of memory in the brain (By similarity). In hippocampal neurons, may mediate actin-dependent BDNF-NTRK2 early endocytic trafficking that triggers dendrite outgrowth (By similarity). Participates in ocular lens morphogenesis, likely by regulating lamellipodia-driven adherens junction formation at the epithelial cell-secondary lens fiber interface (By similarity). Also required for nascent adherens junction assembly in epithelial cells (PubMed:15572692)", "gene_name": "ABI2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NYB9", "name": "Soluble epoxide hydrolase (sEH)", "organism": "Homo sapiens", "uniprot_id": "Q9NYB9" }, { "function": "Peroxisomal trifunctional enzyme possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and delta 3, delta 2-enoyl-CoA isomerase activities. Catalyzes two of the four reactions of the long chain fatty acids peroxisomal beta-oxidation pathway (By similarity). Can also use branched-chain fatty acids such as 2-methyl-2E-butenoyl-CoA as a substrate, which is hydrated into (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA (By similarity). Optimal isomerase for 2,5 double bonds into 3,5 form isomerization in a range of enoyl-CoA species (Probable). Also able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species (By similarity). With HSD17B4, catalyzes the hydration of trans-2-enoyl-CoA and the dehydrogenation of 3-hydroxyacyl-CoA, but with opposite chiral specificity (PubMed:15060085). Regulates the amount of medium-chain dicarboxylic fatty acids which are essential regulators of all fatty acid oxidation pathways (By similarity). Also involved in the degradation of long-chain dicarboxylic acids through peroxisomal beta-oxidation (PubMed:15060085)", "gene_name": "EHHADH", "glycan_count": 0, "glycosylation_sites": [], "id": "Q08426", "name": "FMO3 (Flavin-containing monooxygenase 3)", "organism": "Homo sapiens", "uniprot_id": "Q08426" }, { "function": "Receptor that mediates the recognition, internalization and degradation of oxidatively modified low density lipoprotein (oxLDL) by vascular endothelial cells. OxLDL is a marker of atherosclerosis that induces vascular endothelial cell activation and dysfunction, resulting in pro-inflammatory responses, pro-oxidative conditions and apoptosis. Its association with oxLDL induces the activation of NF-kappa-B through an increased production of intracellular reactive oxygen and a variety of pro-atherogenic cellular responses including a reduction of nitric oxide (NO) release, monocyte adhesion and apoptosis. In addition to binding oxLDL, it acts as a receptor for the HSP70 protein involved in antigen cross-presentation to naive T-cells in dendritic cells, thereby participating in cell-mediated antigen cross-presentation. Also involved in inflammatory process, by acting as a leukocyte-adhesion molecule at the vascular interface in endotoxin-induced inflammation. Also acts as a receptor for advanced glycation end (AGE) products, activated platelets, monocytes, apoptotic cells and both Gram-negative and Gram-positive bacteria", "gene_name": "OLR1", "glycan_count": 0, "glycosylation_sites": [ { "position": 73, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 139, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P78380", "name": "LOX-1", "organism": "Homo sapiens", "uniprot_id": "P78380" }, { "function": "Chemokine, which displays chemotactic activity for T lymphocytes, preferentially Th2 cells, but not monocytes or granulocytes. Therefore plays an important role in a wide range of inflammatory and immunological processes (PubMed:8702936, PubMed:9169480). Acts by binding to CCR4 at T-cell surface (PubMed:10540332, PubMed:9169480). Mediates GM-CSF/CSF2-driven pain and inflammation (PubMed:27525438). In the brain, required to maintain the typical, highly branched morphology of hippocampal microglia under homeostatic conditions. May be important for the appropriate adaptation of microglial morphology and synaptic plasticity to acute lipopolysaccharide (LPS)-induced neuroinflammation (By similarity). Plays a role in wound healing, mainly by inducing fibroblast migration into the wound (By similarity)", "gene_name": "CCL17", "glycan_count": 0, "glycosylation_sites": [], "id": "Q92583", "name": "CCL17", "organism": "Homo sapiens", "uniprot_id": "Q92583" }, { "function": "May play a role not only in inflammatory and immunological responses but also in normal lymphocyte recirculation and homing. May play an important role in trafficking of T-cells in thymus, and T-cell and B-cell migration to secondary lymphoid organs. Binds to chemokine receptor CCR7. Recombinant CCL19 shows potent chemotactic activity for T-cells and B-cells but not for granulocytes and monocytes. Binds to atypical chemokine receptor ACKR4 and mediates the recruitment of beta-arrestin (ARRB1/2) to ACKR4", "gene_name": "CCL19", "glycan_count": 0, "glycosylation_sites": [], "id": "Q99731", "name": "CCL19", "organism": "Homo sapiens", "uniprot_id": "Q99731" }, { "function": "Receptor for gonadotropin releasing hormone (GnRH) that mediates the action of GnRH to stimulate the secretion of the gonadotropic hormones luteinizing hormone (LH) and follicle-stimulating hormone (FSH). This receptor mediates its action by association with G-proteins that activate a phosphatidylinositol-calcium second messenger system. Isoform 2 may act as an inhibitor of GnRH-R signaling", "gene_name": "GNRHR", "glycan_count": 0, "glycosylation_sites": [ { "position": 18, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 102, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P30968", "name": "Gonadotropin-Releasing Hormone Receptor (GnRHR)", "organism": "Homo sapiens", "uniprot_id": "P30968" }, { "function": "CGRP1/CALCA is a peptide hormone that induces vasodilation mediated by the CALCRL-RAMP1 receptor complex (PubMed:1318039, PubMed:33602864, PubMed:9620797). Dilates a variety of vessels including the coronary, cerebral and systemic vasculature. Its abundance in the CNS also points toward a neurotransmitter or neuromodulator role (PubMed:3492492). It also elevates platelet cAMP (PubMed:1318039). CGRP1 can also bind and activate CALCR-RAMP1 (AMYR1) receptor complex (PubMed:38603770)", "gene_name": "CALCA", "glycan_count": 0, "glycosylation_sites": [], "id": "P06881", "name": "Calcitonin Gene-Related Peptide (CGRP)", "organism": "Homo sapiens", "uniprot_id": "P06881" }, { "function": "Scaffolding protein involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes. Component of the 40S ribosomal subunit involved in translational repression (PubMed:23636399). Involved in the initiation of the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation, by promoting ubiquitination of a subset of 40S ribosomal subunits (PubMed:28132843). Binds to and stabilizes activated protein kinase C (PKC), increasing PKC-mediated phosphorylation. May recruit activated PKC to the ribosome, leading to phosphorylation of EIF6. Inhibits the activity of SRC kinases including SRC, LCK and YES1. Inhibits cell growth by prolonging the G0/G1 phase of the cell cycle. Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK heterodimer. Facilitates ligand-independent nuclear translocation of AR following PKC activation, represses AR transactivation activity and is required for phosphorylation of AR by SRC. Modulates IGF1R-dependent integrin signaling and promotes cell spreading and contact with the extracellular matrix. Involved in PKC-dependent translocation of ADAM12 to the cell membrane. Promotes the ubiquitination and proteasome-mediated degradation of proteins such as CLEC1B and HIF1A. Required for VANGL2 membrane localization, inhibits Wnt signaling, and regulates cellular polarization and oriented cell division during gastrulation. Required for PTK2/FAK1 phosphorylation and dephosphorylation. Regulates internalization of the muscarinic receptor CHRM2. Promotes apoptosis by increasing oligomerization of BAX and disrupting the interaction of BAX with the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity. Regulates cell surface expression of some GPCRs such as TBXA2R. Plays a role in regulation of FLT1-mediated cell migration. Involved in the transport of ABCB4 from the Golgi to the apical bile canalicular membrane (PubMed:19674157). Promotes migration of breast carcinoma cells by binding to and activating RHOA (PubMed:20499158). Acts as an adapter for the dephosphorylation and inactivation of AKT1 by promoting recruitment of PP2A phosphatase to AKT1 (By similarity)", "gene_name": "RACK1", "glycan_count": 1, "glycosylation_sites": [], "id": "P63244", "name": "Receptor of activated protein C kinase 1 (RACK1)", "organism": "Homo sapiens", "uniprot_id": "P63244" }, { "function": "Olfactory receptor that is activated by the binding of organosulfur odorants with thioether groups such as (methylthio)methanetiol (MTMT) (By similarity). Also binds odorants acetophenone and benzaldehyde (By similarity). The activity of this receptor is mediated by G proteins which activate adenylyl cyclase (By similarity). May be involved in the molecular processes underlying fasciculation and targeting of olfactory axons (By similarity)", "gene_name": "OR2C1", "glycan_count": 0, "glycosylation_sites": [ { "position": 5, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O95371", "name": "Glyoxalase 2 (GLO2/HAGH)", "organism": "Homo sapiens", "uniprot_id": "O95371" }, { "function": "Has an essential role in spermatogenesis (PubMed:36150389). It is required to repress transposable elements and prevent their mobilization, which is essential for the germline integrity (By similarity). Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons (By similarity). Acts as a co-chaperone via its interaction with HSP90 and is required for the piRNA amplification process, the secondary piRNA biogenesis (By similarity). May be required together with HSP90 in removal of 16 nucleotide ping-pong by-products from Piwi complexes, possibly facilitating turnover of Piwi complexes (By similarity)", "gene_name": "FKBP6", "glycan_count": 0, "glycosylation_sites": [], "id": "O75344", "name": "SHMT2", "organism": "Homo sapiens", "uniprot_id": "O75344" }, { "function": "May function as a chaperone that inhibits aggregation of misfolded proteins (PubMed:12204115). Negatively regulates the unfolded protein response (UPR) through binding to UPR sensors such as ERN1, which in turn inactivates ERN1 signaling (PubMed:24508390). May also regulate the UPR via the EIF2AK3 UPR sensor (PubMed:24508390). Plays a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin (PubMed:15466936)", "gene_name": "PDIA6", "glycan_count": 1, "glycosylation_sites": [], "id": "Q15084", "name": "PDIA6", "organism": "Homo sapiens", "uniprot_id": "Q15084" }, { "function": "Component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. The TIM22 complex forms a twin-pore translocase that uses the membrane potential as the external driving force. In the TIM22 complex, it may act as a docking point for the soluble 70 kDa complex that guides the target proteins in transit through the aqueous mitochondrial intermembrane space", "gene_name": "TIMM10B", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y5J6", "name": "ROMO1", "organism": "Homo sapiens", "uniprot_id": "Q9Y5J6" }, { "function": "Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q) (PubMed:10746566, PubMed:24781757). SDH also oxidizes malate to the non-canonical enol form of oxaloacetate, enol-oxaloacetate (By similarity). Enol-oxaloacetate, which is a potent inhibitor of the succinate dehydrogenase activity, is further isomerized into keto-oxaloacetate (By similarity). Can act as a tumor suppressor (PubMed:20484225)", "gene_name": "SDHA", "glycan_count": 1, "glycosylation_sites": [], "id": "P31040", "name": "SDHA (Succinate dehydrogenase complex subunit A)", "organism": "Homo sapiens", "uniprot_id": "P31040" }, { "function": "ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (By similarity). Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane (By similarity). In addition to its ADP:ATP antiporter activity, also involved in mitochondrial uncoupling and mitochondrial permeability transition pore (mPTP) activity (By similarity). Plays a role in mitochondrial uncoupling by acting as a proton transporter: proton transport uncouples the proton flows via the electron transport chain and ATP synthase to reduce the efficiency of ATP production and cause mitochondrial thermogenesis (By similarity). Proton transporter activity is inhibited by ADP:ATP antiporter activity, suggesting that SLC25A5/ANT2 acts as a master regulator of mitochondrial energy output by maintaining a delicate balance between ATP production (ADP:ATP antiporter activity) and thermogenesis (proton transporter activity) (By similarity). Proton transporter activity requires free fatty acids as cofactor, but does not transport it (By similarity). Probably mediates mitochondrial uncoupling in tissues that do not express UCP1 (By similarity). Also plays a key role in mPTP opening, a non-specific pore that enables free passage of the mitochondrial membranes to solutes of up to 1.5 kDa, and which contributes to cell death (PubMed:31883789). It is however unclear if SLC25A5/ANT2 constitutes a pore-forming component of mPTP or regulates it (By similarity). Acts as a regulator of mitophagy independently of ADP:ATP antiporter activity: promotes mitophagy via interaction with TIMM44, leading to inhibit the presequence translocase TIMM23, thereby promoting stabilization of PINK1 (By similarity). As part of the mitotic spindle-associated MMXD complex it may play a role in chromosome segregation (PubMed:20797633)", "gene_name": "SLC25A5", "glycan_count": 1, "glycosylation_sites": [], "id": "P05141", "name": "ANT2 (Adenine nucleotide translocator 2)", "organism": "Homo sapiens", "uniprot_id": "P05141" }, { "function": "Channel-forming and calcium-conducting subunit of the mitochondrial inner membrane calcium uniporter complex (uniplex), which mediates calcium uptake into the mitochondrial matrix (PubMed:21685886, PubMed:21685888, PubMed:22822213, PubMed:22829870, PubMed:22904319, PubMed:23101630, PubMed:23178883, PubMed:23755363, PubMed:24332854, PubMed:24560927, PubMed:26341627, PubMed:29954988, PubMed:29995857, PubMed:30454562, PubMed:30638448, PubMed:31080062, PubMed:32494073, PubMed:32762847, PubMed:33296646, PubMed:37036971, PubMed:37126688). MCU channel activity is regulated by the calcium-sensor subunits of the uniplex MICU1 and MICU2 (or MICU3) (PubMed:24560927, PubMed:26903221, PubMed:30454562, PubMed:30638448, PubMed:32494073, PubMed:32762847, PubMed:37036971, PubMed:37126688). Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates ATP production, cytoplasmic calcium signals and activation of cell death pathways (PubMed:21685886, PubMed:21685888, PubMed:22822213, PubMed:22829870, PubMed:22904319, PubMed:23101630, PubMed:23178883, PubMed:23755363, PubMed:24332854, PubMed:24560927, PubMed:26341627, PubMed:29954988, PubMed:32494073, PubMed:32762847). Involved in buffering the amplitude of systolic calcium rises in cardiomyocytes (PubMed:22822213). While dispensable for baseline homeostatic cardiac function, acts as a key regulator of short-term mitochondrial calcium loading underlying a 'fight-or-flight' response during acute stress: acts by mediating a rapid increase of mitochondrial calcium in pacemaker cells (PubMed:25603276). Participates in mitochondrial permeability transition during ischemia-reperfusion injury (By similarity). Mitochondrial calcium uptake in skeletal muscle cells is involved in muscle size in adults (By similarity). Regulates synaptic vesicle endocytosis kinetics in central nerve terminal (By similarity). Regulates glucose-dependent insulin secretion in pancreatic beta-cells by regulating mitochondrial calcium uptake (PubMed:22829870, PubMed:22904319). Involved in antigen processing and presentation (By similarity)", "gene_name": "MCU", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8NE86", "name": "MCU (Mitochondrial calcium uniporter)", "organism": "Homo sapiens", "uniprot_id": "Q8NE86" }, { "function": "PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed:20676357). Involved in regulation of the mitochondrial permeability transition pore (mPTP) (PubMed:26387735). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated (PubMed:26387735). In cooperation with mitochondrial p53/TP53 is involved in activating oxidative stress-induced necrosis (PubMed:22726440). Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels (By similarity). Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis (PubMed:19228691)", "gene_name": "PPIF", "glycan_count": 8, "glycosylation_sites": [], "id": "P30405", "name": "Cyclophilin D", "organism": "Homo sapiens", "uniprot_id": "P30405" }, { "function": "Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides (PubMed:17707404, PubMed:29438714, PubMed:33889951, PubMed:7733872). Acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol (PubMed:12492477). Required for the maintenance of physical strength (By similarity)", "gene_name": "PRDX3", "glycan_count": 1, "glycosylation_sites": [], "id": "P30048", "name": "PRDX3 (Peroxiredoxin 3)", "organism": "Homo sapiens", "uniprot_id": "P30048" }, { "function": "Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylation and deglutathionylation of mitochondrial complex I, which in turn regulates the superoxide production by the complex. Overexpression decreases the susceptibility to apoptosis and prevents loss of cardiolipin and cytochrome c release", "gene_name": "GLRX2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NS18", "name": "TRX2 (Thioredoxin 2)", "organism": "Homo sapiens", "uniprot_id": "Q9NS18" }, { "function": "Ligand of the EGF receptor/EGFR and ERBB4. Stimulates EGFR and ERBB4 tyrosine phosphorylation (PubMed:9419975). Contributes to inflammation, wound healing, tissue repair, and oocyte maturation by regulating angiogenesis and vascular remodeling and by stimulating cell proliferation (PubMed:24631357)", "gene_name": "EREG", "glycan_count": 0, "glycosylation_sites": [ { "position": 47, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O14944", "name": "Epiregulin", "organism": "Homo sapiens", "uniprot_id": "O14944" }, { "function": "Ethanolaminephosphotransferase that catalyzes the transfer of phosphoethanolamine (PE) from CDP-ethanolamine to lipid acceptors, the final step in the synthesis of PE via the 'Kennedy' pathway (PubMed:17132865, PubMed:28052917, PubMed:29500230). PE is the second most abundant phospholipid of membranes in mammals and is involved in various membrane-related cellular processes (PubMed:17132865). The enzyme is critical for the synthesis of several PE species and also catalyzes the synthesis of plasmanyl-PE, a lipid required for proper myelination and neurodevelopment, from 1-alkyl-2-acylglycerol (PubMed:29500230)", "gene_name": "SELENOI", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9C0D9", "name": "ZBED6", "organism": "Homo sapiens", "uniprot_id": "Q9C0D9" }, { "function": "Catalyzes the 2-oxoglutarate and iron-dependent C4-lysyl hydroxylation of ETF1 at 'Lys-63' thereby promoting the translational termination efficiency of ETF1", "gene_name": "JMJD4", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H9V9", "name": "Murf1 (TRIM63)", "organism": "Homo sapiens", "uniprot_id": "Q9H9V9" }, { "function": "Neurophysin 1 specifically binds oxytocin", "gene_name": "OXT", "glycan_count": 0, "glycosylation_sites": [], "id": "P01178", "name": "Oxytocin", "organism": "Homo sapiens", "uniprot_id": "P01178" }, { "function": "PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding", "gene_name": "PPIB", "glycan_count": 8, "glycosylation_sites": [ { "position": 148, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P23284", "name": "Cyclophilin", "organism": "Homo sapiens", "uniprot_id": "P23284" }, { "function": "Involved in induction of the epithelial to mesenchymal transition (EMT), formation and maintenance of embryonic mesoderm, growth arrest, survival and cell migration (PubMed:10655587, PubMed:15647282, PubMed:20389281, PubMed:20562920, PubMed:21952048, PubMed:25827072). Binds to 3 E-boxes of the E-cadherin/CDH1 gene promoter and to the promoters of CLDN7 and KRT8 and, in association with histone demethylase KDM1A which it recruits to the promoters, causes a decrease in dimethylated H3K4 levels and represses transcription (PubMed:10655587, PubMed:20389281, PubMed:20562920). The N-terminal SNAG domain competes with histone H3 for the same binding site on the histone demethylase complex formed by KDM1A and RCOR1, and thereby inhibits demethylation of histone H3 at 'Lys-4' (in vitro) (PubMed:20389281, PubMed:21300290, PubMed:23721412). During EMT, involved with LOXL2 in negatively regulating pericentromeric heterochromatin transcription (PubMed:16096638). SNAI1 recruits LOXL2 to pericentromeric regions to oxidize histone H3 and repress transcription which leads to release of heterochromatin component CBX5/HP1A, enabling chromatin reorganization and acquisition of mesenchymal traits (By similarity). Associates with EGR1 and SP1 to mediate tetradecanoyl phorbol acetate (TPA)-induced up-regulation of CDKN2B, possibly by binding to the CDKN2B promoter region 5'-TCACA-3 (PubMed:20121949). In addition, may also activate the CDKN2B promoter by itself (PubMed:20121949)", "gene_name": "SNAI1", "glycan_count": 1, "glycosylation_sites": [ { "position": 112, "type": "O-linked (GlcNAc) serine" } ], "id": "O95863", "name": "Snail", "organism": "Homo sapiens", "uniprot_id": "O95863" }, { "function": "Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Plays a role in shelterin complex assembly. Isoform 1 may have additional role in tethering telomeres to the nuclear matrix", "gene_name": "TINF2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9BSI4", "name": "TINF2", "organism": "Homo sapiens", "uniprot_id": "Q9BSI4" }, { "function": "G-protein-coupled receptor that plays a role in several physiological pathways such as resolution of inflammatory pain and oligodendrocyte differentiation (By similarity). Acts as a receptor for several ligands including prosaposin, osteocalcin or neuroprotectin D1. Ligand binding induces endocytosis, followed by an ERK phosphorylation cascade (PubMed:11439185, PubMed:23690594). Acts as a receptor for osteocalcin (OCN) to regulate oligodendrocyte differentiation and central nervous system myelination. Mechanistically, plays a negative role in oligodendrocyte differentiation and myelination during development via activation of the ERK1/2 signaling pathway. Therefore, regulates the stability of myelin or resistance of myelin itself to demyelination. Upon activation by neuroprotectin D1 (NPD1), promotes the activation of phagocytosis in macrophages as well as the shift in cytokine release toward an anti-inflammatory profile, and thus helps to reverse inflammatory pain. In addition, the increased macrophage phagocytosis mediates protection against sepsis upon pathogen infection. Additionally, extracellular vesicles derived from efferocyte express prosaposin, which binds to macrophage GPR37 to increase expression of the efferocytosis receptor TIM4 via an ERK-AP1-dependent signaling axis, leading to increased macrophage efferocytosis efficiency and accelerated resolution of inflammation (By similarity). May also act as a maturation factor of LRP6, protecting LRP6 from the endoplasmic reticulum (ER)-associated protein degradation (ERAD) and thereby promoting the Wnt/beta-catenin signaling pathway (PubMed:28341812)", "gene_name": "GPR37", "glycan_count": 4, "glycosylation_sites": [ { "position": 36, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 222, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 239, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O15354", "name": "GPR37", "organism": "Homo sapiens", "uniprot_id": "O15354" }, { "function": "", "gene_name": "NITR2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8AWW8", "name": "Muc2", "organism": "Oncorhynchus mykiss", "uniprot_id": "Q8AWW8" }, { "function": "Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Represses MEF2-dependent transcription", "gene_name": "HDAC9", "glycan_count": 0, "glycosylation_sites": [], "id": "O95028", "name": "Claudin2", "organism": "Homo sapiens", "uniprot_id": "Q9UKV0" }, { "function": "Bactericidal C-type lectin which acts exclusively against Gram-positive bacteria and mediates bacterial killing by binding to surface-exposed carbohydrate moieties of peptidoglycan (PubMed:16931762). Binds membrane phospholipids and kills bacteria by forming a hexameric membrane-permeabilizing oligomeric pore (PubMed:24256734)", "gene_name": "REG3A", "glycan_count": 0, "glycosylation_sites": [], "id": "Q06141", "name": "Reg3\u03b2", "organism": "Homo sapiens", "uniprot_id": "Q06141" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9D7L2", "name": "Reg3\u03b3", "organism": "", "uniprot_id": "Q9D7L2" }, { "function": "G-protein coupled receptor for 5-hydroxytryptamine (serotonin) (PubMed:22957663, PubMed:3138543, PubMed:33762731, PubMed:37935376, PubMed:37935377, PubMed:8138923, PubMed:8393041). Also functions as a receptor for various drugs and psychoactive substances (PubMed:22957663, PubMed:3138543, PubMed:33762731, PubMed:38552625, PubMed:8138923, PubMed:8393041). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as adenylate cyclase (PubMed:22957663, PubMed:3138543, PubMed:33762731, PubMed:8138923, PubMed:8393041). HTR1A is coupled to G(i)/G(o) G alpha proteins and mediates inhibitory neurotransmission: signaling inhibits adenylate cyclase activity and activates a phosphatidylinositol-calcium second messenger system that regulates the release of Ca(2+) ions from intracellular stores (PubMed:33762731, PubMed:35610220). Beta-arrestin family members regulate signaling by mediating both receptor desensitization and resensitization processes (PubMed:18476671, PubMed:20363322, PubMed:20945968). Plays a role in the regulation of 5-hydroxytryptamine release and in the regulation of dopamine and 5-hydroxytryptamine metabolism (PubMed:18476671, PubMed:20363322, PubMed:20945968). Plays a role in the regulation of dopamine and 5-hydroxytryptamine levels in the brain, and thereby affects neural activity, mood and behavior (PubMed:18476671, PubMed:20363322, PubMed:20945968). Plays a role in the response to anxiogenic stimuli (PubMed:18476671, PubMed:20363322, PubMed:20945968)", "gene_name": "HTR1A", "glycan_count": 1, "glycosylation_sites": [ { "position": 10, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 11, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 24, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08908", "name": "HTR1A (Serotonin receptor 1A)", "organism": "Homo sapiens", "uniprot_id": "P08908" }, { "function": "Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction", "gene_name": "GNG12", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UBI6", "name": "GNB3 (G protein subunit beta-3)", "organism": "Homo sapiens", "uniprot_id": "Q9UBI6" }, { "function": "Oxidizes L-tryptophan to 5-hydroxy-l-tryptophan in the rate-determining step of serotonin biosynthesis", "gene_name": "TPH1", "glycan_count": 1, "glycosylation_sites": [], "id": "P17752", "name": "TPH1 (Tryptophan hydroxylase 1)", "organism": "Homo sapiens", "uniprot_id": "P17752" }, { "function": "A cytochrome P450 monooxygenase involved in the metabolism of polyunsaturated fatty acids (PUFA) (PubMed:18577768, PubMed:19965576, PubMed:20972997). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase) (PubMed:18577768, PubMed:19965576, PubMed:20972997). Catalyzes the hydroxylation of carbon-hydrogen bonds. Hydroxylates PUFA specifically at the omega-1 position (PubMed:18577768). Catalyzes the epoxidation of double bonds of PUFA (PubMed:19965576, PubMed:20972997). Also metabolizes plant monoterpenes such as limonene. Oxygenates (R)- and (S)-limonene to produce carveol and perillyl alcohol (PubMed:11950794). Responsible for the metabolism of a number of therapeutic agents such as the anticonvulsant drug S-mephenytoin, omeprazole, proguanil, certain barbiturates, diazepam, propranolol, citalopram and imipramine. Hydroxylates fenbendazole at the 4' position (PubMed:23959307)", "gene_name": "CYP2C19", "glycan_count": 1, "glycosylation_sites": [], "id": "P33261", "name": "CYP2C19 (Cytochrome P450 2C19)", "organism": "Homo sapiens", "uniprot_id": "P33261" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Not specified for canine; human: Q10589", "name": "Tetherin (BST-2/CD317/HM1.24)", "organism": "", "uniprot_id": "" }, { "function": "Uniporter that transports zinc(2+) into polarized cells of enterocytes, pancreatic acinar and endoderm cells across the basolateral membrane and participates, notably, in zinc excretion from the intestine by the uptake of zinc from the blood into the intestine (By similarity). The transport mechanism is temperature- and concentration-dependent and saturable (By similarity). In addition, is also a high affinity copper transporter in vitro (PubMed:36454509). Also may regulate glucose-stimulated insulin secretion (GSIS) in islets primarily through the zinc-activated SIRT1-PPARGC1A axis (By similarity). Could regulate the BMP/TGF-beta (bone morphogenetic protein/transforming growth factor-beta) signaling pathway and modulates extracellular matrix (ECM) proteins of the sclera (PubMed:24891338). Plays a role in eye development (PubMed:24891338)", "gene_name": "SLC39A5", "glycan_count": 5, "glycosylation_sites": [ { "position": 50, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 160, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6ZMH5", "name": "ADAMTS-like protein 4 (ADAMTSL4)", "organism": "Homo sapiens", "uniprot_id": "Q6ZMH5" }, { "function": "Effector cytokine of innate and adaptive immune system involved in antimicrobial host defense and maintenance of tissue integrity (PubMed:21350122). IL17A-IL17F signals via IL17RA-IL17RC heterodimeric receptor complex, triggering homotypic interaction of IL17RA and IL17RC chains with TRAF3IP2 adapter through SEFIR domains. This leads to downstream TRAF6-mediated activation of NF-kappa-B and MAPkinase pathways ultimately resulting in transcriptional activation of cytokines, chemokines, antimicrobial peptides and matrix metalloproteinases, with potential strong immune inflammation (PubMed:11574464, PubMed:11591732, PubMed:11591768, PubMed:17911633, PubMed:18684971, PubMed:21350122, PubMed:28827714). IL17A-IL17F is primarily involved in host defense against extracellular bacteria and fungi by inducing neutrophilic inflammation (By similarity). As signature effector cytokine of T-helper 17 cells (Th17), primarily induces neutrophil activation and recruitment at infection and inflammatory sites (By similarity). Stimulates the production of antimicrobial beta-defensins DEFB1, DEFB103A, and DEFB104A by mucosal epithelial cells, limiting the entry of microbes through the epithelial barriers (By similarity). IL17F homodimer can signal via IL17RC homodimeric receptor complex, triggering downstream activation of TRAF6 and NF-kappa-B signaling pathway (PubMed:32187518). Via IL17RC induces transcriptional activation of IL33, a potent cytokine that stimulates group 2 innate lymphoid cells and adaptive T-helper 2 cells involved in pulmonary allergic response to fungi. Likely via IL17RC, promotes sympathetic innervation of peripheral organs by coordinating the communication between gamma-delta T cells and parenchymal cells. Stimulates sympathetic innervation of thermogenic adipose tissue by driving TGFB1 expression (By similarity). Regulates the composition of intestinal microbiota and immune tolerance by inducing antimicrobial proteins that specifically control the growth of commensal Firmicutes and Bacteroidetes (By similarity)", "gene_name": "IL17F", "glycan_count": 1, "glycosylation_sites": [ { "position": 83, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q96PD4", "name": "SERPINA10", "organism": "Homo sapiens", "uniprot_id": "Q96PD4" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04206, P01901", "name": "MHC class I (H2-K1, H2-D1)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "PLAC8", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NZF1", "name": "TFEB", "organism": "Homo sapiens", "uniprot_id": "Q9NZF1" }, { "function": "Transcription factor that acts as a master regulator of melanocyte survival and differentiation as well as melanosome biogenesis (PubMed:10587587, PubMed:22647378, PubMed:27889061, PubMed:9647758). Binds to M-boxes (5'-TCATGTG-3') and symmetrical DNA sequences (E-boxes) (5'-CACGTG-3') found in the promoter of pigmentation genes, such as tyrosinase (TYR) (PubMed:10587587, PubMed:22647378, PubMed:27889061, PubMed:9647758). Involved in the cellular response to amino acid availability by acting downstream of MTOR: in the presence of nutrients, MITF phosphorylation by MTOR promotes its inactivation (PubMed:36608670). Upon starvation or lysosomal stress, inhibition of MTOR induces MITF dephosphorylation, resulting in transcription factor activity (PubMed:36608670). Plays an important role in melanocyte development by regulating the expression of tyrosinase (TYR) and tyrosinase-related protein 1 (TYRP1) (PubMed:10587587, PubMed:22647378, PubMed:27889061, PubMed:9647758). Plays a critical role in the differentiation of various cell types, such as neural crest-derived melanocytes, mast cells, osteoclasts and optic cup-derived retinal pigment epithelium (PubMed:10587587, PubMed:22647378, PubMed:27889061, PubMed:9647758)", "gene_name": "MITF", "glycan_count": 1, "glycosylation_sites": [], "id": "O75030", "name": "MITF", "organism": "Homo sapiens", "uniprot_id": "O75030" }, { "function": "Transcription factor that acts as a master regulator of lysosomal biogenesis and immune response (PubMed:2338243, PubMed:24448649, PubMed:29146937, PubMed:30733432, PubMed:31672913, PubMed:37079666). Specifically recognizes and binds E-box sequences (5'-CANNTG-3'); efficient DNA-binding requires dimerization with itself or with another MiT/TFE family member such as TFEB or MITF (PubMed:24448649). Involved in the cellular response to amino acid availability by acting downstream of MTOR: in the presence of nutrients, TFE3 phosphorylation by MTOR promotes its inactivation (PubMed:24448649, PubMed:31672913, PubMed:36608670). Upon starvation or lysosomal stress, inhibition of MTOR induces TFE3 dephosphorylation, resulting in transcription factor activity (PubMed:24448649, PubMed:31672913, PubMed:36608670). Specifically recognizes and binds the CLEAR-box sequence (5'-GTCACGTGAC-3') present in the regulatory region of many lysosomal genes, leading to activate their expression, thereby playing a central role in expression of lysosomal genes (PubMed:24448649). Maintains the pluripotent state of embryonic stem cells by promoting the expression of genes such as ESRRB; mTOR-dependent TFE3 cytosolic retention and inactivation promotes exit from pluripotency (By similarity). Required to maintain the naive pluripotent state of hematopoietic stem cell; mTOR-dependent cytoplasmic retention of TFE3 promotes the exit of hematopoietic stem cell from pluripotency (PubMed:30733432). TFE3 activity is also involved in the inhibition of neuronal progenitor differentiation (By similarity). Acts as a positive regulator of browning of adipose tissue by promoting expression of target genes; mTOR-dependent phosphorylation promotes cytoplasmic retention of TFE3 and inhibits browning of adipose tissue (By similarity). In association with TFEB, activates the expression of CD40L in T-cells, thereby playing a role in T-cell-dependent antibody responses in activated CD4(+) T-cells and thymus-dependent humoral immunity (By similarity). Specifically recognizes the MUE3 box, a subset of E-boxes, present in the immunoglobulin enhancer (PubMed:2338243). It also binds very well to a USF/MLTF site (PubMed:2338243). Promotes TGF-beta-induced transcription of COL1A2; via its interaction with TSC22D1 at E-boxes in the gene proximal promoter (By similarity). May regulate lysosomal positioning in response to nutrient deprivation by promoting the expression of PIP4P1 (PubMed:29146937)", "gene_name": "TFE3", "glycan_count": 1, "glycosylation_sites": [], "id": "P19532", "name": "TFE3", "organism": "Homo sapiens", "uniprot_id": "P19532" }, { "function": "Cross-linked envelope protein of keratinocytes", "gene_name": "SPRR3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UBC9", "name": "TFEC", "organism": "Homo sapiens", "uniprot_id": "Q9UBC9" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P0DTD1-13", "name": "SARS-CoV-2 NSP13", "organism": "", "uniprot_id": "" }, { "function": "Transcriptional factor (PubMed:16339272, PubMed:9774444). Plays a critical role in neuronal morphogenesis and survival of sensory neurons (By similarity). Represses the corneal epithelium differentiation (PubMed:28916725). Also acts as a metabolic regulator, by modulating insulin sensitivity in pancreatic beta cells and skeletal muscle cells (PubMed:16339272). Inhibits transcriptional inducers of adipogenesis and has a repressive role in the expression of several adipokines, including leptin (PubMed:16339272)", "gene_name": "KLF7", "glycan_count": 1, "glycosylation_sites": [], "id": "O75840", "name": "DC-LAMP (CD208)", "organism": "Homo sapiens", "uniprot_id": "O75840" }, { "function": "Mediates NK cell adhesion and triggers NK cell effector functions. Binds two different NK cell receptors: CD96 and CD226. These interactions accumulates at the cell-cell contact site, leading to the formation of a mature immunological synapse between NK cell and target cell. This may trigger adhesion and secretion of lytic granules and IFN-gamma and activate cytotoxicity of activated NK cells. May also promote NK cell-target cell modular exchange, and PVR transfer to the NK cell. This transfer is more important in some tumor cells expressing a lot of PVR, and may trigger fratricide NK cell activation, providing tumors with a mechanism of immunoevasion. Plays a role in mediating tumor cell invasion and migration", "gene_name": "PVR", "glycan_count": 17, "glycosylation_sites": [ { "position": 105, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 120, "type": "N-linked (GlcNAc...) (complex) asparagine" }, { "position": 188, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 218, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 237, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 278, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 307, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 313, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 360, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 352, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P15151", "name": "CD155 (Polio Virus Receptor, PVR)", "organism": "Homo sapiens", "uniprot_id": "P15151" }, { "function": "Promotes apoptosis by binding to BCL2, hence preventing the formation of protective BCL2-BAX heterodimers", "gene_name": "G0S2", "glycan_count": 0, "glycosylation_sites": [], "id": "P27469", "name": "Connexin 43 (Cx43)", "organism": "Homo sapiens", "uniprot_id": "P27469" }, { "function": "One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell", "gene_name": "GJB1", "glycan_count": 0, "glycosylation_sites": [], "id": "P08034", "name": "Connexin 32 (Cx32)", "organism": "Homo sapiens", "uniprot_id": "P08034" }, { "function": "Structural component of gap junctions (PubMed:16849369, PubMed:17551008, PubMed:19340074, PubMed:19384972, PubMed:21094651, PubMed:26753910). Gap junctions are dodecameric channels that connect the cytoplasm of adjoining cells. They are formed by the docking of two hexameric hemichannels, one from each cell membrane (PubMed:17551008, PubMed:19340074, PubMed:21094651, PubMed:26753910). Small molecules and ions diffuse from one cell to a neighboring cell via the central pore (PubMed:16849369, PubMed:19384972, PubMed:21094651)", "gene_name": "GJB2", "glycan_count": 0, "glycosylation_sites": [], "id": "P29033", "name": "Connexin 26 (Cx26)", "organism": "Homo sapiens", "uniprot_id": "P29033" }, { "function": "One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell", "gene_name": "GJB6", "glycan_count": 0, "glycosylation_sites": [], "id": "O95452", "name": "Connexin 30 (Cx30)", "organism": "Homo sapiens", "uniprot_id": "O95452" }, { "function": "Structural component of lens fiber gap junctions (PubMed:30044662). Gap junctions are dodecameric channels that connect the cytoplasm of adjoining cells (By similarity). They are formed by the docking of two hexameric hemichannels, one from each cell membrane. Small molecules and ions diffuse from one cell to a neighboring cell via the central pore (PubMed:30044662)", "gene_name": "GJA3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y6H8", "name": "Connexin 46 (Cx46)", "organism": "Homo sapiens", "uniprot_id": "Q9Y6H8" }, { "function": "Structural component of eye lens gap junctions (PubMed:18006672, PubMed:19756179). Gap junctions are dodecameric channels that connect the cytoplasm of adjoining cells. They are formed by the docking of two hexameric hemichannels, one from each cell membrane (By similarity). Small molecules and ions diffuse from one cell to a neighboring cell via the central pore (PubMed:18006672, PubMed:19756179)", "gene_name": "GJA8", "glycan_count": 0, "glycosylation_sites": [], "id": "P48165", "name": "Connexin 50 (Cx50)", "organism": "Homo sapiens", "uniprot_id": "P48165" }, { "function": "One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell", "gene_name": "GJA5", "glycan_count": 0, "glycosylation_sites": [], "id": "P36382", "name": "Connexin 31 (Cx31)", "organism": "Homo sapiens", "uniprot_id": "P36382" }, { "function": "One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell", "gene_name": "GJC1", "glycan_count": 0, "glycosylation_sites": [], "id": "P36383", "name": "Connexin 45 (Cx45)", "organism": "Homo sapiens", "uniprot_id": "P36383" }, { "function": "Histone methyltransferase that dimethylates Lys-36 of histone H3 (H3K36me2). Transcriptional intermediary factor capable of both negatively or positively influencing transcription, depending on the cellular context", "gene_name": "NSD1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96L73", "name": "NSD1", "organism": "Homo sapiens", "uniprot_id": "Q96L73" }, { "function": "Inositol 4-phosphatase which mainly acts on phosphatidylinositol 4-phosphate. May be functionally linked to OCRL, which converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol, for a sequential dephosphorylation of phosphatidylinositol 4,5-bisphosphate at the 5 and 4 position of inositol, thus playing an important role in the endocytic recycling (PubMed:25869669). Regulator of TF:TFRC and integrins recycling pathway, is also involved in cell migration mechanisms (PubMed:25869669). Modulates AKT/GSK3B pathway by decreasing AKT and GSK3B phosphorylation (PubMed:17322895). Negatively regulates STAT3 signaling pathway through inhibition of STAT3 phosphorylation and translocation to the nucleus (PubMed:25476455). Functionally important modulator of cardiac myocyte size and of the cardiac response to stress (By similarity). May play a role as negative regulator of axon regeneration after central nervous system injuries (By similarity)", "gene_name": "INPP5F", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9Y2H2", "name": "HS3ST2", "organism": "Homo sapiens", "uniprot_id": "Q9Y2H2" }, { "function": "Functions as an inhibitory receptor that plays a constitutive negative regulatory role on cytolytic function of natural killer (NK) cells, B-cells and T-cells. Activation by Tyr phosphorylation results in recruitment and activation of the phosphatases PTPN6 and PTPN11. It also reduces the increase of intracellular calcium evoked by B-cell receptor ligation. May also play its inhibitory role independently of SH2-containing phosphatases. Modulates cytokine production in CD4+ T-cells, down-regulating IL2 and IFNG production while inducing secretion of transforming growth factor beta. Also down-regulates IgG and IgE production in B-cells as well as IL8, IL10 and TNF secretion. Inhibits proliferation and induces apoptosis in myeloid leukemia cell lines as well as prevents nuclear translocation of NF-kappa-B p65 subunit/RELA and phosphorylation of I-kappa-B alpha/CHUK in these cells. Inhibits the differentiation of peripheral blood precursors towards dendritic cells", "gene_name": "LAIR1", "glycan_count": 21, "glycosylation_sites": [ { "position": 69, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6GTX8", "name": "LAIR1", "organism": "Homo sapiens", "uniprot_id": "Q6GTX8" }, { "function": "ATP-dependent low-affinity peptide transporter which translocates a broad spectrum of peptides from the cytosol to the lysosomal lumen for degradation (PubMed:15863492, PubMed:17977821, PubMed:18434309, PubMed:22641697, PubMed:25646430, PubMed:30353140, PubMed:30877195, PubMed:31417173). Displays a broad peptide length specificity from 6-mer up to at least 59-mer peptides with an optimum of 23-mers (PubMed:15863492, PubMed:25646430). Binds and transports smaller and larger peptides with the same affinity (PubMed:31417173). Favors positively charged, aromatic or hydrophobic residues in the N- and C-terminal positions whereas negatively charged residues as well as asparagine and methionine are not favored (PubMed:15863492, PubMed:17977821, PubMed:18434309)", "gene_name": "ABCB9", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NP78", "name": "ABCF2", "organism": "Homo sapiens", "uniprot_id": "Q9NP78" }, { "function": "Nonselective, voltage-independent cation channel that mediates Na(+) and Ca(2+) influx, leading to increased cytoplasmic Ca(2+) levels (PubMed:11385575, PubMed:11509734, PubMed:11804595, PubMed:12594222, PubMed:15561722, PubMed:16601673, PubMed:19171771, PubMed:20660597, PubMed:25620041, PubMed:27068538, PubMed:27383051, PubMed:28775320, PubMed:29745897, PubMed:30467180, PubMed:31513012, PubMed:34788616). Functions as a ligand-gated ion channel, gated by intracellular adenosine diphosphate ribose (ADP-ribose), Ca(2+), warm temperature, and oxidative stress (PubMed:19171771, PubMed:25620041, PubMed:28775320, PubMed:30467180). The precise physiological activators are under debate; the true, physiological activators may be ADP-ribose and ADP-ribose-2'-phosphate (PubMed:20650899, PubMed:25918360). Binding of ADP-ribose to the cytoplasmic Nudix domain causes a conformation change; the channel is primed but still requires Ca(2+) binding to trigger channel opening (PubMed:19171771, PubMed:25620041, PubMed:28775320, PubMed:29745897, PubMed:30467180). Extracellular Ca(2+) passes through the channel and increases channel activity (PubMed:19171771). Contributes to Ca(2+) release from intracellular stores in response to ADP-ribose (PubMed:19454650). Plays a role in numerous processes that involve signaling via intracellular Ca(2+) levels (Probable). Besides, mediates the release of lysosomal Zn(2+) stores in response to reactive oxygen species, leading to increased cytosolic Zn(2+) levels (PubMed:25562606, PubMed:27068538). Plays a role in mediating behavorial and physiological responses to moderate heat and thereby contributes to body temperature homeostasis. Plays a role in insulin secretion, a process that requires increased cytoplasmic Ca(2+) levels (By similarity). Required for normal IFNG and cytokine secretion and normal innate immune immunity in response to bacterial infection. Required for normal phagocytosis and cytokine release by macrophages exposed to zymosan (in vitro) (PubMed:22493272). Plays a role in dendritic cell differentiation and maturation, and in dendritic cell chemotaxis via its role in regulating cytoplasmic Ca(2+) levels (By similarity). Plays a role in the regulation of the reorganization of the actin cytoskeleton and filopodia formation in response to reactive oxygen species via its role in increasing cytoplasmic Ca(2+) and Zn(2+) levels (PubMed:27068538). Confers susceptibility to cell death following oxidative stress (PubMed:12594222, PubMed:25562606)", "gene_name": "TRPM2", "glycan_count": 1, "glycosylation_sites": [], "id": "O94759", "name": "TRPC1", "organism": "Homo sapiens", "uniprot_id": "O94759" }, { "function": "Bifunctional enzyme (PubMed:12574510). The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides (PubMed:12574510, PubMed:12869654, PubMed:22798687). Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides (By similarity). Also determines steady-state levels of physiological mediators (PubMed:12574510, PubMed:12869654, PubMed:21217101, PubMed:22798687)", "gene_name": "EPHX2", "glycan_count": 1, "glycosylation_sites": [], "id": "P34913", "name": "EPHX2", "organism": "Homo sapiens", "uniprot_id": "P34913" }, { "function": "Essential hepatic enzyme that catalyzes the oxygenation of a wide variety of nitrogen- and sulfur-containing compounds including drugs as well as dietary compounds (PubMed:10759686, PubMed:30381441, PubMed:32156684). Plays an important role in the metabolism of trimethylamine (TMA), via the production of trimethylamine N-oxide (TMAO) metabolite (PubMed:9776311). TMA is generated by the action of gut microbiota using dietary precursors such as choline, choline containing compounds, betaine or L-carnitine. By regulating TMAO concentration, FMO3 directly impacts both platelet responsiveness and rate of thrombus formation (PubMed:29981269)", "gene_name": "FMO3", "glycan_count": 0, "glycosylation_sites": [], "id": "P31513", "name": "FMO2", "organism": "Homo sapiens", "uniprot_id": "P31513" }, { "function": "Interferon-induced antiviral exoribonuclease that acts mainly on single-stranded RNA (PubMed:11401564, PubMed:12594219, PubMed:16033969). Exhibits antiviral activity against RNA viruses including hepatitis C virus (HCV), hepatitis A virus (HAV) and yellow fever virus (YFV) (PubMed:16514659, PubMed:21036379). Inhibition of several viruses such as chikungunya virus (CHIKV) does not involve the degradation of viral RNAs, but rather the inhibition of translation of viral proteins (By similarity). Exerts a translational control over a large panel of non-self RNA substrates while sparing endogenous transcripts. This activity correlates with the protein's ability to localize in cytoplasmic processing bodies (PubMed:31600344). May also act as master regulator of over hundred interferon stimulated genes leading to viral genome translation inhibition (By similarity). May play additional roles in the maturation of snRNAs and rRNAs, and in ribosome biogenesis (PubMed:16514659)", "gene_name": "ISG20", "glycan_count": 0, "glycosylation_sites": [], "id": "Q96AZ6", "name": "ISG20", "organism": "Homo sapiens", "uniprot_id": "Q96AZ6" }, { "function": "Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression, the regulation of cap-dependent protein translation and through survival signaling by phosphorylation of a pro-apoptotic protein, BAD. Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase transcriptional activity. The stabilization of MYC exerted by PIM2 might explain partly the strong synergism between these 2 oncogenes in tumorigenesis. Regulates cap-dependent protein translation in a mammalian target of rapamycin complex 1 (mTORC1)-independent manner and in parallel to the PI3K-Akt pathway. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Promotes cell survival in response to a variety of proliferative signals via positive regulation of the I-kappa-B kinase/NF-kappa-B cascade; this process requires phosphorylation of MAP3K8/COT. Promotes growth factor-independent proliferation by phosphorylation of cell cycle factors such as CDKN1A and CDKN1B. Involved in the positive regulation of chondrocyte survival and autophagy in the epiphyseal growth plate", "gene_name": "PIM2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9P1W9", "name": "PIM2", "organism": "Homo sapiens", "uniprot_id": "Q9P1W9" }, { "function": "Transcription factor that binds DNA in a sequence-specific manner (PubMed:2010090). Participates in the Wnt signaling pathway (By similarity). Activates transcription of target genes in the presence of CTNNB1 and EP300 (By similarity). PIAG antagonizes both Wnt-dependent and Wnt-independent activation by LEF1 (By similarity). TLE1, TLE2, TLE3 and TLE4 repress transactivation mediated by LEF1 and CTNNB1 (PubMed:11266540). Regulates T-cell receptor alpha enhancer function (PubMed:19653274). Required for IL17A expressing gamma-delta T-cell maturation and development, via binding to regulator loci of BLK to modulate expression (By similarity). Acts as a positive regulator of odontoblast differentiation during mesenchymal tooth germ formation, expression is repressed during the bell stage by MSX1-mediated inhibition of CTNNB1 signaling (By similarity). May play a role in hair cell differentiation and follicle morphogenesis (By similarity)", "gene_name": "LEF1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9UJU2", "name": "LEF-1", "organism": "Homo sapiens", "uniprot_id": "Q9UJU2" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P42336 (PIK3CA)", "name": "PI3K", "organism": "", "uniprot_id": "" }, { "function": "Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to form an insoluble fibrin matrix (By similarity). Fibrin has a major function in hemostasis as one of the primary components of blood clots (By similarity). In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization (By similarity). Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo (By similarity). Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway (PubMed:19332769). Maternal fibrinogen is essential for successful pregnancy (By similarity). Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage (By similarity). May also facilitate the immune response via both innate and T-cell mediated pathways (By similarity)", "gene_name": "Fgg", "glycan_count": 1, "glycosylation_sites": [ { "position": 77, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8VCM7", "name": "Adiponectin receptor 2 (AdipoR2)", "organism": "Mus musculus", "uniprot_id": "Q8VCM7" }, { "function": "Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP)", "gene_name": "ARO3", "glycan_count": 0, "glycosylation_sites": [], "id": "P14843", "name": "C-C motif chemokine ligand 2 (Ccl2/MCP-1)", "organism": "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "uniprot_id": "P14843" }, { "function": "Pro-inflammatory cytokine that is involved in a wide variety of processes such as chemotaxis, differentiation, and activation of peripheral immune cells, regulation of cell growth, apoptosis and modulation of angiostatic effects (By similarity) (PubMed:28623423). Plays thereby an important role during viral infections by stimulating the activation and migration of immune cells to the infected sites (PubMed:18624292, PubMed:19017990, PubMed:28468883). Mechanistically, binding of CXCL10 to the CXCR3 receptor activates G protein-mediated signaling and results in downstream activation of phospholipase C-dependent pathway, an increase in intracellular calcium production and actin reorganization. In turn, recruitment of activated Th1 lymphocytes occurs at sites of inflammation (By similarity). Activation of the CXCL10/CXCR3 axis also plays an important role in neurons in response to brain injury for activating microglia, the resident macrophage population of the central nervous system, and directing them to the lesion site. This recruitment is an essential element for neuronal reorganization (PubMed:15456824)", "gene_name": "Cxcl10", "glycan_count": 0, "glycosylation_sites": [], "id": "P17515", "name": "C-X-C motif chemokine ligand 10 (Cxcl10)", "organism": "Mus musculus", "uniprot_id": "P17515" }, { "function": "Cytokine constitutively present intracellularly in nearly all resting non-hematopoietic cells that plays an important role in inflammation and bridges the innate and adaptive immune systems. After binding to its receptor IL1R1 together with its accessory protein IL1RAP, forms the high affinity interleukin-1 receptor complex. Signaling involves the recruitment of adapter molecules such as MYD88, IRAK1 or IRAK4. In turn, mediates the activation of NF-kappa-B and the three MAPK pathways p38, p42/p44 and JNK pathways. Within the cell, acts as an alarmin and cell death results in its liberation in the extracellular space after disruption of the cell membrane to induce inflammation and alert the host to injury or damage. In addition to its role as a danger signal, which occurs when the cytokine is passively released by cell necrosis, directly senses DNA damage and acts as signal for genotoxic stress without loss of cell integrity", "gene_name": "Il1a", "glycan_count": 0, "glycosylation_sites": [ { "position": 46, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 139, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P16598", "name": "Interleukin-1 beta (IL-1\u03b2)", "organism": "Rattus norvegicus", "uniprot_id": "P16598" }, { "function": "Serine protease inhibitor. Inhibits TMPRSS7. Is a primary inhibitor of tissue-type plasminogen activator (PLAT) and urokinase-type plasminogen activator (PLAU). As PLAT inhibitor, it is required for fibrinolysis down-regulation and is responsible for the controlled degradation of blood clots. As PLAU inhibitor, it is involved in the regulation of cell adhesion and spreading. Acts as a regulator of cell migration, independently of its role as protease inhibitor. It is required for stimulation of keratinocyte migration during cutaneous injury repair (By similarity). Involved in cellular and replicative senescence (PubMed:16862142). Plays a role in alveolar type 2 cells senescence in the lung (PubMed:28722352). Is involved in the regulation of cementogenic differentiation of periodontal ligament stem cells, and regulates odontoblast differentiation and dentin formation during odontogenesis (By similarity)", "gene_name": "Serpine1", "glycan_count": 1, "glycosylation_sites": [ { "position": 232, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 288, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 352, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P22777", "name": "Plasminogen activator inhibitor-1 (Serpine1/PAI-1)", "organism": "Mus musculus", "uniprot_id": "P22777" }, { "function": "Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage (PubMed:8675619). Although it has both phospholipase and triglyceride lipase activities it is primarily a triglyceride lipase with low but detectable phospholipase activity (By similarity). Mediates margination of triglyceride-rich lipoprotein particles in capillaries (PubMed:24726386). Recruited to its site of action on vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans (PubMed:20620994, PubMed:24726386, PubMed:27811232)", "gene_name": "Lpl", "glycan_count": 2, "glycosylation_sites": [ { "position": 70, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 386, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P11152", "name": "Lipoprotein lipase (Lpl)", "organism": "Mus musculus", "uniprot_id": "P11152" }, { "function": "Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates (PubMed:15834126, PubMed:19028692, PubMed:20876538, PubMed:22493088, PubMed:28420705). Highly expressed in epithelial cells of the small intestine and its activity is essential for the absorption of dietary fats (By similarity). In liver, plays a role in esterifying exogenous fatty acids to glycerol, and is required to synthesize fat for storage (PubMed:15834126). Also present in female mammary glands, where it produces fat in the milk (By similarity). May be involved in VLDL (very low density lipoprotein) assembly (By similarity). In contrast to DGAT2 it is not essential for survival (PubMed:11959864). Functions as the major acyl-CoA retinol acyltransferase (ARAT) in the skin, where it acts to maintain retinoid homeostasis and prevent retinoid toxicity leading to skin and hair disorders (PubMed:19028692). Exhibits additional acyltransferase activities, includin acyl CoA:monoacylglycerol acyltransferase (MGAT), wax monoester and wax diester synthases (PubMed:15834126). Also able to use 1-monoalkylglycerol (1-MAkG) as an acyl acceptor for the synthesis of monoalkyl-monoacylglycerol (MAMAG) (PubMed:28420705)", "gene_name": "Dgat1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Z2A7", "name": "ATP-binding cassette sub-family G member 1 (Abcg1)", "organism": "Mus musculus", "uniprot_id": "Q9Z2A7" }, { "function": "Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of MET (By similarity)", "gene_name": "Ptpn1", "glycan_count": 1, "glycosylation_sites": [], "id": "P35821", "name": "Protein tyrosine phosphatase 1B (PTPN1)", "organism": "Mus musculus", "uniprot_id": "P35821" }, { "function": "E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation (PubMed:10330192, PubMed:11146632, PubMed:11557750, PubMed:23990462, PubMed:26265139). Plays a role in the maintenance of mitochondrial morphology and promotes mitophagic removal of dysfunctional mitochondria; thereby acts as a protector against apoptosis in response to cellular stress (By similarity). Negatively regulates vascular smooth muscle contraction, via degradation of the transcriptional activator MYOCD and subsequent loss of transcription of genes involved in vascular smooth muscle contraction (By similarity). Promotes survival and proliferation of cardiac smooth muscle cells via ubiquitination and degradation of FOXO1, resulting in subsequent repression of FOXO1-mediated transcription of pro-apoptotic genes (PubMed:19483080). Ubiquitinates ICER-type isoforms of CREM and targets them for proteasomal degradation, thereby acts as a positive effector of MAPK/ERK-mediated inhibition of apoptosis in cardiomyocytes (PubMed:20724525). Inhibits lipopolysaccharide-induced apoptosis and hypertrophy in cardiomyocytes, via ubiquitination and subsequent proteasomal degradation of NFATC3 (PubMed:30980393). Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension (PubMed:10330192, PubMed:11146632, PubMed:11557750, PubMed:23990462). Ubiquitinates NOS1 in concert with Hsp70 and Hsp40 (PubMed:15466472). Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90 (PubMed:10330192, PubMed:11146632, PubMed:15466472). Ubiquitinates CHRNA3 targeting it for endoplasmic reticulum-associated degradation in cortical neurons, as part of the STUB1-VCP-UBXN2A complex (PubMed:26265139). Ubiquitinates and promotes ESR1 proteasomal degradation in response to age-related circulating estradiol (17-beta-estradiol/E2) decline, thereby promotes neuronal apoptosis in response to ischemic reperfusion injury (By similarity). Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation (PubMed:11557750, PubMed:23990462). Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome (PubMed:19713937). Mediates polyubiquitination of CYP3A4 (PubMed:19103148). Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation (PubMed:19567782). Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and promotes ubiquitin-mediated protein degradation (PubMed:27708256). Negatively regulates the suppressive function of regulatory T-cells (Treg) during inflammation by mediating the ubiquitination and degradation of FOXP3 in a HSPA1A/B-dependent manner (PubMed:23973223). Catalyzes monoubiquitination of SIRT6, preventing its degradation by the proteasome (PubMed:24043303). Likely mediates polyubiquitination and down-regulates plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity (PubMed:28813410). Negatively regulates TGF-beta signaling by modulating the basal level of SMAD3 via ubiquitin-mediated degradation (PubMed:24613385). Plays a role in the degradation of TP53 (PubMed:26634371). Mediates ubiquitination of RIPK3 leading to its subsequent proteasome-dependent degradation (PubMed:29883609). May regulate myosin assembly in striated muscles together with UBE4B and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation (PubMed:17369820). Ubiquitinates PPARG in macrophages playing a role in M2 macrophages polarization and angiogenesis (By similarity)", "gene_name": "STUB1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UNE7", "name": "STUB1 (STIP1 homology and U-box containing protein 1)", "organism": "Homo sapiens", "uniprot_id": "Q9UNE7" }, { "function": "Potential cell surface proteins that bind and internalize ligands in the process of receptor-mediated endocytosis", "gene_name": "LRP1B", "glycan_count": 17, "glycosylation_sites": [ { "position": 134, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 190, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 220, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 313, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 360, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 443, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 725, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 758, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 829, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 883, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 919, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1041, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1089, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1145, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1209, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1298, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1502, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1549, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1636, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1754, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1816, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1921, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1983, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2105, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2458, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2488, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2507, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2549, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2626, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2647, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2802, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2892, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3034, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3066, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3076, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3164, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3310, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3316, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3682, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3877, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3894, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3906, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4017, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4204, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4381, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 4420, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NZR2", "name": "SLC2A5 (GLUT5)", "organism": "Homo sapiens", "uniprot_id": "Q9NZR2" }, { "function": "Catalyzes the conjugation of leukotriene A4 with reduced glutathione (GSH) to form leukotriene C4 with high specificity (PubMed:23409838, PubMed:27365393, PubMed:27791009, PubMed:7937884, PubMed:9153254). Can also catalyze the transfer of a glutathionyl group from glutathione (GSH) to 13(S),14(S)-epoxy-docosahexaenoic acid to form maresin conjugate in tissue regeneration 1 (MCTR1), a bioactive lipid mediator that possess potent anti-inflammatory and proresolving actions (PubMed:27791009)", "gene_name": "LTC4S", "glycan_count": 0, "glycosylation_sites": [], "id": "Q16873", "name": "KHK (Ketohexokinase)", "organism": "Homo sapiens", "uniprot_id": "Q16873" }, { "function": "Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Required for chromosome congression and efficiently align the chromosomes on a metaphase plate", "gene_name": "CENPH", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H3R5", "name": "Centromere Protein HEC1", "organism": "Homo sapiens", "uniprot_id": "Q9H3R5" }, { "function": "One of the primary rRNA binding proteins, it binds directly to 3'-end of the 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center. Binds mRNA and the E site tRNA blocking its exit path in the ribosome. This blockage implies that this section of the ribosome must be able to move to release the deacetylated tRNA", "gene_name": "rpsG", "glycan_count": 0, "glycosylation_sites": [], "id": "P17291", "name": "HMG-CoA reductase (Hmgcr)", "organism": "Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)", "uniprot_id": "P17291" }, { "function": "Forms the heterodimeric complex core-binding factor (CBF) with CBFB. RUNX members modulate the transcription of their target genes through recognizing the core consensus binding sequence 5'-TGTGGT-3', or very rarely, 5'-TGCGGT-3', within their regulatory regions via their runt domain, while CBFB is a non-DNA-binding regulatory subunit that allosterically enhances the sequence-specific DNA-binding capacity of RUNX. The heterodimers bind to the core site of a number of enhancers and promoters, including murine leukemia virus, polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM-CSF promoters (By similarity). May be involved in the control of cellular proliferation and/or differentiation. In association with ZFHX3, up-regulates CDKN1A promoter activity following TGF-beta stimulation (PubMed:20599712). CBF complexes repress ZBTB7B transcription factor during cytotoxic (CD8+) T cell development. They bind to RUNX-binding sequence within the ZBTB7B locus acting as transcriptional silencer and allowing for cytotoxic T cell differentiation. CBF complexes binding to the transcriptional silencer is essential for recruitment of nuclear protein complexes that catalyze epigenetic modifications to establish epigenetic ZBTB7B silencing (By similarity). Necessary for the development and survival of sensory neurons expressing parvalbumin (By similarity)", "gene_name": "RUNX3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q13761", "name": "RUNX3", "organism": "Homo sapiens", "uniprot_id": "Q13761" }, { "function": "Catalyzes the synthesis of lactosylceramide (LacCer) via the transfer of galactose from UDP-galactose to glucosylceramide (GlcCer) (PubMed:1551920, PubMed:24498430, PubMed:3099851). LacCer is the starting point in the biosynthesis of all gangliosides (membrane-bound glycosphingolipids) which play pivotal roles in the CNS including neuronal maturation and axonal and myelin formation (By similarity)", "gene_name": "B4GALT6", "glycan_count": 1, "glycosylation_sites": [ { "position": 71, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 75, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 83, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 84, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 99, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 122, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 307, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 367, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UBX8", "name": "MANBA", "organism": "Homo sapiens", "uniprot_id": "Q9UBX8" }, { "function": "Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Two different adapter protein complexes link the clathrin lattice either to the plasma membrane or to the trans-Golgi network. Acts as a component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge (PubMed:15858577, PubMed:16968737, PubMed:21297582). The TACC3/ch-TOG/clathrin complex is required for the maintenance of kinetochore fiber tension (PubMed:23532825). Plays a role in early autophagosome formation (PubMed:20639872). Interaction with DNAJC6 mediates the recruitment of HSPA8 to the clathrin lattice and creates local destabilization of the lattice promoting uncoating (By similarity)", "gene_name": "CLTC", "glycan_count": 1, "glycosylation_sites": [], "id": "Q00610", "name": "CLTC", "organism": "Homo sapiens", "uniprot_id": "Q00610" }, { "function": "Implicated in immunoproteasome assembly and required for efficient antigen processing. The PA28 activator complex enhances the generation of class I binding peptides by altering the cleavage pattern of the proteasome", "gene_name": "PSME1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q06323", "name": "PSME1", "organism": "Homo sapiens", "uniprot_id": "Q06323" }, { "function": "May interact with single-stranded DNA from the far-upstream element (FUSE). May activate gene expression", "gene_name": "FUBP3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96I24", "name": "FUBP3", "organism": "Homo sapiens", "uniprot_id": "Q96I24" }, { "function": "Cytokine that is chemotactic for monocytes but not for neutrophils. Binds to CCR8", "gene_name": "CCL1", "glycan_count": 0, "glycosylation_sites": [ { "position": 52, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P22362", "name": "CCL1 (C-C motif chemokine ligand 1)", "organism": "Homo sapiens", "uniprot_id": "P22362" }, { "function": "Calcium-dependent lectin that acts as a pattern recognition receptor (PRR) of the innate immune system: specifically recognizes and binds alpha-mannans on C.albicans hypheas (PubMed:23911656, PubMed:28652405). Binding of C.albicans alpha-mannans to this receptor complex leads to phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) of FCER1G, triggering activation of SYK, CARD9 and NF-kappa-B, consequently driving maturation of antigen-presenting cells and shaping antigen-specific priming of T-cells toward effector T-helper 1 and T-helper 17 cell subtypes (By similarity). Recognizes also, in a mannose-dependent manner, allergens from house dust mite and fungi, by promoting cysteinyl leukotriene production (By similarity). Recognizes soluble elements from the eggs of Shistosoma mansoni altering adaptive immune responses (By similarity)", "gene_name": "CLEC6A", "glycan_count": 0, "glycosylation_sites": [ { "position": 131, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 170, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6EIG7", "name": "Dectin-2", "organism": "Homo sapiens", "uniprot_id": "Q6EIG7" }, { "function": "Acts as a transcriptional repressor. May function in the assembly and/or enzymatic activity of the mSin3A corepressor complex or in mediating interactions between the complex and other regulatory complexes", "gene_name": "SAP130", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9H0E3", "name": "Zinc finger antiviral protein (ZAP)", "organism": "Homo sapiens", "uniprot_id": "Q9H0E3" }, { "function": "Key transcriptional regulator of type I interferon (IFN)-dependent immune responses and plays a critical role in the innate immune response against DNA and RNA viruses (PubMed:28342865, PubMed:28768858). Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters (PubMed:17574024, PubMed:32972995). Can efficiently activate both the IFN-beta (IFNB) and the IFN-alpha (IFNA) genes and mediate their induction via both the virus-activated, MyD88-independent pathway and the TLR-activated, MyD88-dependent pathway. Induces transcription of ubiquitin hydrolase USP25 mRNA in response to lipopolysaccharide (LPS) or viral infection in a type I IFN-dependent manner (By similarity). Required during both the early and late phases of the IFN gene induction but is more critical for the late than for the early phase. Exists in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, becomes phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization where along with other coactivators it can activate transcription of the type I IFN and ISG genes. Can also play a role in regulating adaptive immune responses by inducing PSMB9/LMP2 expression, either directly or through induction of IRF1. Binds to the Q promoter (Qp) of EBV nuclear antigen 1 a (EBNA1) and may play a role in the regulation of EBV latency. Can activate distinct gene expression programs in macrophages and regulate the anti-tumor properties of primary macrophages (By similarity) (PubMed:11073981, PubMed:12374802, PubMed:15361868, PubMed:17404045)", "gene_name": "IRF7", "glycan_count": 1, "glycosylation_sites": [], "id": "Q92985", "name": "Interferon regulatory factor 7 (IRF7)", "organism": "Homo sapiens", "uniprot_id": "Q92985" }, { "function": "DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of both mitochondrial and nuclear genome stability. Efficiently unwinds G-quadruplex (G4) DNA structures and forked RNA-DNA hybrids. Resolves G4 structures, preventing replication pausing and double-strand breaks (DSBs) at G4 motifs. Involved in the maintenance of telomeric DNA. Inhibits telomere elongation, de novo telomere formation and telomere addition to DSBs via catalytic inhibition of telomerase. Reduces the processivity of telomerase by displacing active telomerase from DNA ends. Releases telomerase by unwinding the short telomerase RNA/telomeric DNA hybrid that is the intermediate in the telomerase reaction. Possesses an intrinsic strand annealing activity", "gene_name": "PIF1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H611", "name": "Growth factor receptor-bound protein 2-associated binding protein 3 (GAB3)", "organism": "Homo sapiens", "uniprot_id": "Q9H611" }, { "function": "Receptor for leukotriene B4, a potent chemoattractant involved in inflammation and immune response", "gene_name": "Ltb4r", "glycan_count": 0, "glycosylation_sites": [ { "position": 4, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 164, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O88855", "name": "GLS1 (Glutaminase 1)", "organism": "Mus musculus", "uniprot_id": "O88855" }, { "function": "Multifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair and genome stability. Proposed to be an universal biosensor for nucleic acids. Promotes host inflammatory response to sterile and infectious signals and is involved in the coordination and integration of innate and adaptive immune responses. In the cytoplasm functions as a sensor and/or chaperone for immunogenic nucleic acids implicating the activation of TLR9-mediated immune responses, and mediates autophagy. Acts as a danger associated molecular pattern (DAMP) molecule that amplifies immune responses during tissue injury. Released to the extracellular environment can bind DNA, nucleosomes, IL-1 beta, CXCL12, AGER isoform 2/sRAGE, lipopolysaccharide (LPS) and lipoteichoic acid (LTA), and activates cells through engagement of multiple surface receptors. In the extracellular compartment fully reduced HMGB1 (released by necrosis) acts as a chemokine, disulfide HMGB1 (actively secreted) as a cytokine, and sulfonyl HMGB1 (released from apoptotic cells) promotes immunological tolerance (PubMed:23446148, PubMed:23519706, PubMed:23994764, PubMed:25048472). Has proangiogenic activity (PubMed:16365390). May be involved in platelet activation. Binds to phosphatidylserine and phosphatidylethanolamide. Bound to RAGE mediates signaling for neuronal outgrowth. May play a role in accumulation of expanded polyglutamine (polyQ) proteins (By similarity)", "gene_name": "Hmgb1", "glycan_count": 1, "glycosylation_sites": [], "id": "P63158", "name": "HMGB1 (High Mobility Group Box 1)", "organism": "Mus musculus", "uniprot_id": "P63158" }, { "function": "Costimulatory molecule that belongs to the immunoglobulin superfamily that plays an important role in T-lymphocyte activation. Acts as the primary auxiliary signal augmenting the MHC/TCR signal in naive T-cells together with the CD28 receptor which is constitutively expressed on the cell surface of T-cells (PubMed:16339518). In turn, activates different signaling pathways such as NF-kappa-B or MAPK leading to the production of different cytokines. In addition, CD28/CD80 costimulatory signal stimulates glucose metabolism and ATP synthesis of T-cells by activating the PI3K/Akt signaling pathway. Acts also as a regulator of PDL1/PDCD1 interactions to limit excess engagement of PDL1 and its inhibitory role in immune responses. Expressed on B-cells, plays a critical role in regulating interactions between B-cells and T-cells in both early and late germinal center responses, which are crucial for the generation of effective humoral immune responses (PubMed:22450810)", "gene_name": "Cd80", "glycan_count": 0, "glycosylation_sites": [ { "position": 93, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 99, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 149, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 189, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 210, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 214, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q00609", "name": "CD80", "organism": "Mus musculus", "uniprot_id": "Q00609" }, { "function": "This is a receptor for interleukin-21", "gene_name": "IL21R", "glycan_count": 3, "glycosylation_sites": [ { "position": 73, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 97, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 125, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 135, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 214, "type": "C-linked (Man) tryptophan" } ], "id": "Q9HBE5", "name": "Interleukin-21 receptor (IL-21R)", "organism": "Homo sapiens", "uniprot_id": "Q9HBE5" }, { "function": "Deubiquitinase that plays a role in the regulation of several processes such as maintenance of synaptic function, cardiac function, inflammatory response or osteoclastogenesis (PubMed:31492742, PubMed:32494592, PubMed:37215988). Abrogates the ubiquitination of multiple proteins including WWTR1/TAZ, EGFR, HIF1A and beta-site amyloid precursor protein cleaving enzyme 1/BACE1. In addition, recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin to maintain a stable pool of monoubiquitin that is a key requirement for the ubiquitin-proteasome and the autophagy-lysosome pathways (By similarity). Regulates amyloid precursor protein/APP processing by promoting BACE1 degradation resulting in decreased amyloid beta production (By similarity). Plays a role in the immune response by regulating the ability of MHC I molecules to reach cross-presentation compartments competent for generating Ag-MHC I complexes (PubMed:31492742). Mediates the 'Lys-48'-linked deubiquitination of the transcriptional coactivator WWTR1/TAZ leading to its stabilization and inhibition of osteoclastogenesis (PubMed:37215988). Deubiquitinates and stabilizes epidermal growth factor receptor EGFR to prevent its degradation and to activate its downstream mediators (PubMed:32494592). Modulates oxidative activity in skeletal muscle by regulating key mitochondrial oxidative proteins (PubMed:33137160). Enhances the activity of hypoxia-inducible factor 1-alpha/HIF1A by abrogateing its VHL E3 ligase-mediated ubiquitination and consequently inhibiting its degradation (By similarity)", "gene_name": "Uchl1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9R0P9", "name": "Ddah1", "organism": "Mus musculus", "uniprot_id": "Q9R0P9" }, { "function": "Odorant receptor", "gene_name": "OR1G1", "glycan_count": 0, "glycosylation_sites": [ { "position": 5, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P47890", "name": "Oct2", "organism": "Homo sapiens", "uniprot_id": "P47890" }, { "function": "", "gene_name": "Zc3h7a", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8R2Q7", "name": "Mate1", "organism": "Mus musculus", "uniprot_id": "Q8R2Q7" }, { "function": "Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (By similarity)", "gene_name": "VHA-c''2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9SLA2", "name": "Kidney injury molecule-1 (Kim-1)", "organism": "Arabidopsis thaliana", "uniprot_id": "Q9SLA2" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P09038 (FGF2)", "name": "Fibroblast Growth Factor (FGF)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04085 (PDGFA)", "name": "Platelet-Derived Growth Factor (PDGF)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "KIAA2013", "glycan_count": 2, "glycosylation_sites": [ { "position": 363, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8IYS2", "name": "CTRP2 (C1QTNF2)", "organism": "Homo sapiens", "uniprot_id": "Q8IYS2" }, { "function": "Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene)", "gene_name": "ENOPH1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UHY7", "name": "AASS", "organism": "Homo sapiens", "uniprot_id": "Q9UHY7" }, { "function": "Acts as an E3 ubiquitin-protein ligase. Promotes SMAD4 ubiquitination, nuclear exclusion and degradation via the ubiquitin proteasome pathway. According to PubMed:16751102, does not promote a decrease in the level of endogenous SMAD4. May act as a transcriptional repressor. Inhibits the transcriptional response to TGF-beta/BMP signaling cascade. Plays a role in the control of cell proliferation. Its association with SMAD2 and SMAD3 stimulates erythroid differentiation of hematopoietic stem/progenitor (By similarity). Monoubiquitinates SMAD4 and acts as an inhibitor of SMAD4-dependent TGF-beta/BMP signaling cascade (Monoubiquitination of SMAD4 hampers its ability to form a stable complex with activated SMAD2/3 resulting in inhibition of TGF-beta/BMP signaling cascade)", "gene_name": "TRIM33", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UPN9", "name": "ECM2", "organism": "Homo sapiens", "uniprot_id": "Q9UPN9" }, { "function": "Extracellular matrix protein that plays significant roles in the vascular system and is required for the maintenance and stability of blood vessel (PubMed:28435016). Affects several essential steps in angiogenesis including endothelial cell proliferation, migration, and tube formation. Positively regulates angiogenesis by acting as a ligand for CD93 receptor (PubMed:28671670, PubMed:28912033)", "gene_name": "MMRN2", "glycan_count": 89, "glycosylation_sites": [ { "position": 63, "type": "O-linked (Fuc...) serine" }, { "position": 67, "type": "O-linked (Fuc) threonine" }, { "position": 115, "type": "O-linked (Fuc) threonine" }, { "position": 205, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 214, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 249, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 261, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 350, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 379, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 439, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 472, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 727, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 765, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 845, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9H8L6", "name": "MMRN1", "organism": "Homo sapiens", "uniprot_id": "Q9H8L6" }, { "function": "Spindle assembly factor required for normal assembly of mitotic spindles. Required for normal assembly of microtubules during apoptosis. Required for chromatin and/or kinetochore dependent microtubule nucleation. Mediates AURKA localization to spindle microtubules (PubMed:18663142, PubMed:19208764, PubMed:37728657). Activates AURKA by promoting its autophosphorylation at 'Thr-288' and protects this residue against dephosphorylation (PubMed:18663142, PubMed:19208764). TPX2 is inactivated upon binding to importin-alpha (PubMed:26165940). At the onset of mitosis, GOLGA2 interacts with importin-alpha, liberating TPX2 from importin-alpha, allowing TPX2 to activate AURKA kinase and stimulate local microtubule nucleation (PubMed:26165940)", "gene_name": "TPX2", "glycan_count": 4, "glycosylation_sites": [], "id": "Q9ULW0", "name": "TPX2", "organism": "Homo sapiens", "uniprot_id": "Q9ULW0" }, { "function": "Factor XII is a serum glycoprotein that participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then trypsin cleaves it to beta-factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa (PubMed:2019570, PubMed:21304106, PubMed:8427954)", "gene_name": "F12", "glycan_count": 27, "glycosylation_sites": [ { "position": 109, "type": "O-linked (Fuc) threonine" }, { "position": 249, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 299, "type": "O-linked (GalNAc...) threonine" }, { "position": 305, "type": "O-linked (GalNAc...) threonine" }, { "position": 308, "type": "O-linked (GalNAc...) serine" }, { "position": 328, "type": "O-linked (GalNAc...) threonine" }, { "position": 329, "type": "O-linked (GalNAc...) threonine" }, { "position": 337, "type": "O-linked (GalNAc...) threonine" }, { "position": 433, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P00748", "name": "Protein induced by vitamin K absence or antagonist-II (PIVKA-II)", "organism": "Homo sapiens", "uniprot_id": "P00748" }, { "function": "Resistance to tetracycline by an active tetracycline efflux. This is an energy-dependent process that decreases the accumulation of the antibiotic in whole cells. This protein functions as a metal-tetracycline/H(+) antiporter", "gene_name": "tetA", "glycan_count": 0, "glycosylation_sites": [], "id": "P02981", "name": "Outer membrane porin F", "organism": "Escherichia coli", "uniprot_id": "P02981" }, { "function": "Light-driven proton pump", "gene_name": "bop", "glycan_count": 0, "glycosylation_sites": [], "id": "P02945", "name": "Bacteriorhodopsin", "organism": "Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)", "uniprot_id": "P02945" }, { "function": "Kappa-casein stabilizes micelle formation, preventing casein precipitation in milk", "gene_name": "CSN3", "glycan_count": 0, "glycosylation_sites": [ { "position": 152, "type": "O-linked (GalNAc...) threonine" }, { "position": 155, "type": "O-linked (GalNAc...) serine" }, { "position": 156, "type": "O-linked (GalNAc...) threonine" }, { "position": 159, "type": "O-linked (GalNAc...) threonine" }, { "position": 165, "type": "O-linked (GalNAc...) threonine" }, { "position": 172, "type": "O-linked (GalNAc...) serine; alternate" }, { "position": 188, "type": "O-linked (GalNAc...) threonine" } ], "id": "Q8SPW8", "name": "CD79A", "organism": "Capra hircus", "uniprot_id": "P02670" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q5E9C6", "name": "CD3\u03b5", "organism": "", "uniprot_id": "" }, { "function": "Usually encoded in the trnK tRNA gene intron. Probably assists in splicing its own and other chloroplast group II introns", "gene_name": "matK", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8WIV4", "name": "CD34", "organism": "Cyrilla racemiflora", "uniprot_id": "Q8WIV4" }, { "function": "Inhibits hemopoiesis and stimulates chemotaxis. Chemotactic in vitro for thymocytes and activated T-cells, but not for B-cells, macrophages, or neutrophils. Shows preferential activity towards naive T-cells. May play a role in mediating homing of lymphocytes to secondary lymphoid organs. Binds to atypical chemokine receptor ACKR4 and mediates the recruitment of beta-arrestin (ARRB1/2) to ACKR4", "gene_name": "CCL21", "glycan_count": 0, "glycosylation_sites": [], "id": "O00585", "name": "CCL21", "organism": "Homo sapiens", "uniprot_id": "O00585" }, { "function": "Translation initiation regulator which represses non-AUG initiated translation and repeat-associated non-AUG (RAN) initiated translation by acting as a competitive inhibitor of eukaryotic translation initiation factor 5 (EIF5) function (PubMed:21745818, PubMed:28981728, PubMed:29470543, PubMed:34260931). Increases the accuracy of translation initiation by impeding EIF5-dependent translation from non-AUG codons by competing with it for interaction with EIF2S2 within the 43S pre-initiation complex (PIC) in an EIF3C-binding dependent manner (PubMed:21745818, PubMed:28981728, PubMed:34260931)", "gene_name": "BZW2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y6E2", "name": "USP36", "organism": "Homo sapiens", "uniprot_id": "Q9Y6E2" }, { "function": "Receptor for a number of inflammatory CC-chemokines including CCL3/MIP-1-alpha, CCL4/MIP-1-beta and RANTES and subsequently transduces a signal by increasing the intracellular calcium ion level. May play a role in the control of granulocytic lineage proliferation or differentiation. Participates in T-lymphocyte migration to the infection site by acting as a chemotactic receptor", "gene_name": "CCR5", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UBT9", "name": "UFM1", "organism": "Homo sapiens", "uniprot_id": "Q9UBT9" }, { "function": "Core component of a Cul9-RING ubiquitin-protein ligase complex composed of CUL9 and RBX1 (PubMed:38605244). The CUL9-RBX1 complex mediates ubiquitination and subsequent degradation of BIRC5 and is required to maintain microtubule dynamics and genome integrity. Acts downstream of the 3M complex, which inhibits the ubiquitination of BIRC5 (PubMed:24793696). The CUL9-RBX1 complex also mediates mono-ubiquitination of p53/TP53 (PubMed:38605244). Acts as a cytoplasmic anchor protein in p53/TP53-associated protein complex. Regulates the subcellular localization of p53/TP53 and its subsequent function (PubMed:12526791, PubMed:17332328). Ubiquitinates apurinic/apyrimidinic endodeoxyribonuclease APEX2 (PubMed:38605244). Ubiquitination by the CUL9-RBX1 complex is predominantly mediated by E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2D2 (PubMed:38605244)", "gene_name": "CUL9", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8IWT3", "name": "UFL1", "organism": "Homo sapiens", "uniprot_id": "Q8IWT3" }, { "function": "E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC7 E2 ligase and transfers it to substrates, promoting their degradation (PubMed:12459480, PubMed:12646171, PubMed:12975321, PubMed:14593114, PubMed:16289116, PubMed:16847254, PubMed:17059562, PubMed:17141218, PubMed:17170702, PubMed:22607976, PubMed:27827840, PubMed:26471130, PubMed:28827405). Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins (PubMed:12459480, PubMed:12646171, PubMed:12975321, PubMed:14593114, PubMed:16289116, PubMed:16847254, PubMed:17059562, PubMed:17141218, PubMed:17170702, PubMed:22607976, PubMed:26471130, PubMed:28842558). Also promotes the degradation of normal but naturally short-lived proteins such as SGK. Protects cells from ER stress-induced apoptosis. Protects neurons from apoptosis induced by polyglutamine-expanded huntingtin (HTT) or unfolded GPR37 by promoting their degradation (PubMed:17141218). Sequesters p53/TP53 in the cytoplasm and promotes its degradation, thereby negatively regulating its biological function in transcription, cell cycle regulation and apoptosis (PubMed:17170702). Mediates the ubiquitination and subsequent degradation of cytoplasmic NFE2L1 (By similarity). During the early stage of B cell development, required for degradation of the pre-B cell receptor (pre-BCR) complex, hence supporting further differentiation into mature B cells (By similarity)", "gene_name": "SYVN1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q86TM6", "name": "HRD1 (SYVN1)", "organism": "Homo sapiens", "uniprot_id": "Q86TM6" }, { "function": "Component of the large ribosomal subunit (PubMed:12962325, PubMed:23636399, PubMed:25901680, PubMed:25957688, PubMed:32669547). Required for proper rRNA processing and maturation of 28S and 5.8S rRNAs (PubMed:25424902)", "gene_name": "RPL27", "glycan_count": 1, "glycosylation_sites": [], "id": "P61353", "name": "RPL26", "organism": "Homo sapiens", "uniprot_id": "P61353" }, { "function": "Catalyzes the reduction of two molecules of cytochrome b5 using NADH as the electron donor", "gene_name": "CYB5R3", "glycan_count": 2, "glycosylation_sites": [], "id": "P00387", "name": "CYB5R3", "organism": "Homo sapiens", "uniprot_id": "P00387" }, { "function": "Phospholipid scramblase involved in autophagy by mediating autophagosomal membrane expansion (PubMed:22456507, PubMed:27510922, PubMed:29437695, PubMed:32513819, PubMed:32610138, PubMed:33106659, PubMed:33468622, PubMed:33850023). Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome (PubMed:16940348, PubMed:22456507, PubMed:33106659). Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through ATG2 (ATG2A or ATG2B) from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion (PubMed:33106659). Also required to supply phosphatidylinositol 4-phosphate to the autophagosome initiation site by recruiting the phosphatidylinositol 4-kinase beta (PI4KB) in a process dependent on ARFIP2, but not ARFIP1 (PubMed:30917996). In addition to autophagy, also plays a role in necrotic cell death (By similarity)", "gene_name": "ATG9A", "glycan_count": 2, "glycosylation_sites": [ { "position": 99, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q7Z3C6", "name": "Atg9A", "organism": "Homo sapiens", "uniprot_id": "Q7Z3C6" }, { "function": "Acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G (PubMed:10702419, PubMed:2039600, PubMed:2110563, PubMed:24121345, PubMed:3462719, PubMed:3533531). Modulates the inflammatory and immune responses after bacterial infection, and after infection by the intracellular parasite L.major. Down-regulates responses to bacterial lipopolysaccharide (LPS) (By similarity). Plays a role in regulating the activation of NF-kappa-B and inflammatory responses (PubMed:10702419, PubMed:24352879). Has antimicrobial activity against mycobacteria, but not against salmonella. Contributes to normal resistance against infection by M.tuberculosis. Required for normal resistance to infection by L.major. Required for normal wound healing, probably by preventing tissue damage by limiting protease activity (By similarity). Together with ELANE, required for normal differentiation and proliferation of bone marrow myeloid cells (PubMed:24352879)", "gene_name": "SLPI", "glycan_count": 0, "glycosylation_sites": [], "id": "P03973", "name": "Secretory leukocyte protease inhibitor (SLPI)", "organism": "Homo sapiens", "uniprot_id": "P03973" }, { "function": "Neutrophil and pancreatic elastase-specific inhibitor of skin. It may prevent elastase-mediated tissue proteolysis. Has been shown to inhibit the alpha-4-beta-2/CHRNA2-CHRNB2 nicotinic acetylcholine receptor and to produce a weak inhibition on Kv11.1/KCNH2/ERG1 and on the transient receptor potential cation channel subfamily V member 1 (TRPV1) (PubMed:29483648)", "gene_name": "PI3", "glycan_count": 0, "glycosylation_sites": [], "id": "P19957", "name": "Elafin", "organism": "Homo sapiens", "uniprot_id": "P19957" }, { "function": "Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion). Recruits other proteins such as TRIM15 to focal adhesion", "gene_name": "PXN", "glycan_count": 1, "glycosylation_sites": [], "id": "P49023", "name": "Paxillin", "organism": "Homo sapiens", "uniprot_id": "P49023" }, { "function": "Antiporter that exports dicarboxylate intermediates of the Krebs cycle in exchange for phosphate plus a proton across the inner membrane of mitochondria, a process driven by mitochondrial motive force with an overall impact on glycolysis, glutaminolysis and glutathione-dependent redox balance. Continuous export of oxaloacetate and related four-carbon dicarboxylates from mitochondrial matrix into the cytosol negatively regulates the oxidation of acetyl-CoA substrates via the Krebs cycle, lowering the ATP/ADP ratio and reactive oxygen species (ROS) production (PubMed:24395786). May mediate inducible proton entry into the mitochondrial matrix affecting ATP turnover as a protection mechanism against oxidative stress. The proton currents are most likely associated with fatty acid flipping across the inner membrane of mitochondria in a metabolic process regulated by free fatty acids and purine nucleotides (By similarity) (PubMed:11171965, PubMed:11278935, PubMed:22524567, PubMed:26182433, PubMed:33373220). Regulates the use of glucose as a source of energy. Required for glucose-induced DRP1-dependent mitochondrial fission and neuron activation in the ventromedial nucleus of the hypothalamus (VMH). This mitochondrial adaptation mechanism modulates the VMH pool of glucose-excited neurons with an impact on systemic glucose homeostasis (By similarity). Regulates ROS levels and metabolic reprogramming of macrophages during the resolution phase of inflammation. Attenuates ROS production in response to IL33 to preserve the integrity of the Krebs cycle required for persistent production of itaconate and subsequent GATA3-dependent differentiation of inflammation-resolving alternatively activated macrophages (By similarity). Can unidirectionally transport anions including L-malate, L-aspartate, phosphate and chloride ions (PubMed:22524567, PubMed:24395786, PubMed:26182433). Does not mediate adaptive thermogenesis (By similarity)", "gene_name": "UCP2", "glycan_count": 0, "glycosylation_sites": [], "id": "P55851", "name": "Uncoupling protein 2 (UCP2)", "organism": "Homo sapiens", "uniprot_id": "P55851" }, { "function": "Sequence-specific transcriptional activator (PubMed:24100448, PubMed:26316623, PubMed:28255014). Recognizes the DNA sequence 5'-C[CA]GGAAGT-3'", "gene_name": "FLI1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q01543", "name": "FLI1", "organism": "Homo sapiens", "uniprot_id": "Q01543" }, { "function": "Cytokine that may play a role in innate and adaptive immune responses. It induces various cytokines such as TNFA/TNF-alpha and IL8. It activates typical cytokine signal pathways of NF-kappa-B and p38 MAPK", "gene_name": "IL32", "glycan_count": 0, "glycosylation_sites": [], "id": "P24001", "name": "IL32", "organism": "Homo sapiens", "uniprot_id": "P24001" }, { "function": "Myeloid inhibitory C-type lectin receptor that acts as a negative regulator of myeloid cell activation (PubMed:14739280, PubMed:15238421, PubMed:16239426, PubMed:34234773, PubMed:38367667, PubMed:38386511, PubMed:39143217). Myeloid cell inhibition is required to limit proinflammatory pathways and protect against excessive inflammation (By similarity). Specifically recognizes and binds various structures, such as neutrophil extracellular traps (NETs) or monosodium urate crystals (PubMed:38367667, PubMed:38386511, PubMed:39143217). Also acts as a pattern-recognition receptor for pathogen-associated molecules, such as plasmodium hemozoin or mycobacterial micolic acid (PubMed:31269448, PubMed:36542980). Ligand-binding induces phosphorylation of its ITIM motif, followed by recruitment of tyrosine-protein phosphatases PTPN6 and PTPN11, which counteract tyrosine-protein kinase SYK, thereby preventing myeloid cell activation (PubMed:14739280, PubMed:16239426, PubMed:34234773). Acts as a pattern-recognition receptor for NETs in neutrophils: specifically recognizes DNA in NETs, leading to inhibit neutrophil activation and limit further NET formation (PubMed:39143217). This regulation is essential for controlling key neutrophil responses and limit NET-mediated inflammatory conditions (By similarity). Also recognizes dead cells by acting as a receptor for monosodium urate crystals, leading to down-regulate neutrophil activation (PubMed:38367667, PubMed:38386511). Binding to monosodium urate crystals also promotes the type I interferon response (By similarity). Acts as an inhibitor of natural killer (NK) cell cytotoxicity (PubMed:15238421). Also acts as an ihibitor of dendritic cell maturation in an IL10-dependent manner (PubMed:16239426)", "gene_name": "CLEC12A", "glycan_count": 0, "glycosylation_sites": [ { "position": 88, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 98, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 165, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q5QGZ9", "name": "MICL (CLEC12A)", "organism": "Homo sapiens", "uniprot_id": "Q5QGZ9" }, { "function": "Probable immunoglobulin-like cell surface receptor. On binding with CD47, mediates cell-cell adhesion. Engagement on T-cells by CD47 on antigen-presenting cells results in enhanced antigen-specific T-cell proliferation and costimulates T-cell activation", "gene_name": "SIRPG", "glycan_count": 1, "glycosylation_sites": [ { "position": 243, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 268, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 309, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 317, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9P1W8", "name": "SLAMF7", "organism": "Homo sapiens", "uniprot_id": "Q9P1W8" }, { "function": "Carries out a dual function: signal transduction and activation of transcription. Involved in IL4/interleukin-4- and IL3/interleukin-3-mediated signaling", "gene_name": "STAT6", "glycan_count": 1, "glycosylation_sites": [], "id": "P42226", "name": "STAT6", "organism": "Homo sapiens", "uniprot_id": "P42226" }, { "function": "ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (PubMed:21586654, PubMed:27693233). Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane (By similarity). In addition to its ADP:ATP antiporter activity, also involved in mitochondrial uncoupling and mitochondrial permeability transition pore (mPTP) activity (PubMed:31883789). Plays a role in mitochondrial uncoupling by acting as a proton transporter: proton transport uncouples the proton flows via the electron transport chain and ATP synthase to reduce the efficiency of ATP production and cause mitochondrial thermogenesis (By similarity). Proton transporter activity is inhibited by ADP:ATP antiporter activity, suggesting that SLC25A4/ANT1 acts as a master regulator of mitochondrial energy output by maintaining a delicate balance between ATP production (ADP:ATP antiporter activity) and thermogenesis (proton transporter activity) (By similarity). Proton transporter activity requires free fatty acids as cofactor, but does not transport it (By similarity). Also plays a key role in mPTP opening, a non-specific pore that enables free passage of the mitochondrial membranes to solutes of up to 1.5 kDa, and which contributes to cell death (PubMed:31883789). It is however unclear if SLC25A4/ANT1 constitutes a pore-forming component of mPTP or regulates it (By similarity). Acts as a regulator of mitophagy independently of ADP:ATP antiporter activity: promotes mitophagy via interaction with TIMM44, leading to inhibit the presequence translocase TIMM23, thereby promoting stabilization of PINK1 (By similarity)", "gene_name": "SLC25A4", "glycan_count": 1, "glycosylation_sites": [], "id": "P12235", "name": "SLC25A4", "organism": "Homo sapiens", "uniprot_id": "P12235" }, { "function": "Ubiquitin-like modifier that plays a role in intracellular transport of GABA(A) receptors and its interaction with the cytoskeleton (PubMed:9892355). Involved in autophagy: while LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation (PubMed:15169837, PubMed:20562859, PubMed:22948227). Through its interaction with the reticulophagy receptor TEX264, participates in the remodeling of subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover (PubMed:31006538). Also required for the local activation of the CUL3(KBTBD6/7) E3 ubiquitin ligase complex, regulating ubiquitination and degradation of TIAM1, a guanyl-nucleotide exchange factor (GEF) that activates RAC1 and downstream signal transduction (PubMed:25684205). Thereby, regulates different biological processes including the organization of the cytoskeleton, cell migration and proliferation (PubMed:25684205). Involved in apoptosis (PubMed:15977068)", "gene_name": "GABARAP", "glycan_count": 0, "glycosylation_sites": [], "id": "O95166", "name": "GABARAP", "organism": "Homo sapiens", "uniprot_id": "O95166" }, { "function": "May function as calcium sensor and modulator, contributing to cellular calcium signaling. May function by interacting with other proteins, such as TPR-containing proteins, and indirectly play a role in many physiological processes such as the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative", "gene_name": "S100A6", "glycan_count": 1, "glycosylation_sites": [], "id": "P06703", "name": "S100A6", "organism": "Homo sapiens", "uniprot_id": "P06703" }, { "function": "Hydrolyzes 6-sulfate groups in N-acetyl-d-glucosaminide units of heparin sulfate and keratan sulfate", "gene_name": "GNS", "glycan_count": 116, "glycosylation_sites": [ { "position": 111, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 117, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 183, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 198, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 210, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 279, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 317, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 362, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 387, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 405, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 422, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 449, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 480, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P15586", "name": "GNS", "organism": "Homo sapiens", "uniprot_id": "P15586" }, { "function": "Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (PubMed:12220505). Cleaves matrix extracellular phosphoglycoprotein MEPE (PubMed:12220505). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen (By similarity). Has also been implicated in tumor invasion and metastasis (PubMed:3972105)", "gene_name": "CTSB", "glycan_count": 12, "glycosylation_sites": [ { "position": 192, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P07858", "name": "CTSB", "organism": "Homo sapiens", "uniprot_id": "P07858" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y6Q8 (human)", "name": "PPAR\u03b3", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P07148 (human)", "name": "FABP1", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01308 (human)", "name": "INS (Insulin)", "organism": "", "uniprot_id": "" }, { "function": "Sphingomyelin synthase that primarily contributes to sphingomyelin synthesis and homeostasis at the plasma membrane. Catalyzes the reversible transfer of phosphocholine moiety in sphingomyelin biosynthesis: in the forward reaction transfers phosphocholine head group of phosphatidylcholine (PC) on to ceramide (CER) to form ceramide phosphocholine (sphingomyelin, SM) and diacylglycerol (DAG) as by-product, and in the reverse reaction transfers phosphocholine from SM to DAG to form PC and CER (PubMed:14685263, PubMed:17449912, PubMed:17982138, PubMed:18370930, PubMed:38388831). The direction of the reaction appears to depend on the levels of CER and DAG in the plasma membrane (PubMed:14685263, PubMed:17449912, PubMed:17982138, PubMed:18370930). Does not use free phosphorylcholine or CDP-choline as donors (PubMed:14685263). Can also transfer phosphoethanolamine head group of phosphatidylethanolamine (PE) on to ceramide (CER) to form ceramide phosphoethanolamine (CPE) (PubMed:19454763). Regulates receptor-mediated signal transduction via mitogenic DAG and proapoptotic CER, as well as via SM, a structural component of membrane rafts that serve as platforms for signal transduction and protein sorting (PubMed:17449912, PubMed:17982138). To a lesser extent, plays a role in secretory transport via regulation of DAG pool at the Golgi apparatus and its downstream effects on PRKD1 (PubMed:18370930, PubMed:21980337). Required for normal bone matrix mineralization (PubMed:30779713)", "gene_name": "SGMS2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8NHU3", "name": "GALNT14", "organism": "Homo sapiens", "uniprot_id": "Q8NHU3" }, { "function": "Might be involved in complement regulation", "gene_name": "CFHR3", "glycan_count": 35, "glycosylation_sites": [ { "position": 108, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 185, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 205, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 309, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q02985", "name": "CFHR3", "organism": "Homo sapiens", "uniprot_id": "Q02985" }, { "function": "Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling", "gene_name": "H4C1", "glycan_count": 1, "glycosylation_sites": [], "id": "P62805", "name": "H4C1 (Histone H4)", "organism": "Homo sapiens", "uniprot_id": "P62805" }, { "function": "Plays a role in the assembly of the HRD1 complex, a complex involved in the ubiquitin-proteasome-dependent process of ER-associated degradation (ERAD)", "gene_name": "FAM8A1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UBU6", "name": "NY-ESO-1", "organism": "Homo sapiens", "uniprot_id": "Q9UBU6" }, { "function": "Binds to activated (phosphorylated) protein-Tyr kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Necessary for the insulin-stimulated increase in glucose uptake and glycogen synthesis in insulin-sensitive tissues. Plays an important role in signaling in response to FGFR1, FGFR2, FGFR3, FGFR4, KITLG/SCF, KIT, PDGFRA and PDGFRB. Likewise, plays a role in ITGB2 signaling (PubMed:17626883, PubMed:19805105, PubMed:7518429). Modulates the cellular response to ER stress by promoting nuclear translocation of XBP1 isoform 2 in a ER stress- and/or insulin-dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement (PubMed:20348923)", "gene_name": "PIK3R1", "glycan_count": 1, "glycosylation_sites": [], "id": "P27986", "name": "PIK3R1 (Phosphoinositide-3-kinase regulatory subunit 1)", "organism": "Homo sapiens", "uniprot_id": "P27986" }, { "function": "Has mitogenic activity and may be involved in maintaining the integrity of the gastric mucosal epithelium", "gene_name": "GKN1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NS71", "name": "REG1\u03b1", "organism": "Homo sapiens", "uniprot_id": "Q9NS71" }, { "function": "Plays an important role in the regulation of dynamic actin-based, cytoskeletal activities. Agonist-dependent changes in LASP1 phosphorylation may also serve to regulate actin-associated ion transport activities, not only in the parietal cell but also in certain other F-actin-rich secretory epithelial cell types (By similarity)", "gene_name": "LASP1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q14847", "name": "LASP1", "organism": "Homo sapiens", "uniprot_id": "Q14847" }, { "function": "Putative regulatory subunit of protein phosphatase 6 (PP6) that may be involved in the recognition of phosphoprotein substrates", "gene_name": "ANKRD44", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8N8A2", "name": "SAMD13", "organism": "Homo sapiens", "uniprot_id": "Q8N8A2" }, { "function": "DNA-binding factor that regulates the expression of a subset of genes and plays a key role in tangential, radial, and lateral expansion of the brain neocortex. Regulates neural stem cells proliferation and the production of intermediate neural progenitors and basal radial glial cells affecting the process of cerebral cortex gyrification. May control the proliferation rate of cells by regulating their progression through key cell-cycle transition points (By similarity)", "gene_name": "TRNP1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6NT89", "name": "MEX3A", "organism": "Homo sapiens", "uniprot_id": "Q6NT89" }, { "function": "Ligand-activated transcription factor key mediator of energy metabolism in adipose tissues (PubMed:35675826). Receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Has a preference for poly-unsaturated fatty acids, such as gamma-linoleic acid and eicosapentanoic acid. Once activated by a ligand, the receptor binds to promoter elements of target genes. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as transcription activator for the acyl-CoA oxidase gene. Decreases expression of NPC1L1 once activated by a ligand", "gene_name": "PPARD", "glycan_count": 0, "glycosylation_sites": [], "id": "Q03181", "name": "PPAR beta/delta", "organism": "Homo sapiens", "uniprot_id": "Q03181" }, { "function": "Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone (By similarity). Exhibits high acyl-CoA specificity for polyunsaturated fatty acyl-CoA, especially docosahexaenoyl-CoA (22:6-CoA, DHA-CoA) (By similarity)", "gene_name": "AGPAT4", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NRZ5", "name": "PLCD4", "organism": "Homo sapiens", "uniprot_id": "Q9NRZ5" }, { "function": "Catalyzes the sequential decarboxylation of the four acetate side chains of uroporphyrinogen to form coproporphyrinogen and participates in the fifth step in the heme biosynthetic pathway (PubMed:11069625, PubMed:11719352, PubMed:14633982, PubMed:18004775, PubMed:21668429). Isomer I or isomer III of uroporphyrinogen may serve as substrate, but only coproporphyrinogen III can ultimately be converted to heme (PubMed:11069625, PubMed:11719352, PubMed:14633982, PubMed:21668429). In vitro also decarboxylates pentacarboxylate porphyrinogen I (PubMed:12071824)", "gene_name": "UROD", "glycan_count": 1, "glycosylation_sites": [], "id": "P06132", "name": "Uroporphyrinogen decarboxylase (UROD)", "organism": "Homo sapiens", "uniprot_id": "P06132" }, { "function": "Insulin-regulated facilitative glucose transporter, which plays a key role in removal of glucose from circulation (PubMed:2211693, PubMed:2645527, PubMed:2649253). Response to insulin is regulated by its intracellular localization: in the absence of insulin, it is efficiently retained intracellularly within storage compartments in muscle and fat cells (PubMed:2211693, PubMed:2645527, PubMed:2649253). Upon insulin stimulation, translocates from these compartments to the cell surface where it transports glucose from the extracellular milieu into the cell (PubMed:2211693, PubMed:2645527, PubMed:2649253)", "gene_name": "Slc2a4", "glycan_count": 1, "glycosylation_sites": [ { "position": 57, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P19357", "name": "GLUT4", "organism": "Rattus norvegicus", "uniprot_id": "P19357" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P35568 (IRS1)", "name": "IRS", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01009 (variant)", "name": "Z-alpha-1 antitrypsin (Z-AAT)", "organism": "", "uniprot_id": "" }, { "function": "Involved in DNA repair and RecF pathway recombination", "gene_name": "recO", "glycan_count": 0, "glycosylation_sites": [], "id": "P51838", "name": "Vesicular Monoamine Transporter 2 (VMAT2/SLC18A2)", "organism": "Coxiella burnetii (strain RSA 493 / Nine Mile phase I)", "uniprot_id": "P51838" }, { "function": "Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium, This receptor is controlled by G proteins. Unable to produce channel activity when expressed alone (PubMed:10659995). Forms a functional channel in association with KCNJ3/GIRK1 (By similarity)", "gene_name": "KCNJ9", "glycan_count": 0, "glycosylation_sites": [], "id": "Q92806", "name": "GIRK2 (KCNJ6)", "organism": "Homo sapiens", "uniprot_id": "Q92806" }, { "function": "Pre-mRNA alternative splicing regulator. Regulates alternative splicing of RBFOX2 to enhance the production of mRNA species that are targeted for nonsense-mediated decay (NMD)", "gene_name": "RBFOX3", "glycan_count": 0, "glycosylation_sites": [], "id": "A6NFN3", "name": "Neuronal Nuclei (NeuN/RBFOX3)", "organism": "Homo sapiens", "uniprot_id": "A6NFN3" }, { "function": "Transcriptional activator that binds to the consensus sequence 5'-AGATAG-3' and plays a key role in cardiac development and function (PubMed:24000169, PubMed:27984724, PubMed:35182466). In cooperation with TBX5, it binds to cardiac super-enhancers and promotes cardiomyocyte gene expression, while it down-regulates endocardial and endothelial gene expression (PubMed:27984724). Involved in bone morphogenetic protein (BMP)-mediated induction of cardiac-specific gene expression. Binds to BMP response element (BMPRE) DNA sequences within cardiac activating regions (By similarity). Acts as a transcriptional activator of ANF in cooperation with NKX2-5 (By similarity). Promotes cardiac myocyte enlargement (PubMed:20081228). Required during testicular development (PubMed:21220346). May play a role in sphingolipid signaling by regulating the expression of sphingosine-1-phosphate degrading enzyme, sphingosine-1-phosphate lyase (PubMed:15734735)", "gene_name": "GATA4", "glycan_count": 1, "glycosylation_sites": [], "id": "P43694", "name": "GATA4", "organism": "Homo sapiens", "uniprot_id": "P43694" }, { "function": "The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Following initial binding to host receptor, membrane fusion is mediated by the fusion machinery composed of gB and the heterodimer gH/gL. May also be involved in the fusion between the virion envelope and the outer nuclear membrane during virion morphogenesis", "gene_name": "gH", "glycan_count": 0, "glycosylation_sites": [ { "position": 18, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 45, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 217, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 317, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 499, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 522, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 760, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 783, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P09260", "name": "Varicella-zoster virus glycoprotein B (gB)", "organism": "Varicella-zoster virus (strain Dumas)", "uniprot_id": "P09260" }, { "function": "Abundant tegument protein. Trans-activates the immediate early genes (By similarity)", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P09264", "name": "Varicella-zoster virus glycoprotein L (gL)", "organism": "Varicella-zoster virus (strain Dumas)", "uniprot_id": "P09264" }, { "function": "Cell adhesion molecule that promotes cell-cell adhesion through heterophilic trans-interactions with nectins-like or other nectins, such as trans-interaction with NECTIN2 at Sertoli-spermatid junctions (PubMed:16216929). Trans-interaction with PVR induces activation of CDC42 and RAC small G proteins through common signaling molecules such as SRC and RAP1 (PubMed:16216929). Induces endocytosis-mediated down-regulation of PVR from the cell surface, resulting in reduction of cell movement and proliferation (PubMed:16216929). Involved in axon guidance by promoting contacts between the commissural axons and the floor plate cells (By similarity). Also involved in the formation of cell-cell junctions, including adherens junctions and synapses (By similarity). Promotes formation of checkerboard-like cellular pattern of hair cells and supporting cells in the auditory epithelium via heterophilic interaction with NECTIN1: NECTIN1 is present in the membrane of hair cells and associates with NECTIN3 on supporting cells, thereby mediating heterotypic adhesion between these two cell types (By similarity). Plays a role in the morphology of the ciliary body (By similarity)", "gene_name": "NECTIN3", "glycan_count": 13, "glycosylation_sites": [ { "position": 73, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 83, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 125, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 186, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 222, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 331, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NQS3", "name": "Nectin-4", "organism": "Homo sapiens", "uniprot_id": "Q9NQS3" }, { "function": "Receptor for TNFSF8/CD30L (PubMed:8543792). May play a role in the regulation of cellular growth and transformation of activated lymphoblasts. Regulates gene expression through activation of NF-kappa-B (By similarity)", "gene_name": "Tnfrsf8", "glycan_count": 1, "glycosylation_sites": [ { "position": 156, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 183, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 229, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q60846", "name": "Kidney Injury Molecule-1 (KIM-1)", "organism": "Mus musculus", "uniprot_id": "Q60846" }, { "function": "Induces caspases and apoptosis. Counters the protective effect of BCL2", "gene_name": "Bid", "glycan_count": 0, "glycosylation_sites": [], "id": "P70444", "name": "BH3 interacting domain death agonist (BID)", "organism": "Mus musculus", "uniprot_id": "P70444" }, { "function": "The insulin-like growth factors possess growth-promoting activity (PubMed:29440408). Major fetal growth hormone in mammals. Plays a key role in regulating fetoplacental development (Probable) (PubMed:12087403, PubMed:2330056). IGF2 is influenced by placental lactogen (Probable). Also involved in tissue differentiation (Probable). In adults, involved in glucose metabolism in adipose tissue, skeletal muscle and liver (Probable). Acts as a ligand for integrin which is required for IGF2 signaling (By similarity). Positively regulates myogenic transcription factor MYOD1 function by facilitating the recruitment of transcriptional coactivators, thereby controlling muscle terminal differentiation (PubMed:16901893). Inhibits myoblast differentiation and modulates metabolism via increasing the mitochondrial respiration rate (PubMed:32557799)", "gene_name": "Igf2", "glycan_count": 0, "glycosylation_sites": [], "id": "P09535", "name": "Insulin-like Growth Factor 2 (IGF-2)", "organism": "Mus musculus", "uniprot_id": "P09535" }, { "function": "Cytokine that acts as a ligand to CD40/TNFRSF5 (By similarity). Costimulates T-cell proliferation and cytokine production (By similarity). Its cross-linking on T-cells generates a costimulatory signal which enhances the production of IL4 and IL10 in conjunction with the TCR/CD3 ligation and CD28 costimulation (By similarity). Induces the activation of NF-kappa-B (By similarity). Induces the activation of kinases MAPK8 and PAK2 in T-cells (By similarity). Mediates B-cell proliferation in the absence of co-stimulus as well as IgE production in the presence of IL4 (PubMed:1374165). Involved in immunoglobulin class switching (PubMed:1374165)", "gene_name": "Cd40lg", "glycan_count": 0, "glycosylation_sites": [ { "position": 239, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P27548", "name": "CD40 ligand (CD40L/TNFSF5)", "organism": "Mus musculus", "uniprot_id": "P27548" }, { "function": "Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. In the heterodimer, FOS and JUN/AP-1 basic regions each seems to interact with symmetrical DNA half sites. On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex at the AP1/SMAD-binding site to regulate TGF-beta-mediated signaling. Has a critical function in regulating the development of cells destined to form and maintain the skeleton. It is thought to have an important role in signal transduction, cell proliferation and differentiation. In growing cells, activates phospholipid synthesis, possibly by activating CDS1 and PI4K2A. This activity requires Tyr-dephosphorylation and association with the endoplasmic reticulum", "gene_name": "FOS", "glycan_count": 2, "glycosylation_sites": [], "id": "P01100", "name": "FOS (Apo-1)", "organism": "Homo sapiens", "uniprot_id": "P01100" }, { "function": "Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state. Plays a role in stress resistance and actin organization (PubMed:17661394). Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins (By similarity)", "gene_name": "Hspb1", "glycan_count": 1, "glycosylation_sites": [], "id": "P14602", "name": "Heat Shock Protein 27 (HSP27)", "organism": "Mus musculus", "uniprot_id": "P14602" }, { "function": "Plays an important role in the degradation of dermatan and keratan sulfates", "gene_name": "GUSB", "glycan_count": 42, "glycosylation_sites": [ { "position": 173, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 272, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 420, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 631, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08236", "name": "\u03b2-glucuronidase", "organism": "Homo sapiens", "uniprot_id": "P08236" }, { "function": "", "gene_name": "4.5", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9T124", "name": "VEGF-B", "organism": "Yersinia phage phiYeO3-12", "uniprot_id": "Q9T124" }, { "function": "Receptor tyrosine kinase which binds promiscuously membrane-bound ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Activated by the ligand ephrin-A1/EFNA1 regulates migration, integrin-mediated adhesion, proliferation and differentiation of cells. Regulates cell adhesion and differentiation through DSG1/desmoglein-1 and inhibition of the ERK1/ERK2 (MAPK3/MAPK1, respectively) signaling pathway. May also participate in UV radiation-induced apoptosis and have a ligand-independent stimulatory effect on chemotactic cell migration. During development, may function in distinctive aspects of pattern formation and subsequently in development of several fetal tissues. Involved for instance in angiogenesis, in early hindbrain development and epithelial proliferation and branching morphogenesis during mammary gland development. Engaged by the ligand ephrin-A5/EFNA5 may regulate lens fiber cells shape and interactions and be important for lens transparency development and maintenance. With ephrin-A2/EFNA2 may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis", "gene_name": "EPHA2", "glycan_count": 8, "glycosylation_sites": [ { "position": 407, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 435, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P29317", "name": "EPHA2", "organism": "Homo sapiens", "uniprot_id": "P29317" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9BX84/Q96QT4", "name": "Magnesium transporter (TRPM6/7)", "organism": "", "uniprot_id": "" }, { "function": "Adhesion G-protein coupled receptor (aGPCR) for steroid hormone 17alpha-hydroxypregnenolone (17-OH), which is involved in cell adhesion and cell-cell interactions (PubMed:39389061). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as RhoA pathway (PubMed:28874577, PubMed:35418682, PubMed:39389061). ADGRG1 is coupled to G(12) and/or G(13) G proteins (GNA12 and GNA13, respectively) and mediates the activation Rho small GTPases (PubMed:22238662, PubMed:28424266, PubMed:35418682, PubMed:39389061). Acts as a potent suppressor of ferroptosis: binding to 17-OH-binding initiates signaling that down-regulates CD36 and alleviates ferroptosis-induced liver injury (By similarity). Ligand-binding also induces cell adhesion activity via association with proteins such as collagen III/COL3A1 and TGM2 (By similarity). Mediates cell matrix adhesion in developing neurons and hematopoietic stem cells (By similarity). Involved in cortical development, specifically in maintenance of the pial basement membrane integrity and in cortical lamination: association with COL3A1 in the developing brain inhibits neuronal migration via activation of the RhoA pathway (PubMed:24531968). Together with TGM2, acts as a regulator of myelination and myelin repair in oligodendrocyte precursor cells (By similarity). Acts as a hemostatic sensor of shear force: G protein-coupled receptor signaling is activated in response to shear force in platelets, promoting G(13) G protein signaling, and platelet shape change and aggregation in a COL3A1-dependent manner (PubMed:33097663). Acts as an inhibitor of VEGFA production thereby inhibiting angiogenesis through a signaling pathway mediated by PRKCA (PubMed:16757564, PubMed:19572147, PubMed:21724588). Plays a role in the maintenance of hematopoietic stem cells in bone marrow niche (By similarity). Plays an essential role in testis development (By similarity)", "gene_name": "ADGRG1", "glycan_count": 30, "glycosylation_sites": [ { "position": 39, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 148, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 171, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 234, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 303, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 324, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 341, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y653", "name": "GPR56 (ADGRG1)", "organism": "Homo sapiens", "uniprot_id": "Q9Y653" }, { "function": "The papain-like proteinase (PL-PRO) is responsible for the cleavages located at the N-terminus of replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF-3 (By similarity)", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P0C6F5", "name": "HBV Core protein", "organism": "Bat coronavirus 279/2005", "uniprot_id": "P0C6F5" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04490", "name": "Herpes Simplex Virus 1 glycoprotein D", "organism": "Human adenovirus B serotype 7", "uniprot_id": "P04490" }, { "function": "Seems to possess an anti-inflammatory activity as it can reverse the barrier-decreasing effects of TNF alpha. Might therefore contribute to the lack of inflammatory reaction seen during infection in spite the of extensive necrosis and massive virus production. Does not seem to be involved in activation of primary macrophages. Does not seem to interact specifically with neutrophils", "gene_name": "GP", "glycan_count": 0, "glycosylation_sites": [ { "position": 41, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 205, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 229, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 239, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 258, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 269, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "Q8JPX7", "name": "Lassa virus glycoprotein", "organism": "Reston ebolavirus (strain Reston-89)", "uniprot_id": "Q66800" }, { "function": "Nuclear receptor that binds DNA as a monomer to ROR response elements (RORE) containing a single core motif half-site 5'-AGGTCA-3' preceded by a short A-T-rich sequence. Key regulator of cellular differentiation, immunity, peripheral circadian rhythm as well as lipid, steroid, xenobiotics and glucose metabolism (PubMed:19381306, PubMed:19965867, PubMed:20203100, PubMed:22789990, PubMed:26160376). Considered to have intrinsic transcriptional activity, have some natural ligands like oxysterols that act as agonists (25-hydroxycholesterol) or inverse agonists (7-oxygenated sterols), enhancing or repressing the transcriptional activity, respectively (PubMed:19965867, PubMed:22789990). Recruits distinct combinations of cofactors to target gene regulatory regions to modulate their transcriptional expression, depending on the tissue, time and promoter contexts. Regulates the circadian expression of clock genes such as CRY1, BMAL1 and NR1D1 in peripheral tissues and in a tissue-selective manner. Competes with NR1D1 for binding to their shared DNA response element on some clock genes such as BMAL1, CRY1 and NR1D1 itself, resulting in NR1D1-mediated repression or RORC-mediated activation of the expression, leading to the circadian pattern of clock genes expression. Therefore influences the period length and stability of the clock. Involved in the regulation of the rhythmic expression of genes involved in glucose and lipid metabolism, including PLIN2 and AVPR1A (PubMed:19965867). Negative regulator of adipocyte differentiation through the regulation of early phase genes expression, such as MMP3. Controls adipogenesis as well as adipocyte size and modulates insulin sensitivity in obesity. In liver, has specific and redundant functions with RORA as positive or negative modulator of expression of genes encoding phase I and Phase II proteins involved in the metabolism of lipids, steroids and xenobiotics, such as SULT1E1. Also plays a role in the regulation of hepatocyte glucose metabolism through the regulation of G6PC1 and PCK1 (PubMed:19965867). Regulates the rhythmic expression of PROX1 and promotes its nuclear localization (PubMed:19381306, PubMed:19965867, PubMed:20203100, PubMed:22789990, PubMed:26160376). Plays an indispensable role in the induction of IFN-gamma dependent anti-mycobacterial systemic immunity (PubMed:26160376)", "gene_name": "RORC", "glycan_count": 0, "glycosylation_sites": [], "id": "P51449", "name": "Retinoic acid receptor-related orphan receptor gamma t (ROR\u03b3t)", "organism": "Homo sapiens", "uniprot_id": "P51449" }, { "function": "", "gene_name": "C1QTNF5", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9BXJ0", "name": "Complement C1q tumor necrosis factor-related protein 5 (CTRP5)", "organism": "Homo sapiens", "uniprot_id": "Q9BXJ0" }, { "function": "Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis", "gene_name": "G6PD", "glycan_count": 1, "glycosylation_sites": [], "id": "P11413", "name": "Glucose-6-phosphate dehydrogenase (G6PD)", "organism": "Homo sapiens", "uniprot_id": "P11413" }, { "function": "Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix", "gene_name": "Cox5a", "glycan_count": 1, "glycosylation_sites": [], "id": "P11240", "name": "Measles virus F protein", "organism": "Rattus norvegicus", "uniprot_id": "P11240" }, { "function": "Involved in oxygen transport from the lung to the various peripheral tissues", "gene_name": "HBAD", "glycan_count": 0, "glycosylation_sites": [], "id": "P15164", "name": "Measles virus M protein", "organism": "Apus apus", "uniprot_id": "P15164" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P11238", "name": "Measles virus H protein", "organism": "", "uniprot_id": "" }, { "function": "Produced by macrophages, IFN-alpha have antiviral activities. Interferon stimulates the production of two enzymes: a protein kinase and an oligoadenylate synthetase", "gene_name": "IFNA1", "glycan_count": 0, "glycosylation_sites": [], "id": "P01562", "name": "Interferon alpha", "organism": "Homo sapiens", "uniprot_id": "P01562" }, { "function": "Destroys radicals which are normally produced within the cells and which are toxic to biological systems", "gene_name": "Sod1", "glycan_count": 1, "glycosylation_sites": [], "id": "P07632", "name": "Superoxide dismutase (SOD)", "organism": "Rattus norvegicus", "uniprot_id": "P07632" }, { "function": "Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling", "gene_name": "H3C1", "glycan_count": 1, "glycosylation_sites": [], "id": "P68431", "name": "Histone H3 (H3K18)", "organism": "Homo sapiens", "uniprot_id": "P68431" }, { "function": "Chromatin-binding protein that acts as an adapter between distinct nucleosome components (H3K36me3 or H2A.Z) and chromatin-modifying complexes, contributing to the regulation of the levels of histone acetylation at actively transcribed genes (PubMed:30228260, PubMed:30327463). Competes with CHD4 and MBD3 for interaction with MTA1 to form a NuRD subcomplex, preventing the formation of full NuRD complex (containing CHD4 and MBD3), leading to recruitment of HDACs to gene promoters resulting in turn in the deacetylation of nearby H3K27 and H2A.Z (PubMed:30228260, PubMed:30327463). Plays a role in facilitating transcriptional elongation and repression of spurious transcription initiation through regulation of histone acetylation (By similarity). Essential for proper mitosis progression (PubMed:28645917)", "gene_name": "PWWP2A", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96N64", "name": "DCBLD1", "organism": "Homo sapiens", "uniprot_id": "Q96N64" }, { "function": "Core component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis (PubMed:11741547, PubMed:14657032, PubMed:22078559, PubMed:23080121, PubMed:24316220, PubMed:26240375, PubMed:27889449, PubMed:28867292, PubMed:29670289, PubMed:30464262, PubMed:30612738, PubMed:31353207, PubMed:37696958, PubMed:38128537, PubMed:9590181, PubMed:9651580, PubMed:9705271). The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases (PubMed:24316220, PubMed:28867292, PubMed:31353207, PubMed:38128537). The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage (PubMed:24316220, PubMed:27889449, PubMed:28867292, PubMed:36050397, PubMed:38128537). Within the MRN complex, MRE11 possesses both single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity (PubMed:11741547, PubMed:22078559, PubMed:24316220, PubMed:26240375, PubMed:27889449, PubMed:29670289, PubMed:31353207, PubMed:36563124, PubMed:9590181, PubMed:9651580, PubMed:9705271). After DSBs, MRE11 is loaded onto DSBs sites and cleaves DNA by cooperating with RBBP8/CtIP to initiate end resection (PubMed:27814491, PubMed:27889449, PubMed:30787182). MRE11 first endonucleolytically cleaves the 5' strand at DNA DSB ends to prevent non-homologous end joining (NHEJ) and licence HR (PubMed:24316220). It then generates a single-stranded DNA gap via 3' to 5' exonucleolytic degradation to create entry sites for EXO1- and DNA2-mediated 5' to 3' long-range resection, which is required for single-strand invasion and recombination (PubMed:24316220, PubMed:28867292). RBBP8/CtIP specifically promotes the endonuclease activity of MRE11 to clear protein-DNA adducts and generate clean double-strand break ends (PubMed:27814491, PubMed:27889449, PubMed:30787182). MRE11 endonuclease activity is also enhanced by AGER/RAGE (By similarity). The MRN complex is also required for DNA damage signaling via activation of the ATM and ATR kinases: the nuclease activity of MRE11 is not required to activate ATM and ATR (PubMed:14657032, PubMed:15064416, PubMed:15790808, PubMed:16622404). The MRN complex is also required for the processing of R-loops (PubMed:31537797). The MRN complex is involved in the activation of the cGAS-STING pathway induced by DNA damage during tumorigenesis: the MRN complex acts by displacing CGAS from nucleosome sequestration, thereby activating it (By similarity). In telomeres the MRN complex may modulate t-loop formation (PubMed:10888888)", "gene_name": "MRE11", "glycan_count": 1, "glycosylation_sites": [], "id": "P49959", "name": "MRE11", "organism": "Homo sapiens", "uniprot_id": "P49959" }, { "function": "Lectin that binds chitooligosaccharides and other glycans with high affinity, but not heparin. Has no chitinase activity", "gene_name": "CHI3L2", "glycan_count": 0, "glycosylation_sites": [ { "position": 35, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q15782", "name": "YKL-39 (CHI3L2)", "organism": "Homo sapiens", "uniprot_id": "Q15782" }, { "function": "Creatine:sodium symporter which mediates the uptake of creatine (PubMed:17465020, PubMed:22644605, PubMed:25861866, PubMed:7945388, PubMed:7953292, PubMed:9882430). Plays an important role in supplying creatine to the brain via the blood-brain barrier (By similarity)", "gene_name": "SLC6A8", "glycan_count": 3, "glycosylation_sites": [ { "position": 192, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 197, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 548, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P48029", "name": "Creatine transporter 1 (CRT-1)", "organism": "Homo sapiens", "uniprot_id": "P48029" }, { "function": "Component of the adaptor protein complex 4 (AP-4). Adaptor protein complexes are vesicle coat components involved both in vesicle formation and cargo selection. They control the vesicular transport of proteins in different trafficking pathways (PubMed:10066790, PubMed:10436028). AP-4 forms a non clathrin-associated coat on vesicles departing the trans-Golgi network (TGN) and may be involved in the targeting of proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system. It is also involved in protein sorting to the basolateral membrane in epithelial cells and the proper asymmetric localization of somatodendritic proteins in neurons. AP-4 is involved in the recognition and binding of tyrosine-based sorting signals found in the cytoplasmic part of cargos, but may also recognize other types of sorting signal (Probable)", "gene_name": "AP4E1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y588", "name": "Glycine transporter 2 (GlyT2)", "organism": "Homo sapiens", "uniprot_id": "Q9UPM8" }, { "function": "Phosphorylates PtdIns and PtdIns4P with a preference for PtdIns (PubMed:10805725, PubMed:11533253, PubMed:9830063). Does not phosphorylate PtdIns(4,5)P2 (PubMed:9830063). May be involved in EGF and PDGF signaling cascades (PubMed:10805725)", "gene_name": "PIK3C2B", "glycan_count": 1, "glycosylation_sites": [], "id": "O00750", "name": "APT1 (Acyl-protein thioesterase 1)", "organism": "Homo sapiens", "uniprot_id": "O00750" }, { "function": "May have a role in immune function. Probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation. May play a role in activation-induced lymphocyte depletion in the thymus, and in neuronal degeneration and glial cell activation in the brain", "gene_name": "CTSE", "glycan_count": 0, "glycosylation_sites": [ { "position": 90, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P14091", "name": "Cathepsin E (CtsE)", "organism": "Homo sapiens", "uniprot_id": "P14091" }, { "function": "Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization either through clathrin-dependent endocytosis or through clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore", "gene_name": "HA", "glycan_count": 0, "glycosylation_sites": [ { "position": 27, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 28, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 40, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 285, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 303, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 497, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P03452", "name": "Influenza B virus hemagglutinin", "organism": "Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)", "uniprot_id": "P03452" }, { "function": "Eukaryotic-type DNA polymerase involved in viral genomic replication. DNA synthesis is protein primed, and acts in a strand displacement replication. Assembles in complex with viral pTP, DBP, host NFIA and host POU2F1/OCT1 on viral origin of replication. The polymerase covalently transfers dCMP onto pTP, thereby initiating complementary strand synthesis", "gene_name": "POL", "glycan_count": 0, "glycosylation_sites": [], "id": "P03261", "name": "Adenovirus fiber protein", "organism": "Human adenovirus C serotype 2", "uniprot_id": "P03261" }, { "function": "", "gene_name": "osh3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9P7N7", "name": "Mycoplasma pneumoniae P1 adhesin", "organism": "Schizosaccharomyces pombe (strain 972 / ATCC 24843)", "uniprot_id": "O13944" }, { "function": "Positive regulator of sigma-B activity. Non-phosphorylated RsbV binds to RsbW, preventing its association with sigma-B. When phosphorylated, releases RsbW, which is then free to complex with and inactivate sigma-B (By similarity)", "gene_name": "rsbV", "glycan_count": 0, "glycosylation_sites": [], "id": "P0C0Q7", "name": "Streptococcus pyogenes M protein", "organism": "Staphylococcus epidermidis", "uniprot_id": "P0C0Q7" }, { "function": "Inhibits the supercoiling activity of DNA gyrase. Acts by inhibiting DNA gyrase at an early step, prior to (or at the step of) binding of DNA by the gyrase. It protects cells against toxins that target DNA gyrase, by inhibiting activity of these toxins and reducing the formation of lethal double-strand breaks in the cell", "gene_name": "sbmC", "glycan_count": 0, "glycosylation_sites": [], "id": "P0A213", "name": "Salmonella OmpA", "organism": "Salmonella typhi", "uniprot_id": "P0A213" }, { "function": "Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-BMAL1|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. CRY1 and CRY2 have redundant functions but also differential and selective contributions at least in defining the pace of the SCN circadian clock and its circadian transcriptional outputs. More potent transcriptional repressor in cerebellum and liver than CRY2, though more effective in lengthening the period of the SCN oscillator. On its side, CRY2 seems to play a critical role in tuning SCN circadian period by opposing the action of CRY1. With CRY2, is dispensable for circadian rhythm generation but necessary for the development of intercellular networks for rhythm synchrony. Capable of translocating circadian clock core proteins such as PER proteins to the nucleus. Interacts with CLOCK-BMAL1 independently of PER proteins and is found at CLOCK-BMAL1-bound sites, suggesting that CRY may act as a molecular gatekeeper to maintain CLOCK-BMAL1 in a poised and repressed state until the proper time for transcriptional activation. Represses the CLOCK-BMAL1 induced transcription of BHLHE40/DEC1. Represses the CLOCK-BMAL1 induced transcription of ATF4, MTA1, KLF10 and NAMPT (By similarity). May repress circadian target genes expression in collaboration with HDAC1 and HDAC2 through histone deacetylation. Mediates the clock-control activation of ATR and modulates ATR-mediated DNA damage checkpoint. In liver, mediates circadian regulation of cAMP signaling and gluconeogenesis by binding to membrane-coupled G proteins and blocking glucagon-mediated increases in intracellular cAMP concentrations and CREB1 phosphorylation. Inhibits hepatic gluconeogenesis by decreasing nuclear FOXO1 levels that down-regulates gluconeogenic gene expression (By similarity). Besides its role in the maintenance of the circadian clock, is also involved in the regulation of other processes. Represses glucocorticoid receptor NR3C1/GR-induced transcriptional activity by binding to glucocorticoid response elements (GREs). Plays a key role in glucose and lipid metabolism modulation, in part, through the transcriptional regulation of genes involved in these pathways, such as LEP or ACSL4 (By similarity). Represses PPARD and its target genes in the skeletal muscle and limits exercise capacity (By similarity). Plays an essential role in the generation of circadian rhythms in the retina (By similarity). Represses the transcriptional activity of NR1I2 (By similarity)", "gene_name": "CRY1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q16526", "name": "Cryptochrome-1 (CRY1)", "organism": "Homo sapiens", "uniprot_id": "Q16526" }, { "function": "Catalyzes the transfer of a phosphate from ATP to alpha-D-galactose and participates in the first committed step in the catabolism of galactose", "gene_name": "GALK1", "glycan_count": 1, "glycosylation_sites": [], "id": "P51570", "name": "Galactokinase 1 (GALK1)", "organism": "Homo sapiens", "uniprot_id": "P51570" }, { "function": "Sequence-specific DNA-binding transcriptional regulator that plays a key role in neurogenesis and neuroendocrine cell differentiation during embryonic and/or fetal development. Binds to the consensus sequence 5'-[TG][TC][TC][TT][GA]GGG[CG]A-3' in target promoters. Acts as a transcriptional repressor of NEUROD1 and INS expression via its interaction with cyclin CCND1 in a cell cycle-independent manner. Negatively regulates skeletal muscle-specific gene expression in endocrine cells of the pituitary by inhibiting the Notch signaling pathway. Represses target gene transcription by recruiting chromatin-modifying factors, such as HDAC1, HDAC2, HDAC3, KDM1A and RCOR1 histone deacetylases. Binds to its own promoter, suggesting autoregulation as a self-control feedback mechanism. Competes with histone H3 for the same binding site on the histone demethylase complex formed by KDM1A and RCOR1, and thereby inhibits demethylation of histone H3 at 'Lys-4' (PubMed:23721412). Promotes the generation and expansion of neuronal basal progenitor cells in the developing neocortex. Involved in the differentiation of endocrine cells of the developing anterior pituitary gland, of the pancreas and intestine, and of sympatho-adrenal cells in the peripheral nervous system. Promotes cell cycle signaling arrest and inhibition of cellular proliferation", "gene_name": "INSM1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q01101", "name": "Insulinoma-associated protein 1 (INSM-1)", "organism": "Homo sapiens", "uniprot_id": "Q01101" }, { "function": "May be involved in the regulation of cell proliferation. Has a cell-proliferation inhibition activity in vitro", "gene_name": "PSCA", "glycan_count": 1, "glycosylation_sites": [ { "position": 31, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O43653", "name": "Prostate stem cell antigen (PSCA)", "organism": "Homo sapiens", "uniprot_id": "O43653" }, { "function": "Immune suppressive molecule that inhibits antigen-specific T-cell activation by acting as a major ligand of LAG3 (PubMed:30580966). Responsible for LAG3 T-cell inhibitory function (PubMed:30580966). Binds LAG3 independently from MHC class II (MHC-II) (PubMed:30580966). Secreted by, and promotes growth of, hepatocytes (PubMed:11470158, PubMed:19880967)", "gene_name": "FGL1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q08830", "name": "FGL1", "organism": "Homo sapiens", "uniprot_id": "Q08830" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02468 (alpha2 subunit)", "name": "Laminin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UM47-2", "name": "Neurofascin-155 (NF155)", "organism": "", "uniprot_id": "" }, { "function": "Multifunctional enzyme that converts the viral RNA genome into dsDNA in viral cytoplasmic capsids. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3'- to 5'-endonucleasic mode. Neo-synthesized pregenomic RNA (pgRNA) are encapsidated together with the P protein, and reverse-transcribed inside the nucleocapsid. Initiation of reverse-transcription occurs first by binding the epsilon loop on the pgRNA genome, and is initiated by protein priming, thereby the 5'-end of (-)DNA is covalently linked to P protein. Partial (+)DNA is synthesized from the (-)DNA template and generates the relaxed circular DNA (RC-DNA) genome. After budding and infection, the RC-DNA migrates in the nucleus, and is converted into a plasmid-like covalently closed circular DNA (cccDNA). The activity of P protein does not seem to be necessary for cccDNA generation, and is presumably released from (+)DNA by host nuclear DNA repair machinery", "gene_name": "P", "glycan_count": 0, "glycosylation_sites": [], "id": "P03160", "name": "HBV core antigen (HBcAg)", "organism": "Woodchuck hepatitis B virus (isolate 1)", "uniprot_id": "P03160" }, { "function": "Calcium-dependent lectin displaying mannose-binding specificity. Induces the formation of Birbeck granules (BGs); is a potent regulator of membrane superimposition and zippering. Binds to sulfated as well as mannosylated glycans, keratan sulfate (KS) and beta-glucans. Facilitates uptake of antigens and is involved in the routing and/or processing of antigen for presentation to T cells. Major receptor on primary Langerhans cells for Candida species, Saccharomyces species, and Malassezia furfur. Protects against human immunodeficiency virus-1 (HIV-1) infection. Binds to high-mannose structures present on the envelope glycoprotein which is followed by subsequent targeting of the virus to the Birbeck granules leading to its rapid degradation", "gene_name": "CD207", "glycan_count": 2, "glycosylation_sites": [ { "position": 87, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 113, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 180, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UJ71", "name": "Kidney Injury Molecule-1 (KIM-1)", "organism": "Homo sapiens", "uniprot_id": "Q9UJ71" }, { "function": "Transcriptional regulator which controls the expression of hepatic genes during the transition of endodermal cells to hepatic progenitor cells, facilitating the recruitment of RNA pol II to the promoters of target genes (PubMed:30597922). Activates the transcription of CYP2C38 (By similarity). Represses the CLOCK-BMAL1 transcriptional activity and is essential for circadian rhythm maintenance and period regulation in the liver and colon cells (PubMed:30530698)", "gene_name": "HNF4A", "glycan_count": 1, "glycosylation_sites": [], "id": "P41235", "name": "HNF4\u03b1", "organism": "Homo sapiens", "uniprot_id": "P41235" }, { "function": "Plays a role in the control of cell growth and differentiation. Promotes osteoblast cell differentiation and terminal mineralization", "gene_name": "NELL1", "glycan_count": 2, "glycosylation_sites": [ { "position": 40, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 53, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 83, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 224, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 294, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 372, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 511, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 562, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 609, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 708, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 732, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 758, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q92832", "name": "Neural epidermal growth factor-like 1 (NELL1)", "organism": "Homo sapiens", "uniprot_id": "Q92832" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P49848/P57663", "name": "Exostosin 1/2 (EXT1/EXT2)", "organism": "", "uniprot_id": "" }, { "function": "Pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. Has bactericidal activity towards Gram-positive bacteria. May kill Gram-positive bacteria by interfering with peptidoglycan biosynthesis. Also binds to Gram-negative bacteria, and has bacteriostatic activity towards Gram-negative bacteria. Plays a role in innate immunity", "gene_name": "PGLYRP3", "glycan_count": 0, "glycosylation_sites": [ { "position": 113, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q96LB9", "name": "Peptidoglycan recognition protein 1 (PGLYRP1)", "organism": "Homo sapiens", "uniprot_id": "Q96LB9" }, { "function": "Exhibits arylsulfatase activity and highly specific endoglucosamine-6-sulfatase activity (PubMed:12368295, PubMed:12686563). It can remove sulfate from the C-6 position of glucosamine within specific subregions of intact heparin (PubMed:12368295, PubMed:12686563). Diminishes HSPG (heparan sulfate proteoglycans) sulfation, inhibits signaling by heparin-dependent growth factors, diminishes proliferation, and facilitates apoptosis in response to exogenous stimulation (PubMed:12686563)", "gene_name": "SULF1", "glycan_count": 44, "glycosylation_sites": [ { "position": 64, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 111, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 131, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 148, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 170, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 197, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 240, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 623, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 773, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 783, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8IWU6", "name": "Sulfatase 1 (SULF1)", "organism": "Homo sapiens", "uniprot_id": "Q8IWU6" }, { "function": "Has RNA-dependent ATPase activity. Represses the transcriptional activity of nuclear receptors", "gene_name": "DDX54", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8TDD1", "name": "Seizure-related 6-like protein 2 (SEZ6L2)", "organism": "Homo sapiens", "uniprot_id": "Q8TDD1" }, { "function": "May have a role in promoting tumor progression. May block the TGFB1-enhanced cell growth", "gene_name": "HYAL1", "glycan_count": 4, "glycosylation_sites": [ { "position": 99, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 216, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 350, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q12794", "name": "Hyaluronidase 1 (HYAL1)", "organism": "Homo sapiens", "uniprot_id": "Q12794" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02453/P02465", "name": "Type I Collagen (COL1A1/COL1A2)", "organism": "", "uniprot_id": "" }, { "function": "Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs", "gene_name": "fimA", "glycan_count": 0, "glycosylation_sites": [], "id": "P04128", "name": "FimH", "organism": "Escherichia coli (strain K12)", "uniprot_id": "P04128" }, { "function": "Required for the biogenesis of type 1 fimbriae. Binds and interact with FimH", "gene_name": "fimC", "glycan_count": 0, "glycosylation_sites": [], "id": "P31697", "name": "PapC", "organism": "Escherichia coli (strain K12)", "uniprot_id": "P31697" }, { "function": "Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture by forming a pore", "gene_name": "hlyA", "glycan_count": 0, "glycosylation_sites": [], "id": "P09983", "name": "HlyA", "organism": "Escherichia coli", "uniprot_id": "P09983" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P24270 (bovine)", "name": "Catalase", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04866 (H), P11250 (F)", "name": "Measles Virus Glycoproteins (Hemagglutinin, Fusion protein)", "organism": "", "uniprot_id": "" }, { "function": "Acts as a ligand for C-C chemokine receptor CCR6. Signals through binding and activation of CCR6 and induces a strong chemotactic response and mobilization of intracellular calcium ions (PubMed:11035086, PubMed:11352563, PubMed:20068036). The ligand-receptor pair CCL20-CCR6 is responsible for the chemotaxis of dendritic cells (DC), effector/memory T-cells and B-cells and plays an important role at skin and mucosal surfaces under homeostatic and inflammatory conditions, as well as in pathology, including cancer and various autoimmune diseases (PubMed:21376174). CCL20 acts as a chemotactic factor that attracts lymphocytes and, slightly, neutrophils, but not monocytes (PubMed:11352563, PubMed:9038201). Involved in the recruitment of both the pro-inflammatory IL17 producing helper T-cells (Th17) and the regulatory T-cells (Treg) to sites of inflammation. Required for optimal migration of thymic natural regulatory T cells (nTregs) and DN1 early thymocyte progenitor cells (By similarity). C-terminal processed forms have been shown to be equally chemotactically active for leukocytes (PubMed:11035086). Positively regulates sperm motility and chemotaxis via its binding to CCR6 which triggers Ca2+ mobilization in the sperm which is important for its motility (PubMed:23765988, PubMed:25122636). Inhibits proliferation of myeloid progenitors in colony formation assays (PubMed:9129037). May be involved in formation and function of the mucosal lymphoid tissues by attracting lymphocytes and dendritic cells towards epithelial cells (By similarity). Possesses antibacterial activity towards E.coli ATCC 25922 and S.aureus ATCC 29213 (PubMed:12149255)", "gene_name": "CCL20", "glycan_count": 0, "glycosylation_sites": [], "id": "P78556", "name": "Chemokine ligand 20 (CCL20)", "organism": "Homo sapiens", "uniprot_id": "P78556" }, { "function": "V region of the variable domain of T cell receptor (TR) alpha chain that participates in the antigen recognition (PubMed:24600447). Alpha-beta T cell receptors are antigen specific receptors which are essential to the immune response and are present on the cell surface of T lymphocytes. Recognize peptide-major histocompatibility (MH) (pMH) complexes that are displayed by antigen presenting cells (APC), a prerequisite for efficient T cell adaptive immunity against pathogens (PubMed:25493333). Binding of alpha-beta TR to pMH complex initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen-activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell growth and differentiation (PubMed:23524462). The T cell repertoire is generated in the thymus, by V-(D)-J rearrangement. This repertoire is then shaped by intrathymic selection events to generate a peripheral T cell pool of self-MH restricted, non-autoaggressive T cells. Post-thymic interaction of alpha-beta TR with the pMH complexes shapes TR structural and functional avidity (PubMed:15040585)", "gene_name": "TRAV29DV5", "glycan_count": 0, "glycosylation_sites": [ { "position": 93, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P04437", "name": "Herpes simplex virus glycoprotein D (gD)", "organism": "Homo sapiens", "uniprot_id": "P04437" }, { "function": "Chemokine-binding protein that inhibits neutrophils' chemotaxis", "gene_name": "gG", "glycan_count": 0, "glycosylation_sites": [ { "position": 28, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 49, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P06484", "name": "Herpes simplex virus glycoprotein H (gH)", "organism": "Human herpesvirus 1 (strain 17)", "uniprot_id": "P06484" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P06485", "name": "Herpes simplex virus glycoprotein L (gL)", "organism": "Human herpesvirus 1 (strain 17)", "uniprot_id": "P06485" }, { "function": "Required for normal progression through mitosis. Involved in chromosome alignment and cytokinesis via regulation of microtubules polymerization", "gene_name": "ANKRD53", "glycan_count": 2, "glycosylation_sites": [], "id": "Q8N9V6", "name": "SEL1L3", "organism": "Homo sapiens", "uniprot_id": "Q8N9V6" }, { "function": "ADP-ribosyltransferase that mediates mono-ADP-ribosylation of glutamate residues on target proteins (PubMed:16061477, PubMed:18851833, PubMed:25043379, PubMed:27796300). In contrast to PARP1 and PARP2, it is not able to mediate poly-ADP-ribosylation (PubMed:25043379). Has been shown to catalyze the mono-ADP-ribosylation of STAT1 at 'Glu-657' and 'Glu-705', thus decreasing STAT1 phosphorylation which negatively regulates pro-inflammatory cytokine production in macrophages in response to IFNG stimulation (PubMed:27796300). However, the role of ADP-ribosylation in the prevention of STAT1 phosphorylation has been called into question and it has been suggested that the inhibition of phosphorylation may be the result of sumoylation of STAT1 'Lys-703' (PubMed:29858569). Mono-ADP-ribosylates STAT6; enhancing STAT6-dependent transcription (PubMed:27796300). In macrophages, positively regulates MRC1 expression in response to IL4 stimulation by promoting STAT6 phosphorylation (PubMed:27796300). Mono-ADP-ribosylates PARP9 (PubMed:27796300)", "gene_name": "PARP14", "glycan_count": 2, "glycosylation_sites": [], "id": "Q460N5", "name": "PARP14", "organism": "Homo sapiens", "uniprot_id": "Q460N5" }, { "function": "Probable adapter protein located at the actin cytoskeleton that promotes cell attachment. Necessary for the migratory capacity of epithelial cells. Overexpression enhances cell adhesion to collagen and fibronectin and suppresses anchorage independent growth. May contribute to tumor cell migratory capacity", "gene_name": "PDLIM2", "glycan_count": 2, "glycosylation_sites": [], "id": "Q96JY6", "name": "PDLIM1", "organism": "Homo sapiens", "uniprot_id": "Q96JY6" }, { "function": "Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity", "gene_name": "FOLH1B", "glycan_count": 1, "glycosylation_sites": [ { "position": 28, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 151, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 168, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 305, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 330, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9HBA9", "name": "TRPV4", "organism": "Homo sapiens", "uniprot_id": "Q9HBA9" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q92508/Q9H244", "name": "Piezo1/2", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q99259/Q05329", "name": "Glutamic Acid Decarboxylase (GAD)", "organism": "", "uniprot_id": "" }, { "function": "Glutamine synthetase that catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine (PubMed:16267323, PubMed:30158707, PubMed:36289327). Its role depends on tissue localization: in the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, it is one of the enzymes responsible for the removal of ammonia (By similarity). Plays a key role in ammonium detoxification during erythropoiesis: the glutamine synthetase activity is required to remove ammonium generated by porphobilinogen deaminase (HMBS) during heme biosynthesis to prevent ammonium accumulation and oxidative stress (By similarity). Essential for proliferation of fetal skin fibroblasts (PubMed:18662667). Independently of its glutamine synthetase activity, required for endothelial cell migration during vascular development: acts by regulating membrane localization and activation of the GTPase RHOJ, possibly by promoting RHOJ palmitoylation (PubMed:30158707). May act as a palmitoyltransferase for RHOJ: able to autopalmitoylate and then transfer the palmitoyl group to RHOJ (PubMed:30158707). Plays a role in ribosomal 40S subunit biogenesis (PubMed:26711351). Through the interaction with BEST2, inhibits BEST2 channel activity by affecting the gating at the aperture in the absence of intracellular L-glutamate, but sensitizes BEST2 to intracellular L-glutamate, which promotes the opening of BEST2 and thus relieves its inhibitory effect on BEST2 (PubMed:36289327)", "gene_name": "GLUL", "glycan_count": 1, "glycosylation_sites": [], "id": "P15104", "name": "Glutamine Synthetase (GS)", "organism": "Homo sapiens", "uniprot_id": "P15104" }, { "function": "Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase. Promotes cell proliferation", "gene_name": "DRD3", "glycan_count": 0, "glycosylation_sites": [ { "position": 12, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 19, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 97, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 173, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P35462", "name": "Dopamine Receptor D3", "organism": "Homo sapiens", "uniprot_id": "P35462" }, { "function": "In the cytoplasm, catalyzes the conversion of glucose-6-phosphate to fructose-6-phosphate, the second step in glycolysis, and the reverse reaction during gluconeogenesis (PubMed:28803808). Besides it's role as a glycolytic enzyme, also acts as a secreted cytokine: acts as an angiogenic factor (AMF) that stimulates endothelial cell motility (PubMed:11437381). Acts as a neurotrophic factor, neuroleukin, for spinal and sensory neurons (PubMed:11004567, PubMed:3352745). It is secreted by lectin-stimulated T-cells and induces immunoglobulin secretion (PubMed:11004567, PubMed:3352745)", "gene_name": "GPI", "glycan_count": 4, "glycosylation_sites": [], "id": "P06744", "name": "Phosphohexose isomerase (PGI/GPI)", "organism": "Homo sapiens", "uniprot_id": "P06744" }, { "function": "Triosephosphate isomerase is an extremely efficient metabolic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis and gluconeogenesis", "gene_name": "TPI1", "glycan_count": 2, "glycosylation_sites": [], "id": "P60174", "name": "Triosephosphate isomerase (TPI1)", "organism": "Homo sapiens", "uniprot_id": "P60174" }, { "function": "Microtubule-associated protein required for initial steps of neuronal dispersion and cortex lamination during cerebral cortex development. May act by competing with the putative neuronal protein kinase DCLK1 in binding to a target protein. May in that way participate in a signaling pathway that is crucial for neuronal interaction before and during migration, possibly as part of a calcium ion-dependent signal transduction pathway. May be part with PAFAH1B1/LIS-1 of overlapping, but distinct, signaling pathways that promote neuronal migration", "gene_name": "DCX", "glycan_count": 0, "glycosylation_sites": [], "id": "O43602", "name": "Doublecortin (DCX)", "organism": "Homo sapiens", "uniprot_id": "O43602" }, { "function": "Binds to the dendritic targeting element and may play a role in mRNA trafficking (By similarity). Part of a ternary complex that binds to the downstream control sequence (DCS) of the pre-mRNA. Mediates exon inclusion in transcripts that are subject to tissue-specific alternative splicing. May interact with single-stranded DNA from the far-upstream element (FUSE). May activate gene expression. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly by recruiting degradation machinery to ARE-containing mRNAs", "gene_name": "KHSRP", "glycan_count": 3, "glycosylation_sites": [], "id": "Q92945", "name": "Brain Lipid-Binding Protein (BLBP)", "organism": "Homo sapiens", "uniprot_id": "Q92945" }, { "function": "Essential component of the apolipoprotein B mRNA editing enzyme complex which is responsible for the postranscriptional editing of a CAA codon for Gln to a UAA codon for stop in APOB mRNA. Binds to APOB mRNA and is probably responsible for docking the catalytic subunit, APOBEC1, to the mRNA to allow it to deaminate its target cytosine. The complex also protects the edited APOB mRNA from nonsense-mediated decay", "gene_name": "A1CF", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NQ94", "name": "Neuronal Nuclei (NeuN/RBFOX3)", "organism": "Homo sapiens", "uniprot_id": "Q9NQ94" }, { "function": "Type I receptor for TGF-beta family ligands BMP9/GDF2 and BMP10 and important regulator of normal blood vessel development. On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. May bind activin as well", "gene_name": "ACVRL1", "glycan_count": 0, "glycosylation_sites": [ { "position": 98, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P37023", "name": "ALK1 (ACVRL1)", "organism": "Homo sapiens", "uniprot_id": "P37023" }, { "function": "On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Can also mediate signaling through the activation of the p38MAPK cascade (PubMed:12045205). Binds to BMP7, BMP2 and, less efficiently, BMP4. Binding is weak but enhanced by the presence of type I receptors for BMPs. Mediates induction of adipogenesis by GDF6. Promotes signaling also by binding to activin A/INHBA (PubMed:24018044)", "gene_name": "BMPR2", "glycan_count": 7, "glycosylation_sites": [ { "position": 55, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 110, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 126, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13873", "name": "BMPR2", "organism": "Homo sapiens", "uniprot_id": "Q13873" }, { "function": "May play a role in the trafficking of activated/effector T-lymphocytes to inflammatory sites and other aspects of activated T-lymphocyte physiology. Chemotactic for monocytes, dendritic cells and natural killer cells. Mild chemoattractant for primary activated T-lymphocytes and a potent chemoattractant for chronically activated T-lymphocytes but has no chemoattractant activity for neutrophils, eosinophils, and resting T-lymphocytes. Binds to CCR4. Processed forms MDC(3-69), MDC(5-69) and MDC(7-69) seem not be active", "gene_name": "CCL22", "glycan_count": 0, "glycosylation_sites": [], "id": "O00626", "name": "CCL22", "organism": "Homo sapiens", "uniprot_id": "O00626" }, { "function": "Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle (By similarity). During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins (By similarity). Can migrate to the cell nucleus where it modulates host functions (By similarity). Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway (PubMed:23522008)", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [ { "position": 138, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 917, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 962, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 994, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P06935", "name": "Japanese encephalitis virus envelope protein", "organism": "West Nile virus", "uniprot_id": "P06935" }, { "function": "Hydrolyzes DNA under acidic conditions with a preference for double-stranded DNA. Plays a major role in the clearance of nucleic acids generated through apoptosis, hence preventing autoinflammation. Necessary for proper fetal development and for definitive erythropoiesis in fetal liver and bone marrow, where it degrades nuclear DNA expelled from erythroid precursor cells", "gene_name": "Dnase2", "glycan_count": 0, "glycosylation_sites": [ { "position": 89, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 215, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 269, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 293, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9QZK8", "name": "Langat virus envelope protein", "organism": "Rattus norvegicus", "uniprot_id": "Q9QZK8" }, { "function": "Chemotactic activity for lymphocytes but not for monocytes or neutrophils. In thymus, mediates medullary accumulation of thymic dendritic cells and contributes to regulatoy T cell development, playing a role in self-tolerance establishment", "gene_name": "XCL1", "glycan_count": 1, "glycosylation_sites": [], "id": "P47992", "name": "XCL1", "organism": "Homo sapiens", "uniprot_id": "P47992" }, { "function": "Histone methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also mediates monomethylation of 'Lys-56' of histone H3 (H3K56me1) in G1 phase, leading to promote interaction between histone H3 and PCNA and regulating DNA replication. Also weakly methylates 'Lys-27' of histone H3 (H3K27me). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. May also methylate histone H1. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53. Also methylates CDYL, WIZ, ACIN1, DNMT1, HDAC1, ERCC6, KLF12 and itself", "gene_name": "EHMT2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96KQ7", "name": "G9a (EHMT2)", "organism": "Homo sapiens", "uniprot_id": "Q96KQ7" }, { "function": "Polycomb group (PcG) protein. Component of the PRC2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene (PubMed:15225548, PubMed:15231737, PubMed:15385962, PubMed:16618801, PubMed:17344414, PubMed:18285464, PubMed:28229514, PubMed:29499137, PubMed:31959557). The PRC2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems (PubMed:12351676, PubMed:12435631, PubMed:15099518, PubMed:15225548, PubMed:15385962, PubMed:15684044, PubMed:16431907, PubMed:18086877, PubMed:18285464). Genes repressed by the PRC2 complex include HOXC8, HOXA9, MYT1 and CDKN2A (PubMed:15231737, PubMed:16618801, PubMed:17200670, PubMed:31959557)", "gene_name": "SUZ12", "glycan_count": 2, "glycosylation_sites": [], "id": "Q15022", "name": "SUZ12", "organism": "Homo sapiens", "uniprot_id": "Q15022" }, { "function": "Regulator of histone methyltransferase complexes that plays an essential role in embryonic development, including heart and liver development, neural tube fusion process and hematopoiesis (PubMed:20075857). Acts as an accessory subunit for the core PRC2 (Polycomb repressive complex 2) complex, which mediates histone H3K27 (H3K27me3) trimethylation on chromatin (PubMed:20075857, PubMed:29499137, PubMed:31959557). Binds DNA and mediates the recruitment of the PRC2 complex to target genes in embryonic stem cells, thereby playing a key role in stem cell differentiation and normal embryonic development (PubMed:20075857). In cardiac cells, it is required to repress expression of cyclin-D1 (CCND1) by activating methylation of 'Lys-9' of histone H3 (H3K9me) by the GLP1/EHMT1 and G9a/EHMT2 histone methyltransferases (By similarity). Also acts as a transcriptional repressor of ANF via its interaction with GATA4 and NKX2-5 (By similarity). Participates in the negative regulation of cell proliferation signaling (By similarity). Does not have histone demethylase activity (By similarity)", "gene_name": "JARID2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q92833", "name": "JARID2", "organism": "Homo sapiens", "uniprot_id": "Q92833" }, { "function": "Nucleic acid-binding protein which is essential for retrotransposition of LINE-1 elements in the genome. Functions as a nucleic acid chaperone binding its own transcript and therefore preferentially mobilizing the transcript from which they are encoded", "gene_name": "L1RE1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UN81", "name": "LINE-1 ORF1p", "organism": "Homo sapiens", "uniprot_id": "Q9UN81" }, { "function": "Mitochondrial glutamate dehydrogenase that catalyzes the conversion of L-glutamate into alpha-ketoglutarate. Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle (PubMed:11032875, PubMed:11254391, PubMed:16023112, PubMed:16959573). Plays a role in insulin homeostasis (PubMed:11297618, PubMed:9571255). May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate (By similarity)", "gene_name": "GLUD1", "glycan_count": 1, "glycosylation_sites": [], "id": "P00367", "name": "Glutamate dehydrogenase (GLDH)", "organism": "Homo sapiens", "uniprot_id": "P00367" }, { "function": "Catalyzes the formation of tuberculosinyl diphosphate from geranylgeranyl diphosphate (GGPP). It could also react with (14R/S)-14,15-oxidoGGPP to generate 3alpha- and 3beta-hydroxytuberculosinyl diphosphate", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O50406", "name": "Early secreted antigenic target 6 kDa (ESAT-6)", "organism": "Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)", "uniprot_id": "O50406" }, { "function": "Transmembrane protein expressed mainly on T-cells resident in mucosa that plays an essential role in immune cell homeostasis. Rapidly expressed on the surface of platelets, T-lymphocytes and NK cells upon activation by various stimuli, such as antigen recognition or cytokine signaling, stimulates different signaling pathways in different cell types (PubMed:24752896, PubMed:26296369, PubMed:35930205). Negatively regulates Th17 cell differentiation through its carbohydrate dependent interaction with galectin-1/LGALS1 present on immature dendritic cells (PubMed:24752896). Association of CD69 cytoplasmic tail with the JAK3/STAT5 signaling pathway regulates the transcription of RORgamma/RORC and, consequently, differentiation toward the Th17 lineage (By similarity). Also acts via the S100A8/S100A9 complex present on peripheral blood mononuclear cells to promote the conversion of naive CD4 T-cells into regulatory T-cells (PubMed:26296369). Acts as an oxidized low-density lipoprotein (oxLDL) receptor in CD4 T-lymphocytes and negatively regulates the inflammatory response by inducing the expression of PDCD1 through the activation of NFAT (PubMed:35930205). Participates in adipose tissue-derived mesenchymal stem cells (ASCs)-mediated protection against P.aeruginosa infection. Mechanistically, specifically recognizes P.aeruginosa to promote ERK1 activation, followed by granulocyte-macrophage colony-stimulating factor (GM-CSF) and other inflammatory cytokines secretion (PubMed:34841721). In eosinophils, induces IL-10 production through the ERK1/2 pathway (By similarity). Negatively regulates the chemotactic responses of effector lymphocytes and dendritic cells (DCs) to sphingosine 1 phosphate/S1P by acting as a S1PR1 receptor agonist and facilitating the internalization and degradation of the receptor (PubMed:37039481)", "gene_name": "CD69", "glycan_count": 3, "glycosylation_sites": [ { "position": 166, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q07108", "name": "CD69", "organism": "Homo sapiens", "uniprot_id": "Q07108" }, { "function": "Displays several functions associated with host defense: it promotes agglutination, bacterial capsular swelling, phagocytosis and complement fixation through its calcium-dependent binding to phosphorylcholine. Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells", "gene_name": "Crp", "glycan_count": 0, "glycosylation_sites": [], "id": "P14847", "name": "CRP", "organism": "Mus musculus", "uniprot_id": "P14847" }, { "function": "Positive regulator of mTOR signaling that functions by triggering the degradation of DEPTOR, an mTOR inhibitor. Involved in the dynamic regulation of mTOR signaling in chondrocyte differentiation during skeletogenesis (PubMed:30232230). Negatively regulates cAMP signaling pathway possibly by acting on CRTC2/TORC2 and CRTC3/TORC3 (Probable). Prevents HDAC4 translocation to the nucleus (By similarity)", "gene_name": "SIK3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y2K2", "name": "DAPK1", "organism": "Homo sapiens", "uniprot_id": "Q9Y2K2" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P0DJI8 (SAA1), Q9NZK5 (SAA4)", "name": "Serum amyloid A (SAA)", "organism": "", "uniprot_id": "" }, { "function": "Probably involved in lipid transport. Can bind sphingosine-1-phosphate, myristic acid, palmitic acid and stearic acid, retinol, all-trans-retinoic acid and 9-cis-retinoic acid", "gene_name": "APOM", "glycan_count": 44, "glycosylation_sites": [ { "position": 135, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O95445", "name": "Apolipoprotein M (ApoM)", "organism": "Homo sapiens", "uniprot_id": "O95445" }, { "function": "Immunophilin protein with PPIase and co-chaperone activities (PubMed:11350175). Component of unligated steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). Plays a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors maintaining the complex into the cytoplasm when unliganded (PubMed:12538866). Acts as a regulator of Akt/AKT1 activity by promoting the interaction between Akt/AKT1 and PHLPP1, thereby enhancing dephosphorylation and subsequent activation of Akt/AKT1 (PubMed:28147277, PubMed:28363942). Interacts with IKBKE and IKBKB which facilitates IKK complex assembly leading to increased IKBKE and IKBKB kinase activity, NF-kappa-B activation, and IFN production (PubMed:26101251, PubMed:31434731)", "gene_name": "FKBP5", "glycan_count": 1, "glycosylation_sites": [], "id": "Q13451", "name": "FKBP5", "organism": "Homo sapiens", "uniprot_id": "Q13451" }, { "function": "Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components", "gene_name": "Lama3", "glycan_count": 0, "glycosylation_sites": [ { "position": 139, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 445, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1354, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1673, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2159, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2261, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2332, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2361, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2498, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2580, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2747, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3094, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 3270, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q61788", "name": "ZO-1", "organism": "Mus musculus", "uniprot_id": "Q61789" }, { "function": "Promotes guanine-nucleotide exchange on ARF1 and ARF3. Promotes the activation of ARF1/ARF3 through replacement of GDP with GTP. Involved in vesicular trafficking. Required for the maintenance of Golgi structure; the function may be independent of its GEF activity. Required for the maturation of integrin beta-1 in the Golgi. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. Proposed to act as A kinase-anchoring protein (AKAP) and may mediate crosstalk between Arf and PKA pathways. Inhibits GAP activity of MYO9B probably through competitive RhoA binding. The function in the nucleus remains to be determined", "gene_name": "ARFGEF1", "glycan_count": 3, "glycosylation_sites": [], "id": "Q9Y6D6", "name": "SHP (NR0B2)", "organism": "Homo sapiens", "uniprot_id": "Q9Y6D6" }, { "function": "", "gene_name": "Mlc1", "glycan_count": 0, "glycosylation_sites": [], "id": "P06742", "name": "CD2", "organism": "Drosophila melanogaster", "uniprot_id": "P06742" }, { "function": "Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class I molecule:peptide complex. The antigens presented by class I peptides are derived from cytosolic proteins while class II derived from extracellular proteins. Interacts simultaneously with the T-cell receptor (TCR) and the MHC class I proteins presented by antigen presenting cells (APCs). In turn, recruits the Src kinase LCK to the vicinity of the TCR-CD3 complex. A palmitoylation site in the cytoplasmic tail of CD8B chain contributes to partitioning of CD8 into the plasma membrane lipid rafts where signaling proteins are enriched. Once LCK recruited, it initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of cytotoxic T-lymphocytes (CTLs). Additionally, plays a critical role in thymic selection of CD8+ T-cells", "gene_name": "Cd8b", "glycan_count": 0, "glycosylation_sites": [ { "position": 34, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P10300", "name": "CD8B", "organism": "Mus musculus", "uniprot_id": "P10300" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8MJZ1", "name": "FCGRT", "organism": "Canis lupus familiaris", "uniprot_id": "Q8MJZ1" }, { "function": "Involved in the endoplasmic reticulum-associated degradation (ERAD) pathway that targets misfolded glycoproteins for degradation in an N-glycan-dependent manner (PubMed:15537790, PubMed:25092655). May initiate ERAD by promoting the first mannose trimming step of ERAD substrates, from Man9GlcNAc2 to Man8GlcNAc2 (PubMed:25092655). Seems to recognize and bind to exposed hydrophobic regions in target proteins (By similarity)", "gene_name": "EDEM2", "glycan_count": 0, "glycosylation_sites": [ { "position": 90, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 112, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 289, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 450, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9BV94", "name": "EDEM", "organism": "Homo sapiens", "uniprot_id": "Q9BV94" }, { "function": "Co-chaperone which acts as a regulator of the Hsp70 chaperone machinery and may be involved in the processing of other ataxia-linked proteins", "gene_name": "SACS", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9NZJ4", "name": "OS9", "organism": "Homo sapiens", "uniprot_id": "Q9NZJ4" }, { "function": "Mediates post-translational transport of precursor polypeptides across endoplasmic reticulum (ER). Proposed to act as a targeting receptor for small presecretory proteins containing short and apolar signal peptides. Targets and properly positions newly synthesized presecretory proteins into the SEC61 channel-forming translocon complex, triggering channel opening for polypeptide translocation to the ER lumen", "gene_name": "SEC62", "glycan_count": 1, "glycosylation_sites": [], "id": "Q99442", "name": "SEC62", "organism": "Homo sapiens", "uniprot_id": "Q99442" }, { "function": "Bone morphogenetic protein (BMP) type I receptor that is involved in a wide variety of biological processes, including bone, heart, cartilage, nervous, and reproductive system development and regulation (PubMed:20628059, PubMed:22977237). As a type I receptor, forms heterotetrameric receptor complexes with the type II receptors AMHR2, ACVR2A or ACVR2B (PubMed:17911401). Upon binding of ligands such as BMP7 or GDF2/BMP9 to the heteromeric complexes, type II receptors transphosphorylate ACVR1 intracellular domain (PubMed:25354296). In turn, ACVR1 kinase domain is activated and subsequently phosphorylates SMAD1/5/8 proteins that transduce the signal (PubMed:9748228). In addition to its role in mediating BMP pathway-specific signaling, suppresses TGFbeta/activin pathway signaling by interfering with the binding of activin to its type II receptor (PubMed:17911401). Besides canonical SMAD signaling, can activate non-canonical pathways such as p38 mitogen-activated protein kinases/MAPKs (By similarity). May promote the expression of HAMP, potentially via its interaction with BMP6 (By similarity)", "gene_name": "ACVR1", "glycan_count": 1, "glycosylation_sites": [ { "position": 102, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q04771", "name": "ALK3 (BMP receptor 1A)", "organism": "Homo sapiens", "uniprot_id": "Q04771" }, { "function": "Transcription factor that binds to the inverted palindrome 5'-GTTAATNATTAAC-3' (PubMed:17924661, PubMed:7900999). Binds to the FPC element in the cAMP regulatory unit of the PLAU gene (By similarity). Transcriptional activity is increased by coactivator PCBD1 (PubMed:24204001)", "gene_name": "HNF1B", "glycan_count": 0, "glycosylation_sites": [], "id": "P35680", "name": "HNF1\u03b2", "organism": "Homo sapiens", "uniprot_id": "P35680" }, { "function": "Tyrosine-protein kinase that acts as a cell-surface receptor for fibroblast growth factors and plays a role in the regulation of cell proliferation, differentiation and migration, and in regulation of lipid metabolism, bile acid biosynthesis, glucose uptake, vitamin D metabolism and phosphate homeostasis. Required for normal down-regulation of the expression of CYP7A1, the rate-limiting enzyme in bile acid synthesis, in response to FGF19. Phosphorylates PLCG1 and FRS2. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Promotes SRC-dependent phosphorylation of the matrix protease MMP14 and its lysosomal degradation. FGFR4 signaling is down-regulated by receptor internalization and degradation; MMP14 promotes internalization and degradation of FGFR4. Mutations that lead to constitutive kinase activation or impair normal FGFR4 inactivation lead to aberrant signaling", "gene_name": "FGFR4", "glycan_count": 10, "glycosylation_sites": [ { "position": 112, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 258, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 290, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 311, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 322, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P22455", "name": "FGF receptor 4 (FGFR4)", "organism": "Homo sapiens", "uniprot_id": "P22455" }, { "function": "Inflammatory caspase that acts as the effector of the non-canonical inflammasome by mediating lipopolysaccharide (LPS)-induced pyroptosis (PubMed:22002608, PubMed:23348507, PubMed:23887873, PubMed:24031018, PubMed:25119034, PubMed:30135078, PubMed:37001519, PubMed:38632402). Also indirectly activates the NLRP3 and NLRP6 inflammasomes (PubMed:26320999, PubMed:30392956, PubMed:37001519). Acts as a thiol protease that cleaves a tetrapeptide after an Asp residue at position P1: catalyzes cleavage of CGAS and GSDMD (PubMed:26375003, PubMed:28314590, PubMed:30392956, PubMed:38632402). In contrast to its human ortholog, does not cleave IL18 (PubMed:37993712, PubMed:37993714). Effector of the non-canonical inflammasome independently of NLRP3 inflammasome and CASP1: the non-canonical inflammasome promotes pyroptosis through GSDMD cleavage without involving secretion of cytokine IL1B and IL18 (PubMed:22002608, PubMed:22895188, PubMed:23348507, PubMed:23887873, PubMed:24031018, PubMed:26320999, PubMed:26375003, PubMed:30135078, PubMed:30589883). In the non-canonical inflammasome, CASP4/CASP11 is activated by direct binding to the lipid A moiety of LPS without the need of an upstream sensor (PubMed:22002608, PubMed:23348507, PubMed:25119034, PubMed:37001519, PubMed:38632402). LPS-binding promotes CASP4/CASP11 activation and CASP4/CASP11-mediated cleavage of GSDMD, followed by pyroptosis of infected cells and their extrusion into the gut lumen (PubMed:22002608, PubMed:23348507, PubMed:25119034, PubMed:38632402). Also indirectly promotes secretion of mature cytokines (IL1A, IL18 and HMGB1) downstream of GSDMD-mediated pyroptosis via activation of the NLRP3 and NLRP6 inflammasomes (By similarity). Involved in NLRP3-dependent CASP1 activation and IL1B and IL18 secretion in response to non-canonical activators, such as UVB radiation or cholera enterotoxin (PubMed:26320999). Involved in NLRP6 inflammasome-dependent activation in response to lipoteichoic acid (LTA), a cell-wall component of Gram-positive bacteria, which leads to CASP1 activation and IL1B and IL18 secretion (PubMed:30392956). Involved in LPS-induced IL6 secretion; this activity may not require caspase enzymatic activity (By similarity). The non-canonical inflammasome is required for innate immunity to cytosolic, but not vacuolar, bacteria (PubMed:23348507). Plays a crucial role in the restriction of S.typhimurium replication in colonic epithelial cells during infection (PubMed:25121752, PubMed:26375003, PubMed:34671164). Activation of the non-canonical inflammasome in brain endothelial cells can lead to excessive pyroptosis, leading to blood-brain barrier breakdown (PubMed:38632402). Pyroptosis limits bacterial replication, while cytokine secretion promotes the recruitment and activation of immune cells and triggers mucosal inflammation (PubMed:25121752). May also act as an activator of adaptive immunity in dendritic cells, following activation by oxidized phospholipid 1-palmitoyl-2-arachidonoyl- sn-glycero-3-phosphorylcholine, an oxidized phospholipid (oxPAPC) (PubMed:27103670). Cleavage of GSDMD is not strictly dependent on the consensus cleavage site but depends on an exosite interface on CASP4/CASP11 that recognizes and binds the Gasdermin-D, C-terminal (GSDMD-CT) part (PubMed:32109412, PubMed:32554464). In contrast, it does not directly process IL1B (PubMed:8702803, PubMed:9038361). During non-canonical inflammasome activation, cuts CGAS and may play a role in the regulation of antiviral innate immune activation (PubMed:28314590)", "gene_name": "Casp4", "glycan_count": 0, "glycosylation_sites": [], "id": "P70343", "name": "Caspase-11", "organism": "Mus musculus", "uniprot_id": "P70343" }, { "function": "Mediates sodium- and chloride-dependent transport of taurine (PubMed:31345061, PubMed:31903486, PubMed:8010975, PubMed:8382624, PubMed:8654117). Mediates transport of beta-alanine (PubMed:8010975). Can also mediate transport of hypotaurine and gamma-aminobutyric acid (GABA) (By similarity)", "gene_name": "SLC6A6", "glycan_count": 2, "glycosylation_sites": [ { "position": 163, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 179, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 190, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P31641", "name": "Taurine transporter (TauT)", "organism": "Homo sapiens", "uniprot_id": "P31641" }, { "function": "Dopamine receptor whose activity is mediated by G proteins which activate adenylyl cyclase", "gene_name": "DRD1", "glycan_count": 0, "glycosylation_sites": [ { "position": 5, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P21728", "name": "DRD1 (Dopamine Receptor D1)", "organism": "Homo sapiens", "uniprot_id": "P21728" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02741 (human)", "name": "C-reactive protein (CRP)", "organism": "", "uniprot_id": "" }, { "function": "A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins (PubMed:11093772, PubMed:14559847, PubMed:15766564, PubMed:19965576, PubMed:7574697). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase) (PubMed:11093772, PubMed:14559847, PubMed:15766564, PubMed:19965576, PubMed:7574697). Primarily catalyzes the epoxidation of double bonds of polyunsaturated fatty acids (PUFA) with a preference for the last double bond (PubMed:15766564, PubMed:19965576, PubMed:7574697). Catalyzes the hydroxylation of carbon-hydrogen bonds. Metabolizes all trans-retinoic acid toward its 4-hydroxylated form (PubMed:11093772). Displays 16-alpha hydroxylase activity toward estrogen steroid hormones, 17beta-estradiol (E2) and estrone (E1) (PubMed:14559847). Plays a role in the oxidative metabolism of xenobiotics. It is the principal enzyme responsible for the metabolism of the anti-cancer drug paclitaxel (taxol) (PubMed:26427316)", "gene_name": "CYP2C8", "glycan_count": 0, "glycosylation_sites": [], "id": "P10632", "name": "CYP2D1", "organism": "Homo sapiens", "uniprot_id": "P10632" }, { "function": "Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments", "gene_name": "Tpm3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q63610", "name": "CYP3A23", "organism": "Rattus norvegicus", "uniprot_id": "Q63610" }, { "function": "Non-specific DNA-binding protein that plays key roles in mitotic nuclear reassembly, chromatin organization, DNA damage response, gene expression and intrinsic immunity against foreign DNA (PubMed:10908652, PubMed:11792822, PubMed:12163470, PubMed:18005698, PubMed:25991860, PubMed:28841419, PubMed:31796734, PubMed:32792394). Contains two non-specific double-stranded DNA (dsDNA)-binding sites which promote DNA cross-bridging (PubMed:9465049). Plays a key role in nuclear membrane reformation at the end of mitosis by driving formation of a single nucleus in a spindle-independent manner (PubMed:28841419). Transiently cross-bridges anaphase chromosomes via its ability to bridge distant DNA sites, leading to the formation of a dense chromatin network at the chromosome ensemble surface that limits membranes to the surface (PubMed:28841419). Also acts as a negative regulator of innate immune activation by restricting CGAS activity toward self-DNA upon acute loss of nuclear membrane integrity (PubMed:32792394). Outcompetes CGAS for DNA-binding, thereby preventing CGAS activation and subsequent damaging autoinflammatory responses (PubMed:32792394). Also involved in DNA damage response: interacts with PARP1 in response to oxidative stress, thereby inhibiting the ADP-ribosyltransferase activity of PARP1 (PubMed:31796734). Involved in the recognition of exogenous dsDNA in the cytosol: associates with exogenous dsDNA immediately after its appearance in the cytosol at endosome breakdown and is required to avoid autophagy (PubMed:25991860). In case of poxvirus infection, has an antiviral activity by blocking viral DNA replication (PubMed:18005698)", "gene_name": "BANF1", "glycan_count": 0, "glycosylation_sites": [], "id": "O60558", "name": "UDP-glucuronosyltransferase 1A9 (UGT1A9)", "organism": "Homo sapiens", "uniprot_id": "O75531" }, { "function": "UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile (PubMed:10702251, PubMed:15470161, PubMed:15472229, PubMed:17442341, PubMed:18674515, PubMed:18719240, PubMed:19022937, PubMed:23288867, PubMed:23756265, PubMed:26220143, PubMed:15231852, PubMed:21422672, PubMed:38211441). Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds (PubMed:15470161, PubMed:18674515, PubMed:23756265). Catalyzes the glucuronidation of endogenous steroid hormones such as androgens (epitestosterone, androsterone) and estrogens (estradiol, epiestradiol, estriol, catechol estrogens) (PubMed:15472229, PubMed:17442341, PubMed:18719240, PubMed:19022937, PubMed:2159463, PubMed:23288867, PubMed:26220143). Also regulates the levels of retinoic acid, a major metabolite of vitamin A involved in apoptosis, cellular growth and differentiation, and embryonic development (PubMed:10702251). Contributes to bile acid (BA) detoxification by catalyzing the glucuronidation of BA substrates, which are natural detergents for dietary lipids absorption (PubMed:23756265). Involved in the glucuronidation of arachidonic acid (AA) and AA-derived eicosanoids including 15-HETE, 20-HETE, PGE2, PGB1 and F2-isoprostanes (8-iso-PGF2alpha and 5-epi-5-F2t-IsoP) (PubMed:15231852, PubMed:38211441). Involved in the glucuronidation of the phytochemical ferulic acid at the phenolic or the carboxylic acid group (PubMed:21422672). Involved in the glucuronidation of the AGTR1 angiotensin receptor antagonist losartan, caderastan and zolarsatan, drugs which can inhibit the effect of angiotensin II (PubMed:18674515). Also metabolizes mycophenolate, an immunosuppressive agent (PubMed:15470161)", "gene_name": "UGT2B7", "glycan_count": 52, "glycosylation_sites": [ { "position": 67, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 68, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 315, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P16662", "name": "UDP-glucuronosyltransferase 2B7 (UGT2B7)", "organism": "Homo sapiens", "uniprot_id": "P16662" }, { "function": "UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile (PubMed:16595710, PubMed:18719240, PubMed:23288867, PubMed:7835232, PubMed:9295060). Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds (PubMed:7835232). Catalyzes the glucuronidation of endogenous steroid hormones such as androgens (testosterone, androsterone) and estrogens (estradiol, epiestradiol, estriol, catechol estrogens) (PubMed:16595710, PubMed:18719240, PubMed:23288867, PubMed:7835232, PubMed:9295060). Displays glucuronidation activity toward several classes of xenobiotic substrates, including phenolic compounds (eugenol, 4-nitrophenol, 4-hydroxybiphenyl) and phenylpropanoids (naringenin, coumarins) (PubMed:7835232). Catalyzes the glucuronidation of monoterpenoid alcohols such as borneol, menthol and isomenthol, a class of natural compounds used in essential oils (By similarity)", "gene_name": "UGT2B15", "glycan_count": 4, "glycosylation_sites": [ { "position": 65, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 316, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 483, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P54855", "name": "UDP-glucuronosyltransferase 2B15 (UGT2B15)", "organism": "Homo sapiens", "uniprot_id": "P54855" }, { "function": "Forms a water-specific channel that provides the plasma membranes of renal collecting duct with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient (PubMed:15509592, PubMed:7510718, PubMed:7524315, PubMed:8140421, PubMed:8584435). Plays an essential role in renal water homeostasis (PubMed:15509592, PubMed:7524315, PubMed:8140421). Could also be permeable to glycerol (PubMed:8584435)", "gene_name": "AQP2", "glycan_count": 0, "glycosylation_sites": [ { "position": 123, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P41181", "name": "Aquaporin-2", "organism": "Homo sapiens", "uniprot_id": "P41181" }, { "function": "Integrin alpha-D/beta-2 is a receptor for ICAM3 and VCAM1. May play a role in the atherosclerotic process such as clearing lipoproteins from plaques and in phagocytosis of blood-borne pathogens, particulate matter, and senescent erythrocytes from the blood", "gene_name": "ITGAD", "glycan_count": 0, "glycosylation_sites": [ { "position": 59, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 87, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 99, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 391, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 690, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 732, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 872, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 956, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1045, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13349", "name": "M-cadherin (M-cad)", "organism": "Homo sapiens", "uniprot_id": "Q13349" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02794 (FTH1)", "name": "Ferritin", "organism": "", "uniprot_id": "" }, { "function": "3'-5' RNA helicase that plays a key role in the male and female germline by promoting transition from mitotic to meiotic divisions in stem cells (PubMed:26318451, PubMed:29033321, PubMed:29970596). Specifically recognizes and binds N6-methyladenosine (m6A)-containing RNAs, a modification present at internal sites of mRNAs and some non-coding RNAs that plays a role in the efficiency of RNA processing and stability (PubMed:26318451, PubMed:29033321). Essential for ensuring a successful progression of the meiotic program in the germline by regulating the level of m6A-containing RNAs (By similarity). Acts by binding and promoting degradation of m6A-containing mRNAs: the 3'-5' RNA helicase activity is required for this process and RNA degradation may be mediated by XRN1 exoribonuclease (PubMed:29033321). Required for both spermatogenesis and oogenesis (By similarity)", "gene_name": "YTHDC2", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9H6S0", "name": "Oligo2", "organism": "Homo sapiens", "uniprot_id": "Q9H6S0" }, { "function": "May act as a modulator of the olfactory signal-transduction cascade", "gene_name": "OMP", "glycan_count": 1, "glycosylation_sites": [], "id": "P47874", "name": "OMP (Olfactory Marker Protein)", "organism": "Homo sapiens", "uniprot_id": "P47874" }, { "function": "Coreceptor for bacterial lipopolysaccharide. In concert with LBP, binds to monomeric lipopolysaccharide and delivers it to the LY96/TLR4 complex, thereby mediating the innate immune response to bacterial lipopolysaccharide (LPS) (PubMed:16148141). Acts via MyD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (PubMed:15895089, PubMed:8612135). Acts as a coreceptor for TLR2:TLR6 heterodimer in response to diacylated lipopeptides and for TLR2:TLR1 heterodimer in response to triacylated lipopeptides, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway (By similarity). Acts as an accessory receptor for M.tuberculosis lipoproteins LprA, LprG and LpqH, in conjunction with coreceptors TLR2 and TLR1. The lipoproteins act as agonists to modulate antigen presenting cell functions in response to the pathogen (PubMed:19362712). Binds electronegative LDL (LDL(-)) and mediates the cytokine release induced by LDL(-) (By similarity)", "gene_name": "Cd14", "glycan_count": 3, "glycosylation_sites": [ { "position": 33, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 147, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 180, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 276, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 317, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P10810", "name": "CD14", "organism": "Mus musculus", "uniprot_id": "P10810" }, { "function": "Mediates inactivation of the lipoprotein lipase LPL, and thereby plays a role in the regulation of triglyceride clearance from the blood serum and in lipid metabolism (PubMed:15837923, PubMed:17609370, PubMed:29899519). May also play a role in regulating glucose homeostasis and insulin sensitivity (PubMed:15837923, PubMed:29899519). Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage (PubMed:14583458, PubMed:17130448, PubMed:21832056). Upon heterologous expression, inhibits the adhesion of endothelial cell to the extracellular matrix (ECM), and inhibits the reorganization of the actin cytoskeleton, formation of actin stress fibers and focal adhesions in endothelial cells that have adhered to ANGPTL4-containing ECM (in vitro) (By similarity). Depending on context, may modulate tumor-related angiogenesis (Probable)", "gene_name": "Angptl4", "glycan_count": 0, "glycosylation_sites": [ { "position": 181, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 236, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 242, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Z1P8", "name": "Enpp2", "organism": "Mus musculus", "uniprot_id": "Q9Z1P8" }, { "function": "Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B)", "gene_name": "ctaC", "glycan_count": 0, "glycosylation_sites": [], "id": "P08306", "name": "Lyz2", "organism": "Paracoccus denitrificans", "uniprot_id": "P08306" }, { "function": "Innate immune receptor which acts as a cytoplasmic sensor of viral nucleic acids and plays a major role in sensing viral infection and in the activation of a cascade of antiviral responses including the induction of type I interferons and pro-inflammatory cytokines. Its ligands include mRNA lacking 2'-O-methylation at their 5' cap and long-dsRNA (>1 kb in length). Upon ligand binding it associates with mitochondria antiviral signaling protein (MAVS/IPS1) which activates the IKK-related kinases: TBK1 and IKBKE which phosphorylate interferon regulatory factors: IRF3 and IRF7 which in turn activate transcription of antiviral immunological genes, including interferons (IFNs); IFN-alpha and IFN-beta. Responsible for detecting the Picornaviridae family members such as encephalomyocarditis virus (EMCV), mengo encephalomyocarditis virus (ENMG), and theiler's murine encephalomyelitis virus (TMEV). Can also detect other viruses such as dengue virus (DENV), west Nile virus (WNV), and reovirus. Also involved in antiviral signaling in response to viruses containing a dsDNA genome, such as vaccinia virus. Plays an important role in amplifying innate immune signaling through recognition of RNA metabolites that are produced during virus infection by ribonuclease L (RNase L). May play an important role in enhancing natural killer cell function and may be involved in growth inhibition and apoptosis in several tumor cell lines", "gene_name": "Ifih1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8R5F7", "name": "Mpeg1", "organism": "Mus musculus", "uniprot_id": "Q8R5F7" }, { "function": "Co-chaperone for HSP/HSP70 proteins. It functions as a nucleotide-exchange factor promoting the release of ADP from HSP70, thereby activating HSP70-mediated protein refolding (PubMed:20223214). Has an essential role in maintaining proteostasis at junctional membrane complexes (JMC), where it may function as a scaffold between the HSPA8 chaperone and JMC proteins enabling correct, HSPA8-dependent JMC protein folding (By similarity). Inhibits both auto-ubiquitination of PRKN and ubiquitination of target proteins by PRKN (By similarity)", "gene_name": "BAG5", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UL15", "name": "BAG5", "organism": "Homo sapiens", "uniprot_id": "Q9UL15" }, { "function": "May play a role in the negative regulation of cell cycle progression", "gene_name": "CRLF3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y6M8", "name": "IGF2BP3", "organism": "Homo sapiens", "uniprot_id": "Q8IUI8" }, { "function": "Secreted protein that functions as a cytokine and growth factor and mediates its signal through cell-surface proteoglycan and non-proteoglycan receptors (PubMed:10212223, PubMed:10772929, PubMed:12084985, PubMed:12122009, PubMed:12573468, PubMed:15466886, PubMed:18469519, PubMed:24458438). Binds cell-surface proteoglycan receptors via their chondroitin sulfate (CS) groups (PubMed:10212223, PubMed:12084985). Thereby regulates many processes like inflammatory response, cell proliferation, cell adhesion, cell growth, cell survival, tissue regeneration, cell differentiation and cell migration (PubMed:10212223, PubMed:10683378, PubMed:10772929, PubMed:12084985, PubMed:12122009, PubMed:12573468, PubMed:15466886, PubMed:22323540, PubMed:24458438). Participates in inflammatory processes by exerting two different activities. Firstly, mediates neutrophils and macrophages recruitment to the sites of inflammation both by direct action by cooperating namely with ITGB2 via LRP1 and by inducing chemokine expression (PubMed:10683378, PubMed:24458438). This inflammation can be accompanied by epithelial cell survival and smooth muscle cell migration after renal and vessel damage, respectively (PubMed:10683378). Secondly, suppresses the development of tolerogenic dendric cells thereby inhibiting the differentiation of regulatory T cells and also promote T cell expansion through NFAT signaling and Th1 cell differentiation (PubMed:22323540). Promotes tissue regeneration after injury or trauma. After heart damage negatively regulates the recruitment of inflammatory cells and mediates cell survival through activation of anti-apoptotic signaling pathways via MAPKs and AKT pathways through the activation of angiogenesis (By similarity). Also facilitates liver regeneration as well as bone repair by recruiting macrophage at trauma site and by promoting cartilage development by facilitating chondrocyte differentiation (By similarity). Plays a role in brain by promoting neural precursor cells survival and growth through interaction with heparan sulfate proteoglycans (By similarity). Binds PTPRZ1 and promotes neuronal migration and embryonic neurons survival (PubMed:10212223). Binds SDC3 or GPC2 and mediates neurite outgrowth and cell adhesion (PubMed:12084985, PubMed:1768439). Binds chondroitin sulfate E and heparin leading to inhibition of neuronal cell adhesion induced by binding with GPC2 (PubMed:12084985). Binds CSPG5 and promotes elongation of oligodendroglial precursor-like cells (By similarity). Also binds ITGA6:ITGB1 complex; this interaction mediates MDK-induced neurite outgrowth (PubMed:15466886, PubMed:1768439). Binds LRP1; promotes neuronal survival (PubMed:10772929). Binds ITGA4:ITGB1 complex; this interaction mediates MDK-induced osteoblast cells migration through PXN phosphorylation (PubMed:15466886). Binds anaplastic lymphoma kinase (ALK) which induces ALK activation and subsequent phosphorylation of the insulin receptor substrate (IRS1), followed by the activation of mitogen-activated protein kinase (MAPK) and PI3-kinase, and the induction of cell proliferation (PubMed:12122009). Promotes epithelial to mesenchymal transition through interaction with NOTCH2 (PubMed:18469519). During arteriogenesis, plays a role in vascular endothelial cell proliferation by inducing VEGFA expression and release which in turn induces nitric oxide synthase expression. Moreover activates vasodilation through nitric oxide synthase activation (By similarity). Negatively regulates bone formation in response to mechanical load by inhibiting Wnt/beta-catenin signaling in osteoblasts (By similarity). In addition plays a role in hippocampal development, working memory, auditory response, early fetal adrenal gland development and the female reproductive system (By similarity)", "gene_name": "MDK", "glycan_count": 1, "glycosylation_sites": [], "id": "P21741", "name": "MDK (Midkine)", "organism": "Homo sapiens", "uniprot_id": "P21741" }, { "function": "Secreted growth factor that mediates its signal through cell-surface proteoglycan and non-proteoglycan receptors (PubMed:11278720, PubMed:16814777, PubMed:19141530). Binds cell-surface proteoglycan receptor via their chondroitin sulfate (CS) groups (PubMed:26896299, PubMed:27445335). Thereby regulates many processes like cell proliferation, cell survival, cell growth, cell differentiation and cell migration in several tissues namely neuron and bone (PubMed:11278720, PubMed:1733956, PubMed:1768439, PubMed:19141530, PubMed:19442624, PubMed:27445335, PubMed:30667096). Also plays a role in synaptic plasticity and learning-related behavior by inhibiting long-term synaptic potentiation (By similarity). Binds PTPRZ1, leading to neutralization of the negative charges of the CS chains of PTPRZ1, inducing PTPRZ1 clustering, thereby causing the dimerization and inactivation of its phosphatase activity leading to increased tyrosine phosphorylation of each of the PTPRZ1 substrates like ALK, CTNNB1 or AFAP1L2 in order to activate the PI3K-AKT pathway (PubMed:10706604, PubMed:16814777, PubMed:17681947, PubMed:27445335, PubMed:30667096). Through PTPRZ1 binding controls oligodendrocyte precursor cell differentiation by enhancing the phosphorylation of AFAP1L2 in order to activate the PI3K-AKT pathway (PubMed:27445335, PubMed:30667096). Forms a complex with PTPRZ1 and integrin alpha-V/beta-3 (ITGAV:ITGB3) that stimulates endothelial cell migration through SRC dephosphorylation and activation that consequently leads to ITGB3 'Tyr-773' phosphorylation (PubMed:19141530). In adult hippocampus promotes dendritic arborization, spine development, and functional integration and connectivity of newborn granule neurons through ALK by activating AKT signaling pathway (By similarity). Binds GPC2 and chondroitin sulfate proteoglycans (CSPGs) at the neuron surface, leading to abrogation of binding between PTPRS and CSPGs and neurite outgrowth promotion (By similarity). Binds SDC3 and mediates bone formation by recruiting and attaching osteoblasts/osteoblast precursors to the sites for new bone deposition (By similarity). Binds ALK and promotes cell survival and cell proliferation through MAPK pathway activation (PubMed:11278720). Inhibits proliferation and enhances differentiation of neural stem cells by inhibiting FGF2-induced fibroblast growth factor receptor signaling pathway (By similarity). Mediates regulatory mechanisms in normal hemostasis and in hematopoietic regeneration and in maintaining the balance of myeloid and lymphoid regeneration (By similarity). In addition may play a role in the female reproductive system, auditory response and the progesterone-induced decidualization pathway (By similarity)", "gene_name": "PTN", "glycan_count": 0, "glycosylation_sites": [], "id": "P21246", "name": "PTN (Pleiotrophin)", "organism": "Homo sapiens", "uniprot_id": "P21246" }, { "function": "Can function as a specific repressor of TGF-beta, activin, and BMP signaling through its interaction with the R-SMAD proteins. Antagonizes TGF-beta-induced cell proliferation arrest", "gene_name": "LEMD3", "glycan_count": 7, "glycosylation_sites": [], "id": "Q9Y2U8", "name": "PCLAF (PCNA clamp associated factor)", "organism": "Homo sapiens", "uniprot_id": "Q9Y2U8" }, { "function": "Stress-responsive protein involved in hormone responses, cell growth, and differentiation. Acts as a tumor suppressor in many cell types. Necessary but not sufficient for p53/TP53-mediated caspase activation and apoptosis. Has a role in cell trafficking, notably of the Schwann cell, and is necessary for the maintenance and development of the peripheral nerve myelin sheath. Required for vesicular recycling of CDH1 and TF. May also function in lipid trafficking. Protects cells from spindle disruption damage. Functions in p53/TP53-dependent mitotic spindle checkpoint. Regulates microtubule dynamics and maintains euploidy", "gene_name": "NDRG1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q92597", "name": "NDRG1 (N-myc downstream-regulated gene 1)", "organism": "Homo sapiens", "uniprot_id": "Q92597" }, { "function": "Replication termination factor which is a component of the elongating replisome (Probable). Required for ATR pathway signaling upon DNA damage and has a positive activity during DNA replication. Might function to facilitate fork pausing at replication fork barriers like the rDNA. May be globally required to stimulate ATR signaling after the fork stalls or encounters a lesion (Probable). Interacts with nascent DNA (PubMed:29290612)", "gene_name": "RTF2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9BY42", "name": "YEATS4", "organism": "Homo sapiens", "uniprot_id": "Q9BY42" }, { "function": "Cell surface receptor that plays an important role in the immune system, particularly in intercellular adhesion, lymphocyte signaling, cytotoxicity and lymphokine secretion mediated by cytotoxic T-cells and NK cells (PubMed:8673704, PubMed:9712030). Functions as a costimulatory receptor upon recognition of target cells, such as virus-infected or tumor cells. Upon binding to its ligands PVR/CD155 or NECTIN2/CD112 on target cells, promotes the cytotoxic activity of NK cells and CTLs, enhancing their ability to kill these cells (PubMed:26755705, PubMed:31253644, PubMed:30591568). Mechanistically, phosphorylation by Src kinases such as LYN of FYN, enables binding to adapter GRB2, leading to activation of VAV1, PI3K and PLCG1. Promotes also activation of kinases ERK and AKT, as well as calcium fluxes (By similarity)", "gene_name": "CD226", "glycan_count": 1, "glycosylation_sites": [ { "position": 32, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 83, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 90, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 97, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 147, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 186, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 198, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 231, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q15762", "name": "CD226", "organism": "Homo sapiens", "uniprot_id": "Q15762" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P05067-APP fragment", "name": "Beta-amyloid (A\u03b2)", "organism": "", "uniprot_id": "" }, { "function": "Involved in complement regulation. The dimerized forms have avidity for tissue-bound complement fragments and efficiently compete with the physiological complement inhibitor CFH", "gene_name": "CFHR5", "glycan_count": 24, "glycosylation_sites": [ { "position": 126, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 400, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9BXR6", "name": "Complement factor H-related protein-3", "organism": "Homo sapiens", "uniprot_id": "Q9BXR6" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q07157 (human)", "name": "ZO-1", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q16625 (human)", "name": "Occludin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P37231 (human)", "name": "PPAR\u03b3", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q99541 (human)", "name": "Plin2", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O60488 (human)", "name": "Acsl4", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O60427 (human)", "name": "Fads1", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P35558 (human)", "name": "Pck1", "organism": "", "uniprot_id": "" }, { "function": "Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate", "gene_name": "asd", "glycan_count": 0, "glycosylation_sites": [], "id": "Q53612", "name": "ClfA (Clumping factor A)", "organism": "Streptomyces akiyoshiensis", "uniprot_id": "Q53612" }, { "function": "Alpha-toxin binds to the membrane of eukaryotic cells (particularly red blood cells, RBC) forming pores, resulting in hemolysis, with the release of low-molecular weight molecules leading to eventual osmotic RBC lysis (PubMed:1587866, PubMed:20624979). Human RBCs bind much less alpha-toxin than do rabbit RBCs (PubMed:1587866, PubMed:20624979). Heptamer oligomerization and pore formation is required for lytic activity (PubMed:1587866, PubMed:20624979)", "gene_name": "hly", "glycan_count": 0, "glycosylation_sites": [], "id": "P09616", "name": "\u03b1-hemolysin", "organism": "Staphylococcus aureus", "uniprot_id": "P09616" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q81ZP7", "name": "BclA (Bacillus collagen-like protein)", "organism": "", "uniprot_id": "Q81ZP7" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P0A564", "name": "ESAT-6", "organism": "", "uniprot_id": "P0A564" }, { "function": "", "gene_name": "Tb07.5F10.300", "glycan_count": 0, "glycosylation_sites": [], "id": "Q57UQ3", "name": "Tb BILBO1", "organism": "Trypanosoma brucei brucei (strain 927/4 GUTat10.1)", "uniprot_id": "Q57UQ3" }, { "function": "Together with IFNAR1, forms the heterodimeric receptor for type I interferons (including interferons alpha, beta, epsilon, omega and kappa) (PubMed:10049744, PubMed:10556041, PubMed:21854986, PubMed:26424569, PubMed:28165510, PubMed:32972995, PubMed:7665574, PubMed:7759950, PubMed:8181059, PubMed:8798579, PubMed:8969169). Type I interferon binding activates the JAK-STAT signaling cascade, resulting in transcriptional activation or repression of interferon-regulated genes that encode the effectors of the interferon response (PubMed:10049744, PubMed:17517919, PubMed:21854986, PubMed:26424569, PubMed:28165510, PubMed:32972995, PubMed:7665574, PubMed:7759950, PubMed:8181059, PubMed:8798579, PubMed:8969169). Mechanistically, type I interferon-binding brings the IFNAR1 and IFNAR2 subunits into close proximity with one another, driving their associated Janus kinases (JAKs) (TYK2 bound to IFNAR1 and JAK1 bound to IFNAR2) to cross-phosphorylate one another (PubMed:10556041, PubMed:11682488, PubMed:12105218, PubMed:21854986, PubMed:32972995). The activated kinases phosphorylate specific tyrosine residues on the intracellular domains of IFNAR1 and IFNAR2, forming docking sites for the STAT transcription factors (STAT1, STAT2 and STAT) (PubMed:11682488, PubMed:12105218, PubMed:21854986, PubMed:32972995). STAT proteins are then phosphorylated by the JAKs, promoting their translocation into the nucleus to regulate expression of interferon-regulated genes (PubMed:12105218, PubMed:28165510, PubMed:9121453)", "gene_name": "IFNAR2", "glycan_count": 9, "glycosylation_sites": [ { "position": 58, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 87, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 116, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 188, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 192, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P48551", "name": "IFNAR2", "organism": "Homo sapiens", "uniprot_id": "P48551" }, { "function": "Non-receptor tyrosine kinase involved in B-lymphocyte development, differentiation and signaling (By similarity). B-cell receptor (BCR) signaling requires a tight regulation of several protein tyrosine kinases and phosphatases, and associated coreceptors (By similarity). Binding of antigen to the B-cell antigen receptor (BCR) triggers signaling that ultimately leads to B-cell activation (By similarity). Signaling through BLK plays an important role in transmitting signals through surface immunoglobulins and supports the pro-B to pre-B transition, as well as the signaling for growth arrest and apoptosis downstream of B-cell receptor (By similarity). Specifically binds and phosphorylates CD79A at 'Tyr-188'and 'Tyr-199', as well as CD79B at 'Tyr-196' and 'Tyr-207' (By similarity). Also phosphorylates the immunoglobulin G receptors FCGR2A, FCGR2B and FCGR2C (PubMed:8756631). With FYN and LYN, plays an essential role in pre-B-cell receptor (pre-BCR)-mediated NF-kappa-B activation (By similarity). Also contributes to BTK activation by indirectly stimulating BTK intramolecular autophosphorylation (By similarity). In pancreatic islets, acts as a modulator of beta-cells function through the up-regulation of PDX1 and NKX6-1 and consequent stimulation of insulin secretion in response to glucose (PubMed:19667185). Phosphorylates CGAS, promoting retention of CGAS in the cytosol (PubMed:30356214)", "gene_name": "BLK", "glycan_count": 0, "glycosylation_sites": [], "id": "P51451", "name": "BLK", "organism": "Homo sapiens", "uniprot_id": "P51451" }, { "function": "Potent chemoattractant for neutrophils, and weaker for dendritic cells. Not chemotactic for T-cells, B-cells, monocytes, natural killer cells or granulocytes. Does not inhibit proliferation of myeloid progenitors in colony formation assays", "gene_name": "CXCL14", "glycan_count": 0, "glycosylation_sites": [], "id": "O95715", "name": "CXCL14", "organism": "Homo sapiens", "uniprot_id": "O95715" }, { "function": "Metalloproteinase that plays an important role in connective tissue organization, development, inflammation and cell migration. Extracellular matrix (ECM) degrading enzyme that show proteolytic activity toward the hyalectan group of chondroitin sulfate proteoglycans (CSPGs) including ACAN, VCAN, BCAN and NCAN (PubMed:16133547, PubMed:18992360). Cleavage within the hyalectans occurs at Glu-Xaa recognition motifs. Plays a role in embryonic development, including limb and cardiac morphogenesis, and skeletal muscle development through its VCAN remodeling properties. Cleaves VCAN in the pericellular matrix surrounding myoblasts, facilitating myoblast contact and fusion which is required for skeletal muscle development and regeneration (By similarity). Participates in development of brown adipose tissue and browning of white adipose tissue (By similarity). Plays an important role for T-lymphocyte migration from draining lymph nodes following viral infection", "gene_name": "ADAMTS5", "glycan_count": 5, "glycosylation_sites": [ { "position": 498, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 570, "type": "C-linked (Man) tryptophan" }, { "position": 573, "type": "C-linked (Man) tryptophan" }, { "position": 582, "type": "O-linked (Fuc...) serine" }, { "position": 728, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 802, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 807, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UNA0", "name": "ADAMTS-5", "organism": "Homo sapiens", "uniprot_id": "Q9UNA0" }, { "function": "Involved in the response to variation in environmental oxygen levels by targeting the hypoxia-inducible transcription factor hif-1 for proteasomal degradation when oxygen levels are normal (around 20%) (PubMed:11595184). By regulating hif-1 expression, plays a role in iron homeostasis, aging, heat acclimation and progeny size (PubMed:12686697, PubMed:19372390, PubMed:22396654). Mediates resistance to enteropathogenic E.coli (PubMed:16091039). Mediates susceptibility to B.thuringiensis pore-forming toxins (PubMed:20011506). Not involved in P.aeruginosa susceptibility (PubMed:20865124)", "gene_name": "vhl-1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q19213", "name": "Paraoxonase-1 (PON-1)", "organism": "Caenorhabditis elegans", "uniprot_id": "Q19213" }, { "function": "Hydrolase that deubiquitinates target proteins such as ARMC5, FOXO4, DEPTOR, KAT5, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN, KMT2E/MLL5 and DAXX (PubMed:11923872, PubMed:15053880, PubMed:16964248, PubMed:18716620, PubMed:25283148, PubMed:25865756, PubMed:26678539, PubMed:28655758, PubMed:33544460, PubMed:35216969). Together with DAXX, prevents MDM2 self-ubiquitination and enhances the E3 ligase activity of MDM2 towards p53/TP53, thereby promoting p53/TP53 ubiquitination and proteasomal degradation (PubMed:15053880, PubMed:16845383, PubMed:18566590, PubMed:20153724). Deubiquitinates p53/TP53, preventing degradation of p53/TP53, and enhances p53/TP53-dependent transcription regulation, cell growth repression and apoptosis (PubMed:25283148). Deubiquitinates p53/TP53 and MDM2 and strongly stabilizes p53/TP53 even in the presence of excess MDM2, and also induces p53/TP53-dependent cell growth repression and apoptosis (PubMed:11923872, PubMed:26786098). Deubiquitination of FOXO4 in presence of hydrogen peroxide is not dependent on p53/TP53 and inhibits FOXO4-induced transcriptional activity (PubMed:16964248). In association with DAXX, is involved in the deubiquitination and translocation of PTEN from the nucleus to the cytoplasm, both processes that are counteracted by PML (PubMed:18716620). Deubiquitinates KMT2E/MLL5 preventing KMT2E/MLL5 proteasomal-mediated degradation (PubMed:26678539). Involved in cell proliferation during early embryonic development. Involved in transcription-coupled nucleotide excision repair (TC-NER) in response to UV damage: recruited to DNA damage sites following interaction with KIAA1530/UVSSA and promotes deubiquitination of ERCC6, preventing UV-induced degradation of ERCC6 (PubMed:22466611, PubMed:22466612). Involved in maintenance of DNA methylation via its interaction with UHRF1 and DNMT1: acts by mediating deubiquitination of UHRF1 and DNMT1, preventing their degradation and promoting DNA methylation by DNMT1 (PubMed:21745816, PubMed:22411829). Deubiquitinates alkylation repair enzyme ALKBH3. OTUD4 recruits USP7 and USP9X to stabilize ALKBH3, thereby promoting the repair of alkylated DNA lesions (PubMed:25944111). Acts as a chromatin regulator via its association with the Polycomb group (PcG) multiprotein PRC1-like complex; may act by deubiquitinating components of the PRC1-like complex (PubMed:20601937). Able to mediate deubiquitination of histone H2B; it is however unsure whether this activity takes place in vivo (PubMed:20601937). Exhibits a preference towards 'Lys-48'-linked ubiquitin chains (PubMed:22689415). Increases regulatory T-cells (Treg) suppressive capacity by deubiquitinating and stabilizing the transcription factor FOXP3 which is crucial for Treg cell function (PubMed:23973222). Plays a role in the maintenance of the circadian clock periodicity via deubiquitination and stabilization of the CRY1 and CRY2 proteins (PubMed:27123980). Deubiquitinates REST, thereby stabilizing REST and promoting the maintenance of neural progenitor cells (PubMed:21258371). Deubiquitinates SIRT7, inhibiting SIRT7 histone deacetylase activity and regulating gluconeogenesis (PubMed:28655758). Involved in the regulation of WASH-dependent actin polymerization at the surface of endosomes and the regulation of endosomal protein recycling (PubMed:26365382). It maintains optimal WASH complex activity and precise F-actin levels via deubiquitination of TRIM27 and WASHC1 (PubMed:26365382). Mediates the deubiquitination of phosphorylated DEPTOR, promoting its stability and leading to decreased mTORC1 signaling (PubMed:35216969)", "gene_name": "USP7", "glycan_count": 2, "glycosylation_sites": [], "id": "Q93009", "name": "CBX4", "organism": "Homo sapiens", "uniprot_id": "Q93009" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "WAB53637", "name": "HPV-31 E6", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "WAB53638", "name": "HPV-31 E7", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "WAB54303", "name": "HPV-52 E6", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "WAB54304", "name": "HPV-52 E7", "organism": "", "uniprot_id": "" }, { "function": "Important regulator of cell cycle progression. Inhibits the kinase activity of CDK2 bound to cyclin A, but has little inhibitory activity on CDK2 bound to SPDYA (PubMed:28666995). Involved in G1 arrest. Potent inhibitor of cyclin E- and cyclin A-CDK2 complexes. Forms a complex with cyclin type D-CDK4 complexes and is involved in the assembly, stability, and modulation of CCND1-CDK4 complex activation. Acts either as an inhibitor or an activator of cyclin type D-CDK4 complexes depending on its phosphorylation state and/or stoichometry", "gene_name": "CDKN1B", "glycan_count": 1, "glycosylation_sites": [], "id": "P46527", "name": "p27 (CDKN1B)", "organism": "Homo sapiens", "uniprot_id": "P46527" }, { "function": "Orphan receptor. May play a role in brain function", "gene_name": "GPR63", "glycan_count": 0, "glycosylation_sites": [ { "position": 16, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 28, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 62, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9BZJ6", "name": "TRPM2", "organism": "Homo sapiens", "uniprot_id": "Q9BZJ6" }, { "function": "Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 2 complex (dynein-2 complex), a motor protein complex that drives the movement of cargos along microtubules within cilia and flagella in concert with the intraflagellar transport (IFT) system (PubMed:23910462, PubMed:25205765, PubMed:29742051, PubMed:31451806). DYNC2I1 plays a major role in retrograde ciliary protein trafficking in cilia and flagella (PubMed:29742051, PubMed:30320547, PubMed:30649997). Also requires to maintain a functional transition zone (PubMed:30320547)", "gene_name": "DYNC2I1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8WVS4", "name": "Charcot-Leyden crystal protein (Galectin-10)", "organism": "Homo sapiens", "uniprot_id": "Q8WVS4" }, { "function": "Specific inhibition of calpain (calcium-dependent cysteine protease). Plays a key role in postmortem tenderization of meat and have been proposed to be involved in muscle protein degradation in living tissue", "gene_name": "CAST", "glycan_count": 0, "glycosylation_sites": [], "id": "P20811", "name": "Eosinophil peroxidase (EPX)", "organism": "Bos taurus", "uniprot_id": "P20811" }, { "function": "Cytotoxin and helminthotoxin with low-efficiency ribonuclease activity. Possesses a wide variety of biological activities. Exhibits antibacterial activity, including cytoplasmic membrane depolarization of preferentially Gram-negative, but also Gram-positive strains. Promotes E.coli outer membrane detachment, alteration of the overall cell shape and partial loss of cell content", "gene_name": "RNASE3", "glycan_count": 0, "glycosylation_sites": [ { "position": 84, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 92, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 119, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P12724", "name": "Eosinophil cationic protein (ECP)", "organism": "Homo sapiens", "uniprot_id": "P12724" }, { "function": "", "gene_name": "ALDOC", "glycan_count": 1, "glycosylation_sites": [], "id": "P09972", "name": "Major basic protein (MBP)", "organism": "Homo sapiens", "uniprot_id": "P09972" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "not available", "name": "ES-62", "organism": "", "uniprot_id": "" }, { "function": "Involved in sperm flagellum assembly (PubMed:34792097, PubMed:35174165). Plays an essential role in the formation of the radial spokes in flagellum axoneme (By similarity)", "gene_name": "CFAP61", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8NHU2", "name": "GALNT14", "organism": "Homo sapiens", "uniprot_id": "Q8NHU2" }, { "function": "Catalyzes the ATP-dependent ligation of histidine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (His-AMP) (PubMed:29235198). Plays a role in axon guidance (PubMed:26072516)", "gene_name": "HARS1", "glycan_count": 1, "glycosylation_sites": [], "id": "P12081", "name": "Jo-1 (Histidyl-tRNA synthetase)", "organism": "Homo sapiens", "uniprot_id": "P12081" }, { "function": "E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2 (PubMed:16297862, PubMed:16316627, PubMed:16472766, PubMed:16880511, PubMed:18022694, PubMed:18361920, PubMed:18641315, PubMed:18845142, PubMed:19675099, PubMed:26347139). Forms a ubiquitin ligase complex in cooperation with the E2 UBE2D2 that is used not only for the ubiquitination of USP4 and IKBKB but also for its self-ubiquitination (PubMed:16880511, PubMed:19675099). Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF(SKP2)-like complexes (PubMed:16880511). A TRIM21-containing SCF(SKP2)-like complex is shown to mediate ubiquitination of CDKN1B ('Thr-187' phosphorylated-form), thereby promoting its degradation by the proteasome (PubMed:16880511). Monoubiquitinates IKBKB that will negatively regulates Tax-induced NF-kappa-B signaling (PubMed:19675099). Negatively regulates IFN-beta production post-pathogen recognition by catalyzing polyubiquitin-mediated degradation of IRF3 (PubMed:18641315). Mediates the ubiquitin-mediated proteasomal degradation of IgG1 heavy chain, which is linked to the VCP-mediated ER-associated degradation (ERAD) pathway (PubMed:18022694). Promotes IRF8 ubiquitination, which enhanced the ability of IRF8 to stimulate cytokine genes transcription in macrophages (By similarity). Plays a role in the regulation of the cell cycle progression (PubMed:16880511). Enhances the decapping activity of DCP2 (PubMed:18361920). Exists as a ribonucleoprotein particle present in all mammalian cells studied and composed of a single polypeptide and one of four small RNA molecules (PubMed:1985094, PubMed:8666824). At least two isoforms are present in nucleated and red blood cells, and tissue specific differences in RO/SSA proteins have been identified (PubMed:8666824). The common feature of these proteins is their ability to bind HY RNAs.2 (PubMed:8666824). Involved in the regulation of innate immunity and the inflammatory response in response to IFNG/IFN-gamma (PubMed:26347139). Organizes autophagic machinery by serving as a platform for the assembly of ULK1, Beclin 1/BECN1 and ATG8 family members and recognizes specific autophagy targets, thus coordinating target recognition with assembly of the autophagic apparatus and initiation of autophagy (PubMed:26347139). Also regulates autophagy through FIP200/RB1CC1 ubiquitination and subsequent decreased protein stability (PubMed:36359729). Represses the innate antiviral response by facilitating the formation of the NMI-IFI35 complex through 'Lys-63'-linked ubiquitination of NMI (PubMed:26342464). During viral infection, promotes cell pyroptosis by mediating 'Lys-6'-linked ubiquitination of ISG12a/IFI27, facilitating its translocation into the mitochondria and subsequent CASP3 activation (PubMed:36426955). When up-regulated through the IFN/JAK/STAT signaling pathway, promotes 'Lys-27'-linked ubiquitination of MAVS, leading to the recruitment of TBK1 and up-regulation of innate immunity (PubMed:29743353). Mediates 'Lys-63'-linked polyubiquitination of G3BP1 in response to heat shock, leading to stress granule disassembly (PubMed:36692217)", "gene_name": "TRIM21", "glycan_count": 1, "glycosylation_sites": [], "id": "P19474", "name": "Ro52 (TRIM21)", "organism": "Homo sapiens", "uniprot_id": "P19474" }, { "function": "Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The activity requires interaction with HSP90alpha. Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'", "gene_name": "SMYD2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NRG4", "name": "SMYD2", "organism": "Homo sapiens", "uniprot_id": "Q9NRG4" }, { "function": "Histone methyltransferase. Specifically methylates 'Lys-4' of histone H3, inducing di- and tri-methylation, but not monomethylation (PubMed:15235609, PubMed:22419068). Also methylates 'Lys-5' of histone H4 (PubMed:22419068). Plays an important role in transcriptional activation as a member of an RNA polymerase complex (PubMed:15235609). Binds DNA containing 5'-CCCTCC-3' or 5'-GAGGGG-3' sequences (PubMed:15235609)", "gene_name": "SMYD3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H7B4", "name": "SMYD3", "organism": "Homo sapiens", "uniprot_id": "Q9H7B4" }, { "function": "Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin", "gene_name": "TUBA1A", "glycan_count": 2, "glycosylation_sites": [], "id": "Q71U36", "name": "\u03b1-tubulin", "organism": "Homo sapiens", "uniprot_id": "Q71U36" }, { "function": "Glycosyltransferase required for the biosynthesis of heparan-sulfate (HS) (PubMed:11390981). Transfers N-acetyl-alpha-D-glucosamine to the nascent HS chain (GlcNAcT-II activity) (PubMed:11390981). Appears to lack GlcNAcT I and GlcAT-II activities (PubMed:11390981)", "gene_name": "EXTL1", "glycan_count": 0, "glycosylation_sites": [ { "position": 269, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q92935", "name": "RAP1GDS1", "organism": "Homo sapiens", "uniprot_id": "Q92935" }, { "function": "Catalyzes the phosphorylation of the purine nucleoside adenosine at the 5' position in an ATP-dependent manner. Serves as a potential regulator of concentrations of extracellular adenosine and intracellular adenine nucleotides", "gene_name": "ADK", "glycan_count": 1, "glycosylation_sites": [], "id": "P55263", "name": "ADK", "organism": "Homo sapiens", "uniprot_id": "P55263" }, { "function": "DNA polymerase that functions in several pathways of DNA repair (PubMed:11457865, PubMed:19806195, PubMed:20693240, PubMed:30250067). Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA (PubMed:11457865, PubMed:19806195). Also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination (PubMed:19806195, PubMed:20693240, PubMed:30250067). Has both template-dependent and template-independent (terminal transferase) DNA polymerase activities (PubMed:10887191, PubMed:10982892, PubMed:12809503, PubMed:14627824, PubMed:15537631, PubMed:19806195). Also has a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity (PubMed:11457865, PubMed:19806195)", "gene_name": "POLL", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9UGP5", "name": "POLL", "organism": "Homo sapiens", "uniprot_id": "Q9UGP5" }, { "function": "Plays an important role in the process of myofiber differentiation and maturation. Probable substrate-recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex, which mediates the ubiquitination of proteins. Probably contributes to catalysis through recognition and positioning of the substrate and the ubiquitin-conjugating enzyme. During myogenesis, controls the ubiquitination and degradation of the specific pool of CTNNB1/beta-catenin located at the sarcolemma (By similarity)", "gene_name": "NEURL2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9BR09", "name": "SULT1B1", "organism": "Homo sapiens", "uniprot_id": "Q9BR09" }, { "function": "Facilitates proton transport across the inner mitochondrial membrane and may dissipate excessive proton gradient associated with oxidative and metabolic stress at neuronal synapses. Regulates glutamate-induced proton conductance in astrocytes, shifting the energy metabolism toward aerobic glycolysis and lactate transfer to neurons for ATP synthesis. Can transport chloride ions with lower efficiency. The transport mechanism remains to be elucidated", "gene_name": "SLC25A27", "glycan_count": 0, "glycosylation_sites": [], "id": "O95847", "name": "ACSL4", "organism": "Homo sapiens", "uniprot_id": "O95847" }, { "function": "Receptor for prostaglandin D2 (PGD2). Coupled to the G(i)-protein. Receptor activation may result in pertussis toxin-sensitive decreases in cAMP levels and Ca(2+) mobilization. PI3K signaling is also implicated in mediating PTGDR2 effects. PGD2 induced receptor internalization. CRTH2 internalization can be regulated by diverse kinases such as, PKC, PKA, GRK2, GPRK5/GRK5 and GRK6. Receptor activation is responsible, at least in part, in immune regulation and allergic/inflammation responses", "gene_name": "PTGDR2", "glycan_count": 0, "glycosylation_sites": [ { "position": 4, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 25, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y5Y4", "name": "CRTH2 (Chemoattractant Receptor-homologous molecule expressed on Th2 cells)", "organism": "Homo sapiens", "uniprot_id": "Q9Y5Y4" }, { "function": "Ubiquitin-like protein which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Covalent attachment to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4 (PubMed:11451954, PubMed:18538659, PubMed:21965678). Plays a role in the regulation of sumoylation status of SETX (PubMed:24105744)", "gene_name": "SUMO3", "glycan_count": 1, "glycosylation_sites": [], "id": "P55854", "name": "SUMO3", "organism": "Homo sapiens", "uniprot_id": "P55854" }, { "function": "Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC (PubMed:15146057, PubMed:17363900). The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation. This subunit plays a role in recruitment of the Nup107-160 subcomplex to the kinetochore (PubMed:15146057, PubMed:17363900)", "gene_name": "SEH1L", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96EE3", "name": "SEH1L", "organism": "Homo sapiens", "uniprot_id": "Q96EE3" }, { "function": "Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme", "gene_name": "FLAD1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8NFF5", "name": "NUP43", "organism": "Homo sapiens", "uniprot_id": "Q8NFF5" }, { "function": "May function as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks", "gene_name": "ARPC5L", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9BPX5", "name": "NUP50", "organism": "Homo sapiens", "uniprot_id": "Q9BPX5" }, { "function": "The alpha-2/delta subunit of voltage-dependent calcium channels regulates calcium current density and activation/inactivation kinetics of the calcium channel. Acts as a regulatory subunit for P/Q-type calcium channel (CACNA1A), N-type (CACNA1B), L-type (CACNA1C OR CACNA1D) but not T-type (CACNA1G) (By similarity)", "gene_name": "CACNA2D3", "glycan_count": 0, "glycosylation_sites": [ { "position": 166, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 309, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 553, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 632, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 793, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8IZS8", "name": "MS4A12", "organism": "Homo sapiens", "uniprot_id": "Q8IZS8" }, { "function": "Contributes to the transcriptional repression of cholesterol 7-alpha-hydroxylase (CYP7A1), the rate-limiting enzyme in bile acid synthesis. Probably inactive as a glycosidase. Increases the ability of FGFR1 and FGFR4 to bind FGF21 (By similarity)", "gene_name": "KLB", "glycan_count": 5, "glycosylation_sites": [ { "position": 71, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 120, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 125, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 211, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 308, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 391, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 554, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 611, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 702, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 706, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 971, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q86Z14", "name": "\u03b2-klotho (KLB)", "organism": "Homo sapiens", "uniprot_id": "Q86Z14" }, { "function": "", "gene_name": "tat", "glycan_count": 0, "glycosylation_sites": [], "id": "Q3S5G7", "name": "Adiponectin (Adipoq)", "organism": "Human immunodeficiency virus type 1", "uniprot_id": "Q3S5G7" }, { "function": "Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus", "gene_name": "Fabp4", "glycan_count": 1, "glycosylation_sites": [], "id": "P04117", "name": "Fatty acid-binding protein 4 (Fabp4)", "organism": "Mus musculus", "uniprot_id": "P04117" }, { "function": "NAD-dependent protein deacetylase that links transcriptional regulation directly to intracellular energetics and participates in the coordination of several separated cellular functions such as cell cycle, response to DNA damage, metabolism, apoptosis and autophagy (PubMed:11250901, PubMed:11672522, PubMed:12651913, PubMed:12887892, PubMed:12960381, PubMed:15175761, PubMed:15220471, PubMed:15632193, PubMed:15744310, PubMed:15788402, PubMed:16098828, PubMed:16366736, PubMed:16790548, PubMed:16892051, PubMed:17098745, PubMed:17347648, PubMed:17620057, PubMed:17901049, PubMed:17936707, PubMed:18004385, PubMed:18296641, PubMed:18371449, PubMed:18477450, PubMed:18662546, PubMed:18662547, PubMed:18687677, PubMed:19299583, PubMed:19356714, PubMed:20167603, PubMed:20817729, PubMed:21176092, PubMed:21187328, PubMed:21189328, PubMed:21622680, PubMed:23160044, PubMed:28883095). Can modulate chromatin function through deacetylation of histones and can promote alterations in the methylation of histones and DNA, leading to transcriptional repression (By similarity). Deacetylates a broad range of transcription factors and coregulators, thereby regulating target gene expression positively and negatively (By similarity). Serves as a sensor of the cytosolic ratio of NAD(+)/NADH which is altered by glucose deprivation and metabolic changes associated with caloric restriction (By similarity). Is essential in skeletal muscle cell differentiation and in response to low nutrients mediates the inhibitory effect on skeletal myoblast differentiation which also involves 5'-AMP-activated protein kinase (AMPK) and nicotinamide phosphoribosyltransferase (NAMPT) (PubMed:12887892, PubMed:18477450). Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes (By similarity). The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus (PubMed:18004385). Deacetylates 'Lys-266' of SUV39H1, leading to its activation (By similarity). Inhibits skeletal muscle differentiation by deacetylating PCAF and MYOD1 (PubMed:12887892). Deacetylates H2A and 'Lys-26' of H1-4 (By similarity). Deacetylates 'Lys-16' of histone H4 (in vitro) (By similarity). Involved in NR0B2/SHP corepression function through chromatin remodeling: Recruited to LRH1 target gene promoters by NR0B2/SHP thereby stimulating histone H3 and H4 deacetylation leading to transcriptional repression (By similarity). Proposed to contribute to genomic integrity via positive regulation of telomere length; however, reports on localization to pericentromeric heterochromatin are conflicting (PubMed:21187328). Proposed to play a role in constitutive heterochromatin (CH) formation and/or maintenance through regulation of the available pool of nuclear SUV39H1 (By similarity). Upon oxidative/metabolic stress decreases SUV39H1 degradation by inhibiting SUV39H1 polyubiquitination by MDM2 (By similarity). This increase in SUV39H1 levels enhances SUV39H1 turnover in CH, which in turn seems to accelerate renewal of the heterochromatin which correlates with greater genomic integrity during stress response (By similarity). Deacetylates 'Lys-382' of p53/TP53 and impairs its ability to induce transcription-dependent proapoptotic program and modulate cell senescence (PubMed:11672522, PubMed:12960381). Deacetylates TAF1B and thereby represses rDNA transcription by the RNA polymerase I (PubMed:11250901). Deacetylates MYC, promotes the association of MYC with MAX and decreases MYC stability leading to compromised transformational capability (By similarity). Deacetylates FOXO3 in response to oxidative stress thereby increasing its ability to induce cell cycle arrest and resistance to oxidative stress but inhibiting FOXO3-mediated induction of apoptosis transcriptional activity; also leading to FOXO3 ubiquitination and protesomal degradation (By similarity). Appears to have a similar effect on MLLT7/FOXO4 in regulation of transcriptional activity and apoptosis (By similarity). Deacetylates DNMT1; thereby impairs DNMT1 methyltransferase-independent transcription repressor activity, modulates DNMT1 cell cycle regulatory function and DNMT1-mediated gene silencing (By similarity). Deacetylates RELA/NF-kappa-B p65 thereby inhibiting its transactivating potential and augments apoptosis in response to TNF-alpha (By similarity). Deacetylates HIF1A, KAT5/TIP60, RB1 and HIC1 (PubMed:17620057). Deacetylates FOXO1, which increases its DNA binding ability and enhances its transcriptional activity leading to increased gluconeogenesis in liver (PubMed:15220471, PubMed:15788402). Inhibits E2F1 transcriptional activity and apoptotic function, possibly by deacetylation (PubMed:16892051). Involved in HES1- and HEY2-mediated transcriptional repression (By similarity). In cooperation with MYCN seems to be involved in transcriptional repression of DUSP6/MAPK3 leading to MYCN stabilization by phosphorylation at 'Ser-62' (By similarity). Deacetylates MEF2D (By similarity). Required for antagonist-mediated transcription suppression of AR-dependent genes which may be linked to local deacetylation of histone H3 (By similarity). Represses HNF1A-mediated transcription (PubMed:21176092). Required for the repression of ESRRG by CREBZF (By similarity). Deacetylates NR1H3 and NR1H2 and deacetylation of NR1H3 at 'Lys-434' positively regulates transcription of NR1H3:RXR target genes, promotes NR1H3 proteasomal degradation and results in cholesterol efflux; a promoter clearing mechanism after reach round of transcription is proposed (PubMed:17936707). Involved in lipid metabolism: deacetylates LPIN1, thereby inhibiting diacylglycerol synthesis (By similarity). Implicated in regulation of adipogenesis and fat mobilization in white adipocytes by repression of PPARG which probably involves association with NCOR1 and SMRT/NCOR2 (PubMed:15175761). Deacetylates p300/EP300 and PRMT1 (PubMed:15632193, PubMed:28883095). Deacetylates ACSS2 leading to its activation, and HMGCS1 deacetylation (PubMed:16790548). Involved in liver and muscle metabolism (By similarity). Through deacetylation and activation of PPARGC1A is required to activate fatty acid oxidation in skeletal muscle under low-glucose conditions and is involved in glucose homeostasis (PubMed:15716268, PubMed:15744310, PubMed:17347648, PubMed:23142079). Involved in regulation of PPARA and fatty acid beta-oxidation in liver (PubMed:19356714). Involved in positive regulation of insulin secretion in pancreatic beta cells in response to glucose; the function seems to imply transcriptional repression of UCP2 (PubMed:16098828, PubMed:16366736, PubMed:17901049). Proposed to deacetylate IRS2 thereby facilitating its insulin-induced tyrosine phosphorylation (PubMed:17901049). Deacetylates SREBF1 isoform SREBP-1C thereby decreasing its stability and transactivation in lipogenic gene expression (By similarity). Involved in DNA damage response by repressing genes which are involved in DNA repair, such as XPC and TP73, deacetylating XRCC6/Ku70, and facilitating recruitment of additional factors to sites of damaged DNA, such as SIRT1-deacetylated NBN can recruit ATM to initiate DNA repair and SIRT1-deacetylated XPA interacts with RPA2 (By similarity). Also involved in DNA repair of DNA double-strand breaks by homologous recombination and specifically single-strand annealing independently of XRCC6/Ku70 and NBN (By similarity). Promotes DNA double-strand breaks by mediating deacetylation of SIRT6 (By similarity). Transcriptional suppression of XPC probably involves an E2F4:RBL2 suppressor complex and protein kinase B (AKT) signaling (By similarity). Transcriptional suppression of TP73 probably involves E2F4 and PCAF (By similarity). Deacetylates WRN thereby regulating its helicase and exonuclease activities and regulates WRN nuclear translocation in response to DNA damage (By similarity). Deacetylates APEX1 at 'Lys-6' and 'Lys-7' and stimulates cellular AP endonuclease activity by promoting the association of APEX1 to XRCC1 (By similarity). Catalyzes deacetylation of ERCC4/XPF, thereby impairing interaction with ERCC1 and nucleotide excision repair (NER) (By similarity). Increases p53/TP53-mediated transcription-independent apoptosis by blocking nuclear translocation of cytoplasmic p53/TP53 and probably redirecting it to mitochondria (By similarity). Deacetylates XRCC6/Ku70 at 'Lys-537' and 'Lys-540' causing it to sequester BAX away from mitochondria thereby inhibiting stress-induced apoptosis (By similarity). Is involved in autophagy, presumably by deacetylating ATG5, ATG7 and MAP1LC3B/ATG8 (PubMed:18296641, PubMed:21189328). Deacetylates AKT1 which leads to enhanced binding of AKT1 and PDK1 to PIP3 and promotes their activation (By similarity). Proposed to play role in regulation of STK11/LBK1-dependent AMPK signaling pathways implicated in cellular senescence which seems to involve the regulation of the acetylation status of STK11/LBK1 (PubMed:18687677). Can deacetylate STK11/LBK1 and thereby increase its activity, cytoplasmic localization and association with STRAD; however, the relevance of such activity in normal cells is unclear (By similarity). In endothelial cells is shown to inhibit STK11/LBK1 activity and to promote its degradation (By similarity). Deacetylates SMAD7 at 'Lys-64' and 'Lys-70' thereby promoting its degradation (PubMed:17098745). Deacetylates CIITA and augments its MHC class II transactivation and contributes to its stability (By similarity). Deacetylates MECOM/EVI1 (By similarity). Deacetylates PML at 'Lys-487' and this deacetylation promotes PML control of PER2 nuclear localization (By similarity). During the neurogenic transition, represses selective NOTCH1-target genes through histone deacetylation in a BCL6-dependent manner and leading to neuronal differentiation (By similarity). Regulates the circadian expression of several core clock genes, including BMAL1, RORC, PER2 and CRY1 and plays a critical role in maintaining a controlled rhythmicity in histone acetylation, thereby contributing to circadian chromatin remodeling (PubMed:18662546, PubMed:18662547, PubMed:19299583). Deacetylates BMAL1 and histones at the circadian gene promoters in order to facilitate repression by inhibitory components of the circadian oscillator (PubMed:18662546, PubMed:18662547, PubMed:19299583). Deacetylates PER2, facilitating its ubiquitination and degradation by the proteasome (PubMed:18662546). Protects cardiomyocytes against palmitate-induced apoptosis (PubMed:21622680). Deacetylates XBP1 isoform 2; deacetylation decreases protein stability of XBP1 isoform 2 and inhibits its transcriptional activity (By similarity). Deacetylates PCK1 and directs its activity toward phosphoenolpyruvate production promoting gluconeogenesis (PubMed:30193097). Involved in the CCAR2-mediated regulation of PCK1 and NR1D1 (By similarity). Deacetylates CTNB1 at 'Lys-49' (By similarity). In POMC (pro-opiomelanocortin) neurons, required for leptin-induced activation of PI3K signaling (PubMed:20620997). Deacetylates SOX9; promoting SOX9 nuclear localization and transactivation activity (PubMed:26910618). Involved in the regulation of centrosome duplication: Deacetylates CENATAC in G1 phase, allowing for SASS6 accumulation on the centrosome and subsequent procentriole assembly (By similarity). Deacetylates NDC80/HEC1 (By similarity). In addition to protein deacetylase activity, also acts as a protein-lysine deacylase by mediating protein delactylation, depropionylation and decrotonylation (PubMed:30026585). Mediates depropionylation of Osterix (SP7) (PubMed:30026585). Catalyzes decrotonylation of histones; it however does not represent a major histone decrotonylase (By similarity). Mediates protein delactylation of TEAD1 and YAP1 (By similarity)", "gene_name": "Sirt1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q923E4", "name": "Sirtuin 1 (Sirt1)", "organism": "Mus musculus", "uniprot_id": "Q923E4" }, { "function": "Interacts strongly with CDK4 and CDK6. Potent inhibitor. Potential effector of TGF-beta induced cell cycle arrest", "gene_name": "CDKN2B", "glycan_count": 0, "glycosylation_sites": [], "id": "P42772", "name": "Cyclin-dependent kinase inhibitor 2A (p16INK4a)", "organism": "Homo sapiens", "uniprot_id": "P42772" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Z0K1", "name": "Cell death-inducing DFFA-like effector A (Cidea)", "organism": "Cavia porcellus", "uniprot_id": "Q9Z0K1" }, { "function": "Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Parts of the peripheral arm of the enzyme, where the electrons from NADH are accepted by flavin mononucleotide (FMN) and then passed along a chain of iron-sulfur clusters by electron tunnelling to the final acceptor ubiquinone. Contains one iron-sulfur cluster", "gene_name": "Ndufv2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9D6J6", "name": "Ubiquinol-cytochrome c reductase core protein 1 (Uqcrc1)", "organism": "Mus musculus", "uniprot_id": "Q9D6J6" }, { "function": "Subunit alpha, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel. These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). With the catalytic subunit beta (ATP5F1B), forms the catalytic core in the F(1) domain. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity)", "gene_name": "Atp5f1a", "glycan_count": 1, "glycosylation_sites": [ { "position": 76, "type": "O-linked (GlcNAc) serine; alternate" } ], "id": "Q03265", "name": "ATP synthase subunit alpha (Atp5a1)", "organism": "Mus musculus", "uniprot_id": "Q03265" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Multiple/Unspecified", "name": "Peptide mass fingerprint (PMF) panel", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6D7Z0", "name": "TIGIT", "organism": "Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672)", "uniprot_id": "Q6D7Z0" }, { "function": "PACAP is a neuropeptide involved in diverse array of physiological processes through activating the PACAP subfamily of class B1 G protein-coupled receptors: VIP receptor 1 (VIPR1), VIP receptor 2 (VIPR2), and PACAP type I receptor (ADCYAP1R1) (PubMed:11175907, PubMed:23800469, PubMed:32047270, PubMed:36385145). Exerts neuroprotective and general cytoprotective effects due to anti-apoptotic, anti-inflammatory, and antioxidant actions (PubMed:23800469). Promotes neuron projection development through the RAPGEF2/Rap1/B-Raf/ERK pathway (PubMed:23800469). In chromaffin cells, induces long-lasting increase of intracellular calcium concentrations and neuroendocrine secretion (By similarity). Involved in the control of glucose homeostasis, induces insulin secretion by pancreatic beta cells (By similarity). PACAP exists in two bioactive forms from proteolysis of the same precursor protein, PACAP27 and PACAP38, which differ by eleven amino acid residues in the C-terminus (PubMed:32047270)", "gene_name": "ADCYAP1", "glycan_count": 0, "glycosylation_sites": [], "id": "P18509", "name": "Pituitary adenylate cyclase-activating polypeptide (PACAP)", "organism": "Homo sapiens", "uniprot_id": "P18509" }, { "function": "Splicing factor binding to exonic or intronic sites and acting as either an activator or repressor of exon inclusion. Exhibits a binding preference for CA-rich elements (PubMed:11809897, PubMed:22570490, PubMed:24164894, PubMed:25623890, PubMed:26051023). Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes and associated with most nascent transcripts (PubMed:2687284). Associates, together with APEX1, to the negative calcium responsive element (nCaRE) B2 of the APEX2 promoter (PubMed:11809897). As part of a ribonucleoprotein complex composed at least of ZNF827, HNRNPK and the circular RNA circZNF827 that nucleates the complex on chromatin, may negatively regulate the transcription of genes involved in neuronal differentiation (PubMed:33174841). Regulates alternative splicing of a core group of genes involved in neuronal differentiation, likely by mediating H3K36me3-coupled transcription elongation and co-transcriptional RNA processing via interaction with CHD8", "gene_name": "HNRNPL", "glycan_count": 1, "glycosylation_sites": [], "id": "P14866", "name": "HNRNPL", "organism": "Homo sapiens", "uniprot_id": "P14866" }, { "function": "Protease that releases SUMO2 and SUMO3 monomers from sumoylated substrates, but has only weak activity against SUMO1 conjugates (PubMed:16608850, PubMed:32832608, PubMed:36050397). Deconjugates SUMO2 from MEF2D, which increases its transcriptional activation capability (PubMed:15743823). Deconjugates SUMO2 and SUMO3 from CDCA8 (PubMed:18946085). Redox sensor that, when redistributed into nucleoplasm, can act as an effector to enhance HIF1A transcriptional activity by desumoylating EP300 (PubMed:19680224). Required for rRNA processing through deconjugation of SUMO2 and SUMO3 from nucleophosmin, NPM1 (PubMed:19015314). Plays a role in the regulation of sumoylation status of ZNF148 (PubMed:18259216). Functions as a component of the Five Friends of Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and subsequent transactivation of ZNF148 target genes (PubMed:22872859). Deconjugates SUMO2 from KAT5 (PubMed:32832608). Catalyzes desumoylation of MRE11 (PubMed:36050397)", "gene_name": "SENP3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H4L4", "name": "SENP3", "organism": "Homo sapiens", "uniprot_id": "Q9H4L4" }, { "function": "Probable substrate recognition component of an ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins", "gene_name": "Lrrc41", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8K1C9", "name": "Folr2 (Folate receptor beta)", "organism": "Mus musculus", "uniprot_id": "Q8K1C9" }, { "function": "Inhibits the activity of dimeric NF-kappa-B/REL complexes by trapping REL (RELA/p65 and NFKB1/p50) dimers in the cytoplasm by masking their nuclear localization signals (PubMed:10097128, PubMed:9990853). On cellular stimulation by immune and pro-inflammatory responses, becomes phosphorylated promoting ubiquitination and degradation, enabling the dimeric RELA to translocate to the nucleus and activate transcription (PubMed:10097128, PubMed:7878466, PubMed:9990853)", "gene_name": "Nfkbia", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Z1E3", "name": "CD69", "organism": "Mus musculus", "uniprot_id": "Q9Z1E3" }, { "function": "Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes (PubMed:10872825). May be involved in the control of cAMP-mediated neural activity and cAMP metabolism in the brain (By similarity)", "gene_name": "Pde7b", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9QXQ1", "name": "CD103 (Integrin alpha E)", "organism": "Mus musculus", "uniprot_id": "Q9QXQ1" }, { "function": "Involved in clearance and endocytosis of hemoglobin/haptoglobin complexes by macrophages and may thereby protect tissues from free hemoglobin-mediated oxidative damage. May play a role in the uptake and recycling of iron, via endocytosis of hemoglobin/haptoglobin and subsequent breakdown of heme. Binds hemoglobin/haptoglobin complexes in a calcium-dependent and pH-dependent manner. Induces a cascade of intracellular signals that involves tyrosine kinase-dependent calcium mobilization, inositol triphosphate production and secretion of IL6 and CSF1 (By similarity)", "gene_name": "Cd163", "glycan_count": 4, "glycosylation_sites": [ { "position": 104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 138, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q2VLH6", "name": "CD163", "organism": "Mus musculus", "uniprot_id": "Q2VLH6" }, { "function": "High affinity receptor for the Fc region of immunoglobulins gamma. Functions in both innate and adaptive immune responses", "gene_name": "Fcgr1", "glycan_count": 1, "glycosylation_sites": [ { "position": 28, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 48, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 69, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 168, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 249, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P26151", "name": "CD64 (Fc\u03b3RI)", "organism": "Mus musculus", "uniprot_id": "P26151" }, { "function": "Catalyzes the interconversion between carbon dioxide and water and the dissociated ions of carbonic acid (i.e. bicarbonate and hydrogen ions)", "gene_name": "Ca9", "glycan_count": 0, "glycosylation_sites": [ { "position": 98, "type": "O-linked (GlcNAc...) threonine" }, { "position": 325, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8K1G1", "name": "CD68", "organism": "Mus musculus", "uniprot_id": "Q8VHB5" }, { "function": "Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling (PubMed:12192039, PubMed:27098453, PubMed:28829046). Controls dorsoventral patterning via two opposing effects; down-regulates CTNNB1 to inhibit the Wnt signaling pathway and ventralize embryos, but also dorsalizes embryos by activating a Wnt-independent JNK signaling pathway (PubMed:12192039). In Wnt signaling, probably facilitates the phosphorylation of CTNNB1 and APC by GSK3B (PubMed:12192039). Likely to function as a tumor suppressor. Enhances TGF-beta signaling by recruiting the RNF111 E3 ubiquitin ligase and promoting the degradation of inhibitory SMAD7 (PubMed:16601693). Also a component of the AXIN1-HIPK2-TP53 complex which controls cell growth, apoptosis and development (PubMed:17210684). Facilitates the phosphorylation of TP53 by HIPK2 upon ultraviolet irradiation (PubMed:17210684)", "gene_name": "AXIN1", "glycan_count": 0, "glycosylation_sites": [], "id": "O15169", "name": "AXIN1", "organism": "Homo sapiens", "uniprot_id": "O15169" }, { "function": "Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. May act as a negative regulator of neural cell growth", "gene_name": "CDH13", "glycan_count": 81, "glycosylation_sites": [ { "position": 52, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 86, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 382, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 500, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 530, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 598, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 638, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 671, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P55290", "name": "T-cadherin", "organism": "Homo sapiens", "uniprot_id": "P55290" }, { "function": "Ligand-dependent transdominant repressor of steroid hormone receptor transcriptional activity including repression of its isoform B, MR and ER. Transrepressional activity may involve recruitment of corepressor NCOR2", "gene_name": "PGR", "glycan_count": 0, "glycosylation_sites": [], "id": "P06401-2", "name": "Progesterone Receptor B (PR-B)", "organism": "Homo sapiens", "uniprot_id": "P06401-2" }, { "function": "Transcriptional activator. Essential for sexual differentiation and formation of the primary steroidogenic tissues (PubMed:27378692). Binds to the Ad4 site found in the promoter region of steroidogenic P450 genes such as CYP11A, CYP11B and CYP21B. Also regulates the AMH/Muellerian inhibiting substance gene as well as the AHCH and STAR genes. 5'-YCAAGGYC-3' and 5'-RRAGGTCA-3' are the consensus sequences for the recognition by NR5A1 (PubMed:27378692). The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional activity. Binds phosphatidylcholine (By similarity). Binds phospholipids with a phosphatidylinositol (PI) headgroup, in particular PI(3,4)P2 and PI(3,4,5)P3. Activated by the phosphorylation of NR5A1 by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation", "gene_name": "NR5A1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q13285", "name": "Steroidogenic Factor 1 (SF-1)", "organism": "Homo sapiens", "uniprot_id": "Q13285" }, { "function": "Transcriptional activator (PubMed:19666519, PubMed:22750565, PubMed:22824924, PubMed:27756709). Regulates SEMA3C and PLXNA2 (PubMed:19666519). Involved in gene regulation specifically in the gastric epithelium (PubMed:9315713). May regulate genes that protect epithelial cells from bacterial infection (PubMed:16968778). Involved in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression (By similarity). Binds to BMP response element (BMPRE) DNA sequences within cardiac activating regions (By similarity). In human skin, controls several physiological processes contributing to homeostasis of the upper pilosebaceous unit. Triggers ductal and sebaceous differentiation as well as limits cell proliferation and lipid production to prevent hyperseborrhoea. Mediates the effects of retinoic acid on sebocyte proliferation, differentiation and lipid production. Also contributes to immune regulation of sebocytes and antimicrobial responses by modulating the expression of anti-inflammatory genes such as IL10 and pro-inflammatory genes such as IL6, TLR2, TLR4, and IFNG. Activates TGFB1 signaling which controls the interfollicular epidermis fate (PubMed:33082341)", "gene_name": "GATA6", "glycan_count": 1, "glycosylation_sites": [], "id": "Q92908", "name": "GATA6", "organism": "Homo sapiens", "uniprot_id": "Q92908" }, { "function": "Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Binds to the DNA sequence 5'-AA[AT]TTTTATTAC-3'", "gene_name": "HOXA10", "glycan_count": 1, "glycosylation_sites": [], "id": "P31260", "name": "Homeobox A10 (HOXA10)", "organism": "Homo sapiens", "uniprot_id": "P31260" }, { "function": "Rab effector involved in exocytosis. May act as scaffold protein. Plays a role in dendrite formation by melanocytes (PubMed:23999003)", "gene_name": "RIMS2", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9UQ26", "name": "Contactin-associated protein 1 (Caspr1)", "organism": "Homo sapiens", "uniprot_id": "Q9UQ26" }, { "function": "Through interaction with TMIGD2, costimulates T-cells in the context of TCR-mediated activation. Enhances T-cell proliferation and cytokine production via an AKT-dependent signaling cascade", "gene_name": "HHLA2", "glycan_count": 1, "glycosylation_sites": [ { "position": 90, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 103, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 318, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UM44", "name": "HHLA2", "organism": "Homo sapiens", "uniprot_id": "Q9UM44" }, { "function": "May regulate nociceptor function and/or development, including the sensation or modulation of pain. Functions as a specific membrane receptor for beta-alanine. Beta-alanine at micromolar doses specifically evoked Ca(2+) influx in cells expressing the receptor. Beta-alanine decreases forskolin-stimulated cAMP production in cells expressing the receptor, suggesting that the receptor couples with G-protein G(q) and G(i)", "gene_name": "MRGPRD", "glycan_count": 0, "glycosylation_sites": [ { "position": 2, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 6, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 16, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 92, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8TDS7", "name": "KIR3DL3", "organism": "Homo sapiens", "uniprot_id": "Q8TDS7" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "PVR: PVR_HUMAN", "name": "CD155", "organism": "", "uniprot_id": "" }, { "function": "Transcriptional repressor that modulates both activator-dependent and basal transcription. Involved in the generation and migration of neural crest cells. Plays a role in mediating RAF1-induced transcriptional repression of the TJ protein, occludin (OCLN) and subsequent oncogenic transformation of epithelial cells (By similarity). Represses BRCA2 expression by binding to its E2-box-containing silencer and recruiting CTBP1 and HDAC1 in breast cells. In epidermal keratinocytes, binds to the E-box in ITGA3 promoter and represses its transcription. Involved in the regulation of ITGB1 and ITGB4 expression and cell adhesion and proliferation in epidermal keratinocytes. Binds to E-box2 domain of BSG and activates its expression during TGFB1-induced epithelial-mesenchymal transition (EMT) in hepatocytes. Represses E-Cadherin/CDH1 transcription via E-box elements. Involved in osteoblast maturation. Binds to RUNX2 and SOC9 promoters and may act as a positive and negative transcription regulator, respectively, in osteoblasts. Binds to CXCL12 promoter via E-box regions in mesenchymal stem cells and osteoblasts. Plays an essential role in TWIST1-induced EMT and its ability to promote invasion and metastasis", "gene_name": "SNAI2", "glycan_count": 0, "glycosylation_sites": [], "id": "O43623", "name": "Slug (SNAI2)", "organism": "Homo sapiens", "uniprot_id": "O43623" }, { "function": "Inhibits translation initiation and cap-dependent translation. May excert its function by hindering the interaction between EIF4A1 and EIF4G. Inhibits the helicase activity of EIF4A. Modulates the activation of JUN kinase. Down-regulates the expression of MAP4K1, thus inhibiting events important in driving invasion, namely, MAPK85 activation and consequent JUN-dependent transcription. May play a role in apoptosis. Tumor suppressor. Inhibits tumor promoter-induced neoplastic transformation. Binds RNA (By similarity)", "gene_name": "PDCD4", "glycan_count": 1, "glycosylation_sites": [], "id": "Q53EL6", "name": "Pdcd4", "organism": "Homo sapiens", "uniprot_id": "Q53EL6" }, { "function": "ATP-dependent RNA helicase which is a subunit of the eIF4F complex involved in cap recognition and is required for mRNA binding to ribosome (PubMed:20156963). In the current model of translation initiation, eIF4A unwinds RNA secondary structures in the 5'-UTR of mRNAs which is necessary to allow efficient binding of the small ribosomal subunit, and subsequent scanning for the initiator codon. As a result, promotes cell proliferation and growth (PubMed:20156963)", "gene_name": "EIF4A1", "glycan_count": 1, "glycosylation_sites": [], "id": "P60842", "name": "eIF4A", "organism": "Homo sapiens", "uniprot_id": "P60842" }, { "function": "Cyclin which controls both the G1/S and the G2/M transition phases of the cell cycle. Functions through the formation of specific serine/threonine protein kinase holoenzyme complexes with the cyclin-dependent protein kinases CDK1 or CDK2. The cyclin subunit confers the substrate specificity of these complexes and differentially interacts with and activates CDK1 and CDK2 throughout the cell cycle", "gene_name": "CCNA2", "glycan_count": 0, "glycosylation_sites": [], "id": "P20248", "name": "Cyclin A", "organism": "Homo sapiens", "uniprot_id": "P20248" }, { "function": "Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2 (PubMed:7499431, PubMed:18541534, PubMed:22195962, PubMed:26942675, PubMed:17683942). This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate (PubMed:18541534, PubMed:22195962, PubMed:26942675). Plays an important role in cellular responses to hypoxia and is important for cell proliferation under hypoxia (PubMed:18541534, PubMed:22195962, PubMed:26942675)", "gene_name": "PDK1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q15118", "name": "Pyruvate dehydrogenase kinase (PDK)", "organism": "Homo sapiens", "uniprot_id": "Q15118" }, { "function": "Promotes the exchange of Ras-bound GDP by GTP (PubMed:8493579). Probably by promoting Ras activation, regulates phosphorylation of MAP kinase MAPK3/ERK1 in response to EGF (PubMed:17339331). Catalytic component of a trimeric complex that participates in transduction of signals from Ras to Rac by promoting the Rac-specific guanine nucleotide exchange factor (GEF) activity (By similarity)", "gene_name": "SOS1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q07889", "name": "SOS1", "organism": "Homo sapiens", "uniprot_id": "Q07889" }, { "function": "Tumor suppressor serine/threonine-protein kinase that controls the activity of AMP-activated protein kinase (AMPK) family members, thereby playing a role in various processes such as cell metabolism, cell polarity, apoptosis and DNA damage response. Acts by phosphorylating the T-loop of AMPK family proteins, thus promoting their activity: phosphorylates PRKAA1, PRKAA2, BRSK1, BRSK2, MARK1, MARK2, MARK3, MARK4, NUAK1, NUAK2, SIK1, SIK2, SIK3 and SNRK but not MELK. Also phosphorylates non-AMPK family proteins such as STRADA, PTEN and possibly p53/TP53. Acts as a key upstream regulator of AMPK by mediating phosphorylation and activation of AMPK catalytic subunits PRKAA1 and PRKAA2 and thereby regulates processes including: inhibition of signaling pathways that promote cell growth and proliferation when energy levels are low, glucose homeostasis in liver, activation of autophagy when cells undergo nutrient deprivation, and B-cell differentiation in the germinal center in response to DNA damage. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton. Required for cortical neuron polarization by mediating phosphorylation and activation of BRSK1 and BRSK2, leading to axon initiation and specification. Involved in DNA damage response: interacts with p53/TP53 and recruited to the CDKN1A/WAF1 promoter to participate in transcription activation. Able to phosphorylate p53/TP53; the relevance of such result in vivo is however unclear and phosphorylation may be indirect and mediated by downstream STK11/LKB1 kinase NUAK1. Also acts as a mediator of p53/TP53-dependent apoptosis via interaction with p53/TP53: translocates to the mitochondrion during apoptosis and regulates p53/TP53-dependent apoptosis pathways. Regulates UV radiation-induced DNA damage response mediated by CDKN1A. In association with NUAK1, phosphorylates CDKN1A in response to UV radiation and contributes to its degradation which is necessary for optimal DNA repair (PubMed:25329316)", "gene_name": "STK11", "glycan_count": 1, "glycosylation_sites": [], "id": "Q15831", "name": "STK11", "organism": "Homo sapiens", "uniprot_id": "Q15831" }, { "function": "Endothelial sialomucin, also called endomucin or mucin-like sialoglycoprotein, which interferes with the assembly of focal adhesion complexes and inhibits interaction between cells and the extracellular matrix", "gene_name": "EMCN", "glycan_count": 7, "glycosylation_sites": [ { "position": 19, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 28, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 98, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 164, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 178, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9ULC0", "name": "EMCN", "organism": "Homo sapiens", "uniprot_id": "Q9ULC0" }, { "function": "May function as adapter protein. Involved in the formation of clusters of actin bundles. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection", "gene_name": "BAIAP2L1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y2M8", "name": "TNFAIP2", "organism": "Homo sapiens", "uniprot_id": "Q9UHR4" }, { "function": "Serine/threonine-protein kinase and endoribonuclease that acts as a key sensor for the endoplasmic reticulum unfolded protein response (UPR) (PubMed:11175748, PubMed:11779464, PubMed:12637535, PubMed:19328063, PubMed:21317875, PubMed:28128204, PubMed:30118681, PubMed:36739529, PubMed:9637683). In unstressed cells, the endoplasmic reticulum luminal domain is maintained in its inactive monomeric state by binding to the endoplasmic reticulum chaperone HSPA5/BiP (PubMed:21317875). Accumulation of misfolded proteins in the endoplasmic reticulum causes release of HSPA5/BiP, allowing the luminal domain to homodimerize, promoting autophosphorylation of the kinase domain and subsequent activation of the endoribonuclease activity (PubMed:21317875). The endoribonuclease activity is specific for XBP1 mRNA and excises 26 nucleotides from XBP1 mRNA (PubMed:11779464, PubMed:21317875, PubMed:24508390). The resulting spliced transcript of XBP1 encodes a transcriptional activator protein that up-regulates expression of UPR target genes (PubMed:11779464, PubMed:21317875, PubMed:24508390). Acts as an upstream signal for ER stress-induced GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of CFTR to cell membrane by modulating the expression and localization of SEC16A (PubMed:21884936, PubMed:28067262)", "gene_name": "ERN1", "glycan_count": 2, "glycosylation_sites": [ { "position": 176, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O75460", "name": "IRE1\u03b1", "organism": "Homo sapiens", "uniprot_id": "O75460" }, { "function": "Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles", "gene_name": "Gsta4", "glycan_count": 1, "glycosylation_sites": [], "id": "P24472", "name": "Glutathione peroxidase (GPx)", "organism": "Mus musculus", "uniprot_id": "P24472" }, { "function": "Adapter required for innate immune defense against viruses (PubMed:16125763, PubMed:16127453, PubMed:16153868, PubMed:16177806, PubMed:19631370, PubMed:20127681, PubMed:20451243, PubMed:21170385, PubMed:23087404, PubMed:27992402, PubMed:33139700, PubMed:37582970). Acts downstream of DHX33, RIGI and IFIH1/MDA5, which detect intracellular dsRNA produced during viral replication, to coordinate pathways leading to the activation of NF-kappa-B, IRF3 and IRF7, and to the subsequent induction of antiviral cytokines such as IFNB and RANTES (CCL5) (PubMed:16125763, PubMed:16127453, PubMed:16153868, PubMed:16177806, PubMed:19631370, PubMed:20127681, PubMed:20451243, PubMed:20628368, PubMed:21170385, PubMed:23087404, PubMed:25636800, PubMed:27736772, PubMed:33110251). Peroxisomal and mitochondrial MAVS act sequentially to create an antiviral cellular state (PubMed:20451243). Upon viral infection, peroxisomal MAVS induces the rapid interferon-independent expression of defense factors that provide short-term protection, whereas mitochondrial MAVS activates an interferon-dependent signaling pathway with delayed kinetics, which amplifies and stabilizes the antiviral response (PubMed:20451243). May activate the same pathways following detection of extracellular dsRNA by TLR3 (PubMed:16153868). May protect cells from apoptosis (PubMed:16125763). Involved in NLRP3 inflammasome activation by mediating NLRP3 recruitment to mitochondria (PubMed:23582325)", "gene_name": "MAVS", "glycan_count": 3, "glycosylation_sites": [], "id": "Q7Z434", "name": "MAVS", "organism": "Homo sapiens", "uniprot_id": "Q7Z434" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P17181/P48551", "name": "IFNAR", "organism": "", "uniprot_id": "" }, { "function": "Serine/threonine-protein kinase which is an important downstream effector of CDC42 and plays a role in the regulation of cytoskeleton reorganization and cell migration (PubMed:15723050, PubMed:9092543, PubMed:9418861). Regulates actin cytoskeletal reorganization via phosphorylation of PPP1R12C and MYL9/MLC2 (PubMed:21457715). In concert with MYO18A and LURAP1, is involved in modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration (PubMed:18854160). Phosphorylates: PPP1R12A, LIMK1 and LIMK2 (PubMed:11340065, PubMed:11399775). May play a role in TFRC-mediated iron uptake (PubMed:20188707). In concert with FAM89B/LRAP25 mediates the targeting of LIMK1 to the lamellipodium resulting in its activation and subsequent phosphorylation of CFL1 which is important for lamellipodial F-actin regulation (By similarity). Triggers the formation of an extrusion apical actin ring required for epithelial extrusion of apoptotic cells (PubMed:29162624)", "gene_name": "CDC42BPA", "glycan_count": 2, "glycosylation_sites": [], "id": "Q5VT25", "name": "CH25H", "organism": "Homo sapiens", "uniprot_id": "Q5VT25" }, { "function": "Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:10097128, PubMed:16371461, PubMed:18782782, PubMed:21911472, PubMed:29593216, PubMed:9859996, PubMed:9990853). Recognizes and binds to phosphorylated target proteins (PubMed:10097128, PubMed:16371461, PubMed:18782782, PubMed:21911472, PubMed:9859996, PubMed:9990853). SCF(BTRC) mediates the ubiquitination of phosphorylated NFKB, ATF4, CDC25A, DLG1, FBXO5, PER1, SMAD3, SMAD4, SNAI1 and probably NFKB2. SCF(BTRC) mediates the ubiquitination of CTNNB1 and participates in Wnt signaling (By similarity). SCF(BTRC) mediates the ubiquitination of NFKBIA, NFKBIB and NFKBIE; the degradation frees the associated NFKB1 to translocate into the nucleus and to activate transcription (PubMed:10097128, PubMed:9859996). Ubiquitination of NFKBIA occurs at 'Lys-21' and 'Lys-22' (PubMed:10097128, PubMed:9859996). The SCF(FBXW11) complex also regulates NF-kappa-B by mediating ubiquitination of phosphorylated NFKB1: specifically ubiquitinates the p105 form of NFKB1, leading to its degradation (By similarity). SCF(BTRC) mediates the ubiquitination of CEP68; this is required for centriole separation during mitosis (By similarity). SCF(BTRC) mediates the ubiquitination and subsequent degradation of nuclear NFE2L1 (PubMed:21911472). Has an essential role in the control of the clock-dependent transcription via degradation of phosphorylated PER1 and PER2 (PubMed:18782782). May be involved in ubiquitination and subsequent proteasomal degradation through a DBB1-CUL4 E3 ubiquitin-protein ligase (By similarity). Required for activation of NFKB-mediated transcription by IL1B, MAP3K14, MAP3K1, IKBKB and TNF (By similarity). Required for proteolytic processing of GLI3 (PubMed:16371461). Mediates ubiquitination of REST, thereby leading to its proteasomal degradation (By similarity). SCF(BTRC) mediates the ubiquitination and subsequent proteasomal degradation of KLF4; thereby negatively regulating cell pluripotency maintenance and embryogenesis (PubMed:29593216). SCF(BTRC) acts as a regulator of mTORC1 signaling pathway by catalyzing ubiquitination and subsequent proteasomal degradation of phosphorylated DEPTOR, TFE3 and MITF (By similarity). SCF(BTRC) directs 'Lys-48'-linked ubiquitination of UBR2 in the T-cell receptor signaling pathway (By similarity)", "gene_name": "Btrc", "glycan_count": 0, "glycosylation_sites": [], "id": "Q3ULA2", "name": "Tropomyosin receptor kinase A (TrkA)", "organism": "Mus musculus", "uniprot_id": "Q3ULA2" }, { "function": "Receptor tyrosine kinase involved in nervous system and probably heart development. Upon binding of its ligand NTF3/neurotrophin-3, NTRK3 autophosphorylates and activates different signaling pathways, including the phosphatidylinositol 3-kinase/AKT and the MAPK pathways, that control cell survival and differentiation", "gene_name": "Ntrk3", "glycan_count": 13, "glycosylation_sites": [ { "position": 68, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 72, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 79, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 133, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 163, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 203, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 218, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 232, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 259, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 267, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 272, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 294, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 375, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 388, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6VNS1", "name": "Tropomyosin receptor kinase C (TrkC)", "organism": "Mus musculus", "uniprot_id": "Q6VNS1" }, { "function": "Pore-forming (alpha) subunit of voltage-gated inwardly rectifying potassium channel (PubMed:10219239, PubMed:10753933, PubMed:10790218, PubMed:10837251, PubMed:11997281, PubMed:12063277, PubMed:18559421, PubMed:22314138, PubMed:22359612, PubMed:26363003, PubMed:27916661, PubMed:9230439, PubMed:9351446, PubMed:9765245). Channel properties are modulated by cAMP and subunit assembly (PubMed:10837251). Characterized by unusual gating kinetics by producing relatively small outward currents during membrane depolarization and large inward currents during subsequent repolarization which reflect a rapid inactivation during depolarization and quick recovery from inactivation but slow deactivation (closing) during repolarization (PubMed:10219239, PubMed:10753933, PubMed:10790218, PubMed:10837251, PubMed:11997281, PubMed:12063277, PubMed:18559421, PubMed:22314138, PubMed:22359612, PubMed:26363003, PubMed:27916661, PubMed:9230439, PubMed:9351446, PubMed:9765245). Forms a stable complex with KCNE1 or KCNE2, and that this heteromultimerization regulates inward rectifier potassium channel activity (PubMed:10219239, PubMed:9230439)", "gene_name": "KCNH2", "glycan_count": 0, "glycosylation_sites": [ { "position": 598, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q12809", "name": "hERG potassium channel", "organism": "Homo sapiens", "uniprot_id": "Q12809" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01732/P10966", "name": "CD8", "organism": "", "uniprot_id": "" }, { "function": "Dual-specificity kinase which possesses both serine/threonine and tyrosine kinase activities. Plays an essential role in ribosomal DNA (rDNA) double-strand break repair and rDNA copy number maintenance (PubMed:33469661). During DNA damage, mediates transcription silencing in part via phosphorylating and enforcing DSB accumulation of the histone methyltransferase EHMT2 (PubMed:32611815). Enhances the transcriptional activity of TCF1/HNF1A and FOXO1. Inhibits epithelial cell migration. Mediates colon carcinoma cell survival in mitogen-poor environments. Inhibits the SHH and WNT1 pathways, thereby enhancing adipogenesis. In addition, promotes expression of the gluconeogenic enzyme glucose-6-phosphatase catalytic subunit 1 (G6PC1)", "gene_name": "DYRK1B", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y463", "name": "DYRK1B", "organism": "Homo sapiens", "uniprot_id": "Q9Y463" }, { "function": "Transcription factor that coordinates proliferation arrest and the differentiation of myeloid progenitors, adipocytes, hepatocytes, and cells of the lung and the placenta. Binds directly to the consensus DNA sequence 5'-T[TG]NNGNAA[TG]-3' acting as an activator on distinct target genes (PubMed:11242107). During early embryogenesis, plays essential and redundant functions with CEBPB. Essential for the transition from common myeloid progenitors (CMP) to granulocyte/monocyte progenitors (GMP). Critical for the proper development of the liver and the lung (By similarity). Necessary for terminal adipocyte differentiation, is required for postnatal maintenance of systemic energy homeostasis and lipid storage (By similarity). To regulate these different processes at the proper moment and tissue, interplays with other transcription factors and modulators. Down-regulates the expression of genes that maintain cells in an undifferentiated and proliferative state through E2F1 repression, which is critical for its ability to induce adipocyte and granulocyte terminal differentiation. Reciprocally E2F1 blocks adipocyte differentiation by binding to specific promoters and repressing CEBPA binding to its target gene promoters. Proliferation arrest also depends on a functional binding to SWI/SNF complex (PubMed:14660596). In liver, regulates gluconeogenesis and lipogenesis through different mechanisms. To regulate gluconeogenesis, functionally cooperates with FOXO1 binding to IRE-controlled promoters and regulating the expression of target genes such as PCK1 or G6PC1. To modulate lipogenesis, interacts and transcriptionally synergizes with SREBF1 in promoter activation of specific lipogenic target genes such as ACAS2. In adipose tissue, seems to act as FOXO1 coactivator accessing to ADIPOQ promoter through FOXO1 binding sites (By similarity)", "gene_name": "CEBPA", "glycan_count": 0, "glycosylation_sites": [], "id": "P49715", "name": "C/EBP\u03b1", "organism": "Homo sapiens", "uniprot_id": "P49715" }, { "function": "Self-ligand receptor of the signaling lymphocytic activation molecule (SLAM) family. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2 (PubMed:19648922). Mediates natural killer (NK) cell activation through a SH2D1A-independent extracellular signal-regulated ERK-mediated pathway (By similarity). Positively regulates NK cell functions by a mechanism dependent on the adapter SH2D1B. In addition to heterotypic NK cells-target cells interactions also homotypic interactions between NK cells may contribute to activation. However, in the absence of SH2D1B, inhibits NK cell function. Also acts inhibitory in T-cells (PubMed:19151721). May play a role in lymphocyte adhesion (By similarity). In LPS-activated monocytes negatively regulates production of pro-inflammatory cytokines (By similarity)", "gene_name": "Slamf7", "glycan_count": 0, "glycosylation_sites": [ { "position": 42, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 95, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 139, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 145, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 156, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8BHK6", "name": "KIM1 (Kidney Injury Molecule-1)", "organism": "Mus musculus", "uniprot_id": "Q8BHK6" }, { "function": "Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells (By similarity). Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction (By similarity). In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA (PubMed:23558171, PubMed:25759381). Plays a role in the assembly of the gamma-tubulin ring complex (gTuRC), which regulates the minus-end nucleation of alpha-beta tubulin heterodimers that grow into microtubule protafilaments (By similarity). Part of the ACTR1A/ACTB filament around which the dynactin complex is built (By similarity). The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity)", "gene_name": "Actb", "glycan_count": 3, "glycosylation_sites": [], "id": "P60710", "name": "\u03b2-actin", "organism": "Mus musculus", "uniprot_id": "P60710" }, { "function": "Stimulates glucose uptake in differentiated adipocytes via the induction of glucose transporter SLC2A1/GLUT1 expression (but not SLC2A4/GLUT4 expression). Activity probably requires the presence of KLB. Regulates systemic glucose homeostasis and insulin sensitivity", "gene_name": "Fgf21", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9JJN1", "name": "Fgf21", "organism": "Mus musculus", "uniprot_id": "Q9JJN1" }, { "function": "Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles. Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules. Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. N6-methyladenosine (m6A) has been shown to alter the local structure in mRNAs and long non-coding RNAs (lncRNAs) via a mechanism named 'm(6)A-switch', facilitating binding of HNRNPC, leading to regulation of mRNA splicing", "gene_name": "Hnrnpc", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9Z204", "name": "HNRNPA2B1", "organism": "Mus musculus", "uniprot_id": "Q9Z204" }, { "function": "Probable flavin reductase in the luminescent systems of different marine bacteria", "gene_name": "luxG", "glycan_count": 0, "glycosylation_sites": [], "id": "P24273", "name": "ALT (Alanine aminotransferase)", "organism": "Aliivibrio fischeri", "uniprot_id": "P24273" }, { "function": "Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins (By similarity). Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro) (PubMed:14741101). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. When secreted, protects cells against apoptosis and against cytolysis by complement: inhibits assembly of the complement membrane attack complex (MAC) by preventing polymerization of C9 pore component of the MAC complex. Intracellular forms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity (By similarity). Following stress, promotes apoptosis (PubMed:12551933). Inhibits apoptosis when associated with the mitochondrial membrane by interference with BAX-dependent release of cytochrome c into the cytoplasm. Plays a role in the regulation of cell proliferation. Following ER stress, suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. When secreted, does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity (By similarity). When secreted, acts as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (PubMed:11865066)", "gene_name": "Clu", "glycan_count": 11, "glycosylation_sites": [ { "position": 102, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 144, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 290, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 327, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 353, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 373, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q06890", "name": "Clusterin", "organism": "Mus musculus", "uniprot_id": "Q06890" }, { "function": "Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex)", "gene_name": "PSMA6", "glycan_count": 1, "glycosylation_sites": [ { "position": 5, "type": "O-linked (GlcNAc) serine" } ], "id": "P60900", "name": "PSMA6", "organism": "Homo sapiens", "uniprot_id": "P60900" }, { "function": "Nucleolar protein that is involved in ribosomal RNA (rRNA) processing (PubMed:33199730). Also plays a role in primary cilia resorption, and cell cycle progression in neurogenesis and neocortex development (PubMed:33199730). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797)", "gene_name": "RRP7A", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y3A4", "name": "SCAF1", "organism": "Homo sapiens", "uniprot_id": "Q9Y3A4" }, { "function": "Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Binds DNA non-specifically. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity)", "gene_name": "ARID1A", "glycan_count": 2, "glycosylation_sites": [], "id": "O14497", "name": "ARID1A", "organism": "Homo sapiens", "uniprot_id": "O14497" }, { "function": "Factor of infectivity and pathogenicity, required for optimal virus replication (PubMed:8151761). Alters numerous pathways of T-lymphocytes function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity (PubMed:25585010). Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells (PubMed:25585010)", "gene_name": "nef", "glycan_count": 0, "glycosylation_sites": [], "id": "P03406", "name": "Nef", "organism": "Human immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI)", "uniprot_id": "P03406" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q13131 (PRKAA1)", "name": "AMP-activated protein kinase (AMPK)", "organism": "", "uniprot_id": "" }, { "function": "Calcium-dependent phospholipid-binding protein that plays a role in calcium-mediated intracellular processes (PubMed:14674885). Involved in the TNF-alpha receptor signaling pathway in a calcium-dependent manner (PubMed:14674885). Exhibits calcium-dependent phospholipid binding properties (PubMed:19539605, PubMed:9430674). Plays a role in neuronal progenitor cell differentiation; induces neurite outgrowth via a AKT-dependent signaling cascade and calcium-independent manner (PubMed:23263657, PubMed:25450385). May recruit target proteins to the cell membrane in a calcium-dependent manner (PubMed:12522145). May function in membrane trafficking (PubMed:9430674). Involved in TNF-alpha-induced NF-kappa-B transcriptional repression by inducing endoprotease processing of the transcription factor NF-kappa-B p65/RELA subunit (PubMed:18212740). Also induces endoprotease processing of NF-kappa-B p50/NFKB1, p52/NFKB2, RELB and REL (PubMed:18212740)", "gene_name": "CPNE1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q99829", "name": "CPNE1", "organism": "Homo sapiens", "uniprot_id": "Q99829" }, { "function": "Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Selectively binds to phosphatidylinositol 3,5-bisphosphate PtdIns(3,5)P2 and PtdIns(3,4)P2 in preference to other phosphoinositides tested. Involved in late stages of cytokinesis. Plays a role in endosomal sorting/trafficking of EGF receptor. Isoform 2 prevents stress-mediated cell death and accumulation of reactive oxygen species when expressed in yeast cells", "gene_name": "CHMP3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y3E7", "name": "FRAT2", "organism": "Homo sapiens", "uniprot_id": "Q9Y3E7" }, { "function": "Receptor for activated thrombin or trypsin coupled to G proteins that stimulate phosphoinositide hydrolysis (PubMed:10079109). May play a role in platelets activation (PubMed:10079109)", "gene_name": "F2RL3", "glycan_count": 0, "glycosylation_sites": [ { "position": 56, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q96RI0", "name": "F2RL1", "organism": "Homo sapiens", "uniprot_id": "Q96RI0" }, { "function": "Sequence-specific DNA-binding transcription factor (PubMed:17717711). Plays a role in hindbrain segmentation by regulating the expression of a subset of homeobox containing genes and in Schwann cell myelination by regulating the expression of genes involved in the formation and maintenance of myelin (By similarity). Binds to two EGR2-consensus sites EGR2A (5'-CTGTAGGAG-3') and EGR2B (5'-ATGTAGGTG-3') in the HOXB3 enhancer and promotes HOXB3 transcriptional activation (By similarity). Binds to specific DNA sites located in the promoter region of HOXA4, HOXB2 and ERBB2 (By similarity). Regulates hindbrain segmentation by controlling the expression of Hox genes, such as HOXA4, HOXB3 and HOXB2, and thereby specifying odd and even rhombomeres (By similarity). Promotes the expression of HOXB3 in the rhombomere r5 in the hindbrain (By similarity). Regulates myelination in the peripheral nervous system after birth, possibly by regulating the expression of myelin proteins, such as MPZ, and by promoting the differentiation of Schwann cells (By similarity). Involved in the development of the jaw openener musculature, probably by playing a role in its innervation through trigeminal motor neurons (By similarity). May play a role in adipogenesis, possibly by regulating the expression of CEBPB (By similarity)", "gene_name": "EGR2", "glycan_count": 3, "glycosylation_sites": [], "id": "P11161", "name": "EGR2", "organism": "Homo sapiens", "uniprot_id": "P11161" }, { "function": "May function as a linker between cadherin adhesion receptors and the cytoskeleton to regulate cell-cell adhesion and differentiation in the nervous system (By similarity). Required for proper regulation of cortical neuronal migration and neurite growth (PubMed:30013181). It acts as a negative regulator of Arp2/3 complex activity and Arp2/3-mediated actin polymerization (PubMed:30013181). It thereby suppresses excessive actin branching which would impair neurite growth and stability (PubMed:30013181). Regulates morphological plasticity of synapses and cerebellar and hippocampal lamination during development. Functions in the control of startle modulation (By similarity)", "gene_name": "CTNNA2", "glycan_count": 1, "glycosylation_sites": [], "id": "P26232", "name": "Collagen VI alpha-1 (Col6a1)", "organism": "Homo sapiens", "uniprot_id": "P26232" }, { "function": "Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape (By similarity). Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts (By similarity)", "gene_name": "Fn1", "glycan_count": 1, "glycosylation_sites": [ { "position": 430, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 528, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 542, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 876, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1006, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1243, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1290, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2154, "type": "O-linked (GalNAc...) threonine" }, { "position": 2198, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P04937", "name": "Fibronectin (Fn1)", "organism": "Rattus norvegicus", "uniprot_id": "P04937" }, { "function": "Cell-surface receptor that plays a role in cell-cell interactions, cell adhesion and migration, helping them to sense and respond to changes in the tissue microenvironment. Participates thereby in a wide variety of cellular functions including the activation, recirculation and homing of T-lymphocytes, hematopoiesis, inflammation and response to bacterial infection. Engages, through its ectodomain, extracellular matrix components such as hyaluronan/HA, collagen, growth factors, cytokines or proteases and serves as a platform for signal transduction by assembling, via its cytoplasmic domain, protein complexes containing receptor kinases and membrane proteases. Such effectors include PKN2, the RhoGTPases RAC1 and RHOA, Rho-kinases and phospholipase C that coordinate signaling pathways promoting calcium mobilization and actin-mediated cytoskeleton reorganization essential for cell migration and adhesion", "gene_name": "Cd44", "glycan_count": 0, "glycosylation_sites": [ { "position": 28, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 60, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 103, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 114, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 124, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 184, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 266, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 274, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 306, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P26051", "name": "CD44", "organism": "Rattus norvegicus", "uniprot_id": "P26051" }, { "function": "Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells", "gene_name": "Actc1", "glycan_count": 1, "glycosylation_sites": [], "id": "P68033", "name": "Actin alpha cardiac muscle 1 (Actc1)", "organism": "Mus musculus", "uniprot_id": "P68033" }, { "function": "Stabilizer of the mucous gel overlying the gastrointestinal mucosa that provides a physical barrier against various noxious agents", "gene_name": "Tff1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q63467", "name": "Myosin heavy chain 3 (Myh3)", "organism": "Rattus norvegicus", "uniprot_id": "Q63467" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P24385 (human)", "name": "Cyclin D1", "organism": "", "uniprot_id": "" }, { "function": "Binds vitamin B12 with femtomolar affinity and protects it from the acidic environment of the stomach", "gene_name": "TCN1", "glycan_count": 11, "glycosylation_sites": [ { "position": 160, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 216, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 316, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 337, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 343, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 349, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 354, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 369, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P20061", "name": "Haptocorrin (Transcobalamin I)", "organism": "Homo sapiens", "uniprot_id": "P20061" }, { "function": "Blocks Ras-mediated inhibition of integrin activation and modulates the ERK MAP kinase cascade. Inhibits RPS6KA3 activities by retaining it in the cytoplasm (By similarity). Inhibits both TNFRSF6- and TNFRSF1A-mediated CASP8 activity and apoptosis. Regulates glucose transport by controlling both the content of SLC2A1 glucose transporters on the plasma membrane and the insulin-dependent trafficking of SLC2A4 from the cell interior to the surface", "gene_name": "PEA15", "glycan_count": 0, "glycosylation_sites": [], "id": "Q15121", "name": "Phosphoprotein enriched in astrocytes 15 (PEA15)", "organism": "Homo sapiens", "uniprot_id": "Q15121" }, { "function": "Required for pre-mRNA splicing as component of the spliceosome (PubMed:11991638, PubMed:12226669, PubMed:22961380, PubMed:28076346, PubMed:28502770, PubMed:29301961, PubMed:29360106). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). Promotes exon-junction complex (EJC) assembly (PubMed:22959432, PubMed:22961380). Hinders EIF4A3 from non-specifically binding RNA and escorts it to the splicing machinery to promote EJC assembly on mature mRNAs. Through its role in EJC assembly, required for nonsense-mediated mRNA decay", "gene_name": "CWC22", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9HCG8", "name": "FGF19", "organism": "Homo sapiens", "uniprot_id": "Q9HCG8" }, { "function": "Integrin alpha-V:beta-6 (ITGAV:ITGB6) is a receptor for fibronectin and cytotactin (PubMed:17158881, PubMed:17545607). It recognizes the sequence R-G-D in its ligands (PubMed:17158881, PubMed:17545607). Internalization of integrin alpha-V/beta-6 via clathrin-mediated endocytosis promotes carcinoma cell invasion (PubMed:17158881, PubMed:17545607). ITGAV:ITGB6 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1 (PubMed:17158881). Integrin alpha-V:beta-6 (ITGAV:ITGB6) mediates R-G-D-dependent release of transforming growth factor beta-1 (TGF-beta-1) from regulatory Latency-associated peptide (LAP), thereby playing a key role in TGF-beta-1 activation (PubMed:15184403, PubMed:22278742, PubMed:28117447)", "gene_name": "ITGB6", "glycan_count": 23, "glycosylation_sites": [ { "position": 48, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 97, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 260, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 387, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 396, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 463, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 471, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 541, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 575, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P18564", "name": "Integrin \u03b26", "organism": "Homo sapiens", "uniprot_id": "P18564" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P25024/P25025", "name": "IL-8 receptor (CXCR1/2)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P17174 (rat)", "name": "Aspartate Aminotransferase (AST)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04764 (rat)", "name": "Alanine Aminotransferase (ALT)", "organism": "", "uniprot_id": "" }, { "function": "Regulatory subunit of anion-selective CLCNKA:BSND and CLCNKB:BSND heteromeric channels involved in basolateral chloride conductance along the nephron to achieve urine concentration and maintain systemic acid-base homeostasis, and in the stria vascularis of the inner ear to establish the endocochlear potential necessary for normal hearing (PubMed:11734858, PubMed:18833191, PubMed:21593186, PubMed:23791703). Most likely acts as a chaperone that allosterically regulates proper sorting of CLCNKA:BSND and CLCNKB:BSND channels at the basolateral plasma membrane domain and functional switch to ion conducting state. Mediates constitutive opening of channel common gates (PubMed:11734858, PubMed:18833191, PubMed:21593186, PubMed:23791703)", "gene_name": "Bsnd", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8VIM4", "name": "Glypican 4", "organism": "Mus musculus", "uniprot_id": "Q8VIM4" }, { "function": "Smooth muscle cells (SM) and cardiac muscle cells-specific transcriptional factor which uses the canonical single or multiple CArG boxes DNA sequence. Acts as a cofactor of serum response factor (SRF) with the potential to modulate SRF-target genes. Plays a crucial role in cardiogenesis, urinary bladder development, and differentiation of the smooth muscle cell lineage (myogenesis). Positively regulates the transcription of genes involved in vascular smooth muscle contraction (By similarity)", "gene_name": "Myocd", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8VIM5", "name": "Glypican 6", "organism": "Mus musculus", "uniprot_id": "Q8VIM5" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P07996 (TSP-1)", "name": "Thrombospondin", "organism": "", "uniprot_id": "" }, { "function": "Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA (PubMed:18029264, PubMed:18272479, PubMed:9278442). When secreted, acts as a signaling molecule that induces immune response through the activation of monocyte/macrophages (PubMed:15851690). Catalyzes the synthesis of the signaling molecule diadenosine tetraphosphate (Ap4A), and thereby mediates disruption of the complex between HINT1 and MITF and the concomitant activation of MITF transcriptional activity (PubMed:14975237, PubMed:19524539, PubMed:23159739, PubMed:5338216)", "gene_name": "KARS1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9HB23", "name": "SPARCL1", "organism": "Homo sapiens", "uniprot_id": "Q15046" }, { "function": "Endothelial orphan receptor that acts as a key regulator of angiogenesis", "gene_name": "ADGRL4", "glycan_count": 31, "glycosylation_sites": [ { "position": 21, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 64, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 74, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 127, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 177, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 188, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 249, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 381, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 395, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9HBW9", "name": "LPA 2 receptor (LPAR2)", "organism": "Homo sapiens", "uniprot_id": "Q9HBW9" }, { "function": "Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia", "gene_name": "GDA", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9Y2T3", "name": "Autotaxin (ENPP2)", "organism": "Homo sapiens", "uniprot_id": "Q9Y2T3" }, { "function": "Adapter protein which binds TBK1 and IKBKE playing a role in antiviral innate immunity (PubMed:14560022, PubMed:21931631). Activates serine/threonine-protein kinase TBK1 and facilitates its oligomerization (PubMed:14560022, PubMed:21931631). Enhances the phosphorylation of NF-kappa-B p65 subunit RELA by TBK1 (PubMed:14560022, PubMed:21931631). Promotes TBK1-induced as well as TNF-alpha or PMA-induced activation of NF-kappa-B (PubMed:14560022, PubMed:21931631). Participates in IFNB promoter activation via TICAM1 (PubMed:15611223)", "gene_name": "AZI2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H6S1", "name": "LOXL3", "organism": "Homo sapiens", "uniprot_id": "Q9H6S1" }, { "function": "Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations, acting as a rate-limiting enzyme in gluconeogenesis. Plays a role in regulating glucose sensing and insulin secretion of pancreatic beta-cells. Appears to modulate glycerol gluconeogenesis in liver. Important regulator of appetite and adiposity; increased expression of the protein in liver after nutrient excess increases circulating satiety hormones and reduces appetite-stimulating neuropeptides and thus seems to provide a feedback mechanism to limit weight gain", "gene_name": "FBP1", "glycan_count": 1, "glycosylation_sites": [], "id": "P09467", "name": "FBP1", "organism": "Homo sapiens", "uniprot_id": "P09467" }, { "function": "Constitutively active calcium selective cation channel thought to be involved in Ca(2+) reabsorption in kidney and intestine (PubMed:11549322, PubMed:18768590). Required for normal Ca(2+) reabsorption in the kidney distal convoluted tubules (By similarity). The channel is activated by low internal calcium level and the current exhibits an inward rectification (PubMed:11549322, PubMed:18768590). A Ca(2+)-dependent feedback regulation includes fast channel inactivation and slow current decay (By similarity). Heteromeric assembly with TRPV6 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating (By similarity)", "gene_name": "TRPV5", "glycan_count": 0, "glycosylation_sites": [ { "position": 358, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NQA5", "name": "TRPV5", "organism": "Homo sapiens", "uniprot_id": "Q9NQA5" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8R2M8 (mouse)", "name": "LSECtin (CLEC4G)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q61790 (mouse)", "name": "LAG-3", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q62386 (mouse)", "name": "IL-17", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q99JB6 (mouse)", "name": "Foxp3", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9WVL2 (mouse)", "name": "Ror\u03b3t", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9QZL0 (mouse)", "name": "Ripk3", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9D2Y4 (mouse)", "name": "Mlkl", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P55210 (mouse)", "name": "Caspase 3", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q01238 (mouse)", "name": "CD44", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NZQ7 (mouse)", "name": "PD-1 (Pdcd1)", "organism": "", "uniprot_id": "" }, { "function": "Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Calcium-binding is required for the activation of calmodulin. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases, such as myosin light-chain kinases and calmodulin-dependent protein kinase type II (CaMK2), and phosphatases", "gene_name": "calm", "glycan_count": 0, "glycosylation_sites": [], "id": "P02594", "name": "HBV Polymerase (RT domain)", "organism": "Electrophorus electricus", "uniprot_id": "P02594" }, { "function": "Mitochondrial transporter that functions as a long-chain fatty acid/LCFA and proton symporter, simultaneously transporting one LCFA and one proton through the inner mitochondrial membrane. However, LCFAs remaining associated with the transporter via their hydrophobic tails, it results in an apparent transport of protons activated by LCFAs. Thereby, dissipates the mitochondrial proton gradient and converts the energy of substrate oxydation into heat instead of ATP (PubMed:23063128). Responsible for thermogenic respiration, a specialized capacity of brown adipose tissue and beige fat that participates in non-shivering adaptive thermogenesis to temperature and diet variations and more generally to the regulation of energy balance (PubMed:19187776, PubMed:23063128, PubMed:27027295, PubMed:9139827). Regulates the production of reactive oxygen species/ROS by mitochondria (PubMed:20416274, PubMed:20466728)", "gene_name": "Ucp1", "glycan_count": 1, "glycosylation_sites": [], "id": "P12242", "name": "UCP1", "organism": "Mus musculus", "uniprot_id": "P12242" }, { "function": "Functions as a stress-inducible and DNA-binding transcription factor that plays a central role in the transcriptional activation of the heat shock response (HSR), leading to the expression of a large class of molecular chaperones, heat shock proteins (HSPs), that protect cells from cellular insult damage (PubMed:11447121, PubMed:12659875, PubMed:12917326, PubMed:15016915, PubMed:18451878, PubMed:1871105, PubMed:1986252, PubMed:25963659, PubMed:26754925, PubMed:7623826, PubMed:7760831, PubMed:8940068, PubMed:8946918, PubMed:9121459, PubMed:9341107, PubMed:9499401, PubMed:9535852, PubMed:9727490). In unstressed cells, is present in a HSP90-containing multichaperone complex that maintains it in a non-DNA-binding inactivated monomeric form (PubMed:11583998, PubMed:16278218, PubMed:9727490). Upon exposure to heat and other stress stimuli, undergoes homotrimerization and activates HSP gene transcription through binding to site-specific heat shock elements (HSEs) present in the promoter regions of HSP genes (PubMed:10359787, PubMed:11583998, PubMed:12659875, PubMed:16278218, PubMed:1871105, PubMed:1986252, PubMed:25963659, PubMed:26754925, PubMed:7623826, PubMed:7935471, PubMed:8455624, PubMed:8940068, PubMed:9499401, PubMed:9727490). Upon heat shock stress, forms a chromatin-associated complex with TTC5/STRAP and p300/EP300 to stimulate HSR transcription, therefore increasing cell survival (PubMed:18451878). Activation is reversible, and during the attenuation and recovery phase period of the HSR, returns to its unactivated form (PubMed:11583998, PubMed:16278218). Binds to inverted 5'-NGAAN-3' pentamer DNA sequences (PubMed:1986252, PubMed:26727489). Binds to chromatin at heat shock gene promoters (PubMed:25963659). Activates transcription of transcription factor FOXR1 which in turn activates transcription of the heat shock chaperones HSPA1A and HSPA6 and the antioxidant NADPH-dependent reductase DHRS2 (PubMed:34723967). Also serves several other functions independently of its transcriptional activity. Involved in the repression of Ras-induced transcriptional activation of the c-fos gene in heat-stressed cells (PubMed:9341107). Positively regulates pre-mRNA 3'-end processing and polyadenylation of HSP70 mRNA upon heat-stressed cells in a symplekin (SYMPK)-dependent manner (PubMed:14707147). Plays a role in nuclear export of stress-induced HSP70 mRNA (PubMed:17897941). Plays a role in the regulation of mitotic progression (PubMed:18794143). Also plays a role as a negative regulator of non-homologous end joining (NHEJ) repair activity in a DNA damage-dependent manner (PubMed:26359349). Involved in stress-induced cancer cell proliferation in a IER5-dependent manner (PubMed:26754925)", "gene_name": "HSF1", "glycan_count": 2, "glycosylation_sites": [], "id": "Q00613", "name": "HSF1", "organism": "Homo sapiens", "uniprot_id": "Q00613" }, { "function": "Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release (PubMed:26865365). Plays a role in spermatogenesis. In association with SHCBP1L may participate in the maintenance of spindle integrity during meiosis in male germ cells (By similarity)", "gene_name": "HSPA2", "glycan_count": 1, "glycosylation_sites": [], "id": "P54652", "name": "HSP72", "organism": "Homo sapiens", "uniprot_id": "P54652" }, { "function": "Acts as a co-chaperone regulating the molecular chaperones HSP70 and HSP90 in folding of steroid receptors, such as the glucocorticoid receptor and the progesterone receptor. Proposed to act as a recycling chaperone by facilitating the return of chaperone substrates to early stages of chaperoning if further folding is required. In vitro, induces ATP-independent dissociation of HSP90 but not of HSP70 from the chaperone-substrate complexes. Recruits NR1I3 to the cytoplasm (By similarity)", "gene_name": "DNAJC7", "glycan_count": 1, "glycosylation_sites": [], "id": "Q99615", "name": "CIDEA", "organism": "Homo sapiens", "uniprot_id": "Q99615" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03165/P03168", "name": "Hepatitis B core-related antigen (HBcrAg)", "organism": "", "uniprot_id": "" }, { "function": "May play a critical role in death receptor-induced apoptosis and may target CASP8 and CASP10 to the nucleus. May regulate degradation of intermediate filaments during apoptosis. May play a role in the general transcription machinery in the nucleus and might be an important regulator of the activity of GTF3C3", "gene_name": "DEDD2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8WXF8", "name": "Cancer Antigen 125 (CA125)", "organism": "Homo sapiens", "uniprot_id": "Q8WXF8" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02649 (ApoB-100)", "name": "Low-density lipoprotein (LDL)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02647 (ApoA-I)", "name": "High-density lipoprotein (HDL)", "organism": "", "uniprot_id": "" }, { "function": "Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney (By similarity). Delivery to lysosomes by the cargo receptor NCOA4 for autophagic degradation and release or iron (PubMed:24695223)", "gene_name": "FTL", "glycan_count": 0, "glycosylation_sites": [], "id": "P02792", "name": "Ferritin light chain (FTL)", "organism": "Homo sapiens", "uniprot_id": "P02792" }, { "function": "Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway", "gene_name": "Vtn", "glycan_count": 4, "glycosylation_sites": [ { "position": 86, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 168, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 241, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P29788", "name": "Vitronectin", "organism": "Mus musculus", "uniprot_id": "P29788" }, { "function": "Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation", "gene_name": "Tf", "glycan_count": 28, "glycosylation_sites": [ { "position": 513, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q921I1", "name": "Transferrin", "organism": "Mus musculus", "uniprot_id": "Q921I1" }, { "function": "Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Also acts as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones. Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline", "gene_name": "Dpp4", "glycan_count": 3, "glycosylation_sites": [ { "position": 83, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 90, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 144, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 213, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 223, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 315, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 328, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 514, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 679, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P28843", "name": "Dipeptidyl peptidase-4", "organism": "Mus musculus", "uniprot_id": "P28843" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q1X72", "name": "Haemopexin", "organism": "", "uniprot_id": "" }, { "function": "May act as a scaffolding protein within caveolar membranes (By similarity). Forms a stable heterooligomeric complex with CAV2 that targets to lipid rafts and drives caveolae formation. Mediates the recruitment of CAVIN proteins (CAVIN1/2/3/4) to the caveolae (PubMed:19546242). Interacts directly with G-protein alpha subunits and can functionally regulate their activity (By similarity). Involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner (By similarity). Recruits CTNNB1 to caveolar membranes and may regulate CTNNB1-mediated signaling through the Wnt pathway (PubMed:10816572). Negatively regulates TGFB1-mediated activation of SMAD2/3 by mediating the internalization of TGFBR1 from membrane rafts leading to its subsequent degradation (By similarity). Binds 20(S)-hydroxycholesterol (20(S)-OHC) (PubMed:34799735)", "gene_name": "Cav1", "glycan_count": 1, "glycosylation_sites": [], "id": "P49817", "name": "Caveolin-1", "organism": "Mus musculus", "uniprot_id": "P49817" }, { "function": "Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2)", "gene_name": "Prdx2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q61171", "name": "Peroxiredoxin 2", "organism": "Mus musculus", "uniprot_id": "Q61171" }, { "function": "Functions both as a transporter that mediates electroneutral anion exchange across the cell membrane and as a structural protein. Component of the ankyrin-1 complex of the erythrocyte membrane; required for normal flexibility and stability of the erythrocyte membrane and for normal erythrocyte shape via the interactions of its cytoplasmic domain with cytoskeletal proteins, glycolytic enzymes, and hemoglobin. Functions as a transporter that mediates the 1:1 exchange of inorganic anions across the erythrocyte membrane. Mediates chloride-bicarbonate exchange in the kidney, and is required for normal acidification of the urine", "gene_name": "Slc4a1", "glycan_count": 1, "glycosylation_sites": [ { "position": 660, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P04919", "name": "Band 3 anion transport protein (Slc4a1)", "organism": "Mus musculus", "uniprot_id": "P04919" }, { "function": "Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping (PubMed:19401332). Required for cortical actin clearance prior to oocyte exocytosis (PubMed:31118423). Promotes cell motility in conjunction with S100A4 (By similarity). During cell spreading, plays an important role in cytoskeleton reorganization, focal contact formation (in the margins but not the central part of spreading cells), and lamellipodial retraction; this function is mechanically antagonized by MYH10 (By similarity)", "gene_name": "Myh9", "glycan_count": 4, "glycosylation_sites": [], "id": "Q8VDD5", "name": "Myosin-9", "organism": "Mus musculus", "uniprot_id": "Q8VDD5" }, { "function": "Uniporter that mediates the transport of copper(1+) from the extracellular space to the cytoplasm, across the plasma membrane (PubMed:11734551, PubMed:16135512, PubMed:17525160, PubMed:19740744, PubMed:20451502, PubMed:20569931, PubMed:23658018) and delivers directly copper(1+) to specific chaperone such as ATOX1, via a copper(1+)- mediated transient interaction between the C-terminal domain and a copper(1+) chaperone, thus controlling intracellular copper(1+) levels (PubMed:11734551, PubMed:16135512, PubMed:17525160, PubMed:19740744, PubMed:20451502, PubMed:20569931, PubMed:23658018, PubMed:26745413). May function in copper(1+) import from the apical membrane thus may drive intestinal copper absorption (By similarity). The copper(1+) transport mechanism is sodium-independent, saturable and of high-affinity (PubMed:11734551). Also mediates the uptake of silver(1+) (PubMed:20569931). May function in the influx of the platinum-containing chemotherapeutic agents (PubMed:20451502, PubMed:20569931). The platinum-containing chemotherapeutic agents uptake is saturable (By similarity). In vitro, mediates the transport of cadmium(2+) into cells (PubMed:33294387). Also participates in the first step of copper(2+) acquisition by cells through a direct transfer of copper(2+) from copper(2+) carriers in blood, such as ALB to the N-terminal domain of SLC31A1, leading to copper(2+) reduction and probably followed by copper(1+) stabilization (PubMed:30489586). In addition, functions as a redox sensor to promote angiogenesis in endothelial cells, in a copper(1+) transport independent manner, by transmitting the VEGF-induced ROS signal through a sulfenylation at Cys-189 leadin g to a subsequent disulfide bond formation between SLC31A1 and KDR (PubMed:35027734). The SLC31A1-KDR complex is then co-internalized to early endosomes, driving a sustained VEGFR2 signaling (PubMed:35027734)", "gene_name": "SLC31A1", "glycan_count": 0, "glycosylation_sites": [ { "position": 15, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 27, "type": "O-linked (GalNAc...) threonine" } ], "id": "O15431", "name": "CTR1 (SLC31A1)", "organism": "Homo sapiens", "uniprot_id": "O15431" }, { "function": "Zinc ion:proton antiporter that could function at the plasma membrane mediating zinc efflux from cells against its electrochemical gradient protecting them from intracellular zinc accumulation and toxicity (PubMed:31471319). Alternatively, could prevent the transport to the plasma membrane of CACNB2, the L-type calcium channels regulatory subunit, through a yet to be defined mechanism. By modulating the expression of these channels at the plasma membrane, could prevent calcium and zinc influx into cells. By the same mechanism, could also prevent L-type calcium channels-mediated heavy metal influx into cells (By similarity). In some cells, could also function as a zinc ion:proton antiporter mediating zinc entry into the lumen of cytoplasmic vesicles. In macrophages, can increase zinc ions concentration into the lumen of cytoplasmic vesicles containing engulfed bacteria and could help inactivate them (PubMed:32441444). Forms a complex with TMC6/EVER1 and TMC8/EVER2 at the ER membrane of keratynocytes which facilitates zinc uptake into the ER (PubMed:18158319). Down-regulates the activity of transcription factors induced by zinc and cytokines (PubMed:18158319)", "gene_name": "SLC30A1", "glycan_count": 2, "glycosylation_sites": [ { "position": 299, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y6M5", "name": "ZnT1 (SLC30A1)", "organism": "Homo sapiens", "uniprot_id": "Q9Y6M5" }, { "function": "Essential for the synthesis of various steroid hormones (PubMed:20547883, PubMed:21636783). Participates in the reduction of mitochondrial cytochrome P450 for steroidogenesis (PubMed:20547883, PubMed:21636783). Transfers electrons from adrenodoxin reductase to CYP11A1, a cytochrome P450 that catalyzes cholesterol side-chain cleavage (PubMed:20547883, PubMed:21636783). Does not form a ternary complex with adrenodoxin reductase and CYP11A1 but shuttles between the two enzymes to transfer electrons (By similarity)", "gene_name": "FDX1", "glycan_count": 0, "glycosylation_sites": [], "id": "P10109", "name": "FDX1", "organism": "Homo sapiens", "uniprot_id": "P10109" }, { "function": "Involved in the intramitochondrial synthesis of acylcarnitines from accumulated acyl-CoA metabolites (PubMed:20538056, PubMed:24780397). Reconverts acylcarnitines back into the respective acyl-CoA esters that can then undergo beta-oxidation, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion. Active with medium (C8-C12) and long-chain (C14-C18) acyl-CoA esters (PubMed:20538056)", "gene_name": "CPT2", "glycan_count": 1, "glycosylation_sites": [], "id": "P23786", "name": "CPT1A", "organism": "Homo sapiens", "uniprot_id": "P23786" }, { "function": "Release of an N-terminal amino acid, cleaves before cysteine, leucine as well as other amino acids. Degrades peptide hormones such as oxytocin, vasopressin and angiotensin III, and plays a role in maintaining homeostasis during pregnancy. May be involved in the inactivation of neuronal peptides in the brain. Cleaves Met-enkephalin and dynorphin. Binds angiotensin IV and may be the angiotensin IV receptor in the brain", "gene_name": "LNPEP", "glycan_count": 65, "glycosylation_sites": [ { "position": 145, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 184, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 215, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 256, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 266, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 368, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 374, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 448, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 525, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 578, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 598, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 664, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 682, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 760, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 834, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 850, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 989, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UIQ6", "name": "Kidney injury molecule-1 (KIM-1)", "organism": "Homo sapiens", "uniprot_id": "Q9UIQ6" }, { "function": "Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems", "gene_name": "SOD2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9P2Z3", "name": "Heat shock protein 90 beta family member 2 (HSP90B2)", "organism": "Homo sapiens", "uniprot_id": "P04179" }, { "function": "Adapter protein containing an immunoreceptor tyrosine-based activation motif (ITAM) that transduces activation signals from various immunoreceptors. As a component of the high-affinity immunoglobulin E (IgE) receptor, mediates allergic inflammatory signaling in mast cells. As a constitutive component of interleukin-3 receptor complex, selectively mediates interleukin 4/IL4 production by basophils, priming T-cells toward effector T-helper 2 subset. Associates with pattern recognition receptors CLEC4D and CLEC4E to form a functional signaling complex in myeloid cells. Binding of mycobacterial trehalose 6,6'-dimycolate (TDM) to this receptor complex leads to phosphorylation of ITAM, triggering activation of SYK, CARD9 and NF-kappa-B, consequently driving maturation of antigen-presenting cells and shaping antigen-specific priming of T-cells toward effector T-helper 1 and T-helper 17 cell subtypes. May function cooperatively with other activating receptors. Functionally linked to integrin beta-2/ITGB2-mediated neutrophil activation. Also involved in integrin alpha-2/ITGA2-mediated platelet activation", "gene_name": "FCER1G", "glycan_count": 1, "glycosylation_sites": [], "id": "P30273", "name": "FCER1G", "organism": "Homo sapiens", "uniprot_id": "P30273" }, { "function": "RNA cytidine acetyltransferase that catalyzes the formation of N(4)-acetylcytidine (ac4C) modification on mRNAs, 18S rRNA and tRNAs (PubMed:25411247, PubMed:25653167, PubMed:30449621, PubMed:35679869). Catalyzes ac4C modification of a broad range of mRNAs, enhancing mRNA stability and translation (PubMed:30449621, PubMed:35679869). mRNA ac4C modification is frequently present within wobble cytidine sites and promotes translation efficiency (PubMed:30449621). Mediates the formation of ac4C at position 1842 in 18S rRNA (PubMed:25411247). May also catalyze the formation of ac4C at position 1337 in 18S rRNA (By similarity). Required for early nucleolar cleavages of precursor rRNA at sites A0, A1 and A2 during 18S rRNA synthesis (PubMed:25411247, PubMed:25653167). Catalyzes the formation of ac4C in serine and leucine tRNAs (By similarity). Requires the tRNA-binding adapter protein THUMPD1 for full tRNA acetyltransferase activity but not for 18S rRNA acetylation (PubMed:25653167). In addition to RNA acetyltransferase activity, also able to acetylate lysine residues of proteins, such as histones, microtubules, p53/TP53 and MDM2, in vitro (PubMed:14592445, PubMed:17631499, PubMed:19303003, PubMed:26882543, PubMed:27993683, PubMed:30165671). The relevance of the protein lysine acetyltransferase activity is however unsure in vivo (PubMed:30449621). Activates telomerase activity by stimulating the transcription of TERT, and may also regulate telomerase function by affecting the balance of telomerase subunit assembly, disassembly, and localization (PubMed:14592445, PubMed:18082603). Involved in the regulation of centrosome duplication by acetylating CENATAC during mitosis, promoting SASS6 proteasome degradation (PubMed:31722219). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797)", "gene_name": "NAT10", "glycan_count": 3, "glycosylation_sites": [], "id": "Q9H0A0", "name": "Rubicon", "organism": "Homo sapiens", "uniprot_id": "Q9H0A0" }, { "function": "As a member of the cohesin complex, involved in sister chromatid cohesion from the time of DNA replication in S phase to their segregation in mitosis, a function that is essential for proper chromosome segregation, post-replicative DNA repair, and the prevention of inappropriate recombination between repetitive regions. The cohesin complex may also play a role in spindle pole assembly during mitosis (By similarity). In interphase, cohesins may function in the control of gene expression by binding to numerous sites within the genome (PubMed:18237772). May control RUNX1 gene expression. Binds to and represses APOB gene promoter (By similarity). May play a role in embryonic gut development, possibly through the regulation of enteric neuron development (By similarity)", "gene_name": "Rad21", "glycan_count": 1, "glycosylation_sites": [], "id": "Q61550", "name": "CD157", "organism": "Mus musculus", "uniprot_id": "Q61550" }, { "function": "DSP may be an important factor in dentinogenesis. DPP may bind high amount of calcium and facilitate initial mineralization of dentin matrix collagen as well as regulate the size and shape of the crystals", "gene_name": "Dspp", "glycan_count": 0, "glycosylation_sites": [ { "position": 54, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 84, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 130, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 190, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 313, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 373, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O70567", "name": "Podocalyxin (Podxl)", "organism": "Mus musculus", "uniprot_id": "P97399" }, { "function": "Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Together with its cognate ligand/functional ligand EFNB2 it is involved in the regulation of cell adhesion and migration, and plays a central role in heart morphogenesis, angiogenesis and blood vessel remodeling and permeability. EPHB4-mediated forward signaling controls cellular repulsion and segregation from EFNB2-expressing cells", "gene_name": "EPHB4", "glycan_count": 10, "glycosylation_sites": [ { "position": 203, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 335, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 426, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P54760", "name": "Ephrin B4 (Ephb4)", "organism": "Homo sapiens", "uniprot_id": "P54760" }, { "function": "Neuronal phosphoprotein that coats synaptic vesicles, and binds to the cytoskeleton. Acts as a regulator of synaptic vesicles trafficking, involved in the control of neurotransmitter release at the pre-synaptic terminal (PubMed:21441247, PubMed:23406870). Also involved in the regulation of axon outgrowth and synaptogenesis (By similarity). The complex formed with NOS1 and CAPON proteins is necessary for specific nitric-oxid functions at a presynaptic level (By similarity)", "gene_name": "SYN1", "glycan_count": 1, "glycosylation_sites": [ { "position": 55, "type": "O-linked (GlcNAc) serine" }, { "position": 87, "type": "O-linked (GlcNAc) threonine" }, { "position": 96, "type": "O-linked (GlcNAc) serine" }, { "position": 103, "type": "O-linked (GlcNAc) serine" }, { "position": 261, "type": "O-linked (GlcNAc) serine" }, { "position": 432, "type": "O-linked (GlcNAc) serine; alternate" }, { "position": 526, "type": "O-linked (GlcNAc) threonine" }, { "position": 564, "type": "O-linked (GlcNAc) threonine" }, { "position": 578, "type": "O-linked (GlcNAc) serine" } ], "id": "P17600", "name": "Synapsin", "organism": "Homo sapiens", "uniprot_id": "P17600" }, { "function": "May catalyze the coenzyme A-dependent acetylation of the 2' hydroxyl or amino group of a broad spectrum of aminoglycosides and confer resistance to aminoglycosides (By similarity). In vitro assays show no significant increase of resistance to aminoglycosides, possibly due to low expression in a heterologous system (PubMed:9159528)", "gene_name": "aac", "glycan_count": 0, "glycosylation_sites": [], "id": "P9WQG9", "name": "Decaprenylphosphoryl-\u03b2-D-ribose 2\u2032-epimerase (DprE1)", "organism": "Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)", "uniprot_id": "P9WQG9" }, { "function": "Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis", "gene_name": "folA", "glycan_count": 0, "glycosylation_sites": [], "id": "P9WNX1", "name": "Dihydrofolate reductase (Mtb-DHFR)", "organism": "Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)", "uniprot_id": "P9WNX1" }, { "function": "May function as an output molecule from the suprachiasmatic nucleus (SCN) that transmits behavioral circadian rhythm. May also function locally within the SCN to synchronize output. Potently contracts gastrointestinal (GI) smooth muscle", "gene_name": "PROK2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9HC23", "name": "Prokineticin-1 (PK-1)", "organism": "Homo sapiens", "uniprot_id": "Q9HC23" }, { "function": "Anti-apoptotic protein which can inhibit apoptosis induced by intrinsic and extrinsic apoptotic stimuli. Can modulate both capacitative Ca2+ entry and inositol 1,4,5-trisphosphate (IP3)-mediated Ca2+ release", "gene_name": "TMBIM4", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9HC24", "name": "Prokineticin-2 (PK-2)", "organism": "Homo sapiens", "uniprot_id": "Q9HC24" }, { "function": "DNA- and RNA-binding protein involved in various processes, such as translational repression, RNA stabilization, mRNA splicing, DNA repair and transcription regulation (PubMed:10817758, PubMed:11698476, PubMed:14718551, PubMed:18809583, PubMed:31358969, PubMed:8188694). Predominantly acts as a RNA-binding protein: binds preferentially to the 5'-[CU]CUGCG-3' RNA motif and specifically recognizes mRNA transcripts modified by C5-methylcytosine (m5C) (PubMed:19561594, PubMed:31358969). Promotes mRNA stabilization: acts by binding to m5C-containing mRNAs and recruiting the mRNA stability maintainer ELAVL1, thereby preventing mRNA decay (PubMed:10817758, PubMed:11698476, PubMed:31358969). Component of the CRD-mediated complex that promotes MYC mRNA stability (PubMed:19029303). Contributes to the regulation of translation by modulating the interaction between the mRNA and eukaryotic initiation factors (By similarity). Plays a key role in RNA composition of extracellular exosomes by defining the sorting of small non-coding RNAs, such as tRNAs, Y RNAs, Vault RNAs and miRNAs (PubMed:27559612, PubMed:29073095). Probably sorts RNAs in exosomes by recognizing and binding C5-methylcytosine (m5C)-containing RNAs (PubMed:28341602, PubMed:29073095). Acts as a key effector of epidermal progenitors by preventing epidermal progenitor senescence: acts by regulating the translation of a senescence-associated subset of cytokine mRNAs, possibly by binding to m5C-containing mRNAs (PubMed:29712925). Also involved in pre-mRNA alternative splicing regulation: binds to splice sites in pre-mRNA and regulates splice site selection (PubMed:12604611). Binds to TSC22D1 transcripts, thereby inhibiting their translation and negatively regulating TGF-beta-mediated transcription of COL1A2 (By similarity). Also able to bind DNA: regulates transcription of the multidrug resistance gene MDR1 is enhanced in presence of the APEX1 acetylated form at 'Lys-6' and 'Lys-7' (PubMed:18809583). Binds to promoters that contain a Y-box (5'-CTGATTGGCCAA-3'), such as MDR1 and HLA class II genes (PubMed:18809583, PubMed:8188694). Promotes separation of DNA strands that contain mismatches or are modified by cisplatin (PubMed:14718551). Has endonucleolytic activity and can introduce nicks or breaks into double-stranded DNA, suggesting a role in DNA repair (PubMed:14718551). The secreted form acts as an extracellular mitogen and stimulates cell migration and proliferation (PubMed:19483673)", "gene_name": "YBX1", "glycan_count": 2, "glycosylation_sites": [], "id": "P67809", "name": "YBX1 (Y-box binding protein 1)", "organism": "Homo sapiens", "uniprot_id": "P67809" }, { "function": "Anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA) and protein kinase C (PKC)", "gene_name": "AKAP12", "glycan_count": 1, "glycosylation_sites": [], "id": "Q02952", "name": "AKAP12", "organism": "Homo sapiens", "uniprot_id": "Q02952" }, { "function": "Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA (PubMed:11535615, PubMed:12399544, PubMed:12446774, PubMed:14559997, PubMed:14988723, PubMed:15311285, PubMed:15650047, PubMed:15665856, PubMed:32357935). May also negatively regulate cell cycle progression during unperturbed cell cycles (PubMed:11535615, PubMed:12399544, PubMed:12446774, PubMed:14559997, PubMed:14988723, PubMed:15311285, PubMed:15650047, PubMed:15665856). This regulation is achieved by a number of mechanisms that together help to preserve the integrity of the genome (PubMed:11535615, PubMed:12399544, PubMed:12446774, PubMed:14559997, PubMed:14988723, PubMed:15311285, PubMed:15650047, PubMed:15665856). Recognizes the substrate consensus sequence [R-X-X-S/T] (PubMed:11535615, PubMed:12399544, PubMed:12446774, PubMed:14559997, PubMed:14988723, PubMed:15311285, PubMed:15650047, PubMed:15665856). Binds to and phosphorylates CDC25A, CDC25B and CDC25C (PubMed:12676583, PubMed:12676925, PubMed:12759351, PubMed:14559997, PubMed:14681206, PubMed:19734889, PubMed:9278511). Phosphorylation of CDC25A at 'Ser-178' and 'Thr-507' and phosphorylation of CDC25C at 'Ser-216' creates binding sites for 14-3-3 proteins which inhibit CDC25A and CDC25C (PubMed:9278511). Phosphorylation of CDC25A at 'Ser-76', 'Ser-124', 'Ser-178', 'Ser-279' and 'Ser-293' promotes proteolysis of CDC25A (PubMed:12676583, PubMed:12676925, PubMed:12759351, PubMed:14681206, PubMed:19734889, PubMed:9278511). Phosphorylation of CDC25A at 'Ser-76' primes the protein for subsequent phosphorylation at 'Ser-79', 'Ser-82' and 'Ser-88' by NEK11, which is required for polyubiquitination and degradation of CDCD25A (PubMed:19734889, PubMed:20090422, PubMed:9278511). Inhibition of CDC25 leads to increased inhibitory tyrosine phosphorylation of CDK-cyclin complexes and blocks cell cycle progression (PubMed:9278511). Also phosphorylates NEK6 (PubMed:18728393). Binds to and phosphorylates RAD51 at 'Thr-309', which promotes the release of RAD51 from BRCA2 and enhances the association of RAD51 with chromatin, thereby promoting DNA repair by homologous recombination (PubMed:15665856). Phosphorylates multiple sites within the C-terminus of TP53, which promotes activation of TP53 by acetylation and promotes cell cycle arrest and suppression of cellular proliferation (PubMed:10673501, PubMed:15659650, PubMed:16511572). Also promotes repair of DNA cross-links through phosphorylation of FANCE (PubMed:17296736). Binds to and phosphorylates TLK1 at 'Ser-743', which prevents the TLK1-dependent phosphorylation of the chromatin assembly factor ASF1A (PubMed:12660173, PubMed:12955071). This may enhance chromatin assembly both in the presence or absence of DNA damage (PubMed:12660173, PubMed:12955071). May also play a role in replication fork maintenance through regulation of PCNA (PubMed:18451105). May regulate the transcription of genes that regulate cell-cycle progression through the phosphorylation of histones (By similarity). Phosphorylates histone H3.1 (to form H3T11ph), which leads to epigenetic inhibition of a subset of genes (By similarity). May also phosphorylate RB1 to promote its interaction with the E2F family of transcription factors and subsequent cell cycle arrest (PubMed:17380128). Phosphorylates SPRTN, promoting SPRTN recruitment to chromatin (PubMed:31316063). Reduces replication stress and activates the G2/M checkpoint, by phosphorylating and inactivating PABIR1/FAM122A and promoting the serine/threonine-protein phosphatase 2A-mediated dephosphorylation and stabilization of WEE1 levels and activity (PubMed:33108758)", "gene_name": "CHEK1", "glycan_count": 1, "glycosylation_sites": [], "id": "O14757", "name": "CHEK1", "organism": "Homo sapiens", "uniprot_id": "O14757" }, { "function": "Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation. Also plays a role in delivery of iron to cells. Mediates iron uptake in capsule cells of the developing kidney. Degraded to release iron upon autophagy activation by nutrient starvation (PubMed:25327288)", "gene_name": "Ftl1", "glycan_count": 1, "glycosylation_sites": [], "id": "P29391", "name": "FTH1", "organism": "Mus musculus", "uniprot_id": "P29391" }, { "function": "Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1 (PubMed:10567565, PubMed:20818336, PubMed:28760339, PubMed:29042532, PubMed:38512451). Binds specifically and directly to substrates containing either a simple or bipartite NLS motif (PubMed:20818336, PubMed:28760339, PubMed:29042532, PubMed:38512451). Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism (PubMed:20818336, PubMed:28760339, PubMed:29042532, PubMed:38512451). At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin (PubMed:20818336, PubMed:28760339, PubMed:29042532, PubMed:38512451). The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (PubMed:20818336, PubMed:28760339, PubMed:29042532, PubMed:38512451). Mediates nuclear import of AARS1, MRTFA and RANBP3 (PubMed:10567565, PubMed:20818336, PubMed:28760339, PubMed:38512451)", "gene_name": "KPNA4", "glycan_count": 0, "glycosylation_sites": [], "id": "O00190", "name": "Golgi phosphoprotein 3 (GOLPH3)", "organism": "Homo sapiens", "uniprot_id": "O00629" }, { "function": "RNA-dependent helicase required for nonsense-mediated decay (NMD) of aberrant mRNAs containing premature stop codons and modulates the expression level of normal mRNAs (PubMed:11163187, PubMed:16086026, PubMed:18172165, PubMed:21145460, PubMed:21419344, PubMed:24726324). Is recruited to mRNAs upon translation termination and undergoes a cycle of phosphorylation and dephosphorylation; its phosphorylation appears to be a key step in NMD (PubMed:11544179, PubMed:25220460). Recruited by release factors to stalled ribosomes together with the SMG1C protein kinase complex to form the transient SURF (SMG1-UPF1-eRF1-eRF3) complex (PubMed:19417104). In EJC-dependent NMD, the SURF complex associates with the exon junction complex (EJC) (located 50-55 or more nucleotides downstream from the termination codon) through UPF2 and allows the formation of an UPF1-UPF2-UPF3 surveillance complex which is believed to activate NMD (PubMed:21419344). Phosphorylated UPF1 is recognized by EST1B/SMG5, SMG6 and SMG7 which are thought to provide a link to the mRNA degradation machinery involving exonucleolytic and endonucleolytic pathways, and to serve as adapters to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation and allowing the recycling of NMD factors (PubMed:12554878). UPF1 can also activate NMD without UPF2 or UPF3, and in the absence of the NMD-enhancing downstream EJC indicative for alternative NMD pathways (PubMed:18447585). Plays a role in replication-dependent histone mRNA degradation at the end of phase S; the function is independent of UPF2 (PubMed:16086026, PubMed:18172165). For the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed (PubMed:18447585, PubMed:25220460). The ATPase activity of UPF1 is required for disassembly of mRNPs undergoing NMD (PubMed:21145460). Together with UPF2 and dependent on TDRD6, mediates the degradation of mRNA harboring long 3'UTR by inducing the NMD machinery (By similarity). Also capable of unwinding double-stranded DNA and translocating on single-stranded DNA (PubMed:30218034)", "gene_name": "UPF1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q92900", "name": "GM130", "organism": "Homo sapiens", "uniprot_id": "Q92900" }, { "function": "Precursor of the transcription factor form (Processed cyclic AMP-dependent transcription factor ATF-6 beta), which is embedded in the endoplasmic reticulum membrane (PubMed:11256944). Endoplasmic reticulum stress promotes processing of this form, releasing the transcription factor form that translocates into the nucleus, where it activates transcription of genes involved in the unfolded protein response (UPR) (PubMed:11256944)", "gene_name": "ATF6B", "glycan_count": 6, "glycosylation_sites": [ { "position": 476, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 505, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 610, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 627, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 676, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q99941", "name": "Activating transcription factor 6 (ATF6)", "organism": "Homo sapiens", "uniprot_id": "Q99941" }, { "function": "E3 ubiquitin-protein ligase that participates in multiple biological processes including cell survival, differentiation, apoptosis, and in particular, the innate immune response (PubMed:27981609, PubMed:28747347). Participates in the activation of interferon-gamma signaling by promoting proteasomal degradation of the repressor SOCS1 (PubMed:12163497). Plays a positive role in the TNFalpha and IL-1beta signaling pathways. Mechanistically, induces the 'Lys-63'-linked polyubiquitination of MAP3K7/TAK1 component leading to the activation of NF-kappa-B (PubMed:22084099, PubMed:23152791, PubMed:27981609, PubMed:34871740). Also modulates STAT3 activity through negative regulation of PIAS3, either by degradation of PIAS3 through the ubiquitin-proteasome pathway or exclusion of PIAS3 from the nucleus (PubMed:20516148). Negatively regulates TLR3/4-mediated innate immune response by catalyzing 'Lys-6'- and 'Lys-33'-linked polyubiquitination of TICAM1 and thereby disrupting the TICAM1-TBK1 interaction (PubMed:28747347)", "gene_name": "TRIM8", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9BZR9", "name": "Tripartite motif-containing protein 10 (TRIM10)", "organism": "Homo sapiens", "uniprot_id": "Q9BZR9" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P14679 (human)", "name": "Tyrosinase (TYR)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P17643 (human)", "name": "Tyrosinase-related protein 1 (TYRP-1)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P40967 (human)", "name": "Premelanosome protein (SILV/PMEL)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O75030 (human)", "name": "Microphthalmia-associated transcription factor (MITF)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P35222 (human)", "name": "\u03b2-catenin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P49841 (human)", "name": "Glycogen synthase kinase 3 beta (GSK3\u03b2)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y2T1 (human)", "name": "Axin2", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8N8D1 (human)", "name": "Dapper homolog 2 (Dact2)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "Hyal1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8R4P8", "name": "Pneumolysin", "organism": "Mus musculus", "uniprot_id": "Q8R4P8" }, { "function": "Possible role in sperm motility", "gene_name": "Ldhc", "glycan_count": 1, "glycosylation_sites": [], "id": "P00342", "name": "Lactate dehydrogenase (LDH)", "organism": "Mus musculus", "uniprot_id": "P00342" }, { "function": "Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Implicated in cytokinesis, receptor capping, and cell locomotion (By similarity)", "gene_name": "MYL12A", "glycan_count": 1, "glycosylation_sites": [], "id": "P19105", "name": "Heat Shock Protein 70 (HSP70)", "organism": "Homo sapiens", "uniprot_id": "P19105" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P38658", "name": "Glucose-Regulated Protein 94 (GRP94)", "organism": "Schistosoma mansoni", "uniprot_id": "P38658" }, { "function": "Receptor for lutropin-choriogonadotropic hormone (PubMed:11847099). The activity of this receptor is mediated by G proteins which activate adenylate cyclase (PubMed:11847099)", "gene_name": "LHCGR", "glycan_count": 0, "glycosylation_sites": [ { "position": 99, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 174, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 195, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 291, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 299, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 313, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P22888", "name": "Luteinizing Hormone Receptor (LHR)", "organism": "Homo sapiens", "uniprot_id": "P22888" }, { "function": "Plays a key role in steroid hormone synthesis by enhancing the metabolism of cholesterol into pregnenolone. Mediates the transfer of cholesterol from the outer mitochondrial membrane to the inner mitochondrial membrane where it is cleaved to pregnenolone", "gene_name": "STAR", "glycan_count": 0, "glycosylation_sites": [], "id": "P49675", "name": "Steroidogenic Acute Regulatory Protein (STAR)", "organism": "Homo sapiens", "uniprot_id": "P49675" }, { "function": "Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate) (PubMed:5499971). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa (Probable)", "gene_name": "CKM", "glycan_count": 0, "glycosylation_sites": [], "id": "P00563", "name": "Creatine kinase (CK)", "organism": "Oryctolagus cuniculus", "uniprot_id": "P00563" }, { "function": "Involved in oxygen transport from the lung to the various peripheral tissues", "gene_name": "HBA", "glycan_count": 1, "glycosylation_sites": [], "id": "P01966", "name": "Hemoglobin", "organism": "Bos taurus", "uniprot_id": "P01966" }, { "function": "Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters (By similarity)", "gene_name": "WNT16", "glycan_count": 1, "glycosylation_sites": [ { "position": 143, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 189, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 311, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UBV4", "name": "Wnt16b", "organism": "Homo sapiens", "uniprot_id": "Q9UBV4" }, { "function": "Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase which sumoylates CHD3/Mi2-alpha, causing its release from DNA (PubMed:27068747). This results in suppression of CHD3/Mi2-alpha transcription repression, increased recruitment of RNA polymerase II to gene promoters and positive regulation of transcription including H1-5 and ribosomal proteins such as: RPS6, RPL10A, and RPL12 (PubMed:12663651, PubMed:17209048, PubMed:17220279, PubMed:27068747). The resulting increased transcriptional activity drives cell proliferation (PubMed:12663651, PubMed:17220279). Binds to 5'-TGTCG[CT]GA[CT]A-3' consensus sequences in gene promoters of ribosomal proteins (PubMed:12663651, PubMed:17209048, PubMed:17220279, PubMed:27068747)", "gene_name": "ZBED1", "glycan_count": 0, "glycosylation_sites": [], "id": "O96006", "name": "Wnt2b", "organism": "Homo sapiens", "uniprot_id": "O96006" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O75197/O75581", "name": "LRP5/6", "organism": "", "uniprot_id": "" }, { "function": "Promotes adhesion of endothelial cells through interaction with the alpha-v/beta-3 integrin receptor. Inhibits formation of vascular-like structures. May be involved in regulation of vascular morphogenesis of remodeling in embryonic development", "gene_name": "Edil3", "glycan_count": 0, "glycosylation_sites": [ { "position": 73, "type": "O-linked (GalNAc...) threonine" }, { "position": 88, "type": "O-linked (Fuc...) threonine" }, { "position": 140, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O35475", "name": "Stearoyl-CoA Desaturase 1 (SCD1)", "organism": "Mus musculus", "uniprot_id": "O35474" }, { "function": "Ligand-activated transcription factor. Key regulator of lipid metabolism. Activated by the endogenous ligand 1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphocholine (16:0/18:1-GPC). Activated by oleylethanolamide, a naturally occurring lipid that regulates satiety. Receptor for peroxisome proliferators such as hypolipidemic drugs and fatty acids. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as a transcription activator for the ACOX1 and P450 genes. Transactivation activity requires heterodimerization with RXRA and is antagonized by NR2C2. May be required for the propagation of clock information to metabolic pathways regulated by PER2", "gene_name": "Ppara", "glycan_count": 0, "glycosylation_sites": [], "id": "P23204", "name": "Peroxisome Proliferator-Activated Receptor Alpha (PPAR-\u03b1)", "organism": "Mus musculus", "uniprot_id": "P23204" }, { "function": "The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. RAB5A is required for the fusion of plasma membranes and early endosomes (PubMed:10818110, PubMed:14617813, PubMed:15378032, PubMed:16410077). Contributes to the regulation of filopodia extension (PubMed:14978216). Required for the exosomal release of SDCBP, CD63, PDCD6IP and syndecan (PubMed:22660413). Regulates maturation of apoptotic cell-containing phagosomes, probably downstream of DYN2 and PIK3C3 (By similarity)", "gene_name": "RAB5A", "glycan_count": 1, "glycosylation_sites": [ { "position": 120, "type": "(Microbial infection) N-beta-linked (GlcNAc) arginine" } ], "id": "P20339", "name": "Rab5", "organism": "Homo sapiens", "uniprot_id": "P20339" }, { "function": "The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (PubMed:38538795). In its active state, RAB7A binds to a variety of effector proteins playing a key role in the regulation of endo-lysosomal trafficking. Governs early-to-late endosomal maturation, microtubule minus-end as well as plus-end directed endosomal migration and positioning, and endosome-lysosome transport through different protein-protein interaction cascades. Also plays a central role in growth-factor-mediated cell signaling, nutrient-transportor mediated nutrient uptake, neurotrophin transport in the axons of neurons and lipid metabolism. Also involved in regulation of some specialized endosomal membrane trafficking, such as maturation of melanosomes, pathogen-induced phagosomes (or vacuoles) and autophagosomes. Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. Plays a role in the fusion of phagosomes with lysosomes. In concert with RAC1, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. Controls the endosomal trafficking and neurite outgrowth signaling of NTRK1/TRKA (PubMed:11179213, PubMed:12944476, PubMed:14617358, PubMed:20028791, PubMed:21255211). Regulates the endocytic trafficking of the EGF-EGFR complex by regulating its lysosomal degradation. Involved in the ADRB2-stimulated lipolysis through lipophagy, a cytosolic lipase-independent autophagic pathway (By similarity). Required for the exosomal release of SDCBP, CD63 and syndecan (PubMed:22660413). Required for vesicular trafficking and cell surface expression of ACE2 (PubMed:33147445). May play a role in PRPH neuronal intermediate filament assembly (By similarity)", "gene_name": "RAB7A", "glycan_count": 1, "glycosylation_sites": [], "id": "P51149", "name": "Rab7", "organism": "Homo sapiens", "uniprot_id": "P51149" }, { "function": "Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation. This is one of the isozymes catalyzing that reaction. Also able to catalyze the synthesis of chito-oligosaccharide depending on the substrate (By similarity)", "gene_name": "HAS1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q92839", "name": "Hyaluronic Acid Synthase 1 (HAS1)", "organism": "Homo sapiens", "uniprot_id": "Q92839" }, { "function": "Chemotactic for interleukin-activated T-cells but not unstimulated T-cells, neutrophils or monocytes. Induces calcium release in activated T-cells. Binds to CXCR3. May play an important role in CNS diseases which involve T-cell recruitment. May play a role in skin immune responses", "gene_name": "CXCL11", "glycan_count": 0, "glycosylation_sites": [], "id": "Q92840", "name": "Hyaluronic Acid Synthase 2 (HAS2)", "organism": "Homo sapiens", "uniprot_id": "O14625" }, { "function": "Transcriptional repressor involved in organogenesis. Plays an essential role in ureteric bud invasion during kidney development", "gene_name": "SALL1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NSC2", "name": "Hyaluronic Acid Synthase 3 (HAS3)", "organism": "Homo sapiens", "uniprot_id": "Q9NSC2" }, { "function": "Receptor for hyaluronic acid (HA) (By similarity). Involved in cell motility (By similarity). When hyaluronan binds to HMMR, the phosphorylation of a number of proteins, including PTK2/FAK1 occurs. May also be involved in cellular transformation and metastasis formation, and in regulating extracellular-regulated kinase (ERK) activity. May act as a regulator of adipogenisis (By similarity)", "gene_name": "HMMR", "glycan_count": 1, "glycosylation_sites": [ { "position": 133, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 477, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 567, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 588, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O75330", "name": "RHAMM (HMMR)", "organism": "Homo sapiens", "uniprot_id": "O75330" }, { "function": "", "gene_name": "TMEM40", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8WWA1", "name": "HARE (Stabilin-2)", "organism": "Homo sapiens", "uniprot_id": "Q8WWA1" }, { "function": "Essential bifunctional enzyme that catalyzes both the N-deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Plays a role in determining the extent and pattern of sulfation of heparan sulfate. Required for the exosomal release of SDCBP, CD63 and syndecan (PubMed:22660413)", "gene_name": "NDST2", "glycan_count": 0, "glycosylation_sites": [ { "position": 233, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 350, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 400, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 666, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 726, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 802, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P52849", "name": "Mannosidase II (ManII)", "organism": "Homo sapiens", "uniprot_id": "P52849" }, { "function": "Binds to oocyte zona pellucida in vivo. May play a role in the fertilization process and/or early embryonic development", "gene_name": "OVGP1", "glycan_count": 1, "glycosylation_sites": [ { "position": 402, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 441, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 580, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 596, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 648, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q12889", "name": "OVGP1", "organism": "Homo sapiens", "uniprot_id": "Q12889" }, { "function": "Plays a role in sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs) via its interaction with the ESCRT-I complex (endosomal sorting complex required for transport I), and possibly also other ESCRT complexes (PubMed:18434552, PubMed:21757351). May act as a negative regulator of Ras-mediated mitogenic activity (PubMed:18434552). Plays a role in ciliogenesis (PubMed:20393563)", "gene_name": "PTPN23", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H3S7", "name": "Glypican 2 (GPC2)", "organism": "Homo sapiens", "uniprot_id": "Q9H3S7" }, { "function": "", "gene_name": "CTAG1A", "glycan_count": 0, "glycosylation_sites": [], "id": "P78358", "name": "Junctional Adhesion Molecule-A (JAM-A)", "organism": "Homo sapiens", "uniprot_id": "P78358" }, { "function": "Orphan nuclear receptor that binds DNA as a monomer to the 5'-TCAAGGCCA-3' sequence and controls expression of target genes: regulates key biological processes, such as early embryonic development, cholesterol and bile acid synthesis pathways, as well as liver and pancreas morphogenesis (PubMed:16289203, PubMed:18410128, PubMed:21614002, PubMed:32433991, PubMed:38409506, PubMed:9786908). Ligand-binding causes conformational change which causes recruitment of coactivators, promoting target gene activation (PubMed:21614002). The specific ligand is unknown, but specific phospholipids, such as phosphatidylethanolamine, phosphatidylserine, dilauroyl phosphatidylcholine and diundecanoyl phosphatidylcholine can act as ligand in vitro (PubMed:15707893, PubMed:15723037, PubMed:15897460, PubMed:21614002, PubMed:22504882, PubMed:23737522, PubMed:26416531, PubMed:26553876). Acts as a pioneer transcription factor, which unwraps target DNA from histones and elicits local opening of closed chromatin (PubMed:38409506). Plays a central role during preimplantation stages of embryonic development (By similarity). Plays a minor role in zygotic genome activation (ZGA) by regulating a small set of two-cell stage genes (By similarity). Plays a major role in morula development (2-16 cells embryos) by acting as a master regulator at the 8-cell stage, controlling expression of lineage-specifying transcription factors and genes involved in mitosis, telomere maintenance and DNA repair (By similarity). Zygotic NR5A2 binds to both closed and open chromatin with other transcription factors, often at SINE B1/Alu repeats DNA elements, promoting chromatin accessibility at nearby regulatory regions (By similarity). Also involved in the epiblast stage of development and embryonic stem cell pluripotency, by promoting expression of POU5F1/OCT4 (PubMed:27984042). Regulates other processes later in development, such as formation of connective tissue in lower jaw and middle ear, neural stem cell differentiation, ovarian follicle development and Sertoli cell differentiation (By similarity). Involved in exocrine pancreas development and acinar cell differentiation (By similarity). Acts as an essential transcriptional regulator of lipid metabolism (PubMed:20159957). Key regulator of cholesterol 7-alpha-hydroxylase gene (CYP7A) expression in liver (PubMed:10359768). Also acts as a negative regulator of inflammation in different organs, such as, liver and pancreas (PubMed:20159957). Protects against intestinal inflammation via its ability to regulate glucocorticoid production (By similarity). Plays an anti-inflammatory role during the hepatic acute phase response by acting as a corepressor: inhibits the hepatic acute phase response by preventing dissociation of the N-Cor corepressor complex (PubMed:20159957). Acts as a regulator of immunity by promoting lymphocyte T-cell development, proliferation and effector functions (By similarity). Also involved in resolution of endoplasmic reticulum stress in the liver (By similarity)", "gene_name": "NR5A2", "glycan_count": 0, "glycosylation_sites": [], "id": "O00482", "name": "Liver Receptor Homolog-1 (LRH-1)", "organism": "Homo sapiens", "uniprot_id": "O00482" }, { "function": "Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. Implicated in regulating a variety of cellular processes, including cellular growth, senescence, differentiation, apoptosis, angiogenesis, and neoplastic transformation. Involved in myogenesis by inhibiting skeletal muscle and cardiac myocyte differentiation and promoting muscle precursor cells proliferation. Inhibits the binding of E2A-containing protein complexes to muscle creatine kinase E-box enhancer. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-BMAL1 heterodimer", "gene_name": "ID3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q02535", "name": "Inhibitor of differentiation 1 (ID1)", "organism": "Homo sapiens", "uniprot_id": "Q02535" }, { "function": "Required to induce the formation and stabilization of endoplasmic reticulum (ER) tubules (PubMed:24262037, PubMed:25612671, PubMed:27619977). They regulate membrane morphogenesis in the ER by promoting tubular ER production (PubMed:24262037, PubMed:25612671, PubMed:27619977, PubMed:27786289). They influence nuclear envelope expansion, nuclear pore complex formation and proper localization of inner nuclear membrane proteins (PubMed:26906412). However each isoform have specific functions mainly depending on their tissue expression specificities (Probable)", "gene_name": "RTN4", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9NQC3", "name": "Nogo-A", "organism": "Homo sapiens", "uniprot_id": "Q9NQC3" }, { "function": "Carries out a dual function: signal transduction and activation of transcription (PubMed:29844444). Mediates cellular responses to the cytokine KITLG/SCF and other growth factors. Binds to the GAS element and activates PRL-induced transcription. Positively regulates hematopoietic/erythroid differentiation", "gene_name": "STAT5B", "glycan_count": 1, "glycosylation_sites": [], "id": "P51692", "name": "Signal Transducer and Activator of Transcription 5B (STAT5B)", "organism": "Homo sapiens", "uniprot_id": "P51692" }, { "function": "Constituent of ilotropin, which is a partially purified preparation of cellophane wrapping (CW) pancreata. Capable of initiating duct cell proliferation, a prerequisite for islet neogenesis", "gene_name": "INGAP", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9QYF7", "name": "Mobp (Myelin-Associated Oligodendrocyte Basic Protein)", "organism": "Mesocricetus auratus", "uniprot_id": "Q92778" }, { "function": "Component of the cytosolic iron-sulfur protein assembly (CIA) complex, a multiprotein complex that mediates the incorporation of iron-sulfur cluster into extramitochondrial Fe/S proteins. Seems to negatively regulate the level of HIF1A expression, although this effect could be indirect", "gene_name": "CIAO3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H6Q4", "name": "CD34", "organism": "Homo sapiens", "uniprot_id": "Q9H6Q4" }, { "function": "Transcriptional activator required for the development of normal hearing, sense of balance and kidney function. Required for the expression of SLC26A4/PDS, JAG1 and COCH in a subset of epithelial cells and the development of the endolymphatic system in the inner ear. Also required for the expression of SLC4A1/AE1, SLC4A9/AE4, ATP6V1B1 and the differentiation of intercalated cells in the epithelium of distal renal tubules (By similarity)", "gene_name": "FOXI1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q12951", "name": "FOXD1", "organism": "Homo sapiens", "uniprot_id": "Q12951" }, { "function": "Required for optimal lysosomal function (PubMed:21224396). Blocks EGF-stimulated EGFR intraluminal sorting and degradation. Conversely by binding with the phosphatidylinositol 4,5-bisphosphate, regulates its PIP5K1C interaction, inhibits HGS ubiquitination and relieves LAPTM4B inhibition of EGFR degradation (PubMed:25588945). Recruits SLC3A2 and SLC7A5 (the Leu transporter) to the lysosome, promoting entry of leucine and other essential amino acid (EAA) into the lysosome, stimulating activation of proton-transporting vacuolar (V)-ATPase protein pump (V-ATPase) and hence mTORC1 activation (PubMed:25998567). Plays a role as negative regulator of TGFB1 production in regulatory T cells (PubMed:26126825). Binds ceramide and facilitates its exit from late endosome in order to control cell death pathways (PubMed:26280656)", "gene_name": "LAPTM4B", "glycan_count": 0, "glycosylation_sites": [], "id": "Q86VI4", "name": "LAPTM4B", "organism": "Homo sapiens", "uniprot_id": "Q86VI4" }, { "function": "Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits (PubMed:20378773, PubMed:21823654, PubMed:27686148). A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam complexes show there is considerable movement of all 5 proteins (PubMed:26744406, PubMed:26900875, PubMed:26901871, PubMed:27686148)", "gene_name": "bamA", "glycan_count": 0, "glycosylation_sites": [], "id": "P0A940", "name": "BamC", "organism": "Escherichia coli (strain K12)", "uniprot_id": "P0A940" }, { "function": "With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm (Probable). Plays a role in resistance to environmental stress, and a role in outer membrane functionality and cell shape (PubMed:11906175, PubMed:361695). Non-covalently binds peptidoglycan (Probable) (PubMed:25135663). Acts as a porin with low permeability that allows slow penetration of small solutes (PubMed:1370823, PubMed:20004640, PubMed:21069910). A very abundant protein, there can be up to 210,000 OmpA molecules per cell (PubMed:24766808). Reconstitution in unilamellar lipid vesicles shows only about 3% of the protein is in an open conformation, which allows diffusion of L-arabinose at a rate comparable to that of OmpF porin; the pores interconvert very rarely (PubMed:7517935). Native and reconstituted protein forms ion channels with 2 conductance states of (50-80 pS) and (260-320 pS); the states are interconvertible in this study. Interconversion requires refolding of the periplasmic domain (PubMed:10636850). Small pores are converted into large pores by increasing temperature; in this model the C-terminal periplasmic domain forms 8 more beta sheets to form a larger pore (PubMed:15850404). The center of the isolated beta-barrel is polar and has a central gate (involving Glu-73, Lys-103, Glu-149 and Arg-159, sandwiched between Tyr-29, Phe-40 and Tyr-94), with no obvious passage for water or ions (Probable) (PubMed:9808047). Gating involves the Glu-73-Arg-159 salt bridge; gate opening probably involves formation of alternate salt bridges Glu-149-Arg-159 and Glu-73-Lys-103 (PubMed:17041590). Modeling suggests that non-covalent binding of OmpA (from the outer membrane) and TolR (from the inner membrane) to peptidoglycan maintains the position of the cell wall in the periplasm, holding it approximately equidistant from both the inner and outer membranes. Trimeric Lpp controls the width of the periplasm, adjusts its tilt angle to accommodate to the available space, and can compensate in part for an absence of OmpA (Probable)", "gene_name": "ompA", "glycan_count": 0, "glycosylation_sites": [], "id": "P0A910", "name": "OmpA", "organism": "Escherichia coli (strain K12)", "uniprot_id": "P0A910" }, { "function": "Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import (Probable). In addition, binds D-galactose and D-glucose and plays a role in the chemotaxis towards these two sugars by interacting with the Trg chemoreceptor (PubMed:3057628, PubMed:4927373). Chemotaxis requires MglB, but not MglA or MglC (PubMed:6294056)", "gene_name": "mglB", "glycan_count": 0, "glycosylation_sites": [], "id": "P0AEE5", "name": "NagE", "organism": "Escherichia coli (strain K12)", "uniprot_id": "P0AEE5" }, { "function": "Catalyzes the deamidation of nicotinamide (NAM) into nicotinate (PubMed:4399474, PubMed:8726014). Likely functions in the cyclical salvage pathway for production of NAD from nicotinamide (PubMed:4399474)", "gene_name": "pncA", "glycan_count": 0, "glycosylation_sites": [], "id": "P21369", "name": "FadL", "organism": "Escherichia coli (strain K12)", "uniprot_id": "P21369" }, { "function": "Oocyte-specific protein tyrosine kinase that phosphorylates and inhibits CDK1/CDC2 and acts as a key regulator of meiosis during both prophase I and metaphase II (PubMed:29606300). Required to maintain meiotic arrest in oocytes during the germinal vesicle (GV) stage, a long period of quiescence at dictyate prophase I, by phosphorylating CDK1 at 'Tyr-15', leading to inhibit CDK1 activity and prevent meiotic reentry. Also required for metaphase II exit during egg activation by phosphorylating CDK1 at 'Tyr-15', to ensure exit from meiosis in oocytes and promote pronuclear formation (By similarity)", "gene_name": "WEE2", "glycan_count": 1, "glycosylation_sites": [], "id": "P0C1S8", "name": "PBP2a", "organism": "Homo sapiens", "uniprot_id": "P0C1S8" }, { "function": "Forms pores that allow passive diffusion of small molecules across the outer membrane", "gene_name": "ompC", "glycan_count": 0, "glycosylation_sites": [], "id": "P06996", "name": "OmpC", "organism": "Escherichia coli (strain K12)", "uniprot_id": "P06996" }, { "function": "Outer membrane channel, which is required for the function of several efflux systems such as AcrAB-TolC, AcrEF-TolC, EmrAB-TolC and MacAB-TolC. These systems are involved in export of antibiotics and other toxic compounds from the cell. TolC is also involved in import of colicin E1 into the cells", "gene_name": "tolC", "glycan_count": 0, "glycosylation_sites": [], "id": "P02930", "name": "TolC", "organism": "Escherichia coli (strain K12)", "uniprot_id": "P02930" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01906/P01909", "name": "HLA-DQ2/DQ8", "organism": "", "uniprot_id": "" }, { "function": "Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins during skeletal muscle atrophy. Recognizes TERF1", "gene_name": "FBXO32", "glycan_count": 1, "glycosylation_sites": [], "id": "Q969P5", "name": "Atrogin-1 (FBXO32)", "organism": "Homo sapiens", "uniprot_id": "Q969P5" }, { "function": "Acts as a transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle differentiation. Together with MYF5 and MYOG, co-occupies muscle-specific gene promoter core region during myogenesis. Induces fibroblasts to differentiate into myoblasts. Interacts with and is inhibited by the twist protein. This interaction probably involves the basic domains of both proteins (By similarity)", "gene_name": "MYOD1", "glycan_count": 1, "glycosylation_sites": [], "id": "P15172", "name": "MyoD", "organism": "Homo sapiens", "uniprot_id": "P15172" }, { "function": "Ca(2+)-dependent receptor for myeloid cells that binds to carbohydrates on neutrophils and monocytes. Mediates the interaction of activated endothelial cells or platelets with leukocytes. The ligand recognized is sialyl-Lewis X. Mediates rapid rolling of leukocyte rolling over vascular surfaces during the initial steps in inflammation through interaction with SELPLG. Mediates cell-cell interactions and cell adhesion via the interaction with integrin alpha-IIb/beta3 (ITGA2B:ITGB3) and integrin alpha-V/beta-3 (ITGAV:ITGB3) (By similarity)", "gene_name": "Selp", "glycan_count": 0, "glycosylation_sites": [ { "position": 45, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 54, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 107, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 212, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 347, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 456, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 603, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 654, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 661, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 679, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P98106", "name": "Familial Intrahepatic Cholestasis 1 Protein (FIC1)", "organism": "Rattus norvegicus", "uniprot_id": "P98106" }, { "function": "Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation", "gene_name": "M", "glycan_count": 0, "glycosylation_sites": [ { "position": 20, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P06821", "name": "Matrix protein 2 (M2)", "organism": "Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)", "uniprot_id": "P06821" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P22442", "name": "Polymerase acidic protein (PA)", "organism": "Bromelia plumieri", "uniprot_id": "P22442" }, { "function": "Lipid kinase that can phosphorylate both monoacylglycerol and diacylglycerol to form lysophosphatidic acid (LPA) and phosphatidic acid (PA), respectively (PubMed:15939762). Does not phosphorylate sphingosine (PubMed:15939762). Phosphorylates ceramide (By similarity). Phosphorylates 1,2-dioleoylglycerol more rapidly than 2,3-dioleoylglycerol (By similarity). Independently of its lipid kinase activity, acts as a component of the TIM22 complex (PubMed:28712724, PubMed:28712726). The TIM22 complex mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane by forming a twin-pore translocase that uses the membrane potential as the external driving force (PubMed:28712724, PubMed:28712726). In the TIM22 complex, required for the import of a subset of metabolite carriers into mitochondria, such as ANT1/SLC25A4 and SLC25A24, while it is not required for the import of TIMM23 (PubMed:28712724). Overexpression increases the formation and secretion of LPA, resulting in transactivation of EGFR and activation of the downstream MAPK signaling pathway, leading to increased cell growth (PubMed:15939762)", "gene_name": "AGK", "glycan_count": 0, "glycosylation_sites": [], "id": "Q53H12", "name": "AGK", "organism": "Homo sapiens", "uniprot_id": "Q53H12" }, { "function": "Scaffold protein involved in different aspects of polarized cell differentiation regulating epithelial and neuronal morphogenesis and T-cell polarization (PubMed:15182672, PubMed:16344308, PubMed:16965391, PubMed:18641685, PubMed:18716323, PubMed:19041750, PubMed:27380321). Via its interaction with CRTAM, required for the late phase polarization of a subset of CD4+ T-cells, which in turn regulates TCR-mediated proliferation and IFNG and IL22 production (By similarity). Plays a role in cell directional movement, cell orientation, cell sheet organization and Golgi complex polarization at the cell migration front (By similarity). Promotes epithelial cell layer barrier function via maintaining cell-cell adhesion (By similarity). Most probably functions in the establishment of apico-basal cell polarity (PubMed:16344308, PubMed:19041750). May function in cell proliferation regulating progression from G1 to S phase and as a positive regulator of apoptosis for instance during acinar morphogenesis of the mammary epithelium (PubMed:16965391, PubMed:19041750). May regulate cell invasion via MAPK-mediated cell migration and adhesion (PubMed:18641685, PubMed:18716323). May play a role in exocytosis and in the targeting of synaptic vesicles to synapses (PubMed:15182672). Functions as an activator of Rac GTPase activity (PubMed:15182672)", "gene_name": "SCRIB", "glycan_count": 2, "glycosylation_sites": [], "id": "Q14160", "name": "SCRIB", "organism": "Homo sapiens", "uniprot_id": "Q14160" }, { "function": "Receptor for MSH (alpha, beta and gamma) and ACTH (PubMed:11442765, PubMed:11707265, PubMed:1325670, PubMed:1516719, PubMed:8463333). The activity of this receptor is mediated by G proteins which activate adenylate cyclase (PubMed:11707265, PubMed:1325670, PubMed:16463023, PubMed:19737927). Mediates melanogenesis, the production of eumelanin (black/brown) and phaeomelanin (red/yellow), via regulation of cAMP signaling in melanocytes (PubMed:31097585)", "gene_name": "MC1R", "glycan_count": 1, "glycosylation_sites": [ { "position": 29, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q01726", "name": "MC1R", "organism": "Homo sapiens", "uniprot_id": "Q01726" }, { "function": "Bidirectional uniporter involved in the facilitative transport of nucleosides and nucleobases, and contributes to maintaining their cellular homeostasis (PubMed:10722669, PubMed:12527552, PubMed:12590919, PubMed:16214850, PubMed:21795683, PubMed:9396714, PubMed:9478986). Functions as a Na(+)-independent, passive transporter (PubMed:9478986). Involved in the transport of nucleosides such as inosine, adenosine, uridine, thymidine, cytidine and guanosine (PubMed:10722669, PubMed:12527552, PubMed:12590919, PubMed:16214850, PubMed:21795683, PubMed:9396714, PubMed:9478986). Also able to transport purine nucleobases (hypoxanthine, adenine, guanine) and pyrimidine nucleobases (thymine, uracil) (PubMed:16214850, PubMed:21795683). Involved in nucleoside transport at basolateral membrane of kidney cells, allowing liver absorption of nucleoside metabolites (PubMed:12527552). Mediates apical nucleoside uptake into Sertoli cells, thereby regulating the transport of nucleosides in testis across the blood-testis-barrier (PubMed:23639800). Mediates both the influx and efflux of hypoxanthine in skeletal muscle microvascular endothelial cells to control the amount of intracellular hypoxanthine available for xanthine oxidase-mediated ROS production (By similarity)", "gene_name": "SLC29A2", "glycan_count": 0, "glycosylation_sites": [ { "position": 48, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 57, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 225, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q14542", "name": "ENT2", "organism": "Homo sapiens", "uniprot_id": "Q14542" }, { "function": "Acts as a membrane potential-dependent organic anion transporter, the transport requires a low concentration of chloride ions (PubMed:22460716). Mediates chloride-dependent transport of urate (PubMed:22460716). Mediates sodium-independent high affinity transport of thyroid hormones including L-thyroxine (T4) and 3,3',5-triiodo-L-thyronine (T3) (PubMed:30367059, PubMed:34937426). Can actively transport inorganic phosphate into cells via Na(+) cotransport (PubMed:22460716)", "gene_name": "SLC17A4", "glycan_count": 0, "glycosylation_sites": [ { "position": 47, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 56, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 66, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 75, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 90, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y2C5", "name": "CMAS (CMP-sialic acid synthetase)", "organism": "Homo sapiens", "uniprot_id": "Q9Y2C5" }, { "function": "Histone deacetylase that catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (PubMed:28497810). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (By similarity). Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR (PubMed:12724404). Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development (By similarity). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:16428440, PubMed:28977666). Component of the SIN3B complex that represses transcription and counteracts the histone acetyltransferase activity of EP300 through the recognition H3K27ac marks by PHF12 and the activity of the histone deacetylase HDAC2 (PubMed:37137925). Also deacetylates non-histone targets: deacetylates TSHZ3, thereby regulating its transcriptional repressor activity (PubMed:19343227). May be involved in the transcriptional repression of circadian target genes, such as PER1, mediated by CRY1 through histone deacetylation (By similarity). Involved in MTA1-mediated transcriptional corepression of TFF1 and CDKN1A (PubMed:21965678). In addition to protein deacetylase activity, also acts as a protein-lysine deacylase by recognizing other acyl groups: catalyzes removal of (2E)-butenoyl (crotonyl), lactoyl (lactyl) and 2-hydroxyisobutanoyl (2-hydroxyisobutyryl) acyl groups from lysine residues, leading to protein decrotonylation, delactylation and de-2-hydroxyisobutyrylation, respectively (PubMed:28497810, PubMed:29192674, PubMed:35044827)", "gene_name": "HDAC2", "glycan_count": 2, "glycosylation_sites": [], "id": "Q92769", "name": "HDAC2", "organism": "Homo sapiens", "uniprot_id": "Q92769" }, { "function": "Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone", "gene_name": "NDUFB2", "glycan_count": 0, "glycosylation_sites": [], "id": "O95178", "name": "NDUFA9", "organism": "Homo sapiens", "uniprot_id": "O95178" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Not specified (mosquito ortholog)", "name": "CD151", "organism": "", "uniprot_id": "" }, { "function": "Chemoattractant active on T-lymphocytes and monocytes but not neutrophils. Activates the C-X-C chemokine receptor CXCR4 to induce a rapid and transient rise in the level of intracellular calcium ions and chemotaxis. Also binds to atypical chemokine receptor ACKR3, which activates the beta-arrestin pathway and acts as a scavenger receptor for SDF-1. Binds to the allosteric site (site 2) of integrins and activates integrins ITGAV:ITGB3, ITGA4:ITGB1 and ITGA5:ITGB1 in a CXCR4-independent manner (By similarity). Acts as a positive regulator of monocyte migration and a negative regulator of monocyte adhesion via the LYN kinase. Stimulates migration of monocytes and T-lymphocytes through its receptors, CXCR4 and ACKR3, and decreases monocyte adherence to surfaces coated with ICAM-1, a ligand for beta-2 integrins. SDF1A/CXCR4 signaling axis inhibits beta-2 integrin LFA-1 mediated adhesion of monocytes to ICAM-1 through LYN kinase. Plays a protective role after myocardial infarction. Induces down-regulation and internalization of ACKR3 expressed in various cells (By similarity). Has several critical functions during embryonic development; required for B-cell lymphopoiesis, myelopoiesis in bone marrow and heart ventricular septum formation. Stimulates the proliferation of bone marrow-derived B-cell progenitors in the presence of IL7 as well as growth of stromal cell-dependent pre-B-cells (PubMed:8134392)", "gene_name": "Cxcl12", "glycan_count": 0, "glycosylation_sites": [], "id": "P40224", "name": "CXCL12", "organism": "Mus musculus", "uniprot_id": "P40224" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O08870", "name": "PLD1 (Phospholipase D1)", "organism": "", "uniprot_id": "O08870" }, { "function": "Terminal enzyme of the cyclooxygenase (COX)-2-mediated prostaglandin E2 (PGE2) biosynthetic pathway (PubMed:10869354, PubMed:11795891). Catalyzes the glutathione-dependent oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) in response to inflammatory stimuli (PubMed:10869354, PubMed:11795891). Plays a key role in inflammation response, fever and pain (PubMed:12835414, PubMed:14566340). Also catalyzes the oxidoreduction of endocannabinoids into prostaglandin glycerol esters and PGG2 into 15-hydroperoxy-PGE2. In addition, displays low glutathione transferase and glutathione-dependent peroxidase activities, toward 1-chloro-2,4-dinitrobenzene and 5-hydroperoxyicosatetraenoic acid (5-HPETE), respectively (By similarity)", "gene_name": "Ptges", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9JM51", "name": "P2Y1 (P2ry1)", "organism": "Mus musculus", "uniprot_id": "Q9JM51" }, { "function": "May play a role in the process of maturation of dendritic cells (By similarity). Required for the development of cerebellar granule cells", "gene_name": "Tmem176b", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9R1Q6", "name": "PTEN", "organism": "Mus musculus", "uniprot_id": "Q9R1Q6" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O88567", "name": "UCP2", "organism": "", "uniprot_id": "O88567" }, { "function": "Probable Polycomb group (PcG) protein involved in transcriptional regulation mediated by ligand-bound nuclear hormone receptors, such as retinoic acid receptors (RARs) and peroxisome proliferator-activated receptor gamma (PPARG) (PubMed:16606617). Acts as a coactivator of RARA and RXRA through association with NCOA1 (PubMed:16606617). Acts as a corepressor for PPARG and suppresses its adipocyte differentiation-inducing activity (By similarity). Non-catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1) (PubMed:20436459, PubMed:30664650, PubMed:36180891). Acts as a sensor of N(6)-methyladenine methylation on DNA (6mA): recognizes and binds 6mA DNA, leading to its ubiquitination and degradation by TRIP12, thereby inactivating the PR-DUB complex and regulating Polycomb silencing (PubMed:30982744). The PR-DUB complex is an epigenetic regulator of gene expression and acts as a transcriptional coactivator, affecting genes involved in development, cell communication, signaling, cell proliferation and cell viability (PubMed:30664650, PubMed:36180891). ASXL1, ASXL2 and ASXL3 function redundantly in the PR-DUB complex (By similarity) (PubMed:30664650). The ASXL proteins are essential for chromatin recruitment and transcriptional activation of associated genes (By similarity). ASXL1 and ASXL2 are important for BAP1 protein stability (PubMed:30664650). Together with BAP1, negatively regulates epithelial-mesenchymal transition (EMT) of trophoblast stem cells during placental development by regulating genes involved in epithelial cell integrity, cell adhesion and cytoskeletal organization (PubMed:34170818)", "gene_name": "ASXL1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8IXJ9", "name": "ASXL1", "organism": "Homo sapiens", "uniprot_id": "Q8IXJ9" }, { "function": "Component of the 17S U2 SnRNP complex of the spliceosome, a large ribonucleoprotein complex that removes introns from transcribed pre-mRNAs (PubMed:12234937, PubMed:27720643, PubMed:32494006, PubMed:34822310). The 17S U2 SnRNP complex (1) directly participates in early spliceosome assembly and (2) mediates recognition of the intron branch site during pre-mRNA splicing by promoting the selection of the pre-mRNA branch-site adenosine, the nucleophile for the first step of splicing (PubMed:32494006, PubMed:34822310). Within the 17S U2 SnRNP complex, SF3B1 is part of the SF3B subcomplex, which is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence in pre-mRNA (PubMed:12234937). Sequence independent binding of SF3A and SF3B subcomplexes upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA (PubMed:12234937). May also be involved in the assembly of the 'E' complex (PubMed:10882114). Also acts as a component of the minor spliceosome, which is involved in the splicing of U12-type introns in pre-mRNAs (PubMed:15146077, PubMed:33509932). Together with other U2 snRNP complex components may also play a role in the selective processing of microRNAs (miRNAs) from the long primary miRNA transcript, pri-miR-17-92 (By similarity)", "gene_name": "SF3B1", "glycan_count": 1, "glycosylation_sites": [], "id": "O75533", "name": "SF3B1", "organism": "Homo sapiens", "uniprot_id": "O75533" }, { "function": "", "gene_name": "SETBP1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y6X0", "name": "SETBP1", "organism": "Homo sapiens", "uniprot_id": "Q9Y6X0" }, { "function": "Found in sweat, has an antimicrobial activity during early bacterial colonization (PubMed:11694882, PubMed:23426625). The secreted peptide assembles into homohexameric complexes that can associate with and also insert into pathogen membranes (PubMed:23426625). Once inserted in bacteria membranes forms anion channels probably altering the transmembrane potential essential for bacterial survival (PubMed:23426625). Highly effective against E.coli, E.faecalis, S.aureus and C.albicans (PubMed:11694882). Optimal pH and salt concentration resemble the conditions in sweat (PubMed:11694882). Also exhibits proteolytic activity, cleaving on the C-terminal side of Arg and, to a lesser extent, Lys residues (PubMed:17448443)", "gene_name": "DCD", "glycan_count": 2, "glycosylation_sites": [ { "position": 30, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" }, { "position": 38, "type": "O-linked (Xyl...) (chondroitin sulfate) serine" } ], "id": "P81605", "name": "Pro-dermcidin (pro-DCD)", "organism": "Homo sapiens", "uniprot_id": "P81605" }, { "function": "Transcription factor that is involved in embryonic development, establishment of tissue-specific gene expression and regulation of gene expression in differentiated tissues. Is thought to act as a 'pioneer' factor opening the compacted chromatin for other proteins through interactions with nucleosomal core histones and thereby replacing linker histones at target enhancer and/or promoter sites. Binds DNA with the consensus sequence 5'-[AC]A[AT]T[AG]TT[GT][AG][CT]T[CT]-3' (By similarity). In embryonic development is required for notochord formation. Involved in the development of multiple endoderm-derived organ systems such as the liver, pancreas and lungs; FOXA1 and FOXA2 seem to have at least in part redundant roles. Originally described as a transcription activator for a number of liver genes such as AFP, albumin, tyrosine aminotransferase, PEPCK, etc. Interacts with the cis-acting regulatory regions of these genes. Involved in glucose homeostasis; regulates the expression of genes important for glucose sensing in pancreatic beta-cells and glucose homeostasis. Involved in regulation of fat metabolism. Binds to fibrinogen beta promoter and is involved in IL6-induced fibrinogen beta transcriptional activation", "gene_name": "FOXA2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y261", "name": "FoxO3\u03b1", "organism": "Homo sapiens", "uniprot_id": "Q9Y261" }, { "function": "Involved in innate immunity against invading pathogens. Adapter used by TLR3, TLR4 (through TICAM2) and TLR5 to mediate NF-kappa-B and interferon-regulatory factor (IRF) activation, and to induce apoptosis (PubMed:12471095, PubMed:12539043, PubMed:14739303, PubMed:28747347, PubMed:35215908). Ligand binding to these receptors results in TRIF recruitment through its TIR domain (PubMed:12471095, PubMed:12539043, PubMed:14739303). Distinct protein-interaction motifs allow recruitment of the effector proteins TBK1, TRAF6 and RIPK1, which in turn, lead to the activation of transcription factors IRF3 and IRF7, NF-kappa-B and FADD respectively (PubMed:12471095, PubMed:12539043, PubMed:14739303). Phosphorylation by TBK1 on the pLxIS motif leads to recruitment and subsequent activation of the transcription factor IRF3 to induce expression of type I interferon and exert a potent immunity against invading pathogens (PubMed:25636800). Component of a multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and plays a role in the activation of a cascade of antiviral responses including the induction of pro-inflammatory cytokines (By similarity)", "gene_name": "TICAM1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8IUC6", "name": "TRIF", "organism": "Homo sapiens", "uniprot_id": "Q8IUC6" }, { "function": "Important role in the capacity of milk to transport calcium phosphate", "gene_name": "CSN1S1", "glycan_count": 1, "glycosylation_sites": [], "id": "P02662", "name": "Alpha-casein", "organism": "Bos taurus", "uniprot_id": "P02662" }, { "function": "Kappa-casein stabilizes micelle formation, preventing casein precipitation in milk", "gene_name": "CSN3", "glycan_count": 21, "glycosylation_sites": [ { "position": 142, "type": "O-linked (GalNAc...) threonine" }, { "position": 152, "type": "O-linked (GalNAc...) threonine" }, { "position": 153, "type": "O-linked (GalNAc...) serine" }, { "position": 154, "type": "O-linked (GalNAc...) threonine" }, { "position": 157, "type": "O-linked (GalNAc...) threonine" }, { "position": 163, "type": "O-linked (GalNAc...) threonine" }, { "position": 170, "type": "O-linked (GalNAc...) serine; alternate" }, { "position": 186, "type": "O-linked (GalNAc...) threonine; partial" } ], "id": "P02668", "name": "\u03ba-casein", "organism": "Bos taurus", "uniprot_id": "P02668" }, { "function": "Important role in determination of the surface properties of the casein micelles", "gene_name": "CSN2", "glycan_count": 1, "glycosylation_sites": [], "id": "P02666", "name": "\u03b2-casein", "organism": "Bos taurus", "uniprot_id": "P02666" }, { "function": "Plays an important role in the final stage of carbohydrate digestion. Isomaltase activity is specific for both alpha-1,4- and alpha-1,6-oligosaccharides", "gene_name": "SI", "glycan_count": 5, "glycosylation_sites": [ { "position": 99, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 437, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 455, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 823, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 855, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 904, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 926, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1235, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1303, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1340, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1354, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1403, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1535, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1572, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1675, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1748, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1763, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1815, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P14410", "name": "Sucrase-Isomaltase (SI)", "organism": "Homo sapiens", "uniprot_id": "P14410" }, { "function": "Putative taste receptor. TAS1R2/TAS1R3 recognizes diverse natural and synthetic sweeteners", "gene_name": "TAS1R2", "glycan_count": 0, "glycosylation_sites": [ { "position": 84, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 248, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 292, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 312, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 368, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 428, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 487, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 527, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8TE23", "name": "T1R2 (TAS1R2)", "organism": "Homo sapiens", "uniprot_id": "Q8TE23" }, { "function": "Putative taste receptor. TAS1R1/TAS1R3 responds to the umami taste stimulus (the taste of monosodium glutamate). TAS1R2/TAS1R3 recognizes diverse natural and synthetic sweeteners. TAS1R3 is essential for the recognition and response to the disaccharide trehalose (By similarity). Sequence differences within and between species can significantly influence the selectivity and specificity of taste responses", "gene_name": "TAS1R3", "glycan_count": 4, "glycosylation_sites": [ { "position": 85, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 130, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 264, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 285, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 380, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 411, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 432, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 475, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q7RTX0", "name": "T1R3 (TAS1R3)", "organism": "Homo sapiens", "uniprot_id": "Q7RTX0" }, { "function": "The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (PubMed:33795473). TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (PubMed:33795473). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:33795473). The TFIID complex structure can be divided into 3 modules TFIID-A, TFIID-B, and TFIID-C (PubMed:33795473). TAF3 forms the TFIID-A module together with TAF5 and TBP (PubMed:33795473). Required in complex with TBPL2 for the differentiation of myoblasts into myocytes (PubMed:11438666). The TAF3-TBPL2 complex replaces TFIID at specific promoters at an early stage in the differentiation process (PubMed:11438666)", "gene_name": "TAF3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q5VWG9", "name": "Asprosin", "organism": "Homo sapiens", "uniprot_id": "Q5VWG9" }, { "function": "", "gene_name": "Ccm2l", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8VCC6", "name": "Olfr734", "organism": "Mus musculus", "uniprot_id": "Q8VCC6" }, { "function": "Odorant receptor", "gene_name": "OR1N2", "glycan_count": 0, "glycosylation_sites": [ { "position": 8, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8NGR9", "name": "OR4M1", "organism": "Homo sapiens", "uniprot_id": "Q8NGR9" }, { "function": "Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids, phosphatidylserines (PS) and phosphatidylethanolamines (PE), from the outer to the inner leaflet of intracellular membranes (PubMed:30018401). May contribute to the maintenance of membrane lipid asymmetry in endosome compartment (PubMed:30018401)", "gene_name": "ATP11B", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y2G3", "name": "Insulin-induced gene 1", "organism": "Homo sapiens", "uniprot_id": "Q9Y2G3" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "A7JZL3", "name": "Akkermansia muciniphila", "organism": "", "uniprot_id": "A7JZL3" }, { "function": "Involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. Substrates include POMC, renin, enkephalin, dynorphin, somatostatin, insulin and AGRP", "gene_name": "PCSK1", "glycan_count": 3, "glycosylation_sites": [ { "position": 173, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 401, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 632, "type": "O-linked (GalNAc...) threonine" } ], "id": "P29120", "name": "Prohormone Convertase 1 (PC1)", "organism": "Homo sapiens", "uniprot_id": "P29120" }, { "function": "Receptor for ADIPOQ, an essential hormone secreted by adipocytes that regulates glucose and lipid metabolism (PubMed:12802337, PubMed:25855295). Required for normal body fat and glucose homeostasis. ADIPOQ-binding activates a signaling cascade that leads to increased PPARA activity, and ultimately to increased fatty acid oxidation and glucose uptake. Has intermediate affinity for globular and full-length adiponectin. Required for normal revascularization after chronic ischemia caused by severing of blood vessels (By similarity)", "gene_name": "ADIPOR2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q86V24", "name": "Adiponectin receptor 2 (AdipoR2)", "organism": "Homo sapiens", "uniprot_id": "Q86V24" }, { "function": "Catalyzes the interconversion of (R)- and (S)-stereoisomers of alpha-methyl-branched-chain fatty acyl-CoA esters (PubMed:10655068, PubMed:11060359, PubMed:7649182). Acts only on coenzyme A thioesters, not on free fatty acids, and accepts as substrates a wide range of alpha-methylacyl-CoAs, including pristanoyl-CoA, trihydroxycoprostanoyl-CoA (an intermediate in bile acid synthesis), and arylpropionic acids like the anti-inflammatory drug ibuprofen (2-(4-isobutylphenyl)propionic acid) but neither 3-methyl-branched nor linear-chain acyl-CoAs (PubMed:10655068, PubMed:11060359, PubMed:7649182)", "gene_name": "AMACR", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UHK6", "name": "Alpha-methylacyl-CoA racemase (AMACR)", "organism": "Homo sapiens", "uniprot_id": "Q9UHK6" }, { "function": "Regulates high density lipoprotein (HDL) cholesterol metabolism by promoting the ubiquitination and degradation of the oxysterols receptors LXR (NR1H2 and NR1H3)", "gene_name": "TTC39B", "glycan_count": 0, "glycosylation_sites": [], "id": "Q5VTQ0", "name": "Membrane-bound O-acyltransferase domain-containing 7 (MBOAT7)", "organism": "Homo sapiens", "uniprot_id": "Q5VTQ0" }, { "function": "NPY is implicated in the control of feeding and in secretion of gonadotrophin-release hormone", "gene_name": "NPY", "glycan_count": 0, "glycosylation_sites": [], "id": "P01303", "name": "Neuropeptide Y (NPY)", "organism": "Homo sapiens", "uniprot_id": "P01303" }, { "function": "Plays a role in weight homeostasis. Involved in the control of feeding behavior through the central melanocortin system. Acts as alpha melanocyte-stimulating hormone antagonist by inhibiting cAMP production mediated by stimulation of melanocortin receptors within the hypothalamus and adrenal gland. Has very low activity with MC5R (By similarity). Is an inverse agonist for MC3R and MC4R being able to suppress their constitutive activity. It promotes MC3R and MC4R endocytosis in an arrestin-dependent manner", "gene_name": "AGRP", "glycan_count": 0, "glycosylation_sites": [], "id": "O00253", "name": "Agouti-related protein (AgRP)", "organism": "Homo sapiens", "uniprot_id": "O00253" }, { "function": "Satiety factor closely associated with the actions of leptin and neuropeptide Y; this anorectic peptide inhibits both normal and starvation-induced feeding and completely blocks the feeding response induced by neuropeptide Y and regulated by leptin in the hypothalamus. It promotes neuronal development and survival in vitro", "gene_name": "CARTPT", "glycan_count": 1, "glycosylation_sites": [], "id": "Q16568", "name": "Cocaine- and Amphetamine-Regulated Transcript Protein (CARTPT)", "organism": "Homo sapiens", "uniprot_id": "Q16568" }, { "function": "Receptor for MSH (alpha, beta and gamma) and ACTH. This receptor is mediated by G proteins which activate adenylate cyclase. Required for expression of anticipatory patterns of activity and wakefulness during periods of limited nutrient availability and for the normal regulation of circadian clock activity in the brain", "gene_name": "MC3R", "glycan_count": 0, "glycosylation_sites": [ { "position": 2, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 16, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 28, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P41968", "name": "Melanocortin 3 Receptor (MC3R)", "organism": "Homo sapiens", "uniprot_id": "P41968" }, { "function": "Lectin-type cell surface receptor which may play a role in antigen capturing by dendritic cells (PubMed:11748283, PubMed:21880719, PubMed:25995448). Specifically recognizes non-sialylated galactose-terminated biantennary glycans containing the trisaccharide epitope Gal(beta1-3/4)GlcNAc(beta1-2)Man (PubMed:21880719, PubMed:25995448). Binds to serum IgG (PubMed:25995448). Efficiently targets ligand into antigen-processing and peptide-loading compartments for presentation to T-cells (PubMed:11748283). May mediate potent inhibition of induction of IFN-alpha/beta expression in plasmacytoid dendritic cells (PubMed:11748283, PubMed:21880719). May act as a signaling receptor that activates protein-tyrosine kinases and mobilizes intracellular calcium (PubMed:11748283)", "gene_name": "CLEC4C", "glycan_count": 0, "glycosylation_sites": [ { "position": 110, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 137, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 164, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8WTT0", "name": "KACL (CLEC2A)", "organism": "Homo sapiens", "uniprot_id": "Q8WTT0" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P22303 (Electrophorus electricus, assay source)", "name": "Acetylcholinesterase (AChE)", "organism": "", "uniprot_id": "" }, { "function": "Apoptosis regulator that functions through different apoptotic signaling pathways (PubMed:15102863, PubMed:20673843, PubMed:27076518). Plays a roles as pro-apoptotic protein that positively regulates intrinsic apoptotic process in a BAX- and BAK1-dependent manner or in a BAX- and BAK1-independent manner (PubMed:15102863, PubMed:27076518). In response to endoplasmic reticulum stress promotes mitochondrial apoptosis through downstream BAX/BAK1 activation and positive regulation of PERK-mediated unfolded protein response (By similarity). Activates apoptosis independently of heterodimerization with survival-promoting BCL2 and BCL2L1 through induction of mitochondrial outer membrane permeabilization, in a BAX- and BAK1-independent manner, in response to inhibition of ERAD-proteasome degradation system, resulting in cytochrome c release (PubMed:27076518). In response to DNA damage, mediates intrinsic apoptotic process in a TP53-dependent manner (PubMed:15102863). Plays a role in granulosa cell apoptosis by CASP3 activation (PubMed:20673843). Plays a roles as anti-apoptotic protein during neuronal apoptotic process, by negatively regulating poly ADP-ribose polymerase-dependent cell death through regulation of neuronal calcium homeostasis and mitochondrial bioenergetics in response to NMDA excitation (By similarity). In addition to its role in apoptosis, may regulate trophoblast cell proliferation during the early stages of placental development, by acting on G1/S transition through regulation of CCNE1 expression (PubMed:19942931). May also play a role as an inducer of autophagy by disrupting interaction between MCL1 and BECN1 (PubMed:24113155)", "gene_name": "BOK", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UMX3", "name": "NIX (BNIP3L)", "organism": "Homo sapiens", "uniprot_id": "Q9UMX3" }, { "function": "GFAP, a class-III intermediate filament, is a cell-specific marker that, during the development of the central nervous system, distinguishes astrocytes from other glial cells", "gene_name": "Gfap", "glycan_count": 2, "glycosylation_sites": [], "id": "P03995", "name": "Glial Fibrillary Acidic Protein (GFAP)", "organism": "Mus musculus", "uniprot_id": "P03995" }, { "function": "Essential for mitotic growth. Mediates organelle inheritance", "gene_name": "MDM1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q01846", "name": "BRN3A (POU4F1)", "organism": "Saccharomyces cerevisiae (strain ATCC 204508 / S288c)", "uniprot_id": "Q01846" }, { "function": "Primary component of whey, it binds retinol and is probably involved in the transport of that molecule", "gene_name": "LGB", "glycan_count": 8, "glycosylation_sites": [], "id": "P02754", "name": "\u03b2-Lactoglobulin (BLG)", "organism": "Bos taurus", "uniprot_id": "P02754" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P29459 (p35), P29460 (p40)", "name": "IL-12", "organism": "", "uniprot_id": "" }, { "function": "E3 ubiquitin-protein ligase that acts as a regulator of the TORC1 signaling pathway (PubMed:33594058, PubMed:35114100). Positively regulates the TORC1 signaling pathway independently of arginine levels: acts by catalyzing 'Lys-29'-polyubiquitination and degradation of CASTOR1, releasing the GATOR2 complex from CASTOR1 (PubMed:33594058). Also negatively regulates the TORC1 signaling pathway in response to leucine deprivation: acts by mediating 'Lys-63'-linked polyubiquitination of SESN2, promoting SESN2-interaction with the GATOR2 complex (PubMed:35114100). Also involved in protein trafficking and localization (PubMed:23129617, PubMed:23353890, PubMed:24387786, PubMed:27808481, PubMed:32409562). Acts as a regulator of synaptic transmission by mediating ubiquitination and degradation of AMPAR receptor GluA2/GRIA2 (PubMed:23129617, PubMed:33650289). Does not catalyze ubiquitination of GluA1/GRIA1 (PubMed:23129617). Also acts as a regulator of the recycling endosome pathway by mediating ubiquitination of VAMP3 (PubMed:23353890). Regulates lysosome positioning by catalyzing ubiquitination and degradation of ARL8B (PubMed:27808481). Plays a role in growth regulation involved in G1/S transition by mediating, possibly by mediating ubiquitination of SLC22A18 (PubMed:16314844). Acts with a limited set of E2 enzymes, such as UBE2D1 and UBE2N (PubMed:33650289)", "gene_name": "RNF167", "glycan_count": 0, "glycosylation_sites": [ { "position": 33, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 79, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9H6Y7", "name": "CD34", "organism": "Homo sapiens", "uniprot_id": "Q9H6Y7" }, { "function": "Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Within the 20S core complex, PSMB5 displays a chymotrypsin-like activity", "gene_name": "PSMB5", "glycan_count": 1, "glycosylation_sites": [], "id": "P28074", "name": "Carfilzomib target: Proteasome subunit beta type-5 (PSMB5)", "organism": "Homo sapiens", "uniprot_id": "P28074" }, { "function": "Participates in the initial step of the glucosylceramide-based glycosphingolipid/GSL synthetic pathway at the cytosolic surface of the Golgi (PubMed:1532799, PubMed:8643456). Catalyzes the transfer of glucose from UDP-glucose to ceramide to produce glucosylceramide/GlcCer (such as beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine) (PubMed:1532799, PubMed:8643456). GlcCer is the core component of glycosphingolipids/GSLs, amphipathic molecules consisting of a ceramide lipid moiety embedded in the outer leaflet of the membrane, linked to one of hundreds of different externally oriented oligosaccharide structures (PubMed:8643456). Glycosphingolipids are essential components of membrane microdomains that mediate membrane trafficking and signal transduction, implicated in many fundamental cellular processes, including growth, differentiation, migration, morphogenesis, cell-to-cell and cell-to-matrix interactions (By similarity). They are required for instance in the proper development and functioning of the nervous system (By similarity). As an example of their role in signal transduction, they regulate the leptin receptor/LEPR in the leptin-mediated signaling pathway (By similarity). They also play an important role in the establishment of the skin barrier regulating keratinocyte differentiation and the proper assembly of the cornified envelope (By similarity). The biosynthesis of GSLs is also required for the proper intestinal endocytic uptake of nutritional lipids (By similarity). Catalyzes the synthesis of xylosylceramide/XylCer (such as beta-D-xylosyl-(1<->1')-N-acylsphing-4-enine) using UDP-Xyl as xylose donor (PubMed:33361282)", "gene_name": "UGCG", "glycan_count": 1, "glycosylation_sites": [], "id": "Q16739", "name": "Ceramide galactosyltransferase (UGT8)", "organism": "Homo sapiens", "uniprot_id": "Q16739" }, { "function": "Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is essential for late-stage differentiation of M.xanthus", "gene_name": "sigB", "glycan_count": 0, "glycosylation_sites": [], "id": "P19433", "name": "Gamma-glutamyl transferase (GGT)", "organism": "Myxococcus xanthus", "uniprot_id": "P19433" }, { "function": "Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers (PubMed:2207090, PubMed:6504138, PubMed:7704569). Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin (PubMed:2207090, PubMed:6504138, PubMed:7704569). Implicated in neuronal migration (By similarity)", "gene_name": "TUBB2B", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6B856", "name": "Glutamate dehydrogenase (GLDH)", "organism": "Bos taurus", "uniprot_id": "Q6B856" }, { "function": "As an RNA helicase, unwinds RNA and alters RNA structures through ATP binding and hydrolysis. Involved in multiple cellular processes, including pre-mRNA splicing, alternative splicing, rRNA processing and miRNA processing, as well as transcription regulation (By similarity) (PubMed:12368261). Plays a role in innate immunity. Specifically restricts bunyavirus infection, including Rift Valley fever virus (RVFV) or La Crosse virus (LACV), but not vesicular stomatitis virus (VSV), in an interferon- and DROSHA-independent manner (PubMed:25126784)", "gene_name": "Rm62", "glycan_count": 0, "glycosylation_sites": [], "id": "P19109", "name": "Alkaline phosphatase (ALP)", "organism": "Drosophila melanogaster", "uniprot_id": "P19109" }, { "function": "", "gene_name": "aspC", "glycan_count": 0, "glycosylation_sites": [], "id": "P00509", "name": "Aspartate aminotransferase (AST)", "organism": "Escherichia coli (strain K12)", "uniprot_id": "P00509" }, { "function": "May play a role in mediating neutrophil activation and chemotaxis", "gene_name": "LSP1", "glycan_count": 1, "glycosylation_sites": [], "id": "P33241", "name": "LSP1", "organism": "Homo sapiens", "uniprot_id": "P33241" }, { "function": "Transcriptional coactivator for CREB1 which activates transcription through both consensus and variant cAMP response element (CRE) sites. Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated and acts independently of CREB1 'Ser-133' phosphorylation. Enhances the interaction of CREB1 with TAF4. Regulates gluconeogenesis as a component of the LKB1/AMPK/TORC2 signaling pathway. Regulates the expression of specific genes such as the steroidogenic gene, StAR. Potent coactivator of PPARGC1A and inducer of mitochondrial biogenesis in muscle cells. Also coactivator for TAX activation of the human T-cell leukemia virus type 1 (HTLV-1) long terminal repeats (LTR)", "gene_name": "CRTC2", "glycan_count": 2, "glycosylation_sites": [], "id": "Q53ET0", "name": "Cyclic AMP-Regulated Transcriptional Coactivator 2 (CRTC2)", "organism": "Homo sapiens", "uniprot_id": "Q53ET0" }, { "function": "Aquaglyceroporins form homotetrameric transmembrane channels, with each monomer independently mediating glycerol and water transport across the plasma membrane along their osmotic gradient (PubMed:11952783, PubMed:30420639, PubMed:30423801, PubMed:36737436, PubMed:9405233). Could also be permeable to urea (PubMed:9405233). Mediates the efflux of glycerol, formed upon triglyceride hydrolysis, to avoid its accumulation in adipocytes and to make it available to other tissues. In the kidney, mediates the reabsorption of glycerol, preventing its loss in urine, again participating to energy homeostasis. In pancreatic beta cells, it also mediates the efflux of glycerol, regulating its intracellular levels (By similarity)", "gene_name": "AQP7", "glycan_count": 0, "glycosylation_sites": [], "id": "O14520", "name": "Mitochondrial Glycerol-3-Phosphate Dehydrogenase (mGPDH)", "organism": "Homo sapiens", "uniprot_id": "O14520" }, { "function": "RNA cytosine C(5)-methyltransferase that methylates cytosine to 5-methylcytosine (m5C) in various RNAs, such as tRNAs, mRNAs and some long non-coding RNAs (lncRNAs) (PubMed:17071714, PubMed:22995836, PubMed:31199786, PubMed:31358969). Involved in various processes, such as epidermal stem cell differentiation, testis differentiation and maternal to zygotic transition during early development: acts by increasing protein synthesis; cytosine C(5)-methylation promoting tRNA stability and preventing mRNA decay (PubMed:31199786). Methylates cytosine to 5-methylcytosine (m5C) at positions 34 and 48 of intron-containing tRNA(Leu)(CAA) precursors, and at positions 48, 49 and 50 of tRNA(Gly)(GCC) precursors (PubMed:17071714, PubMed:22995836, PubMed:31199786). tRNA methylation is required generation of RNA fragments derived from tRNAs (tRFs) (PubMed:31199786). Also mediates C(5)-methylation of mitochondrial tRNAs (PubMed:31276587). Catalyzes cytosine C(5)-methylation of mRNAs, leading to stabilize them and prevent mRNA decay: mRNA stabilization involves YBX1 that specifically recognizes and binds m5C-modified transcripts (PubMed:22395603, PubMed:31358969, PubMed:34556860). Cytosine C(5)-methylation of mRNAs also regulates mRNA export: methylated transcripts are specifically recognized by THOC4/ALYREF, which mediates mRNA nucleo-cytoplasmic shuttling (PubMed:28418038). Also mediates cytosine C(5)-methylation of non-coding RNAs, such as vault RNAs (vtRNAs), promoting their processing into regulatory small RNAs (PubMed:23871666). Cytosine C(5)-methylation of vtRNA VTRNA1.1 promotes its processing into small-vault RNA4 (svRNA4) and regulates epidermal differentiation (PubMed:31186410). May act downstream of Myc to regulate epidermal cell growth and proliferation (By similarity). Required for proper spindle assembly and chromosome segregation, independently of its methyltransferase activity (PubMed:19596847)", "gene_name": "NSUN2", "glycan_count": 3, "glycosylation_sites": [], "id": "Q08J23", "name": "NSUN2", "organism": "Homo sapiens", "uniprot_id": "Q08J23" }, { "function": "Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate and the reversible oxidation of (S)-malate to oxaloacetate", "gene_name": "PHGDH", "glycan_count": 1, "glycosylation_sites": [], "id": "O43175", "name": "PHGDH", "organism": "Homo sapiens", "uniprot_id": "O43175" }, { "function": "Functions as an mRNA export adapter; component of the transcription/export (TREX) complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA (PubMed:15833825, PubMed:15998806, PubMed:17190602). TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NXF1 pathway (PubMed:15833825, PubMed:15998806, PubMed:17190602). Involved in the nuclear export of intronless mRNA; proposed to be recruited to intronless mRNA by ATP-bound DDX39B (PubMed:17984224). Plays a key role in mRNP recognition and mRNA packaging by bridging the mRNP-bound EJC and the TREX core complex (PubMed:37020021). TREX recruitment occurs via an interaction between ALYREF/THOC4 and the cap-binding protein NCBP1 (PubMed:15833825, PubMed:15998806, PubMed:17190602, PubMed:37020021). Required for TREX complex assembly and for linking DDX39B to the cap-binding complex (CBC) (PubMed:15998806, PubMed:17984224, PubMed:37020021). Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NXF1 pathway) (PubMed:11675789, PubMed:11707413, PubMed:11979277, PubMed:15833825, PubMed:15998806, PubMed:17190602, PubMed:18364396, PubMed:22144908, PubMed:22893130, PubMed:23222130, PubMed:25662211). In conjunction with THOC5 functions in NXF1-NXT1 mediated nuclear export of HSP70 mRNA; both proteins enhance the RNA binding activity of NXF1 and are required for NXF1 localization to the nuclear rim (PubMed:19165146). Involved in mRNA export of C5-methylcytosine (m5C)-containing mRNAs: specifically recognizes and binds m5C mRNAs and mediates their nucleo-cytoplasmic shuttling (PubMed:28418038). Acts as a chaperone and promotes the dimerization of transcription factors containing basic leucine zipper (bZIP) domains and thereby promotes transcriptional activation (PubMed:10488337). Involved in transcription elongation and genome stability (PubMed:12438613)", "gene_name": "ALYREF", "glycan_count": 1, "glycosylation_sites": [], "id": "Q86V81", "name": "ALYREF", "organism": "Homo sapiens", "uniprot_id": "Q86V81" }, { "function": "", "gene_name": "HSPB7", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UBY9", "name": "Cystatin F", "organism": "Homo sapiens", "uniprot_id": "Q9UBY9" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Multiple", "name": "Nicotinic acetylcholine receptor (nAChR)", "organism": "", "uniprot_id": "" }, { "function": "Antagonist of fibroblast growth factor (FGF) pathways via inhibition of FGF-mediated phosphorylation of ERK1/2 (By similarity). Thereby acts as an antagonist of FGF-induced retinal lens fiber differentiation, may inhibit limb bud outgrowth and may negatively modulate respiratory organogenesis (By similarity). Inhibits TGFB-induced epithelial-to-mesenchymal transition in retinal lens epithelial cells (By similarity). Inhibits CBL/C-CBL-mediated EGFR ubiquitination (PubMed:17974561)", "gene_name": "SPRY2", "glycan_count": 1, "glycosylation_sites": [], "id": "O43597", "name": "SPRY1", "organism": "Homo sapiens", "uniprot_id": "O43597" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P59594 (SARS-CoV-1)", "name": "Spike protein (S)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "R9UQ53 (MERS-CoV)", "name": "Spike protein (S)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04578 (HIV-1)", "name": "gp41", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q05328 (Marburgvirus)", "name": "GP (Glycoprotein)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P15423 (HCoV-229E)", "name": "Spike protein (S)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6Q1S2 (HCoV-NL63)", "name": "Spike protein (S)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "U3NAI2 (HCoV-HKU1)", "name": "Spike protein (S)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "U3NAI2 (HCoV-OC43)", "name": "Spike protein (S)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "MW591993 (CCoV-HuPn-2018)", "name": "Spike protein (S)", "organism": "", "uniprot_id": "" }, { "function": "Protein involved in various processes, such as stress granule formation and innate immunity (PubMed:12642610, PubMed:20180778, PubMed:23279204, PubMed:30510222, PubMed:30804210). Plays an essential role in stress granule formation (PubMed:12642610, PubMed:20180778, PubMed:23279204, PubMed:32302570, PubMed:32302571, PubMed:32302572, PubMed:34739333, PubMed:35977029, PubMed:36183834, PubMed:36279435, PubMed:36692217, PubMed:37379838). Stress granules are membraneless compartments that store mRNAs and proteins, such as stalled translation pre-initiation complexes, in response to stress (PubMed:12642610, PubMed:20180778, PubMed:23279204, PubMed:27022092, PubMed:32302570, PubMed:32302571, PubMed:32302572, PubMed:36279435, PubMed:37379838). Promotes formation of stress granules phase-separated membraneless compartment by undergoing liquid-liquid phase separation (LLPS) upon unfolded RNA-binding: functions as a molecular switch that triggers RNA-dependent LLPS in response to a rise in intracellular free RNA concentrations (PubMed:32302570, PubMed:32302571, PubMed:32302572, PubMed:34739333, PubMed:36279435, PubMed:36692217). Also acts as an ATP- and magnesium-dependent helicase: unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency (PubMed:9889278). Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA (PubMed:9889278). Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends (PubMed:9889278). Plays an essential role in innate immunity by promoting CGAS and RIGI activity (PubMed:30510222, PubMed:30804210). Participates in the DNA-triggered cGAS/STING pathway by promoting the DNA binding and activation of CGAS (PubMed:30510222). Triggers the condensation of cGAS, a process probably linked to the formation of membrane-less organelles (PubMed:34779554). Also enhances RIGI-induced type I interferon production probably by helping RIGI at sensing pathogenic RNA (PubMed:30804210). May also act as a phosphorylation-dependent sequence-specific endoribonuclease in vitro: Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR (PubMed:11604510)", "gene_name": "G3BP1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q13283", "name": "GTPase-activating protein-binding protein 1 (G3BP1)", "organism": "Homo sapiens", "uniprot_id": "Q13283" }, { "function": "Probable cytoskeletal component that directly or indirectly plays an important role in neurofilament architecture. May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Controls degradation of TBCB. Controls degradation of MAP1B and MAP1S, and is critical for neuronal maintenance and survival", "gene_name": "GAN", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H2C0", "name": "Syntaxin 17 (STX17)", "organism": "Homo sapiens", "uniprot_id": "Q9H2C0" }, { "function": "Possible role in transport between endoplasmic reticulum and Golgi", "gene_name": "YIF1A", "glycan_count": 1, "glycosylation_sites": [], "id": "O95070", "name": "Vesicle-associated membrane protein 8 (VAMP8)", "organism": "Homo sapiens", "uniprot_id": "O95070" }, { "function": "Plays a role in pre-mRNA splicing and in the regulation of alternative splicing events. Activates exon skipping of its own pre-mRNA during muscle cell differentiation. Binds to the polypyrimidine tract of introns. May promote RNA looping when bound to two separate polypyrimidine tracts in the same pre-mRNA. May promote the binding of U2 snRNP to pre-mRNA. Cooperates with RAVER1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre-mRNA. Represses the splicing of MAPT/Tau exon 10 (PubMed:15009664). Binds to polypyrimidine-rich controlling element (PCE) of CFTR and promotes exon skipping of CFTR exon 9, thereby antagonizing TIA1 and its role in exon inclusion of CFTR exon 9 (PubMed:14966131). Plays a role in the splicing of pyruvate kinase PKM by binding repressively to a polypyrimidine tract flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (PubMed:20010808). In case of infection by picornaviruses, binds to the viral internal ribosome entry site (IRES) and stimulates the IRES-mediated translation (PubMed:21518806)", "gene_name": "PTBP1", "glycan_count": 2, "glycosylation_sites": [], "id": "P26599", "name": "PTBP1", "organism": "Homo sapiens", "uniprot_id": "P26599" }, { "function": "NAD-dependent protein-lysine deacylase that can act both as a deacetylase or deacylase (desuccinylase, depropionylase, deglutarylase and dedecanoylase), depending on the context (PubMed:22722849, PubMed:26907567, PubMed:30653310, PubMed:31542297, PubMed:35939806). Specifically mediates deacetylation of histone H3 at 'Lys-18' (H3K18Ac) (PubMed:22722849, PubMed:30420520, PubMed:35939806). In contrast to other histone deacetylases, displays strong preference for a specific histone mark, H3K18Ac, directly linked to control of gene expression (PubMed:22722849, PubMed:30653310). H3K18Ac is mainly present around the transcription start site of genes and has been linked to activation of nuclear hormone receptors; SIRT7 thereby acts as a transcription repressor (PubMed:22722849). Moreover, H3K18 hypoacetylation has been reported as a marker of malignancy in various cancers and seems to maintain the transformed phenotype of cancer cells (PubMed:22722849). Also able to mediate deacetylation of histone H3 at 'Lys-36' (H3K36Ac) in the context of nucleosomes (PubMed:30653310). Also mediates deacetylation of non-histone proteins, such as ATM, CDK9, DDX21, DDB1, FBL, FKBP5/FKBP51, GABPB1, RAN, RRP9/U3-55K and POLR1E/PAF53 (PubMed:24207024, PubMed:26867678, PubMed:28147277, PubMed:28426094, PubMed:28790157, PubMed:28886238, PubMed:30540930, PubMed:30944854, PubMed:31075303). Enriched in nucleolus where it stimulates transcription activity of the RNA polymerase I complex (PubMed:16618798, PubMed:19174463, PubMed:24207024). Acts by mediating the deacetylation of the RNA polymerase I subunit POLR1E/PAF53, thereby promoting the association of RNA polymerase I with the rDNA promoter region and coding region (PubMed:16618798, PubMed:19174463, PubMed:24207024). In response to metabolic stress, SIRT7 is released from nucleoli leading to hyperacetylation of POLR1E/PAF53 and decreased RNA polymerase I transcription (PubMed:24207024). Required to restore the transcription of ribosomal RNA (rRNA) at the exit from mitosis (PubMed:19174463). Promotes pre-ribosomal RNA (pre-rRNA) cleavage at the 5'-terminal processing site by mediating deacetylation of RRP9/U3-55K, a core subunit of the U3 snoRNP complex (PubMed:26867678). Mediates 'Lys-37' deacetylation of Ran, thereby regulating the nuclear export of NF-kappa-B subunit RELA/p65 (PubMed:31075303). Acts as a regulator of DNA damage repair by mediating deacetylation of ATM during the late stages of DNA damage response, promoting ATM dephosphorylation and deactivation (PubMed:30944854). Suppresses the activity of the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes by mediating deacetylation of DDB1, which prevents the interaction between DDB1 and CUL4 (CUL4A or CUL4B) (PubMed:28886238). Activates RNA polymerase II transcription by mediating deacetylation of CDK9, thereby promoting 'Ser-2' phosphorylation of the C-terminal domain (CTD) of RNA polymerase II (PubMed:28426094). Deacetylates FBL, promoting histone-glutamine methyltransferase activity of FBL (PubMed:30540930). Acts as a regulator of mitochondrial function by catalyzing deacetylation of GABPB1 (By similarity). Regulates Akt/AKT1 activity by mediating deacetylation of FKBP5/FKBP51 (PubMed:28147277). Required to prevent R-loop-associated DNA damage and transcription-associated genomic instability by mediating deacetylation and subsequent activation of DDX21, thereby overcoming R-loop-mediated stalling of RNA polymerases (PubMed:28790157). In addition to protein deacetylase activity, also acts as a protein-lysine deacylase (PubMed:27436229, PubMed:27997115, PubMed:31542297). Acts as a protein depropionylase by mediating depropionylation of Osterix (SP7), thereby regulating bone formation by osteoblasts (By similarity). Acts as a histone deglutarylase by mediating deglutarylation of histone H4 on 'Lys-91' (H4K91glu); a mark that destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes (PubMed:31542297). Acts as a histone desuccinylase: in response to DNA damage, recruited to DNA double-strand breaks (DSBs) and catalyzes desuccinylation of histone H3 on 'Lys-122' (H3K122succ), thereby promoting chromatin condensation and DSB repair (PubMed:27436229). Also promotes DSB repair by promoting H3K18Ac deacetylation, regulating non-homologous end joining (NHEJ) (By similarity). Along with its role in DNA repair, required for chromosome synapsis during prophase I of female meiosis by catalyzing H3K18Ac deacetylation (By similarity). Involved in transcriptional repression of LINE-1 retrotransposon via H3K18Ac deacetylation, and promotes their association with the nuclear lamina (PubMed:31226208). Required to stabilize ribosomal DNA (rDNA) heterochromatin and prevent cellular senescence induced by rDNA instability (PubMed:29728458). Acts as a negative regulator of SIRT1 by preventing autodeacetylation of SIRT1, restricting SIRT1 deacetylase activity (By similarity)", "gene_name": "SIRT7", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NRC8", "name": "SIRT7", "organism": "Homo sapiens", "uniprot_id": "Q9NRC8" }, { "function": "Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis", "gene_name": "PFKP", "glycan_count": 1, "glycosylation_sites": [ { "position": 540, "type": "O-linked (GlcNAc) serine" } ], "id": "Q01813", "name": "Phosphofructokinase, platelet type (PFKP)", "organism": "Homo sapiens", "uniprot_id": "Q01813" }, { "function": "Isoform specifically expressed during embryogenesis that has low pyruvate kinase activity by itself and requires allosteric activation by D-fructose 1,6-bisphosphate (FBP) for pyruvate kinase activity (PubMed:18337823, PubMed:20847263). In addition to its pyruvate kinase activity in the cytoplasm, also acts as a regulator of transcription in the nucleus by acting as a protein kinase (PubMed:18191611, PubMed:21620138, PubMed:22056988, PubMed:22306293, PubMed:22901803, PubMed:24120661). Translocates into the nucleus in response to various signals, such as EGF receptor activation, and homodimerizes, leading to its conversion into a protein threonine- and tyrosine-protein kinase (PubMed:22056988, PubMed:22306293, PubMed:22901803, PubMed:24120661, PubMed:26787900). Catalyzes phosphorylation of STAT3 at 'Tyr-705' and histone H3 at 'Thr-11' (H3T11ph), leading to activate transcription (PubMed:22306293, PubMed:22901803, PubMed:24120661). Its ability to activate transcription plays a role in cancer cells by promoting cell proliferation and promote tumorigenesis (PubMed:18337823, PubMed:22901803, PubMed:26787900). Promotes the expression of the immune checkpoint protein CD274 in BMAL1-deficient macrophages (By similarity). May also act as a translation regulator for a subset of mRNAs, independently of its pyruvate kinase activity: associates with subpools of endoplasmic reticulum-associated ribosomes, binds directly to the mRNAs translated at the endoplasmic reticulum and promotes translation of these endoplasmic reticulum-destined mRNAs (By similarity). Plays a role in caspase independent cell death of tumor cells (PubMed:17308100)", "gene_name": "PKM", "glycan_count": 1, "glycosylation_sites": [], "id": "P14618-1", "name": "Pyruvate kinase M2 (PKM2)", "organism": "Homo sapiens", "uniprot_id": "P14618-1" }, { "function": "Destroys radicals which are normally produced within the cells and which are toxic to biological systems", "gene_name": "HEL-S-44", "glycan_count": 0, "glycosylation_sites": [], "id": "V9HWC9", "name": "Superoxide dismutase [Cu\u2013Zn] (HEL-S-44)", "organism": "Homo sapiens", "uniprot_id": "V9HWC9" }, { "function": "May be a growth regulator and have a role in specifying neural systems involved in processing somatosensory information, as well as in face and body structure formation", "gene_name": "SHOX2", "glycan_count": 0, "glycosylation_sites": [], "id": "O60902", "name": "Short stature homeobox protein 2 (SHOX2)", "organism": "Homo sapiens", "uniprot_id": "O60902" }, { "function": "Ubiquitin-like modifier that increases cell-surface expression of kappa-type opioid receptor through facilitating anterograde intracellular trafficking of the receptor (PubMed:16431922). Involved in formation of autophagosomal vacuoles (PubMed:20404487). While LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation (PubMed:20404487). Through its interaction with the reticulophagy receptor TEX264, participates in the remodeling of subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover (PubMed:31006537, PubMed:31006538)", "gene_name": "GABARAPL1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H0R8", "name": "GABARAPL1", "organism": "Homo sapiens", "uniprot_id": "Q9H0R8" }, { "function": "Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399, PubMed:25901680, PubMed:25957688, PubMed:28257692). The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules (PubMed:23636399, PubMed:25901680, PubMed:25957688). The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain (PubMed:23636399, PubMed:25901680, PubMed:25957688). The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:23636399, PubMed:25901680, PubMed:25957688). Plays an important role in translational accuracy (PubMed:28257692). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797)", "gene_name": "RPS23", "glycan_count": 2, "glycosylation_sites": [], "id": "P62266", "name": "RPS23", "organism": "Homo sapiens", "uniprot_id": "P62266" }, { "function": "Reduces disulfideprotein thioredoxin (Trx) to its dithiol-containing form (PubMed:8577704). Homodimeric flavoprotein involved in the regulation of cellular redox reactions, growth and differentiation. Contains a selenocysteine residue at the C-terminal active site that is essential for catalysis (Probable). Also has reductase activity on hydrogen peroxide (H2O2) (PubMed:10849437)", "gene_name": "TXNRD1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q16881", "name": "TXNRD1", "organism": "Homo sapiens", "uniprot_id": "Q16881" }, { "function": "Involved in membrane protein trafficking at the base of the ciliary organelle. Mediates recruitment onto plasma membrane of the BBSome complex which would constitute a coat complex required for sorting of specific membrane proteins to the primary cilia (PubMed:20603001). Together with BBS1, is necessary for correct trafficking of PKD1 to primary cilia (By similarity). Together with the BBSome complex and LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation (PubMed:22072986). May regulate cilia assembly and disassembly and subsequent ciliary signaling events such as the Wnt signaling cascade (PubMed:20207729). Isoform 2 may be required for proper retinal function and organization (By similarity)", "gene_name": "ARL6", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H0F7", "name": "OSGIN1", "organism": "Homo sapiens", "uniprot_id": "Q9H0F7" }, { "function": "Involved in T-cell adhesion processes and in spontaneous rosette formation with erythrocytes. Plays a role in a late step of leukocyte extravasation helping leukocytes to overcome the endothelial basement membrane. Acts at the same site as, but independently of, PECAM1. Involved in T-cell adhesion processes (By similarity)", "gene_name": "CD99", "glycan_count": 3, "glycosylation_sites": [], "id": "P14209", "name": "CD99", "organism": "Homo sapiens", "uniprot_id": "P14209" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P10155/P19474", "name": "Anti-SSA/Ro antibody (Ro60/Ro52)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P08637/P13591", "name": "CD16+CD56+ NK cell marker", "organism": "", "uniprot_id": "" }, { "function": "Plays a role in odontogenesis", "gene_name": "SSUH2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y2M2", "name": "P-selectin glycoprotein ligand-1 (PSGL-1)", "organism": "Homo sapiens", "uniprot_id": "Q9Y2M2" }, { "function": "May be involved in transcriptional regulation", "gene_name": "ZNF101", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8IZC7", "name": "TROP2", "organism": "Homo sapiens", "uniprot_id": "Q8IZC7" }, { "function": "", "gene_name": "TMOD4", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NZQ9-2", "name": "Claudin 18.2", "organism": "Homo sapiens", "uniprot_id": "Q9NZQ9-2" }, { "function": "Substrate recognition component of both SCF (SKP1-CUL1-F-box protein) and DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes. Substrate recognition component of the SCF(FBXW5) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of SASS6 during S phase, leading to prevent centriole reduplication. The SCF(FBXW5) complex also mediates ubiquitination and degradation of actin-regulator EPS8 during G2 phase, leading to the transient degradation of EPS8 and subsequent cell shape changes required to allow mitotic progression. Substrate-specific adapter of the DCX(FBXW5) E3 ubiquitin-protein ligase complex which mediates the polyubiquitination and subsequent degradation of TSC2. May also act as a negative regulator of MAP3K7/TAK1 signaling in the interleukin-1B (IL1B) signaling pathway", "gene_name": "FBXW5", "glycan_count": 2, "glycosylation_sites": [], "id": "Q969U6", "name": "Atrogin-1 (FBXO32)", "organism": "Homo sapiens", "uniprot_id": "Q969U6" }, { "function": "Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred substrates. The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A. Also able to hydrolyze 5-phosphoribose 1-diphosphate", "gene_name": "NUDT11", "glycan_count": 1, "glycosylation_sites": [], "id": "Q96G61", "name": "GMPPB (GDP-mannose pyrophosphorylase B)", "organism": "Homo sapiens", "uniprot_id": "Q96G61" }, { "function": "", "gene_name": "bdhA", "glycan_count": 0, "glycosylation_sites": [], "id": "Q04944", "name": "AMH (Anti-Mullerian Hormone)", "organism": "Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W)", "uniprot_id": "Q04944" }, { "function": "Growth factor of the TGF-beta superfamily that plays essential roles in many developmental processes including cartilage and bone formation (PubMed:31019025). Also plays an important role in the regulation of HAMP/hepcidin expression and iron metabolism by acting as a ligand for hemojuvelin/HJV (PubMed:26582087). Also acts to promote expression of HAMP, potentially via the interaction with its receptor BMPR1A/ALK3 (PubMed:30097509, PubMed:31800957). Initiates the canonical BMP signaling cascade by associating with type I receptor ACVR1 and type II receptor ACVR2B (PubMed:18070108). In turn, ACVR1 propagates signal by phosphorylating SMAD1/5/8 that travel to the nucleus and act as activators and repressors of transcription of target. Can also signal through non-canonical pathway such as TAZ-Hippo signaling cascade to modulate VEGF signaling by regulating VEGFR2 expression (PubMed:33021694)", "gene_name": "BMP6", "glycan_count": 3, "glycosylation_sites": [ { "position": 241, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 269, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 386, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 404, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 454, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P22004", "name": "BMP6", "organism": "Homo sapiens", "uniprot_id": "P22004" }, { "function": "Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease (By similarity)", "gene_name": "DKK2", "glycan_count": 1, "glycosylation_sites": [ { "position": 52, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UBU2", "name": "NY-ESO-1 (CTAG1B)", "organism": "Homo sapiens", "uniprot_id": "Q9UBU2" }, { "function": "Antigen-presenting major histocompatibility complex class I (MHCI) molecule. In complex with B2M/beta 2 microglobulin displays primarily viral and tumor-derived peptides on antigen-presenting cells for recognition by alpha-beta T cell receptor (TCR) on HLA-A-restricted CD8-positive T cells, guiding antigen-specific T cell immune response to eliminate infected or transformed cells (PubMed:10449296, PubMed:12138174, PubMed:12393434, PubMed:1402688, PubMed:15893615, PubMed:17189421, PubMed:19543285, PubMed:21498667, PubMed:24192765, PubMed:24395804, PubMed:2456340, PubMed:2784196, PubMed:28250417, PubMed:7504010, PubMed:7694806, PubMed:9862734). May also present self-peptides derived from the signal sequence of secreted or membrane proteins, although T cells specific for these peptides are usually inactivated to prevent autoreactivity (PubMed:25880248, PubMed:7506728, PubMed:7679507). Both the peptide and the MHC molecule are recognized by TCR, the peptide is responsible for the fine specificity of antigen recognition and MHC residues account for the MHC restriction of T cells (PubMed:12796775, PubMed:18275829, PubMed:19542454, PubMed:28250417). Typically presents intracellular peptide antigens of 8 to 13 amino acids that arise from cytosolic proteolysis via IFNG-induced immunoproteasome or via endopeptidase IDE/insulin-degrading enzyme (PubMed:17079320, PubMed:17189421, PubMed:20364150, PubMed:26929325, PubMed:27049119). Can bind different peptides containing allele-specific binding motifs, which are mainly defined by anchor residues at position 2 and 9 (PubMed:7504010, PubMed:9862734)", "gene_name": "HLA-A", "glycan_count": 0, "glycosylation_sites": [ { "position": 110, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01891", "name": "HLA-A*31:01", "organism": "Homo sapiens", "uniprot_id": "P04439" }, { "function": "Antigen-presenting major histocompatibility complex class I (MHCI) molecule. In complex with B2M/beta 2 microglobulin displays primarily viral and tumor-derived peptides on antigen-presenting cells for recognition by alpha-beta T cell receptor (TCR) on HLA-A-restricted CD8-positive T cells, guiding antigen-specific T cell immune response to eliminate infected or transformed cells (PubMed:10449296, PubMed:12138174, PubMed:12393434, PubMed:1402688, PubMed:15893615, PubMed:17189421, PubMed:19543285, PubMed:21498667, PubMed:24192765, PubMed:24395804, PubMed:2456340, PubMed:2784196, PubMed:28250417, PubMed:7504010, PubMed:7694806, PubMed:9862734). May also present self-peptides derived from the signal sequence of secreted or membrane proteins, although T cells specific for these peptides are usually inactivated to prevent autoreactivity (PubMed:25880248, PubMed:7506728, PubMed:7679507). Both the peptide and the MHC molecule are recognized by TCR, the peptide is responsible for the fine specificity of antigen recognition and MHC residues account for the MHC restriction of T cells (PubMed:12796775, PubMed:18275829, PubMed:19542454, PubMed:28250417). Typically presents intracellular peptide antigens of 8 to 13 amino acids that arise from cytosolic proteolysis via IFNG-induced immunoproteasome or via endopeptidase IDE/insulin-degrading enzyme (PubMed:17079320, PubMed:17189421, PubMed:20364150, PubMed:26929325, PubMed:27049119). Can bind different peptides containing allele-specific binding motifs, which are mainly defined by anchor residues at position 2 and 9 (PubMed:7504010, PubMed:9862734)", "gene_name": "HLA-A", "glycan_count": 0, "glycosylation_sites": [ { "position": 110, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P30450", "name": "HLA-A*24:02", "organism": "Homo sapiens", "uniprot_id": "P04439" }, { "function": "Antigen-presenting major histocompatibility complex class I (MHCI) molecule. In complex with B2M/beta 2 microglobulin displays primarily viral and tumor-derived peptides on antigen-presenting cells for recognition by alpha-beta T cell receptor (TCR) on HLA-B-restricted CD8-positive T cells, guiding antigen-specific T cell immune response to eliminate infected or transformed cells (PubMed:23209413, PubMed:25808313, PubMed:29531227, PubMed:9620674). May also present self-peptides derived from the signal sequence of secreted or membrane proteins, although T cells specific for these peptides are usually inactivated to prevent autoreactivity (PubMed:18991276, PubMed:7743181). Both the peptide and the MHC molecule are recognized by TCR, the peptide is responsible for the fine specificity of antigen recognition and MHC residues account for the MHC restriction of T cells (PubMed:24600035, PubMed:29531227, PubMed:9620674). Typically presents intracellular peptide antigens of 8 to 13 amino acids that arise from cytosolic proteolysis via constitutive proteasome and IFNG-induced immunoproteasome (PubMed:23209413). Can bind different peptides containing allele-specific binding motifs, which are mainly defined by anchor residues at position 2 and 9 (PubMed:25808313, PubMed:29531227)", "gene_name": "HLA-B", "glycan_count": 0, "glycosylation_sites": [ { "position": 110, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P30462", "name": "HLA-B*13:01", "organism": "Homo sapiens", "uniprot_id": "P01889" }, { "function": "Antigen-presenting major histocompatibility complex class I (MHCI) molecule. In complex with B2M/beta 2 microglobulin displays primarily viral and tumor-derived peptides on antigen-presenting cells for recognition by alpha-beta T cell receptor (TCR) on HLA-B-restricted CD8-positive T cells, guiding antigen-specific T cell immune response to eliminate infected or transformed cells (PubMed:23209413, PubMed:25808313, PubMed:29531227, PubMed:9620674). May also present self-peptides derived from the signal sequence of secreted or membrane proteins, although T cells specific for these peptides are usually inactivated to prevent autoreactivity (PubMed:18991276, PubMed:7743181). Both the peptide and the MHC molecule are recognized by TCR, the peptide is responsible for the fine specificity of antigen recognition and MHC residues account for the MHC restriction of T cells (PubMed:24600035, PubMed:29531227, PubMed:9620674). Typically presents intracellular peptide antigens of 8 to 13 amino acids that arise from cytosolic proteolysis via constitutive proteasome and IFNG-induced immunoproteasome (PubMed:23209413). Can bind different peptides containing allele-specific binding motifs, which are mainly defined by anchor residues at position 2 and 9 (PubMed:25808313, PubMed:29531227)", "gene_name": "HLA-B", "glycan_count": 0, "glycosylation_sites": [ { "position": 110, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P30487", "name": "HLA-B*51:01", "organism": "Homo sapiens", "uniprot_id": "P01889" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P12830 (human)", "name": "E-cadherin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P10721 (human)", "name": "c-KIT", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P21880 (human)", "name": "Mast cell tryptase", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9D3S2 (FCoV)", "name": "Feline coronavirus spike protein", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03374 (FeLV)", "name": "Feline leukaemia virus envelope glycoprotein", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03375 (FIV)", "name": "Feline immunodeficiency virus envelope glycoprotein", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P19429 (human)", "name": "Troponin I", "organism": "", "uniprot_id": "" }, { "function": "Monooxygenase catalytic activity (PubMed:38442170). Involved in regulation of cytokinesis; promotes RHOA activity, probably acting locally at the midbody in late cytokinesis (PubMed:38442170). Monooxygenase activity is involved in stabilizing transient structures between daughter cells, termed intercellular bridges, before abscission (PubMed:38442170). Regulates differentiation and proliferation through the regulation of cell death (PubMed:11459809, PubMed:14570898)", "gene_name": "OSGIN1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UJX0", "name": "Kidney injury molecule-1 (KIM-1)", "organism": "Homo sapiens", "uniprot_id": "Q9UJX0" }, { "function": "Receptor for endothelin-1. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of binding affinities for ET-A is: ET1 > ET2 >> ET3", "gene_name": "EDNRA", "glycan_count": 3, "glycosylation_sites": [ { "position": 29, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 62, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P25101", "name": "Endothelin-1 receptor type A (ETAR)", "organism": "Homo sapiens", "uniprot_id": "P25101" }, { "function": "Metalloprotease (PubMed:16585064, PubMed:39672391). Was previously shown to degrade COMP (PubMed:16585064). However, a later study found no activity against COMP (PubMed:39672391)", "gene_name": "ADAMTS7", "glycan_count": 4, "glycosylation_sites": [ { "position": 94, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 693, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 778, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UKP4", "name": "ADAMTS7", "organism": "Homo sapiens", "uniprot_id": "Q9UKP4" }, { "function": "Dopamine receptor whose activity is mediated by G proteins which activate adenylyl cyclase", "gene_name": "DRD5", "glycan_count": 0, "glycosylation_sites": [ { "position": 7, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 222, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P21918", "name": "DRD5", "organism": "Homo sapiens", "uniprot_id": "P21918" }, { "function": "", "gene_name": "PRR36", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H3X1", "name": "Glutathione Peroxidase 6 (GPX6)", "organism": "Homo sapiens", "uniprot_id": "Q9H6K5" }, { "function": "Involved in the degradation process of misfolded endoplasmic reticulum (ER) luminal proteins. Participates in the transfer of misfolded proteins from the ER to the cytosol, where they are destroyed by the proteasome in a ubiquitin-dependent manner. Probably acts by serving as a linker between DERL1, which mediates the retrotranslocation of misfolded proteins into the cytosol, and the ATPase complex VCP, which mediates the translocation and ubiquitination", "gene_name": "SELENOS", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9BQE4", "name": "Selenoprotein T (SelT)", "organism": "Homo sapiens", "uniprot_id": "Q9BQE4" }, { "function": "Involved in the control of reactive oxygen species levels and the regulation of mitochondrial redox homeostasis (PubMed:24601690). Maintains thioredoxin in a reduced state. May play a role in redox-regulated cell signaling", "gene_name": "TXNRD2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NNW7", "name": "Thioredoxin Reductase 2 (TrxR2)", "organism": "Homo sapiens", "uniprot_id": "Q9NNW7" }, { "function": "Hydrolase that can remove conjugated ubiquitin from target proteins such as p53/TP53, RPS2/us5, RPS3/us3, RPS10/eS10, BECN1, SNX3 and CFTR (PubMed:11439350, PubMed:18632802, PubMed:31981475). Acts as an essential regulator of p53/TP53 stability: in unstressed cells, specifically deubiquitinates p53/TP53 in the cytoplasm, leading to counteract MDM2 action and stabilize p53/TP53 (PubMed:20096447). Following DNA damage, translocates to the nucleus and deubiquitinates p53/TP53, leading to regulate the p53/TP53-dependent DNA damage response (PubMed:20096447). Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes (PubMed:21962518). In turn, PIK3C3/VPS34-containing complexes regulate USP10 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13 (PubMed:21962518). Does not deubiquitinate MDM2 (PubMed:20096447). Plays a key role in 40S ribosome subunit recycling when a ribosome has stalled during translation: acts both by inhibiting formation of stress granules, which store stalled translation pre-initiation complexes, and mediating deubiquitination of 40S ribosome subunits (PubMed:27022092, PubMed:31981475, PubMed:34348161, PubMed:34469731). Acts as a negative regulator of stress granules formation by lowering G3BP1 and G3BP2 valence, thereby preventing G3BP1 and G3BP2 ability to undergo liquid-liquid phase separation (LLPS) and assembly of stress granules (PubMed:11439350, PubMed:27022092, PubMed:32302570). Promotes 40S ribosome subunit recycling following ribosome dissociation in response to ribosome stalling by mediating deubiquitination of 40S ribosomal proteins RPS2/us5, RPS3/us3 and RPS10/eS10, thereby preventing their degradation by the proteasome (PubMed:31981475, PubMed:34348161, PubMed:34469731). Part of a ribosome quality control that takes place when ribosomes have stalled during translation initiation (iRQC): USP10 acts by removing monoubiquitination of RPS2/us5 and RPS3/us3, promoting 40S ribosomal subunit recycling (PubMed:34469731). Deubiquitinates CFTR in early endosomes, enhancing its endocytic recycling (PubMed:19398555). Involved in a TANK-dependent negative feedback response to attenuate NF-kappa-B activation via deubiquitinating IKBKG or TRAF6 in response to interleukin-1-beta (IL1B) stimulation or upon DNA damage (PubMed:25861989). Deubiquitinates TBX21 leading to its stabilization (PubMed:24845384). Plays a negative role in the RLR signaling pathway upon RNA virus infection by blocking the RIGI-mediated MAVS activation. Mechanistically, removes the unanchored 'Lys-63'-linked polyubiquitin chains of MAVS to inhibit its aggregation, essential for its activation (PubMed:37582970)", "gene_name": "USP10", "glycan_count": 1, "glycosylation_sites": [], "id": "Q14694", "name": "USP10", "organism": "Homo sapiens", "uniprot_id": "Q14694" }, { "function": "Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA (PubMed:10531356, PubMed:11152681, PubMed:11747828, PubMed:12411503, PubMed:15737618, PubMed:17709427, PubMed:20159986, PubMed:20810653, PubMed:21081503, PubMed:21258366, PubMed:21917714, PubMed:22269951). Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles (PubMed:11747828, PubMed:12411503, PubMed:17709427). Methylates SUPT5H and may regulate its transcriptional elongation properties (PubMed:12718890). May methylate the N-terminal region of MBD2 (PubMed:16428440). Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. Methylates histone H2A and H4 'Arg-3' during germ cell development (By similarity). Methylates histone H3 'Arg-8', which may repress transcription (By similarity). Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage (By similarity). Methylates RPS10. Attenuates EGF signaling through the MAPK1/MAPK3 pathway acting at 2 levels. First, monomethylates EGFR; this enhances EGFR 'Tyr-1197' phosphorylation and PTPN6 recruitment, eventually leading to reduced SOS1 phosphorylation (PubMed:21258366, PubMed:21917714). Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 signaling proteins and reducing their catalytic activity (PubMed:21917714). Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation. Methylates HOXA9 (PubMed:22269951). Methylates and regulates SRGAP2 which is involved in cell migration and differentiation (PubMed:20810653). Acts as a transcriptional corepressor in CRY1-mediated repression of the core circadian component PER1 by regulating the H4R3 dimethylation at the PER1 promoter (By similarity). Methylates GM130/GOLGA2, regulating Golgi ribbon formation (PubMed:20421892). Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner (PubMed:25284789). Symmetrically methylates POLR2A, a modification that allows the recruitment to POLR2A of proteins including SMN1/SMN2 and SETX. This is required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination (PubMed:26700805). Along with LYAR, binds the promoter of gamma-globin HBG1/HBG2 and represses its expression (PubMed:25092918). Symmetrically methylates NCL (PubMed:21081503). Methylates p53/TP53; methylation might possibly affect p53/TP53 target gene specificity (PubMed:19011621). Involved in spliceosome maturation and mRNA splicing in prophase I spermatocytes through the catalysis of the symmetrical arginine dimethylation of SNRPB (small nuclear ribonucleoprotein-associated protein) and the interaction with tudor domain-containing protein TDRD6 (By similarity)", "gene_name": "PRMT5", "glycan_count": 1, "glycosylation_sites": [], "id": "O14744", "name": "PRMT5", "organism": "Homo sapiens", "uniprot_id": "O14744" }, { "function": "Non-catalytic component of the methylosome complex, composed of PRMT5, WDR77 and CLNS1A, which modifies specific arginines to dimethylarginines in several spliceosomal Sm proteins and histones (PubMed:11756452). This modification targets Sm proteins to the survival of motor neurons (SMN) complex for assembly into small nuclear ribonucleoprotein core particles. Might play a role in transcription regulation. The methylosome complex also methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage (PubMed:23071334)", "gene_name": "WDR77", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9BQA1", "name": "MEP50", "organism": "Homo sapiens", "uniprot_id": "Q9BQA1" }, { "function": "The small GTPases Rab are key regulators in vesicle trafficking (PubMed:24788816). Essential for maintaining the integrity of the endosome-trans-Golgi network structure (By similarity). Together with LRRK2, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose 6 phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner (PubMed:24788816). Recruits LRRK2 to the Golgi complex and stimulates LRRK2 kinase activity (PubMed:29212815, PubMed:38127736). Stimulates phosphorylation of RAB10 'Thr-73' by LRRK2 (PubMed:38127736). Regulates neuronal process morphology in the intact central nervous system (CNS) (By similarity). May play a role in the formation of typhoid toxin transport intermediates during Salmonella enterica serovar Typhi (S.typhi) epithelial cell infection (PubMed:22042847)", "gene_name": "RAB29", "glycan_count": 0, "glycosylation_sites": [], "id": "O14966", "name": "ATP2A3", "organism": "Homo sapiens", "uniprot_id": "O14966" }, { "function": "Capsid protein. Probably binds RNA and plays a role in packaging (By similarity)", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P24402", "name": "Polymerase acidic protein (PA)", "organism": "Broad bean mottle virus", "uniprot_id": "P24402" }, { "function": "Inhibits post-transcriptional processing of cellular pre-mRNA, by binding and inhibiting two cellular proteins that are required for the 3'-end processing of cellular pre-mRNAs: the 30 kDa cleavage and polyadenylation specificity factor/CPSF4 and the poly(A)-binding protein 2/PABPN1. In turn, unprocessed 3' end pre-mRNAs accumulate in the host nucleus and are no longer exported to the cytoplasm. Cellular protein synthesis is thereby shut off very early after virus infection. Viral protein synthesis is not affected by the inhibition of the cellular 3' end processing machinery because the poly(A) tails of viral mRNAs are produced by the viral polymerase through a stuttering mechanism. Prevents the establishment of the cellular antiviral state by inhibiting TRIM25-mediated RIGI ubiquitination, which normally triggers the antiviral transduction signal that leads to the activation of type I IFN genes by transcription factors IRF3 and IRF7. Also binds poly(A) and U6 snRNA. Inhibits the integrated stress response (ISR) in the infected cell by blocking dsRNA binding by EIF2AK2/PKR and further phosphorylation of EIF2S1/EIF-2ALPHA. Stress granule formation is thus inhibited, which allows protein synthesis and viral replication", "gene_name": "NS", "glycan_count": 0, "glycosylation_sites": [], "id": "P03495", "name": "Non-structural protein (NS)", "organism": "Influenza A virus (strain A/Udorn/307/1972 H3N2)", "uniprot_id": "P03495" }, { "function": "Plays a role in the export of proteins that lack a signal peptide and are secreted by an alternative pathway. Binds two calcium ions per subunit. Binds one copper ion. Binding of one copper ion does not interfere with calcium binding. Required for the copper-dependent stress-induced export of IL1A and FGF1. The calcium-free protein binds to lipid vesicles containing phosphatidylserine, but not to vesicles containing phosphatidylcholine (By similarity)", "gene_name": "S100A13", "glycan_count": 1, "glycosylation_sites": [], "id": "Q99584", "name": "S100A12", "organism": "Homo sapiens", "uniprot_id": "Q99584" }, { "function": "Cytokine with antiviral, antitumour and immunomodulatory activities. Plays a critical role in the antiviral host defense, predominantly in the epithelial tissues. Acts as a ligand for the heterodimeric class II cytokine receptor composed of IL10RB and IFNLR1, and receptor engagement leads to the activation of the JAK/STAT signaling pathway resulting in the expression of IFN-stimulated genes (ISG), which mediate the antiviral state. Has a restricted receptor distribution and therefore restricted targets: is primarily active in epithelial cells and this cell type-selective action is because of the epithelial cell-specific expression of its receptor IFNLR1. Seems not to be essential for early virus-activated host defense in vaginal infection, but plays an important role in Toll-like receptor (TLR)-induced antiviral defense. Plays a significant role in the antiviral immune defense in the intestinal epithelium. Exerts an immunomodulatory effect by up-regulating MHC class I antigen expression", "gene_name": "IFNL2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8IZJ0", "name": "IFNLR1", "organism": "Homo sapiens", "uniprot_id": "Q8IZJ0" }, { "function": "Postsynaptic density scaffolding protein. Binds and cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-associated ITPR1 receptors, it aids the coupling of surface receptors to intracellular calcium release. Isoforms can be differently regulated and may play an important role in maintaining the plasticity at glutamatergic synapses. Negatively regulates T cell activation by inhibiting the calcineurin-NFAT pathway. Acts by competing with calcineurin/PPP3CA for NFAT protein binding, hence preventing NFAT activation by PPP3CA (PubMed:18218901)", "gene_name": "HOMER3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NSC5", "name": "Homer-3", "organism": "Homo sapiens", "uniprot_id": "Q9NSC5" }, { "function": "G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling activates a phosphatidylinositol-calcium second messenger system. May participate in the central action of glutamate in the CNS, such as long-term potentiation in the hippocampus and long-term depression in the cerebellum (PubMed:24603153, PubMed:28886343, PubMed:7476890). May function in the light response in the retina (By similarity). Induces GRID1 and GRID2 cation-channel activation via GNAQ-PLC-PKC pathway in dopaminergic neurons and cerebellar Purkinje cell, respectively (PubMed:24357660, PubMed:27276689)", "gene_name": "GRM1", "glycan_count": 0, "glycosylation_sites": [ { "position": 98, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 223, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 397, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 515, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13255", "name": "mGluR1 (Metabotropic Glutamate Receptor 1)", "organism": "Homo sapiens", "uniprot_id": "Q13255" }, { "function": "Inositol 1,4,5-trisphosphate-gated calcium channel that, upon inositol 1,4,5-trisphosphate binding, mediates calcium release from the endoplasmic reticulum (ER) (PubMed:10620513, PubMed:27108797). Undergoes conformational changes upon ligand binding, suggesting structural flexibility that allows the channel to switch from a closed state, capable of interacting with its ligands such as 1,4,5-trisphosphate and calcium, to an open state, capable of transferring calcium ions across the ER membrane (By similarity). Cytoplasmic calcium released from the ER triggers apoptosis by the activation of CAMK2 complex (By similarity). Involved in the regulation of epithelial secretion of electrolytes and fluid through the interaction with AHCYL1 (By similarity). Part of a complex composed of HSPA9, ITPR1 and VDAC1 that regulates mitochondrial calcium-dependent apoptosis by facilitating calcium transport from the ER lumen to the mitochondria intermembrane space thus providing calcium for the downstream calcium channel MCU that directly releases it into mitochondria matrix (By similarity). Regulates fertilization and egg activation by tuning the frequency and amplitude of calcium oscillations (By similarity)", "gene_name": "ITPR1", "glycan_count": 13, "glycosylation_sites": [ { "position": 2512, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q14643", "name": "Ins(1,4,5)P3 receptor (ITPR1)", "organism": "Homo sapiens", "uniprot_id": "Q14643" }, { "function": "GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Has a substantial GAP activity toward CDC42 and RAC1 and less toward RHOA. Has a role in regulating adhesion of hematopoietic cells to the extracellular matrix. Binds phosphoinositides, and has the highest affinity for phosphatidylinositol 3,4,5-trisphosphate, followed by phosphatidylinositol 3,4-bisphosphate and phosphatidylinositol 4,5-bisphosphate", "gene_name": "ARHGAP9", "glycan_count": 14, "glycosylation_sites": [], "id": "Q9BRR9", "name": "ARHGAP26 (anti-Ca)", "organism": "Homo sapiens", "uniprot_id": "Q9BRR9" }, { "function": "Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). May play a role in platelet secretion (By similarity)", "gene_name": "SEPTIN5", "glycan_count": 0, "glycosylation_sites": [], "id": "Q99719", "name": "Septin-5", "organism": "Homo sapiens", "uniprot_id": "Q99719" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P35439 (GluN1 subunit)", "name": "N-methyl-D-aspartate receptor (NMDAR)", "organism": "", "uniprot_id": "" }, { "function": "Intracellular G-protein coupled receptor for trace amines, which recognizes endogenous amine-containing metabolites such as beta-phenylethylamine (beta-PEA), 3-iodothyronamine (T1AM), isoamylamine (IAA), cadaverine (CAD), cyclohexylamine (CHA), p-tyramine (p-TYR), trimethylamine (TMA), octopamine and tryptamine (PubMed:11459929, PubMed:11723224, PubMed:15718104, PubMed:31399635, PubMed:36100653, PubMed:37935376, PubMed:37935377, PubMed:37963465, PubMed:38168118). Also functions as a receptor for various drugs and psychoactive substances, such as amphetamine and methamphetamine (PubMed:31399635, PubMed:37935376, PubMed:37935377). Unresponsive to classical biogenic amines, such as epinephrine and histamine and only partially activated by dopamine and serotonin (PubMed:11459929, PubMed:11723224). Expressed in both the central and peripheral nervous system: TAAR1 activation regulates the activity of several neurotransmitter signaling pathways by (1) decreasing the basal firing rates of the neurons involved and by (2) lowering the sensitivity of receptors to neurotransmitters (PubMed:37935376, PubMed:37935377, PubMed:37963465, PubMed:38168118). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors (PubMed:31399635, PubMed:37935376, PubMed:37963465). TAAR1 is coupled with different G(i)/G(o)-, G(s)- or G(q)/G(11) classes of G alpha proteins depending on the ligand (PubMed:31399635, PubMed:37935376, PubMed:37963465). CAD-binding is coupled to G(i)/G(o) G alpha proteins and mediates inhibition of adenylate cyclase activity (PubMed:37935376, PubMed:37963465). T1AM- or beta-PEA-binding is coupled to G(s) G alpha proteins and mediates activation of adenylate cyclase activity (PubMed:37935376, PubMed:37963465). CHA- or IAA-binding is coupled to G(q)/G(11) G alpha proteins and activates phospholipase C-beta, releasing diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) second messengers (PubMed:37935376, PubMed:37963465). TMA-binding is coupled with all three G(i)/G(o)-, G(s)- or G(q)/G(11) G alpha protein subtypes (PubMed:37935376, PubMed:37963465). Amphetamine-binding is coupled with G(s)- or G(12)/G(13) G alpha protein subtypes (PubMed:31399635)", "gene_name": "TAAR1", "glycan_count": 0, "glycosylation_sites": [ { "position": 10, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 17, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q96RJ0", "name": "Leucine-rich glioma-inactivated 1 (LGI1)", "organism": "Homo sapiens", "uniprot_id": "Q96RJ0" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UBS5 (GABBR1)", "name": "Gamma-aminobutyric acid B receptor (GABAB)", "organism": "", "uniprot_id": "" }, { "function": "Probable kinase that may be involved in a calcium-signaling pathway controlling neuronal migration in the developing brain. May also participate in functions of the mature nervous system", "gene_name": "DCLK1", "glycan_count": 1, "glycosylation_sites": [], "id": "O15075", "name": "DCLK1", "organism": "Homo sapiens", "uniprot_id": "O15075" }, { "function": "Mediates depolymerization of hyaluronic acid (HA) via the cell membrane-associated clathrin-coated pit endocytic pathway. Binds to hyaluronic acid. Hydrolyzes high molecular weight hyaluronic acid to produce an intermediate-sized product, a process that may occur through rapid vesicle endocytosis and recycling without intracytoplasmic accumulation or digestion in lysosomes. Involved in hyaluronan catabolism in the dermis of the skin and arthritic synovium. Positively regulates epithelial-mesenchymal transition (EMT), and hence tumor cell growth, invasion and cancer dissemination. In collaboration with HSPA5/BIP, promotes cancer cell migration in a calcium and PKC-dependent manner. May be involved in hearing", "gene_name": "CEMIP", "glycan_count": 4, "glycosylation_sites": [ { "position": 119, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 165, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 312, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 370, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 420, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 889, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 921, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8WUJ3", "name": "CEMIP", "organism": "Homo sapiens", "uniprot_id": "Q8WUJ3" }, { "function": "Activator of ubiquitin ligase activity of RING-type zinc finger-containing E3 ubiquitin-protein ligases that acts as a repressor of autophagy (PubMed:20864041, PubMed:31267705). May enhance ubiquitin ligase activity of TRIM28 and stimulate p53/TP53 ubiquitination by TRIM28. Proposed to act through recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at the E3:substrate complex (PubMed:17942928, PubMed:20864041). May play a role in embryonal development and tumor transformation or aspects of tumor progression (PubMed:17942928, PubMed:20864041). In vitro promotes cell viability in melanoma cell lines (PubMed:17942928). Antigen recognized on a melanoma by autologous cytolytic T-lymphocytes (PubMed:8113684)", "gene_name": "MAGEA3", "glycan_count": 0, "glycosylation_sites": [], "id": "P43357", "name": "MAGE-A3", "organism": "Homo sapiens", "uniprot_id": "P43357" }, { "function": "Plays a major role in tight junction-specific obliteration of the intercellular space", "gene_name": "CLDN6", "glycan_count": 1, "glycosylation_sites": [], "id": "P56747", "name": "Claudin 6 (CLDN6)", "organism": "Homo sapiens", "uniprot_id": "P56747" }, { "function": "Probable serine protease which may play a role in cellular senescence. Overexpression inhibits cell growth and induce G1 cell cycle arrest", "gene_name": "TMPRSS11A", "glycan_count": 0, "glycosylation_sites": [ { "position": 153, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 303, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6ZMR5", "name": "MFSD2A", "organism": "Homo sapiens", "uniprot_id": "Q6ZMR5" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P25445 (human ortholog)", "name": "FAS (Fas cell surface death receptor)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P42574 (human ortholog)", "name": "Caspase 3", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01375 (human ortholog)", "name": "TNF-\u03b1 (Tumor necrosis factor alpha)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O60603 (human ortholog)", "name": "TLR2 (Toll-like receptor 2)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P42224 (human ortholog)", "name": "STAT1a", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q00978 (human ortholog)", "name": "IRF9 (Interferon regulatory factor 9)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y239 (human ortholog)", "name": "NOD1", "organism": "", "uniprot_id": "" }, { "function": "Tyrosine-protein kinase that acts as a cell-surface receptor for PDGFA, PDGFB and PDGFC and plays an essential role in the regulation of embryonic development, cell proliferation, survival and chemotaxis. Depending on the context, promotes or inhibits cell proliferation and cell migration. Plays an important role in the differentiation of bone marrow-derived mesenchymal stem cells. Required for normal skeleton development and cephalic closure during embryonic development. Required for normal development of the mucosa lining the gastrointestinal tract, and for recruitment of mesenchymal cells and normal development of intestinal villi. Plays a role in cell migration and chemotaxis in wound healing. Plays a role in platelet activation, secretion of agonists from platelet granules, and in thrombin-induced platelet aggregation. Binding of its cognate ligands - homodimeric PDGFA, homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or homodimeric PDGFC -leads to the activation of several signaling cascades; the response depends on the nature of the bound ligand and is modulated by the formation of heterodimers between PDGFRA and PDGFRB. Phosphorylates PIK3R1, PLCG1, and PTPN11. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate, mobilization of cytosolic Ca(2+) and the activation of protein kinase C. Phosphorylates PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and thereby mediates activation of the AKT1 signaling pathway. Mediates activation of HRAS and of the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3 and STAT5A and/or STAT5B. Receptor signaling is down-regulated by protein phosphatases that dephosphorylate the receptor and its down-stream effectors, and by rapid internalization of the activated receptor", "gene_name": "Pdgfra", "glycan_count": 4, "glycosylation_sites": [ { "position": 42, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 76, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 89, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 103, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 179, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 353, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 359, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 458, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 468, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 506, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P26618", "name": "Platelet-derived growth factor receptor alpha (PDGFR\u03b1)", "organism": "Mus musculus", "uniprot_id": "P26618" }, { "function": "Structural component of lipid droplets, which is required for the formation and maintenance of lipid storage droplets (PubMed:34077757). Required for the transport of mannose 6-phosphate receptors (MPR) from endosomes to the trans-Golgi network (PubMed:9590177)", "gene_name": "PLIN3", "glycan_count": 1, "glycosylation_sites": [], "id": "O60664", "name": "Perilipin 3 (PLIN3)", "organism": "Homo sapiens", "uniprot_id": "O60664" }, { "function": "Catalytic subunit beta, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (Probable) (PubMed:37244256). ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel (PubMed:37244256). These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk (PubMed:37244256). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (Probable). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). With the subunit alpha (ATP5F1A), forms the catalytic core in the F(1) domain (PubMed:37244256)", "gene_name": "ATP5F1B", "glycan_count": 1, "glycosylation_sites": [ { "position": 106, "type": "O-linked (GlcNAc) serine" } ], "id": "P06576", "name": "F1F0-ATP synthase", "organism": "Homo sapiens", "uniprot_id": "P06576" }, { "function": "Aquaporins form homotetrameric transmembrane channels, with each monomer independently mediating water transport across the plasma membrane along its osmotic gradient (PubMed:8812490). Unlike classical aquaporins, AQP6 is an intracellular channel with selective anion permeability, particularly for nitrate, and exhibits very low water permeability (By similarity). It may also facilitate the transport of gases, such as CO2 and NH4(+), as demonstrated in vitro (By similarity)", "gene_name": "AQP6", "glycan_count": 0, "glycosylation_sites": [], "id": "Q13520", "name": "Urea transporter", "organism": "Homo sapiens", "uniprot_id": "Q13520" }, { "function": "Functions as a sodium-dependent neutral amino acid transporter. Exhibits preference for the branched-chain amino acids, particularly leucine, valine and isoleucine and methionine. Can also transport low-affinity substrates such as alanine, phenylalanine, glutamine and pipecolic acid. Mediates the saturable, pH-sensitive and electrogenic cotransport of proline and sodium ions with a stoichiometry of 1:1. May have a role as transporter for neurotransmitter precursors into neurons. In contrast to other members of the neurotransmitter transporter family, does not appear to be chloride-dependent", "gene_name": "SLC6A15", "glycan_count": 3, "glycosylation_sites": [ { "position": 187, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 213, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 383, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 394, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9H2J7", "name": "Creatinine transporter", "organism": "Homo sapiens", "uniprot_id": "Q9H2J7" }, { "function": "V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:17576170, PubMed:20176268)", "gene_name": "IGLV2-23", "glycan_count": 1, "glycosylation_sites": [], "id": "P01705", "name": "Interleukin-4 (IL-4)", "organism": "Homo sapiens", "uniprot_id": "P01705" }, { "function": "Plays a major role in the induction and maintenance of cellular transformation. Acts mainly as an oncoprotein by stimulating the destruction of many host cell key regulatory proteins. E6 associates with host UBE3A/E6-AP ubiquitin-protein ligase, and inactivates tumor suppressors TP53 and TP73 by targeting them to the 26S proteasome for degradation. In turn, DNA damage and chromosomal instabilities increase and lead to cell proliferation and cancer development. The complex E6/E6AP targets several other substrates to degradation via the proteasome including host DLG1 or NFX1, a repressor of human telomerase reverse transcriptase (hTERT). The resulting increased expression of hTERT prevents the shortening of telomere length leading to cell immortalization. Other cellular targets including BAK1, Fas-associated death domain-containing protein (FADD) and procaspase 8, are degraded by E6/E6AP causing inhibition of apoptosis. E6 also inhibits immune response by interacting with host IRF3 and TYK2. These interactions prevent IRF3 transcriptional activities and inhibit TYK2-mediated JAK-STAT activation by interferon alpha resulting in inhibition of the interferon signaling pathway", "gene_name": "E6", "glycan_count": 0, "glycosylation_sites": [], "id": "P03126", "name": "HPV E6", "organism": "Human papillomavirus type 16", "uniprot_id": "P03126" }, { "function": "Serine/threonine-protein kinase involved in the control of the cell cycle; essential for meiosis, but dispensable for mitosis (PubMed:10499802, PubMed:10884347, PubMed:10995386, PubMed:10995387, PubMed:11051553, PubMed:11113184, PubMed:12944431, PubMed:15800615, PubMed:17495531, PubMed:19966300, PubMed:20935635, PubMed:21262353, PubMed:21596315, PubMed:28216226, PubMed:28666995). Phosphorylates CABLES1, CTNNB1, CDK2AP2, ERCC6, NBN, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, NPAT, EZH2 (PubMed:10499802, PubMed:10995386, PubMed:10995387, PubMed:11051553, PubMed:11113184, PubMed:12944431, PubMed:15800615, PubMed:19966300, PubMed:20935635, PubMed:21262353, PubMed:21596315, PubMed:28216226). Triggers duplication of centrosomes and DNA (PubMed:11051553). Acts at the G1-S transition to promote the E2F transcriptional program and the initiation of DNA synthesis, and modulates G2 progression; controls the timing of entry into mitosis/meiosis by controlling the subsequent activation of cyclin B/CDK1 by phosphorylation, and coordinates the activation of cyclin B/CDK1 at the centrosome and in the nucleus (PubMed:18372919, PubMed:19238148, PubMed:19561645). Crucial role in orchestrating a fine balance between cellular proliferation, cell death, and DNA repair in embryonic stem cells (ESCs) (PubMed:18372919, PubMed:19238148, PubMed:19561645). Activity of CDK2 is maximal during S phase and G2; activated by interaction with cyclin E during the early stages of DNA synthesis to permit G1-S transition, and subsequently activated by cyclin A2 (cyclin A1 in germ cells) during the late stages of DNA replication to drive the transition from S phase to mitosis, the G2 phase (PubMed:18372919, PubMed:19238148, PubMed:19561645). EZH2 phosphorylation promotes H3K27me3 maintenance and epigenetic gene silencing (PubMed:20935635). Cyclin E/CDK2 prevents oxidative stress-mediated Ras-induced senescence by phosphorylating MYC (PubMed:19966300). Involved in G1-S phase DNA damage checkpoint that prevents cells with damaged DNA from initiating mitosis; regulates homologous recombination-dependent repair by phosphorylating BRCA2, this phosphorylation is low in S phase when recombination is active, but increases as cells progress towards mitosis (PubMed:15800615, PubMed:20195506, PubMed:21319273). In response to DNA damage, double-strand break repair by homologous recombination a reduction of CDK2-mediated BRCA2 phosphorylation (PubMed:15800615). Involved in regulation of telomere repair by mediating phosphorylation of NBN (PubMed:28216226). Phosphorylation of RB1 disturbs its interaction with E2F1 (PubMed:10499802). NPM1 phosphorylation by cyclin E/CDK2 promotes its dissociates from unduplicated centrosomes, thus initiating centrosome duplication (PubMed:11051553). Cyclin E/CDK2-mediated phosphorylation of NPAT at G1-S transition and until prophase stimulates the NPAT-mediated activation of histone gene transcription during S phase (PubMed:10995386, PubMed:10995387). Required for vitamin D-mediated growth inhibition by being itself inactivated (PubMed:20147522). Involved in the nitric oxide- (NO) mediated signaling in a nitrosylation/activation-dependent manner (PubMed:20079829). USP37 is activated by phosphorylation and thus triggers G1-S transition (PubMed:21596315). CTNNB1 phosphorylation regulates insulin internalization (PubMed:21262353). Phosphorylates FOXP3 and negatively regulates its transcriptional activity and protein stability (By similarity). Phosphorylates ERCC6 which is essential for its chromatin remodeling activity at DNA double-strand breaks (PubMed:29203878). Acts as a regulator of the phosphatidylinositol 3-kinase/protein kinase B signal transduction by mediating phosphorylation of the C-terminus of protein kinase B (PKB/AKT1 and PKB/AKT2), promoting its activation (PubMed:24670654)", "gene_name": "CDK2", "glycan_count": 1, "glycosylation_sites": [], "id": "P24941", "name": "CDK2", "organism": "Homo sapiens", "uniprot_id": "P24941" }, { "function": "Antigen-presenting major histocompatibility complex class I (MHCI) molecule. In complex with B2M/beta 2 microglobulin displays primarily viral and tumor-derived peptides on antigen-presenting cells for recognition by alpha-beta T cell receptor (TCR) on HLA-B-restricted CD8-positive T cells, guiding antigen-specific T cell immune response to eliminate infected or transformed cells (PubMed:23209413, PubMed:25808313, PubMed:29531227, PubMed:9620674). May also present self-peptides derived from the signal sequence of secreted or membrane proteins, although T cells specific for these peptides are usually inactivated to prevent autoreactivity (PubMed:18991276, PubMed:7743181). Both the peptide and the MHC molecule are recognized by TCR, the peptide is responsible for the fine specificity of antigen recognition and MHC residues account for the MHC restriction of T cells (PubMed:24600035, PubMed:29531227, PubMed:9620674). Typically presents intracellular peptide antigens of 8 to 13 amino acids that arise from cytosolic proteolysis via constitutive proteasome and IFNG-induced immunoproteasome (PubMed:23209413). Can bind different peptides containing allele-specific binding motifs, which are mainly defined by anchor residues at position 2 and 9 (PubMed:25808313, PubMed:29531227)", "gene_name": "HLA-B", "glycan_count": 21, "glycosylation_sites": [ { "position": 110, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P01889", "name": "HLA-B*15:02", "organism": "Homo sapiens", "uniprot_id": "P01889" }, { "function": "Receptor for endogenous opioids such as beta-endorphin and endomorphin (PubMed:10529478, PubMed:12589820, PubMed:7891175, PubMed:7905839, PubMed:7957926, PubMed:9689128). Receptor for natural and synthetic opioids including morphine, heroin, DAMGO, fentanyl, etorphine, buprenorphin and methadone (PubMed:10529478, PubMed:10836142, PubMed:12589820, PubMed:19300905, PubMed:7891175, PubMed:7905839, PubMed:7957926, PubMed:9689128). Also activated by enkephalin peptides, such as Met-enkephalin or Met-enkephalin-Arg-Phe, with higher affinity for Met-enkephalin-Arg-Phe (By similarity). Agonist binding to the receptor induces coupling to an inactive GDP-bound heterotrimeric G-protein complex and subsequent exchange of GDP for GTP in the G-protein alpha subunit leading to dissociation of the G-protein complex with the free GTP-bound G-protein alpha and the G-protein beta-gamma dimer activating downstream cellular effectors (PubMed:7905839). The agonist- and cell type-specific activity is predominantly coupled to pertussis toxin-sensitive G(i) and G(o) G alpha proteins, GNAI1, GNAI2, GNAI3 and GNAO1 isoforms Alpha-1 and Alpha-2, and to a lesser extent to pertussis toxin-insensitive G alpha proteins GNAZ and GNA15 (PubMed:12068084). They mediate an array of downstream cellular responses, including inhibition of adenylate cyclase activity and both N-type and L-type calcium channels, activation of inward rectifying potassium channels, mitogen-activated protein kinase (MAPK), phospholipase C (PLC), phosphoinositide/protein kinase (PKC), phosphoinositide 3-kinase (PI3K) and regulation of NF-kappa-B (By similarity). Also couples to adenylate cyclase stimulatory G alpha proteins (By similarity). The selective temporal coupling to G-proteins and subsequent signaling can be regulated by RGSZ proteins, such as RGS9, RGS17 and RGS4 (By similarity). Phosphorylation by members of the GPRK subfamily of Ser/Thr protein kinases and association with beta-arrestins is involved in short-term receptor desensitization (By similarity). Beta-arrestins associate with the GPRK-phosphorylated receptor and uncouple it from the G-protein thus terminating signal transduction (By similarity). The phosphorylated receptor is internalized through endocytosis via clathrin-coated pits which involves beta-arrestins (By similarity). The activation of the ERK pathway occurs either in a G-protein-dependent or a beta-arrestin-dependent manner and is regulated by agonist-specific receptor phosphorylation (By similarity). Acts as a class A G-protein coupled receptor (GPCR) which dissociates from beta-arrestin at or near the plasma membrane and undergoes rapid recycling (By similarity). Receptor down-regulation pathways are varying with the agonist and occur dependent or independent of G-protein coupling (By similarity). Endogenous ligands induce rapid desensitization, endocytosis and recycling (By similarity). Heterooligomerization with other GPCRs can modulate agonist binding, signaling and trafficking properties (By similarity)", "gene_name": "OPRM1", "glycan_count": 0, "glycosylation_sites": [ { "position": 9, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 12, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 33, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 40, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 48, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P35372", "name": "OPRM1 (\u03bc-opioid receptor)", "organism": "Homo sapiens", "uniprot_id": "P35372" }, { "function": "Key player in the regulation of energy balance and body weight control. Once released into the circulation, has central and peripheral effects by binding LEPR, found in many tissues, which results in the activation of several major signaling pathways (By similarity). In the hypothalamus, acts as an appetite-regulating factor that induces a decrease in food intake and an increase in energy consumption by inducing anorexinogenic factors and suppressing orexigenic neuropeptides, also regulates bone mass and secretion of hypothalamo-pituitary-adrenal hormones. In the periphery, increases basal metabolism, influences reproductive function, regulates pancreatic beta-cell function and insulin secretion, is pro-angiogenic for endothelial cell and affects innate and adaptive immunity (By similarity). In the arcuate nucleus of the hypothalamus, activates by depolarization POMC neurons inducing FOS and SOCS3 expression to release anorexigenic peptides and inhibits by hyperpolarization NPY neurons inducing SOCS3 with a consequent reduction on release of orexigenic peptides (By similarity). In addition to its known satiety inducing effect, has a modulatory role in nutrient absorption. In the intestine, reduces glucose absorption by enterocytes by activating PKC and leading to a sequential activation of p38, PI3K and ERK signaling pathways which exerts an inhibitory effect on glucose absorption (By similarity). Acts as a growth factor on certain tissues, through the activation of different signaling pathways increases expression of genes involved in cell cycle regulation such as CCND1, via JAK2-STAT3 pathway, or VEGFA, via MAPK1/3 and PI3K-AKT1 pathways (By similarity). May also play an apoptotic role via JAK2-STAT3 pathway and up-regulation of BIRC5 expression. Pro-angiogenic, has mitogenic activity on vascular endothelial cells and plays a role in matrix remodeling by regulating the expression of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs). In innate immunity, modulates the activity and function of neutrophils by increasing chemotaxis and the secretion of oxygen radicals. Increases phagocytosis by macrophages and enhances secretion of pro-inflammatory mediators. Increases cytotoxic ability of NK cells. Plays a pro-inflammatory role, in synergy with IL1B, by inducing NOS2 which promotes the production of IL6, IL8 and Prostaglandin E2, through a signaling pathway that involves JAK2, PI3K, MAP2K1/MEK1 and MAPK14/p38 (By similarity). In adaptive immunity, promotes the switch of memory T-cells towards T helper-1 cell immune responses (By similarity). Increases CD4(+)CD25(-) T-cell proliferation and reduces autophagy during TCR (T-cell receptor) stimulation, through MTOR signaling pathway activation and BCL2 up-regulation (By similarity)", "gene_name": "LEP", "glycan_count": 0, "glycosylation_sites": [], "id": "P50595", "name": "Leptin", "organism": "Bos taurus", "uniprot_id": "P50595" }, { "function": "Structural component of specialized membrane microdomains known as tetraspanin-enriched microdomains (TERMs), which act as platforms for receptor clustering and signaling. Essential for trafficking and compartmentalization of CD19 receptor on the surface of activated B cells. Upon initial encounter with microbial pathogens, enables the assembly of CD19-CR2/CD21 and B cell receptor (BCR) complexes at signaling TERMs, lowering the threshold dose of antigen required to trigger B cell clonal expansion and antibody production. In T cells, facilitates the localization of CD247/CD3 zeta at antigen-induced synapses with B cells, providing for costimulation and polarization toward T helper type 2 phenotype. Present in MHC class II compartments, may also play a role in antigen presentation (By similarity). Can act both as positive and negative regulator of homotypic or heterotypic cell-cell fusion processes. Positively regulates sperm-egg fusion and may be involved in acrosome reaction. In myoblasts, associates with CD9 and PTGFRN and inhibits myotube fusion during muscle regeneration (By similarity). In macrophages, associates with CD9 and beta-1 and beta-2 integrins, and prevents macrophage fusion into multinucleated giant cells specialized in ingesting complement-opsonized large particles (By similarity). Also prevents the fusion of mononuclear cell progenitors into osteoclasts in charge of bone resorption (By similarity). May regulate the compartmentalization of enzymatic activities. In T cells, defines the subcellular localization of dNTPase SAMHD1 and permits its degradation by the proteasome, thereby controlling intracellular dNTP levels (By similarity). Also involved in cell adhesion and motility. Positively regulates integrin-mediated adhesion of macrophages, particularly relevant for the inflammatory response in the lung (By similarity)", "gene_name": "Cd81", "glycan_count": 0, "glycosylation_sites": [], "id": "Q62745", "name": "Adiponectin", "organism": "Rattus norvegicus", "uniprot_id": "Q62745" }, { "function": "Thiol protease that acts as a major effector caspase involved in the execution phase of apoptosis (PubMed:16469926, PubMed:8934524). Following cleavage and activation by initiator caspases (CASP8, CASP9 and/or CASP10), mediates execution of apoptosis by catalyzing cleavage of many proteins (PubMed:16469926, PubMed:8934524). At the onset of apoptosis, it proteolytically cleaves poly(ADP-ribose) polymerase PARP1 at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9 (CASP6, CASP7 and CASP9, respectively). Cleaves and inactivates interleukin-18 (IL18) (By similarity). Triggers cell adhesion in sympathetic neurons through RET cleavage (By similarity). Cleaves IL-1 beta between an Asp and an Ala, releasing the mature cytokine which is involved in a variety of inflammatory processes (By similarity). Cleaves and inhibits serine/threonine-protein kinase AKT1 in response to oxidative stress (PubMed:12124386). Acts as an inhibitor of type I interferon production during virus-induced apoptosis by mediating cleavage of antiviral proteins CGAS, IRF3 and MAVS, thereby preventing cytokine overproduction (PubMed:30878284). Also involved in pyroptosis by mediating cleavage and activation of gasdermin-E (GSDME) (By similarity). Cleaves XRCC4 and phospholipid scramblase proteins XKR4, XKR8 and XKR9, leading to promote phosphatidylserine exposure on apoptotic cell surface (PubMed:25231987, PubMed:33725486). Cleaves BIRC6 following inhibition of BIRC6-caspase binding by DIABLO/SMAC (By similarity)", "gene_name": "Casp3", "glycan_count": 1, "glycosylation_sites": [], "id": "P70677", "name": "Caspase-3", "organism": "Mus musculus", "uniprot_id": "P70677" }, { "function": "SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. VAMP8 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane via its interaction with the STX17-SNAP29 binary t-SNARE complex (PubMed:23217709, PubMed:25686604). Also required for dense-granule secretion in platelets (PubMed:12130530). Also plays a role in regulated enzyme secretion in pancreatic acinar cells (By similarity). Involved in the abscission of the midbody during cell division, which leads to completely separate daughter cells (By similarity). Involved in the homotypic fusion of early and late endosomes (By similarity). Also participates in the activation of type I interferon antiviral response through a TRIM6-dependent mechanism (PubMed:31694946)", "gene_name": "VAMP8", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9BV40", "name": "SNAP29", "organism": "Homo sapiens", "uniprot_id": "Q9BV40" }, { "function": "In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins", "gene_name": "KRTAP4-7", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9BYR0", "name": "STX17", "organism": "Homo sapiens", "uniprot_id": "Q9BYR0" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P05067 (derived)", "name": "\u03b2-amyloid (A\u03b2)", "organism": "", "uniprot_id": "" }, { "function": "Transcriptional activator (PubMed:15555580). Important for maintenance of pluripotency in embryonic stem cells (By similarity). Binds directly to the POU5F1 distal enhancer and the NANOG proximal promoter, and enhances expression of both genes (By similarity). Can also bind to numerous other gene promoters and regulates expression of many other pluripotency factors, either directly or indirectly (By similarity). Promotes inhibition of MAPK signaling during embryonic stem cell differentiation (By similarity)", "gene_name": "ZNF322", "glycan_count": 2, "glycosylation_sites": [], "id": "Q6U7Q0", "name": "Adropin", "organism": "Homo sapiens", "uniprot_id": "Q6U7Q0" }, { "function": "Mediates thiol-dependent retention in the early secretory pathway, forming mixed disulfides with substrate proteins through its conserved CRFS motif (PubMed:11847130, PubMed:14517240). Inhibits the calcium channel activity of ITPR1 (PubMed:15652484). May have a role in the control of oxidative protein folding in the endoplasmic reticulum (PubMed:11847130, PubMed:14517240, PubMed:29858230). Required to retain ERO1A and ERO1B in the endoplasmic reticulum (PubMed:11847130, PubMed:29858230)", "gene_name": "ERP44", "glycan_count": 6, "glycosylation_sites": [], "id": "Q9BS26", "name": "ERp44", "organism": "Homo sapiens", "uniprot_id": "Q9BS26" }, { "function": "Required for MUC2 post-transcriptional synthesis and secretion. May play a role in the production of mucus by intestinal cells (By similarity). Proto-oncogene that may play a role in cell migration, cell differentiation and cell growth. Promotes cell adhesion (PubMed:23274113)", "gene_name": "AGR2", "glycan_count": 0, "glycosylation_sites": [], "id": "O95994", "name": "AGR2", "organism": "Homo sapiens", "uniprot_id": "O95994" }, { "function": "Required for calcium-mediated regulation of ciliary beat frequency and mucociliary clearance in the airway. Might be involved in the regulation of intracellular calcium in tracheal epithelial cells", "gene_name": "AGR3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8TD06", "name": "AGR3", "organism": "Homo sapiens", "uniprot_id": "Q8TD06" }, { "function": "Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Can also sulfate Gal residues in desulfated dermatan sulfate. Preferentially sulfates in GlcA->GalNAc unit than in IdoA->GalNAc unit. Does not form 4, 6-di-O-sulfated GalNAc when chondroitin sulfate C is used as an acceptor", "gene_name": "CHST11", "glycan_count": 3, "glycosylation_sites": [ { "position": 205, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 223, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 321, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 342, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NPF2", "name": "Dermatan-4-O-sulfotransferase 1 (D4ST1)", "organism": "Homo sapiens", "uniprot_id": "Q9NPF2" }, { "function": "Synthesizes selenophosphate from selenide and ATP", "gene_name": "SEPHS2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q99611", "name": "SEPHS2 (Selenophosphate synthetase 2)", "organism": "Homo sapiens", "uniprot_id": "Q99611" }, { "function": "Facilitates the differentiation and the cornification of keratinocytes", "gene_name": "S100A11", "glycan_count": 1, "glycosylation_sites": [], "id": "P31949", "name": "S100A1", "organism": "Homo sapiens", "uniprot_id": "P31949" }, { "function": "Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins", "gene_name": "GLRX", "glycan_count": 2, "glycosylation_sites": [], "id": "P35754", "name": "Glutaredoxin 1 (GLRX1)", "organism": "Homo sapiens", "uniprot_id": "P35754" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P15636", "name": "Glutathione S-transferase placental form (GST-P)", "organism": "Achromobacter lyticus", "uniprot_id": "P15636" }, { "function": "Dual methyltransferase that catalyzes methylation of elongation factor 1-alpha (EEF1A1 and EEF1A2) at two different positions, and is therefore involved in the regulation of mRNA translation (PubMed:30143613, PubMed:30612740). Via its C-terminus, methylates EEF1A1 and EEF1A2 at the N-terminal residue 'Gly-2' (PubMed:30143613). Via its N-terminus dimethylates EEF1A1 and EEF1A2 at residue 'Lys-55' (PubMed:30143613, PubMed:30612740). Has no activity towards core histones H2A, H2B, H3 and H4 (PubMed:30612740)", "gene_name": "METTL13", "glycan_count": 2, "glycosylation_sites": [], "id": "Q8N6R0", "name": "GALNTL6", "organism": "Homo sapiens", "uniprot_id": "Q8N6R0" }, { "function": "", "gene_name": "TMEM217", "glycan_count": 2, "glycosylation_sites": [ { "position": 39, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 156, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8N7C4", "name": "GALNT8", "organism": "Homo sapiens", "uniprot_id": "Q8N7C4" }, { "function": "Atypical E3 ubiquitin-protein ligase which specifically mediates ubiquitination of threonine and serine residues on target proteins, instead of ubiquitinating lysine residues (PubMed:29643511). Shows esterification activity towards both threonine and serine, with a preference for threonine, and acts via two essential catalytic cysteine residues that relay ubiquitin to its substrate via thioester intermediates (PubMed:29643511). Interacts with the E2 enzymes UBE2D1, UBE2D3, UBE2E1 and UBE2L3 (PubMed:18308511, PubMed:29643511). Plays a key role in neural development, probably by mediating ubiquitination of threonine residues on target proteins (Probable). Involved in different processes such as regulation of neurite outgrowth, synaptic growth, synaptogenesis and axon degeneration (By similarity). Required for the formation of major central nervous system axon tracts (By similarity). Required for proper axon growth by regulating axon navigation and axon branching: acts by regulating the subcellular location and stability of MAP3K12/DLK (By similarity). Required for proper localization of retinogeniculate projections but not for eye-specific segregation (By similarity). Regulates axon guidance in the olfactory system (By similarity). Involved in Wallerian axon degeneration, an evolutionarily conserved process that drives the loss of damaged axons: acts by promoting destabilization of NMNAT2, probably via ubiquitination of NMNAT2 (By similarity). Catalyzes ubiquitination of threonine and/or serine residues on NMNAT2, consequences of threonine and/or serine ubiquitination are however unknown (PubMed:29643511). Regulates the internalization of TRPV1 in peripheral sensory neurons (By similarity). Mediates ubiquitination and subsequent proteasomal degradation of TSC2/tuberin (PubMed:18308511, PubMed:27278822). Independently of the E3 ubiquitin-protein ligase activity, also acts as a guanosine exchange factor (GEF) for RAN in neurons of dorsal root ganglia (PubMed:26304119). May function as a facilitator or regulator of transcriptional activation by MYC (PubMed:9689053). Acts in concert with HUWE1 to regulate the circadian clock gene expression by promoting the lithium-induced ubiquination and degradation of NR1D1 (PubMed:20534529)", "gene_name": "MYCBP2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y6E4", "name": "MAN2A2", "organism": "Homo sapiens", "uniprot_id": "O75592" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02671 (alpha chain)", "name": "Fibrinogen", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q02297 (NRG1)", "name": "Neuregulin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P12109 (COL6A1)", "name": "Collagen VI", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P12643 (BMP2)", "name": "Bone Morphogenetic Protein (BMP)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q4QFJ2", "name": "Trypanothione reductase", "organism": "Leishmania major", "uniprot_id": "Q4QFJ2" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q4QFJ1", "name": "CYP51 (Sterol 14\u03b1-demethylase)", "organism": "Leishmania major", "uniprot_id": "Q4QFJ1" }, { "function": "Destroys radicals which are normally produced within the cells and which are toxic to biological systems", "gene_name": "FESODA", "glycan_count": 0, "glycosylation_sites": [], "id": "A4HTI0", "name": "FeSODA (Iron superoxide dismutase A)", "organism": "Leishmania infantum", "uniprot_id": "A4HTI0" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P08186", "name": "CD36", "organism": "", "uniprot_id": "P08186" }, { "function": "Ligand-activated transcription factor. Key regulator of lipid metabolism. Activated by the endogenous ligand 1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphocholine (16:0/18:1-GPC). Activated by oleylethanolamide, a naturally occurring lipid that regulates satiety. Receptor for peroxisome proliferators such as hypolipidemic drugs and fatty acids. Regulates the peroxisomal beta-oxidation pathway of fatty acids. Functions as a transcription activator for the ACOX1 and P450 genes. Transactivation activity requires heterodimerization with RXRA and is antagonized by NR2C2. May be required for the propagation of clock information to metabolic pathways regulated by PER2", "gene_name": "Ppara", "glycan_count": 0, "glycosylation_sites": [], "id": "PPARA_MOUSE", "name": "Peroxisome proliferator-activated receptor alpha (PPAR\u03b1)", "organism": "Mus musculus", "uniprot_id": "P23204" }, { "function": "Binds low density lipoprotein /LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits. Forms a ternary complex with PGRMC1 and TMEM97 receptors which increases LDLR-mediated LDL internalization", "gene_name": "Ldlr", "glycan_count": 2, "glycosylation_sites": [ { "position": 97, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 273, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 462, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P35951", "name": "Low-density lipoprotein receptor (LDLR)", "organism": "Mus musculus", "uniprot_id": "P35951" }, { "function": "Seed storage protein", "gene_name": "GLUA2", "glycan_count": 0, "glycosylation_sites": [], "id": "P07731", "name": "Alanine aminotransferase (ALT)", "organism": "Oryza sativa subsp. japonica", "uniprot_id": "P07730" }, { "function": "Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation", "gene_name": "Tf", "glycan_count": 15, "glycosylation_sites": [ { "position": 512, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P12346", "name": "Aspartate aminotransferase (AST)", "organism": "Rattus norvegicus", "uniprot_id": "P12346" }, { "function": "Polyol dehydrogenase that catalyzes the reversible NAD(+)-dependent oxidation of various sugar alcohols. Is mostly active with D-sorbitol (D-glucitol), L-threitol, xylitol and ribitol as substrates, leading to the C2-oxidized products D-fructose, L-erythrulose, D-xylulose, and D-ribulose, respectively (PubMed:3365415). Is a key enzyme in the polyol pathway that interconverts glucose and fructose via sorbitol, which constitutes an important alternate route for glucose metabolism. The polyol pathway is believed to be involved in the etiology of diabetic complications, such as diabetic neuropathy and retinopathy, induced by hyperglycemia (PubMed:12962626, PubMed:25105142, PubMed:29966615). May play a role in sperm motility by using sorbitol as an alternative energy source for sperm motility (PubMed:16278369). May have a more general function in the metabolism of secondary alcohols since it also catalyzes the stereospecific oxidation of (2R,3R)-2,3-butanediol. To a lesser extent, can also oxidize L-arabinitol, galactitol and D-mannitol and glycerol in vitro. Oxidizes neither ethanol nor other primary alcohols. Cannot use NADP(+) as the electron acceptor (PubMed:3365415)", "gene_name": "SORD", "glycan_count": 3, "glycosylation_sites": [], "id": "Q00796", "name": "Retinol-binding protein 4 (RBP4)", "organism": "Homo sapiens", "uniprot_id": "Q00796" }, { "function": "Transcription factor involved in unfolded protein response (UPR). In the absence of endoplasmic reticulum (ER) stress, inserted into ER membranes, with N-terminal DNA-binding and transcription activation domains oriented toward the cytosolic face of the membrane. In response to ER stress, transported to the Golgi, where it is cleaved in a site-specific manner by resident proteases S1P/MBTPS1 and S2P/MBTPS2. The released N-terminal cytosolic domain is translocated to the nucleus to effect transcription of specific target genes. Plays a critical role in chondrogenesis by activating the transcription of SEC23A, which promotes the transport and secretion of cartilage matrix proteins, and possibly that of ER biogenesis-related genes (By similarity). In a neuroblastoma cell line, protects cells from ER stress-induced death (PubMed:17178827). In vitro activates transcription of target genes via direct binding to the CRE site (PubMed:17178827)", "gene_name": "CREB3L2", "glycan_count": 2, "glycosylation_sites": [ { "position": 480, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 504, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 517, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q70SY1", "name": "CREB3L1", "organism": "Homo sapiens", "uniprot_id": "Q70SY1" }, { "function": "Promotes apoptosis by activating caspases in the cytochrome c/Apaf-1/caspase-9 pathway. Acts by opposing the inhibitory activity of inhibitor of apoptosis proteins (IAP). Inhibits the activity of BIRC6/BRUCE by inhibiting its binding to caspases (PubMed:15200957, PubMed:36758104, PubMed:36758105, PubMed:36758106)", "gene_name": "DIABLO", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NR28", "name": "Smac/DIABLO", "organism": "Homo sapiens", "uniprot_id": "Q9NR28" }, { "function": "", "gene_name": "PRKCB", "glycan_count": 0, "glycosylation_sites": [], "id": "P05771-2", "name": "PKC\u03b2II", "organism": "Homo sapiens", "uniprot_id": "P05771-2" }, { "function": "Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec)", "gene_name": "SARS2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NP81", "name": "Fn14 (TWEAKR)", "organism": "Homo sapiens", "uniprot_id": "Q9NP81" }, { "function": "Has an antimicrobial activity", "gene_name": "LEAP2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q969E1", "name": "LEAP2", "organism": "Homo sapiens", "uniprot_id": "Q969E1" }, { "function": "Adapter protein for several members of the tyrosine kinase receptor family. Involved in multiple signaling pathways mediated by Janus kinase (JAK) and receptor tyrosine kinases, including the receptors of insulin (INS), insulin-like growth factor 1 (IGF1), nerve growth factor (NGF), brain-derived neurotrophic factor (BDNF), glial cell line-derived neurotrophic factor (GDNF), platelet-derived growth factor (PDGF) and fibroblast growth factors (FGFs). In growth hormone (GH) signaling, autophosphorylated ('Tyr-813') JAK2 recruits SH2B1, which in turn is phosphorylated by JAK2 on tyrosine residues. These phosphotyrosines form potential binding sites for other signaling proteins. GH also promotes serine/threonine phosphorylation of SH2B1 and these phosphorylated residues may serve to recruit other proteins to the GHR-JAK2-SH2B1 complexes, such as RAC1. In leptin (LEP) signaling, binds to and potentiates the activation of JAK2 by globally enhancing downstream pathways. In response to leptin, binds simultaneously to both, JAK2 and IRS1 or IRS2, thus mediating formation of a complex of JAK2, SH2B1 and IRS1 or IRS2. Mediates tyrosine phosphorylation of IRS1 and IRS2, resulting in activation of the PI 3-kinase pathway. Acts as a positive regulator of NGF-mediated activation of the Akt/Forkhead pathway; prolongs NGF-induced phosphorylation of AKT1 on 'Ser-473' and AKT1 enzymatic activity. Enhances the kinase activity of the cytokine receptor-associated tyrosine kinase JAK2 and of other receptor tyrosine kinases, such as FGFR3 and NTRK1. For JAK2, the mechanism seems to involve dimerization of both, SH2B1 and JAK2. Enhances RET phosphorylation and kinase activity. Isoforms seem to be differentially involved in IGF1 and PDGF-induced mitogenesis (By similarity)", "gene_name": "SH2B1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NRF2", "name": "SH2B1", "organism": "Homo sapiens", "uniprot_id": "Q9NRF2" }, { "function": "Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation", "gene_name": "FBXO28", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NVF7", "name": "FAIM2", "organism": "Homo sapiens", "uniprot_id": "Q9NVF7" }, { "function": "May regulate calcium-dependent activities in the endoplasmic reticulum lumen or post-ER compartment", "gene_name": "RCN1", "glycan_count": 96, "glycosylation_sites": [ { "position": 53, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q15293", "name": "RCN1", "organism": "Homo sapiens", "uniprot_id": "Q15293" }, { "function": "Probably plays a role in the formation and regulation of the tight junction (TJ) paracellular permeability barrier", "gene_name": "CGN", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9P2M7", "name": "CPLANE1", "organism": "Homo sapiens", "uniprot_id": "Q9P2M7" }, { "function": "Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity (PubMed:18594507). In dorsal pons neurons, involved in the regulation of sleep/wake behaviors (By similarity)", "gene_name": "ADRB1", "glycan_count": 0, "glycosylation_sites": [ { "position": 14, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P07700", "name": "\u03b21-adrenergic receptor (\u03b21AR)", "organism": "Meleagris gallopavo", "uniprot_id": "P07700" }, { "function": "Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine", "gene_name": "Adrb2", "glycan_count": 0, "glycosylation_sites": [ { "position": 6, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 15, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P10608", "name": "\u03b22-adrenergic receptor (\u03b22AR)", "organism": "Rattus norvegicus", "uniprot_id": "P10608" }, { "function": "Guanine nucleotide-binding proteins (G proteins) function as transducers in numerous signaling pathways controlled by G protein-coupled receptors (GPCRs) (PubMed:12391161, PubMed:17110384, PubMed:21488135, PubMed:26206488, PubMed:8702665, PubMed:10200251). The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state (PubMed:12391161, PubMed:17110384, PubMed:10200251). Signaling by an activated GPCR promotes GDP release and GTP binding (PubMed:12391161, PubMed:17110384, PubMed:10200251). The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal (PubMed:12391161, PubMed:17110384, PubMed:10200251). Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (PubMed:12391161, PubMed:17110384, PubMed:10200251). Signaling involves the activation of adenylyl cyclases, resulting in increased levels of the signaling molecule cAMP (PubMed:17110384, PubMed:26206488, PubMed:26206488, PubMed:8702665). Functions downstream of beta-adrenergic receptors (PubMed:21488135). Stimulates the Ras signaling pathway via RAPGEF2 (PubMed:12391161)", "gene_name": "GNAS", "glycan_count": 0, "glycosylation_sites": [], "id": "P63092", "name": "G\u03b1s protein", "organism": "Homo sapiens", "uniprot_id": "P63092" }, { "function": "Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades (PubMed:18434541, PubMed:33762731, PubMed:34239069, PubMed:35610220, PubMed:37935376, PubMed:37935377, PubMed:37963465, PubMed:38552625, PubMed:8774883, PubMed:38918398). The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state (PubMed:18434541, PubMed:8774883). Signaling by an activated GPCR promotes GDP release and GTP binding (PubMed:18434541, PubMed:8774883). The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal (PubMed:18434541, PubMed:8774883). Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (PubMed:18434541, PubMed:8774883). Signaling is mediated via effector proteins, such as adenylate cyclase: inhibits adenylate cyclase activity of ADCY1, ADCY5 and ADCY6, leading to decreased intracellular cAMP levels (PubMed:8119955). The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. Required for normal cytokinesis during mitosis (PubMed:17635935). Required for cortical dynein-dynactin complex recruitment during metaphase (PubMed:22327364)", "gene_name": "GNAI1", "glycan_count": 2, "glycosylation_sites": [], "id": "P63096", "name": "G\u03b1i protein", "organism": "Homo sapiens", "uniprot_id": "P63096" }, { "function": "Functions in regulating agonist-mediated G-protein coupled receptor (GPCR) signaling by mediating both receptor desensitization and resensitization processes. During homologous desensitization, beta-arrestins bind to the GPRK-phosphorylated receptor and sterically preclude its coupling to the cognate G-protein; the binding appears to require additional receptor determinants exposed only in the active receptor conformation. The beta-arrestins target many receptors for internalization by acting as endocytic adapters (CLASPs, clathrin-associated sorting proteins) and recruiting the GPRCs to the adapter protein 2 complex 2 (AP-2) in clathrin-coated pits (CCPs). However, the extent of beta-arrestin involvement appears to vary significantly depending on the receptor, agonist and cell type. Internalized arrestin-receptor complexes traffic to intracellular endosomes, where they remain uncoupled from G-proteins. Two different modes of arrestin-mediated internalization occur. Class A receptors, like ADRB2, OPRM1, ENDRA, D1AR and ADRA1B dissociate from beta-arrestin at or near the plasma membrane and undergo rapid recycling. Class B receptors, like AVPR2, AGTR1, NTSR1, TRHR and TACR1 internalize as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptors, for extended periods of time. Receptor resensitization then requires that receptor-bound arrestin is removed so that the receptor can be dephosphorylated and returned to the plasma membrane. Involved in internalization of P2RY4 and UTP-stimulated internalization of P2RY2. Involved in phosphorylation-dependent internalization of OPRD1 ands subsequent recycling. Involved in the degradation of cAMP by recruiting cAMP phosphodiesterases to ligand-activated receptors. Beta-arrestins function as multivalent adapter proteins that can switch the GPCR from a G-protein signaling mode that transmits short-lived signals from the plasma membrane via small molecule second messengers and ion channels to a beta-arrestin signaling mode that transmits a distinct set of signals that are initiated as the receptor internalizes and transits the intracellular compartment. Acts as a signaling scaffold for MAPK pathways such as MAPK1/3 (ERK1/2). ERK1/2 activated by the beta-arrestin scaffold is largely excluded from the nucleus and confined to cytoplasmic locations such as endocytic vesicles, also called beta-arrestin signalosomes. Recruits c-Src/SRC to ADRB2 resulting in ERK activation. GPCRs for which the beta-arrestin-mediated signaling relies on both ARRB1 and ARRB2 (codependent regulation) include ADRB2, F2RL1 and PTH1R. For some GPCRs the beta-arrestin-mediated signaling relies on either ARRB1 or ARRB2 and is inhibited by the other respective beta-arrestin form (reciprocal regulation). Inhibits ERK1/2 signaling in AGTR1- and AVPR2-mediated activation (reciprocal regulation). Is required for SP-stimulated endocytosis of NK1R and recruits c-Src/SRC to internalized NK1R resulting in ERK1/2 activation, which is required for the antiapoptotic effects of SP. Is involved in proteinase-activated F2RL1-mediated ERK activity. Acts as a signaling scaffold for the AKT1 pathway. Is involved in alpha-thrombin-stimulated AKT1 signaling. Is involved in IGF1-stimulated AKT1 signaling leading to increased protection from apoptosis. Involved in activation of the p38 MAPK signaling pathway and in actin bundle formation. Involved in F2RL1-mediated cytoskeletal rearrangement and chemotaxis. Involved in AGTR1-mediated stress fiber formation by acting together with GNAQ to activate RHOA. Appears to function as signaling scaffold involved in regulation of MIP-1-beta-stimulated CCR5-dependent chemotaxis. Involved in attenuation of NF-kappa-B-dependent transcription in response to GPCR or cytokine stimulation by interacting with and stabilizing CHUK. May serve as nuclear messenger for GPCRs. Involved in OPRD1-stimulated transcriptional regulation by translocating to CDKN1B and FOS promoter regions and recruiting EP300 resulting in acetylation of histone H4. Involved in regulation of LEF1 transcriptional activity via interaction with DVL1 and/or DVL2 Also involved in regulation of receptors other than GPCRs. Involved in Toll-like receptor and IL-1 receptor signaling through the interaction with TRAF6 which prevents TRAF6 autoubiquitination and oligomerization required for activation of NF-kappa-B and JUN. Binds phosphoinositides. Binds inositolhexakisphosphate (InsP6) (By similarity). Involved in IL8-mediated granule release in neutrophils. Required for atypical chemokine receptor ACKR2-induced RAC1-LIMK1-PAK1-dependent phosphorylation of cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. Involved in the internalization of the atypical chemokine receptor ACKR3. Negatively regulates the NOTCH signaling pathway by mediating the ubiquitination and degradation of NOTCH1 by ITCH. Participates in the recruitment of the ubiquitin-protein ligase to the receptor (PubMed:23886940)", "gene_name": "ARRB1", "glycan_count": 1, "glycosylation_sites": [], "id": "P49407", "name": "\u03b2-arrestin 1", "organism": "Homo sapiens", "uniprot_id": "P49407" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q08462/Q08463", "name": "Adenylyl cyclase V/VI", "organism": "", "uniprot_id": "" }, { "function": "Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase", "gene_name": "PRKAR2A", "glycan_count": 1, "glycosylation_sites": [], "id": "P13861", "name": "PKA regulatory subunit RII\u03b1", "organism": "Homo sapiens", "uniprot_id": "P13861" }, { "function": "Voltage-sensitive calcium channel that gives rise to T-type calcium currents. T-type calcium channels belong to the 'low-voltage activated (LVA)' group. A particularity of this type of channel is an opening at quite negative potentials, and a voltage-dependent inactivation (PubMed:11073957). T-type channels serve pacemaking functions in both central neurons and cardiac nodal cells and support calcium signaling in secretory cells and vascular smooth muscle (Probable). They may also be involved in the modulation of firing patterns of neurons. In the adrenal zona glomerulosa, participates in the signaling pathway leading to aldosterone production in response to either AGT/angiotensin II, or hyperkalemia (By similarity)", "gene_name": "Cacna1h", "glycan_count": 0, "glycosylation_sites": [ { "position": 192, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 271, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1477, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9EQ60", "name": "Ryanodine receptor 2 (RyR2)", "organism": "Rattus norvegicus", "uniprot_id": "Q9EQ60" }, { "function": "Receptor on natural killer (NK) cells for class I MHC", "gene_name": "Klra8", "glycan_count": 0, "glycosylation_sites": [ { "position": 87, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 104, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q60682", "name": "Nrf2", "organism": "Mus musculus", "uniprot_id": "Q60682" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6NZV0", "name": "Keap1", "organism": "", "uniprot_id": "" }, { "function": "Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS", "gene_name": "Kpna3", "glycan_count": 1, "glycosylation_sites": [], "id": "O35344", "name": "SREBP1", "organism": "Mus musculus", "uniprot_id": "O35344" }, { "function": "Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression", "gene_name": "Eif3c", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8R1B4", "name": "ACC-1", "organism": "Mus musculus", "uniprot_id": "Q8R1B4" }, { "function": "Coreceptor for bacterial lipopolysaccharide. In concert with LBP, binds to monomeric lipopolysaccharide and delivers it to the LY96/TLR4 complex, thereby mediating the innate immune response to bacterial lipopolysaccharide (LPS). Acts via MyD88, TIRAP and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Acts as a coreceptor for TLR2:TLR6 heterodimer in response to diacylated lipopeptides and for TLR2:TLR1 heterodimer in response to triacylated lipopeptides, these clusters trigger signaling from the cell surface and subsequently are targeted to the Golgi in a lipid-raft dependent pathway. Binds electronegative LDL (LDL(-)) and mediates the cytokine release induced by LDL(-) (By similarity)", "gene_name": "Cd14", "glycan_count": 0, "glycosylation_sites": [ { "position": 39, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 46, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 153, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 186, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 282, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q63691", "name": "Bax", "organism": "Rattus norvegicus", "uniprot_id": "Q63691" }, { "function": "Cysteine protease that plays essential roles in programmed cell death, axonal degeneration, development and innate immunity (PubMed:19133298, PubMed:22858542, PubMed:27032039, PubMed:28864531, PubMed:30420425, PubMed:32298652, PubMed:8663580). Acts as a non-canonical executioner caspase during apoptosis: localizes in the nucleus and cleaves the nuclear structural protein NUMA1 and lamin A/LMNA thereby inducing nuclear shrinkage and fragmentation (PubMed:11953316, PubMed:17401638, PubMed:8663580, PubMed:9463409). Lamin-A/LMNA cleavage is required for chromatin condensation and nuclear disassembly during apoptotic execution (PubMed:11953316). Acts as a regulator of liver damage by promoting hepatocyte apoptosis: in absence of phosphorylation by AMP-activated protein kinase (AMPK), catalyzes cleavage of BID, leading to cytochrome c release, thereby participating in nonalcoholic steatohepatitis (PubMed:32029622). Cleaves PARK7/DJ-1 in cells undergoing apoptosis (By similarity). Involved in intrinsic apoptosis by mediating cleavage of RIPK1 (PubMed:22858542). Furthermore, cleaves many transcription factors such as NF-kappa-B and cAMP response element-binding protein/CREBBP (PubMed:10559921, PubMed:14657026). Cleaves phospholipid scramblase proteins XKR4 and XKR9 (By similarity). In addition to apoptosis, involved in different forms of programmed cell death (PubMed:32298652). Plays an essential role in defense against viruses by acting as a central mediator of the ZBP1-mediated pyroptosis, apoptosis, and necroptosis (PANoptosis), independently of its cysteine protease activity (PubMed:32298652). PANoptosis is a unique inflammatory programmed cell death, which provides a molecular scaffold that allows the interactions and activation of machinery required for inflammasome/pyroptosis, apoptosis and necroptosis (PubMed:32298652). Mechanistically, interacts with RIPK3 and enhances the interaction between RIPK3 and ZBP1, leading to ZBP1-mediated inflammasome activation and cell death (PubMed:32298652). Plays an essential role in axon degeneration during axon pruning which is the remodeling of axons during neurogenesis but not apoptosis (By similarity). Regulates B-cell programs both during early development and after antigen stimulation (By similarity)", "gene_name": "CASP6", "glycan_count": 2, "glycosylation_sites": [], "id": "P55212", "name": "Caspase-3", "organism": "Homo sapiens", "uniprot_id": "P55212" }, { "function": "Probably involved in differentiation", "gene_name": "Ahsg", "glycan_count": 4, "glycosylation_sites": [ { "position": 99, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 156, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 176, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P29699", "name": "Fetuin A (FETUA)", "organism": "Mus musculus", "uniprot_id": "P29699" }, { "function": "Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. Cytochrome c1 is a catalytic core subunit containing a c-type heme. It transfers electrons from the [2Fe-2S] iron-sulfur cluster of the Rieske protein to cytochrome c", "gene_name": "Cyc1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9D0M3", "name": "Ribophorin I (RPN1)", "organism": "Mus musculus", "uniprot_id": "Q9D0M3" }, { "function": "Hardly reversible, non-competitive, and potent inhibitor of CPA1, CPA2 and CPA4 (By similarity). May play a role in inflammation", "gene_name": "Lxn", "glycan_count": 0, "glycosylation_sites": [], "id": "P70202", "name": "Serpin H1 (SERPH1)", "organism": "Mus musculus", "uniprot_id": "P70202" }, { "function": "Highly potent vasoconstrictor", "gene_name": "Uts2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9QZQ4", "name": "Semicarbazide-sensitive amine oxidase (AOC3)", "organism": "Rattus norvegicus", "uniprot_id": "Q9QZQ4" }, { "function": "Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways", "gene_name": "Fgb", "glycan_count": 3, "glycosylation_sites": [ { "position": 384, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8K0E8", "name": "Factor XIII-A (F13A)", "organism": "Mus musculus", "uniprot_id": "Q8K0E8" }, { "function": "Contributes to histone modification (PubMed:16600877, PubMed:16829960, PubMed:19103755, PubMed:19131338, PubMed:19556245, PubMed:20018852). May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4' (PubMed:16829960). As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3 (PubMed:19556245). H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation (PubMed:18840606). As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues (PubMed:19103755, PubMed:20018852). May regulate osteoblasts differentiation (By similarity). In association with RBBP5 and ASH2L, stimulates the histone methyltransferase activities of KMT2A, KMT2B, KMT2C, KMT2D, SETD1A and SETD1B (PubMed:21220120, PubMed:22266653)", "gene_name": "WDR5", "glycan_count": 1, "glycosylation_sites": [], "id": "P61964", "name": "Ribonucleoprotein A2/B1 (ROA2)", "organism": "Homo sapiens", "uniprot_id": "P61964" }, { "function": "Generates phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as second messengers (PubMed:9516481). May play a role in SDF1A-stimulated chemotaxis (By similarity)", "gene_name": "Pik3c2g", "glycan_count": 0, "glycosylation_sites": [], "id": "O70173", "name": "PI3K", "organism": "Rattus norvegicus", "uniprot_id": "O70173" }, { "function": "AKT1 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis (PubMed:9228007, PubMed:11882383, PubMed:21432781, PubMed:21620960). This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates (PubMed:11882383, PubMed:21432781, PubMed:21620960). Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported (PubMed:11882383, PubMed:21432781, PubMed:21620960). AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface (PubMed:10400692, PubMed:9632753). Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling (By similarity). Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport (By similarity). AKT also regulates the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven (By similarity). AKT also regulates cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating the mTORC1 signaling pathway, and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. Also regulates the mTORC1 signaling pathway by catalyzing phosphorylation of CASTOR1 and DEPDC5. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation (By similarity). Part of a positive feedback loop of mTORC2 signaling by mediating phosphorylation of MAPKAP1/SIN1, promoting mTORC2 activation (By similarity). AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF-kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1 (By similarity). AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis (PubMed:12107176). Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis (By similarity). Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI(3)P-5 activity (PubMed:15546921). The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth (By similarity). Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor 1 (IGF1) (By similarity). AKT mediates the antiapoptotic effects of IGF1 (By similarity). Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly (By similarity). May be involved in the regulation of the placental development (By similarity). Phosphorylates STK4/MST1 at 'Thr-120' and 'Thr-387' leading to inhibition of its: kinase activity, nuclear translocation, autophosphorylation and ability to phosphorylate FOXO3. Phosphorylates STK3/MST2 at 'Thr-117' and 'Thr-384' leading to inhibition of its: cleavage, kinase activity, autophosphorylation at Thr-180, binding to RASSF1 and nuclear translocation. Phosphorylates SRPK2 and enhances its kinase activity towards SRSF2 and ACIN1 and promotes its nuclear translocation. Phosphorylates RAF1 at 'Ser-259' and negatively regulates its activity. Phosphorylation of BAD stimulates its pro-apoptotic activity. Phosphorylates KAT6A at 'Thr-369' and this phosphorylation inhibits the interaction of KAT6A with PML and negatively regulates its acetylation activity towards p53/TP53. Phosphorylates palladin (PALLD), modulating cytoskeletal organization and cell motility. Phosphorylates prohibitin (PHB), playing an important role in cell metabolism and proliferation. Phosphorylates CDKN1A, for which phosphorylation at 'Thr-145' induces its release from CDK2 and cytoplasmic relocalization. These recent findings indicate that the AKT1 isoform has a more specific role in cell motility and proliferation. Phosphorylates CLK2 thereby controlling cell survival to ionizing radiation (By similarity). Phosphorylates PCK1 at 'Ser-90', reducing the binding affinity of PCK1 to oxaloacetate and changing PCK1 into an atypical protein kinase activity using GTP as donor (By similarity). Also acts as an activator of TMEM175 potassium channel activity in response to growth factors: forms the lysoK(GF) complex together with TMEM175 and acts by promoting TMEM175 channel activation, independently of its protein kinase activity (By similarity). Acts as a negative regulator of the cGAS-STING pathway by mediating phosphorylation of CGAS during mitosis, leading to its inhibition (By similarity). Acts as a regulator of mitochondrial calcium uptake by mediating phosphorylation of MICU1 in the mitochondrial intermembrane space, impairing MICU1 maturation (By similarity). Acts as an inhibitor of tRNA methylation by mediating phosphorylation of the N-terminus of METTL1, thereby inhibiting METTL1 methyltransferase activity (By similarity). In response to LPAR1 receptor pathway activation, phosphorylates Rabin8/RAB3IP which alters its activity and phosphorylates WDR44 which induces WDR44 binding to Rab11, thereby switching Rab11 vesicular function from preciliary trafficking to endocytic recycling (By similarity)", "gene_name": "Akt1", "glycan_count": 1, "glycosylation_sites": [ { "position": 126, "type": "O-linked (GlcNAc) serine; alternate" }, { "position": 129, "type": "O-linked (GlcNAc) serine; alternate" }, { "position": 305, "type": "O-linked (GlcNAc) threonine" }, { "position": 312, "type": "O-linked (GlcNAc) threonine" }, { "position": 473, "type": "O-linked (GlcNAc) serine; alternate" } ], "id": "P47196", "name": "Akt", "organism": "Rattus norvegicus", "uniprot_id": "P47196" }, { "function": "Transcription factor that plays a key role in the response to oxidative stress: binds to antioxidant response (ARE) elements present in the promoter region of many cytoprotective genes, such as phase 2 detoxifying enzymes, and promotes their expression, thereby neutralizing reactive electrophiles (PubMed:16314513). In normal conditions, ubiquitinated and degraded in the cytoplasm by the BCR(KEAP1) complex. In response to oxidative stress, electrophile metabolites inhibit activity of the BCR(KEAP1) complex, promoting nuclear accumulation of NFE2L2/NRF2, heterodimerization with one of the small Maf proteins and binding to ARE elements of cytoprotective target genes. The NFE2L2/NRF2 pathway is also activated in response to selective autophagy: autophagy promotes interaction between KEAP1 and SQSTM1/p62 and subsequent inactivation of the BCR(KEAP1) complex, leading to NFE2L2/NRF2 nuclear accumulation and expression of cytoprotective genes (By similarity). The NFE2L2/NRF2 pathway is also activated during the unfolded protein response (UPR), contributing to redox homeostasis and cell survival following endoplasmic reticulum stress (By similarity). May also be involved in the transcriptional activation of genes of the beta-globin cluster by mediating enhancer activity of hypersensitive site 2 of the beta-globin locus control region (By similarity). Also plays an important role in the regulation of the innate immune response. It is a critical regulator of the innate immune response and survival during sepsis by maintaining redox homeostasis and restraint of the dysregulation of pro-inflammatory signaling pathways like MyD88-dependent and -independent and TNF-alpha signaling. Suppresses macrophage inflammatory response by blocking pro-inflammatory cytokine transcription and the induction of IL6. Binds to the proximity of pro-inflammatory genes in macrophages and inhibits RNA Pol II recruitment. The inhibition is independent of the Nrf2-binding motif and reactive oxygen species level (By similarity). Represses antiviral cytosolic DNA sensing by suppressing the expression of the adapter protein STING1 and decreasing responsiveness to STING1 agonists while increasing susceptibility to infection with DNA viruses (By similarity)", "gene_name": "Nfe2l2", "glycan_count": 0, "glycosylation_sites": [ { "position": 461, "type": "N-linked (Glc) (glycation) lysine" }, { "position": 471, "type": "N-linked (Glc) (glycation) lysine" }, { "position": 486, "type": "N-linked (Glc) (glycation) lysine" }, { "position": 498, "type": "N-linked (Glc) (glycation) arginine" }, { "position": 568, "type": "N-linked (Glc) (glycation) arginine" }, { "position": 573, "type": "N-linked (Glc) (glycation) lysine" } ], "id": "O54968", "name": "Nrf-2", "organism": "Rattus norvegicus", "uniprot_id": "O54968" }, { "function": "Catalyzes the oxidative cleavage of heme at the alpha-methene bridge carbon, released as carbon monoxide (CO), to generate biliverdin IXalpha, while releasing the central heme iron chelate as ferrous iron (PubMed:1575508, PubMed:1935972, PubMed:3865203). Affords protection against programmed cell death and this cytoprotective effect relies on its ability to catabolize free heme and prevent it from sensitizing cells to undergo apoptosis (By similarity)", "gene_name": "Hmox1", "glycan_count": 0, "glycosylation_sites": [], "id": "P06762", "name": "HO-1", "organism": "Rattus norvegicus", "uniprot_id": "P06762" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P09486 (mouse)", "name": "Secreted acidic cysteine-rich glycoprotein (SPARC)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P11087/P08123 (mouse)", "name": "Collagen type I (COL1A1/COL1A2)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P12032 (mouse)", "name": "Tissue inhibitor of metalloproteinases 1 (TIMP1)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P28653 (mouse)", "name": "Decorin (DCN)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P18206 (mouse)", "name": "Vinculin (VCL)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Z1J9 (mouse)", "name": "Cellular communication network factor 2 (CCN2/CTGF)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P08727 (mouse)", "name": "Keratin 19 (KRT19)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P62737 (mouse)", "name": "Alpha-smooth muscle actin (ACTA2)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03995 (mouse)", "name": "Glial fibrillary acidic protein (GFAP)", "organism": "", "uniprot_id": "" }, { "function": "Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events", "gene_name": "PRDX5", "glycan_count": 1, "glycosylation_sites": [], "id": "P30044", "name": "Peroxiredoxin 5 (PRDX5)", "organism": "Homo sapiens", "uniprot_id": "P30044" }, { "function": "Important for the control of mitochondrial reactive oxygen species homeostasis, apoptosis regulation and cell viability (PubMed:12032145, PubMed:12080052, PubMed:26626369) Is involved in various redox reactions including the reduction of protein disulfide bonds, through the reversible oxidation of its active center dithiol to a disulfide (By similarity)", "gene_name": "TXN2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q99757", "name": "Thioredoxin 2 (TRX2)", "organism": "Homo sapiens", "uniprot_id": "Q99757" }, { "function": "Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane", "gene_name": "SPTAN1", "glycan_count": 3, "glycosylation_sites": [], "id": "Q13813", "name": "Spectrin alpha-II (SNTF fragment)", "organism": "Homo sapiens", "uniprot_id": "Q13813" }, { "function": "Deubiquitinase that plays a role in the regulation of several processes such as maintenance of synaptic function, cardiac function, inflammatory response or osteoclastogenesis (PubMed:22212137, PubMed:23359680). Abrogates the ubiquitination of multiple proteins including WWTR1/TAZ, EGFR, HIF1A and beta-site amyloid precursor protein cleaving enzyme 1/BACE1 (PubMed:22212137, PubMed:25615526). In addition, recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin to maintain a stable pool of monoubiquitin that is a key requirement for the ubiquitin-proteasome and the autophagy-lysosome pathways (PubMed:12408865, PubMed:8639624, PubMed:9774100). Regulates amyloid precursor protein/APP processing by promoting BACE1 degradation resulting in decreased amyloid beta production (PubMed:22212137). Plays a role in the immune response by regulating the ability of MHC I molecules to reach cross-presentation compartments competent for generating Ag-MHC I complexes (By similarity). Mediates the 'Lys-48'-linked deubiquitination of the transcriptional coactivator WWTR1/TAZ leading to its stabilization and inhibition of osteoclastogenesis (By similarity). Deubiquitinates and stabilizes epidermal growth factor receptor EGFR to prevent its degradation and to activate its downstream mediators (By similarity). Modulates oxidative activity in skeletal muscle by regulating key mitochondrial oxidative proteins (By similarity). Enhances the activity of hypoxia-inducible factor 1-alpha/HIF1A by abrogateing its VHL E3 ligase-mediated ubiquitination and consequently inhibiting its degradation (PubMed:25615526)", "gene_name": "UCHL1", "glycan_count": 1, "glycosylation_sites": [], "id": "P09936", "name": "Ubiquitin C-terminal hydrolase L1 (UCH-L1)", "organism": "Homo sapiens", "uniprot_id": "P09936" }, { "function": "Protease inhibitor that inhibits trypsin and trypsin-like serine proteases (in vitro). Inhibits plasmin and thrombin with lower efficiency (in vitro)", "gene_name": "SERPINA9", "glycan_count": 0, "glycosylation_sites": [ { "position": 101, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 390, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q86WD7", "name": "PROM2", "organism": "Homo sapiens", "uniprot_id": "Q86WD7" }, { "function": "Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it is required for the complex integrity and its localization at DSBs. Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates (PubMed:24075985, PubMed:26195665). In these 2 complexes, it is probably required to maintain the stability of BABAM2 and help the 'Lys-63'-linked deubiquitinase activity mediated by BRCC3/BRCC36 component. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1 (PubMed:26195665). Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activity by enhancing its stability and cell surface expression (PubMed:24075985). Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination (PubMed:24075985)", "gene_name": "BABAM1", "glycan_count": 3, "glycosylation_sites": [], "id": "Q9NWV8", "name": "FAM175B", "organism": "Homo sapiens", "uniprot_id": "Q9NWV8" }, { "function": "Functions as an endocytic receptor on a small subset of myeloid cells specialized for the uptake and processing of material from dead cells. Recognizes filamentous form of actin in association with particular actin-binding domains of cytoskeletal proteins, including spectrin, exposed when cell membranes are damaged, and mediate the cross-presentation of dead-cell associated antigens in a Syk-dependent manner", "gene_name": "CLEC9A", "glycan_count": 0, "glycosylation_sites": [ { "position": 81, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 223, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6UXN8", "name": "LRRTM4", "organism": "Homo sapiens", "uniprot_id": "Q6UXN8" }, { "function": "", "gene_name": "CYSTM1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H1C7", "name": "COL19A1", "organism": "Homo sapiens", "uniprot_id": "Q9H1C7" }, { "function": "Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mostly by degradation of proteins that access the endocytic route, where they are processed by lysosomal proteases and other hydrolases. Exogenous antigens that have been endocytosed by the APC are thus readily available for presentation via MHC II molecules, and for this reason this antigen presentation pathway is usually referred to as exogenous. As membrane proteins on their way to degradation in lysosomes as part of their normal turn-over are also contained in the endosomal/lysosomal compartments, exogenous antigens must compete with those derived from endogenous components. Autophagy is also a source of endogenous peptides, autophagosomes constitutively fuse with MHC class II loading compartments. In addition to APCs, other cells of the gastrointestinal tract, such as epithelial cells, express MHC class II molecules and CD74 and act as APCs, which is an unusual trait of the GI tract. To produce a MHC class II molecule that presents an antigen, three MHC class II molecules (heterodimers of an alpha and a beta chain) associate with a CD74 trimer in the ER to form a heterononamer. Soon after the entry of this complex into the endosomal/lysosomal system where antigen processing occurs, CD74 undergoes a sequential degradation by various proteases, including CTSS and CTSL, leaving a small fragment termed CLIP (class-II-associated invariant chain peptide). The removal of CLIP is facilitated by HLA-DM via direct binding to the alpha-beta-CLIP complex so that CLIP is released. HLA-DM stabilizes MHC class II molecules until primary high affinity antigenic peptides are bound. The MHC II molecule bound to a peptide is then transported to the cell membrane surface. In B-cells, the interaction between HLA-DM and MHC class II molecules is regulated by HLA-DO. Primary dendritic cells (DCs) also to express HLA-DO. Lysosomal microenvironment has been implicated in the regulation of antigen loading into MHC II molecules, increased acidification produces increased proteolysis and efficient peptide loading", "gene_name": "HLA-DRB4", "glycan_count": 11, "glycosylation_sites": [ { "position": 48, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P13762", "name": "HLA-DOB", "organism": "Homo sapiens", "uniprot_id": "P13762" }, { "function": "Multifunctional protein that may affect its functions by regulating the activity of small GTPases, such as RAC1 and RALA (PubMed:12919680, PubMed:25074804, PubMed:26158537, PubMed:28869598). Required for normal progress through the cell cycle, both during interphase and during mitosis (PubMed:12919680, PubMed:23388455, PubMed:26158537). Required for the presence of normal levels of MAD2L1, AURKB and BIRC5 on inner centromeres during mitosis, and for normal attachment of kinetochores to mitotic spindles (PubMed:12919680, PubMed:26158537). Required for normal organization of the microtubule cytoskeleton in interphase cells (PubMed:23388455). Functions as guanine nucleotide exchange factor (GEF) for RALA (PubMed:26158537). Interferes with the activation of RAC1 by guanine nucleotide exchange factors (PubMed:25074804). Prevents accumulation of active, GTP-bound RAC1, and suppresses RAC1-mediated reorganization of the actin cytoskeleton and formation of membrane protrusions (PubMed:25074804, PubMed:28869598). Required for normal cellular responses to contacts with the extracellular matrix of adjacent cells, and for directional cell migration in response to a fibronectin gradient (in vitro) (PubMed:25074804, PubMed:28869598)", "gene_name": "RCC2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NPV8", "name": "Serum amyloid A4 (SAA4)", "organism": "Homo sapiens", "uniprot_id": "Q9P258" }, { "function": "Precursor of the catalytic component of the C3 and C5 convertase complexes, which are part of the complement pathway, a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system (PubMed:12878586, PubMed:17027507, PubMed:18204047, PubMed:39914456). Component C2 is part of the classical, lectin and GZMK complement systems (PubMed:12878586, PubMed:17027507, PubMed:18204047, PubMed:39914456)", "gene_name": "C2", "glycan_count": 55, "glycosylation_sites": [ { "position": 29, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 112, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 290, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 333, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 467, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 471, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 621, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 651, "type": "N-linked (GlcNAc...) (complex) asparagine" } ], "id": "P06681", "name": "Complement C2", "organism": "Homo sapiens", "uniprot_id": "P06681" }, { "function": "Receptor tyrosine kinase involved in nervous system and probably heart development. Upon binding of its ligand NTF3/neurotrophin-3, NTRK3 autophosphorylates and activates different signaling pathways, including the phosphatidylinositol 3-kinase/AKT and the MAPK pathways, that control cell survival and differentiation", "gene_name": "NTRK3", "glycan_count": 2, "glycosylation_sites": [ { "position": 72, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 79, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 133, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 163, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 203, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 218, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 232, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 259, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 267, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 272, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 294, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 375, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 388, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q16288", "name": "NTRK3", "organism": "Homo sapiens", "uniprot_id": "Q16288" }, { "function": "Acts as a transcriptional repressor (PubMed:17974029). Has mitogenic activity for fibroblasts (PubMed:11751870, PubMed:26845719). Heparin-binding protein (PubMed:15491618)", "gene_name": "HDGF", "glycan_count": 1, "glycosylation_sites": [], "id": "P51858", "name": "HDGF", "organism": "Homo sapiens", "uniprot_id": "P51858" }, { "function": "Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products", "gene_name": "ALAS1", "glycan_count": 1, "glycosylation_sites": [], "id": "P13196", "name": "ALAS1", "organism": "Homo sapiens", "uniprot_id": "P13196" }, { "function": "Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products (PubMed:14643893, PubMed:21252495, PubMed:21309041, PubMed:21653323, PubMed:32499479, PubMed:34492704). Contributes significantly to heme formation during erythropoiesis (PubMed:2050125)", "gene_name": "ALAS2", "glycan_count": 0, "glycosylation_sites": [], "id": "P22557", "name": "ALAS2", "organism": "Homo sapiens", "uniprot_id": "P22557" }, { "function": "Uniporter that mediates the transport of extracellular choline and ethanolamine into cells, thereby playing a key role in phospholipid biosynthesis (PubMed:37100056, PubMed:38693265, PubMed:38778100, PubMed:39306721). Choline and ethanolamine are the precursors of phosphatidylcholine and phosphatidylethanolamine, respectively, the two most abundant phospholipids (PubMed:38693265, PubMed:38778100). Transport is not coupled with proton transport and is exclusively driven by the choline (or ethanolamine) gradient across the plasma membrane (PubMed:38693265, PubMed:38778100). Also acts as a heme b transporter that mediates heme efflux from the cytoplasm to the extracellular compartment (PubMed:15369674, PubMed:20610401, PubMed:22483575, PubMed:23187127, PubMed:27923065)", "gene_name": "FLVCR1", "glycan_count": 1, "glycosylation_sites": [ { "position": 265, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y5Y0", "name": "Flvcr1a", "organism": "Homo sapiens", "uniprot_id": "Q9Y5Y0" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02452 (type I)", "name": "Collagen", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02468 (alpha-1)", "name": "Laminin", "organism": "", "uniprot_id": "" }, { "function": "Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [ { "position": 134, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 150, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 908, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 986, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P03314", "name": "Envelope protein E (Flavivirus)", "organism": "Yellow fever virus (strain 17D vaccine)", "uniprot_id": "P03314" }, { "function": "Receptor for platelet activating factor, a chemotactic phospholipid mediator that possesses potent inflammatory, smooth-muscle contractile and hypotensive activity. Seems to mediate its action via a G protein that activates a phosphatidylinositol-calcium second messenger system", "gene_name": "PTAFR", "glycan_count": 0, "glycosylation_sites": [ { "position": 169, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P25105", "name": "Platelet-activating factor receptor (PAFR)", "organism": "Homo sapiens", "uniprot_id": "P25105" }, { "function": "Metastasis suppressor protein in malignant melanomas and in some breast cancers. May regulate events downstream of cell-matrix adhesion, perhaps involving cytoskeletal reorganization. Generates a C-terminally amidated peptide, metastin which functions as the endogenous ligand of the G-protein coupled receptor GPR54. Activation of the receptor inhibits cell proliferation and cell migration, key characteristics of tumor metastasis. Kp-10 is a decapeptide derived from the primary translation product, isolated in conditioned medium of first trimester trophoblast. Kp-10, but not other kisspeptins, increased intracellular Ca(2+) levels in isolated first trimester trophoblasts. Kp-10 is a paracrine/endocrine regulator in fine-tuning trophoblast invasion generated by the trophoblast itself. The receptor is also essential for normal gonadotropin-released hormone physiology and for puberty. The hypothalamic KiSS1/GPR54 system is a pivotal factor in central regulation of the gonadotropic axis at puberty and in adulthood", "gene_name": "KISS1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q15726", "name": "Kisspeptin", "organism": "Homo sapiens", "uniprot_id": "Q15726" }, { "function": "High affinity receptor for N-formyl-methionyl peptides (fMLP), which are powerful neutrophil chemotactic factors (PubMed:10514456, PubMed:15153520, PubMed:2161213, PubMed:2176894). Binding of fMLP to the receptor stimulates intracellular calcium mobilization and superoxide anion release (PubMed:15153520, PubMed:15210802, PubMed:1712023, PubMed:2161213). This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system (PubMed:10514456, PubMed:1712023). Receptor for TAFA4, mediates its effects on chemoattracting macrophages, promoting phagocytosis and increasing ROS release (PubMed:25109685). Receptor for cathepsin CTSG, leading to increased phagocyte chemotaxis (PubMed:15210802)", "gene_name": "FPR1", "glycan_count": 0, "glycosylation_sites": [ { "position": 4, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 10, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P21462", "name": "FMLP receptor (FPR1)", "organism": "Homo sapiens", "uniprot_id": "P21462" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8X6Y9", "name": "Pneumolysin (PLY)", "organism": "Escherichia coli O157:H7", "uniprot_id": "Q7AEZ5" }, { "function": "Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types", "gene_name": "CDH6", "glycan_count": 79, "glycosylation_sites": [ { "position": 49, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 255, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 399, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 437, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 455, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 536, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P55285", "name": "Cadherin-6 (CDH6)", "organism": "Homo sapiens", "uniprot_id": "P55285" }, { "function": "Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence or presence of hormone ligand, acts mainly as an activator of gene expression due to weak binding to corepressors (PubMed:12554770). The RXRA/RARB heterodimer can act as a repressor on the DR1 element and as an activator on the DR5 element (PubMed:29021580). In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function (By similarity)", "gene_name": "RARB", "glycan_count": 2, "glycosylation_sites": [], "id": "P10826", "name": "Retinoic acid receptor beta (RAR-\u03b2)", "organism": "Homo sapiens", "uniprot_id": "P10826" }, { "function": "Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence of ligand, acts mainly as an activator of gene expression due to weak binding to corepressors. Required for limb bud development. In concert with RARA or RARB, required for skeletal growth, matrix homeostasis and growth plate function (By similarity)", "gene_name": "RARG", "glycan_count": 0, "glycosylation_sites": [], "id": "P13631", "name": "Retinoic acid receptor gamma (RAR-\u03b3)", "organism": "Homo sapiens", "uniprot_id": "P13631" }, { "function": "Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Acts synergistically with MAP3K13 to regulate the activation of NF-kappa-B in the cytosol (By similarity). Required for the maintenance of physical strength (By similarity)", "gene_name": "Prdx3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Z0V6", "name": "CYP7A1", "organism": "Rattus norvegicus", "uniprot_id": "Q9Z0V6" }, { "function": "Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation", "gene_name": "Prdx4", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Z0V5", "name": "CYP8B1", "organism": "Rattus norvegicus", "uniprot_id": "Q9Z0V5" }, { "function": "As a component of the hypothalamic-pituitary-thyroid axis, it controls the secretion of thyroid-stimulating hormone (TSH) and is involved in thyroid hormone synthesis regulation. It also operates as modulator of hair growth. It promotes hair-shaft elongation, prolongs the hair cycle growth phase (anagen) and antagonizes its termination (catagen) by TGFB2. It stimulates proliferation and inhibits apoptosis of hair matrix keratinocytes", "gene_name": "TRH", "glycan_count": 0, "glycosylation_sites": [], "id": "P20396", "name": "Thyrotropin-releasing hormone (TRH)", "organism": "Homo sapiens", "uniprot_id": "P20396" }, { "function": "Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues. Fibrillin-1-containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus where they provide tensile strength and have anchoring roles. Fibrillin-1 also plays a key role in tissue homeostasis through specific interactions with growth factors, such as the bone morphogenetic proteins (BMPs), growth and differentiation factors (GDFs) and latent transforming growth factor-beta-binding proteins (LTBPs), cell-surface integrins and other extracellular matrix protein and proteoglycan components (By similarity). Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively (PubMed:20855508). Negatively regulates osteoclastogenesis by binding and sequestering an osteoclast differentiation and activation factor TNFSF11. This leads to disruption of TNFSF11-induced Ca(2+) signaling and impairment of TNFSF11-mediated nuclear translocation and activation of transcription factor NFATC1 which regulates genes important for osteoclast differentiation and function (PubMed:24039232). Mediates cell adhesion via its binding to cell surface receptors integrins ITGAV:ITGB3 and ITGA5:ITGB1. Binds heparin and this interaction plays an important role in the assembly of microfibrils (By similarity)", "gene_name": "Fbn1", "glycan_count": 5, "glycosylation_sites": [ { "position": 268, "type": "O-linked (Glc) serine" }, { "position": 450, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 473, "type": "O-linked (Glc) serine" }, { "position": 512, "type": "O-linked (Glc) serine" }, { "position": 1069, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1137, "type": "O-linked (Glc) serine" }, { "position": 1151, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1220, "type": "O-linked (Glc) serine" }, { "position": 1304, "type": "O-linked (Glc) serine" }, { "position": 1347, "type": "O-linked (Glc) serine" }, { "position": 1371, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1388, "type": "O-linked (Glc) serine" }, { "position": 1486, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1510, "type": "O-linked (Glc) serine" }, { "position": 1583, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1630, "type": "O-linked (Glc) serine" }, { "position": 1671, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1705, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1715, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1832, "type": "O-linked (Glc) serine" }, { "position": 1873, "type": "O-linked (Glc) serine" }, { "position": 1904, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1913, "type": "O-linked (Glc) serine" }, { "position": 1955, "type": "O-linked (Glc) serine" }, { "position": 2037, "type": "O-linked (Glc) serine" }, { "position": 2079, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2150, "type": "O-linked (Glc) serine" }, { "position": 2180, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2229, "type": "O-linked (Glc) serine" }, { "position": 2315, "type": "O-linked (Glc) serine" }, { "position": 2467, "type": "O-linked (Glc) serine" }, { "position": 2549, "type": "O-linked (Glc) serine" }, { "position": 2630, "type": "O-linked (Glc) serine" }, { "position": 2736, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2752, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 2769, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q61554", "name": "Adiponectin", "organism": "Mus musculus", "uniprot_id": "Q61554" }, { "function": "Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex)", "gene_name": "Psma5", "glycan_count": 1, "glycosylation_sites": [ { "position": 198, "type": "O-linked (GlcNAc) serine" } ], "id": "Q9Z2U1", "name": "Acyl-CoA oxidase 1 (ACO1)", "organism": "Mus musculus", "uniprot_id": "Q9Z2U1" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O88475", "name": "Sterol regulatory element-binding protein 2 (SREBP2)", "organism": "", "uniprot_id": "O88475" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P19838 (p65 subunit)", "name": "NF-\u03baB", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P31749 (AKT1)", "name": "AKT", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01857 (heavy chain)", "name": "Immunoglobulin G (IgG)", "organism": "", "uniprot_id": "" }, { "function": "Guanylyl cyclase that catalyzes synthesis of cyclic GMP (cGMP) from GTP (PubMed:11950846, PubMed:1718270, PubMed:22436048, PubMed:22521417, PubMed:23269669). Receptor for the E.coli heat-stable enterotoxin; E.coli enterotoxin markedly stimulates the accumulation of cGMP in mammalian cells expressing GUCY2C (PubMed:1680854, PubMed:1718270). Also activated by the endogenous peptides guanylin and uroguanylin (PubMed:8381596)", "gene_name": "GUCY2C", "glycan_count": 1, "glycosylation_sites": [ { "position": 32, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 75, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 79, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 195, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 284, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 307, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 345, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 402, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P25092", "name": "Guanylyl Cyclase C (GCC)", "organism": "Homo sapiens", "uniprot_id": "P25092" }, { "function": "Responsible for the post-translational oxidative deamination of peptidyl lysine residues in precursors to fibrous collagen and elastin (PubMed:26838787). Regulator of Ras expression. May play a role in tumor suppression. Plays a role in the aortic wall architecture (By similarity)", "gene_name": "LOX", "glycan_count": 32, "glycosylation_sites": [ { "position": 81, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 97, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 144, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P28300", "name": "LOX", "organism": "Homo sapiens", "uniprot_id": "P28300" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6NRJ9", "name": "TIGIT", "organism": "", "uniprot_id": "" }, { "function": "Functions as a transport protein in the blood stream. Binds various ligands in the interior of its beta-barrel domain (By similarity). Appears to function in modulating the activity of the immune system during the acute-phase reaction (By similarity)", "gene_name": "ORM1", "glycan_count": 48, "glycosylation_sites": [ { "position": 34, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 57, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 94, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 136, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q3SZR3", "name": "Bovine Lactoferrin (bLf)", "organism": "Bos taurus", "uniprot_id": "Q3SZR3" }, { "function": "S1 region attaches the virion to the cell membrane by interacting with host ANPEP/aminopeptidase N, initiating the infection. Binding to the receptor probably induces conformational changes in the S glycoprotein unmasking the fusion peptide of S2 region and activating membranes fusion. S2 region belongs to the class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes", "gene_name": "S", "glycan_count": 0, "glycosylation_sites": [], "id": "P15423", "name": "HCoV-229E Spike Protein (S)", "organism": "Human coronavirus 229E", "uniprot_id": "P15423" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6FGU6", "name": "67 kDa laminin receptor", "organism": "", "uniprot_id": "" }, { "function": "Uniport that mediates the transport of neutral amino acids such as L-leucine, L-isoleucine, L-valine, and L-phenylalanine (PubMed:12930836). The transport activity is sodium ions-independent, electroneutral and mediated by a facilitated diffusion (PubMed:12930836)", "gene_name": "SLC43A1", "glycan_count": 1, "glycosylation_sites": [ { "position": 57, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 212, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 229, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O75387", "name": "Organic Anion Transporter 3 (OAT3/SLC22A8)", "organism": "Homo sapiens", "uniprot_id": "O75387" }, { "function": "Non-receptor tyrosine kinase involved in various processes such as cell growth, development, or differentiation. Mediates essential signaling events in both innate and adaptive immunity and plays a crucial role in hematopoiesis during T-cells development. In the cytoplasm, plays a pivotal role in signal transduction via its association with type I receptors sharing the common subunit gamma such as IL2R, IL4R, IL7R, IL9R, IL15R and IL21R. Following ligand binding to cell surface receptors, phosphorylates specific tyrosine residues on the cytoplasmic tails of the receptor, creating docking sites for STATs proteins. Subsequently, phosphorylates the STATs proteins once they are recruited to the receptor. Phosphorylated STATs then form homodimer or heterodimers and translocate to the nucleus to activate gene transcription. For example, upon IL2R activation by IL2, JAK1 and JAK3 molecules bind to IL2R beta (IL2RB) and gamma chain (IL2RG) subunits inducing the tyrosine phosphorylation of both receptor subunits on their cytoplasmic domain. Then, STAT5A and STAT5B are recruited, phosphorylated and activated by JAK1 and JAK3. Once activated, dimerized STAT5 translocates to the nucleus and promotes the transcription of specific target genes in a cytokine-specific fashion", "gene_name": "JAK3", "glycan_count": 1, "glycosylation_sites": [], "id": "P52333", "name": "JAK3 (Janus kinase 3)", "organism": "Homo sapiens", "uniprot_id": "P52333" }, { "function": "Non-receptor tyrosine-protein kinase that plays an essential role in the selection and maturation of developing T-cells in the thymus and in the function of mature T-cells. Plays a key role in T-cell antigen receptor (TCR)-linked signal transduction pathways. Constitutively associated with the cytoplasmic portions of the CD4 and CD8 surface receptors. Association of the TCR with a peptide antigen-bound MHC complex facilitates the interaction of CD4 and CD8 with MHC class II and class I molecules, respectively, thereby recruiting the associated LCK protein to the vicinity of the TCR/CD3 complex. LCK then phosphorylates tyrosine residues within the immunoreceptor tyrosine-based activation motifs (ITAM) of the cytoplasmic tails of the TCR-gamma chains and CD3 subunits, initiating the TCR/CD3 signaling pathway. Once stimulated, the TCR recruits the tyrosine kinase ZAP70, that becomes phosphorylated and activated by LCK. Following this, a large number of signaling molecules are recruited, ultimately leading to lymphokine production. LCK also contributes to signaling by other receptor molecules. Associates directly with the cytoplasmic tail of CD2, which leads to hyperphosphorylation and activation of LCK. Also plays a role in the IL2 receptor-linked signaling pathway that controls the T-cell proliferative response. Binding of IL2 to its receptor results in increased activity of LCK. Is expressed at all stages of thymocyte development and is required for the regulation of maturation events that are governed by both pre-TCR and mature alpha beta TCR. Phosphorylates other substrates including RUNX3, PTK2B/PYK2, the microtubule-associated protein MAPT, RHOH or TYROBP. Interacts with FYB2 (PubMed:27335501)", "gene_name": "LCK", "glycan_count": 1, "glycosylation_sites": [], "id": "P06239", "name": "Lck (Lymphocyte-specific protein tyrosine kinase)", "organism": "Homo sapiens", "uniprot_id": "P06239" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P11802/P24941", "name": "CDK4/6 (Cyclin-dependent kinases 4/6)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03437 (H1 subtype)", "name": "Hemagglutinin (HA)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03466 (N1 subtype)", "name": "Neuraminidase (NA)", "organism": "", "uniprot_id": "" }, { "function": "Receptor for the chemotactic and inflammatory peptide anaphylatoxin C3a. This receptor stimulates chemotaxis, granule enzyme release and superoxide anion production", "gene_name": "C3AR1", "glycan_count": 2, "glycosylation_sites": [ { "position": 9, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 194, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 266, "type": "O-linked (GalNAc...) serine" } ], "id": "Q16581", "name": "C3a Receptor", "organism": "Homo sapiens", "uniprot_id": "Q16581" }, { "function": "Forms pH-gated heterotrimeric sodium channels that act as postsynaptic excitatory receptors in the nervous system (PubMed:10842183, PubMed:11587714, PubMed:9744806, PubMed:9886053). Upon extracellular acidification, these channels generate a biphasic current with a fast inactivating and a slow sustained phase (PubMed:10842183, PubMed:9744806, PubMed:9886053). ASIC3 is more sensitive to protons and gates between closed, open, and desensitized states faster than other ASICs (By similarity). Displays high selectivity for sodium ions but can also permit the permeation of other cations (PubMed:9744806, PubMed:9886053). As a neuronal acid sensor, probably contributes to mechanoreception, acid nociception, and heat nociception (By similarity). By forming heterotrimeric channels with ASIC2, generates a biphasic current with a fast inactivating and a slow sustained phase, which in sensory neurons is proposed to mediate the pain induced by acidosis that occurs in ischemic, damaged or inflamed tissues (By similarity)", "gene_name": "ASIC3", "glycan_count": 1, "glycosylation_sites": [ { "position": 175, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 398, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UHC3", "name": "Endostatin", "organism": "Homo sapiens", "uniprot_id": "Q9UHC3" }, { "function": "In epithelial cells, the heterodimer gE/gI is required for the cell-to-cell spread of the virus, by sorting nascent virions to cell junctions. Once the virus reaches the cell junctions, virus particles can spread to adjacent cells extremely rapidly through interactions with cellular receptors that accumulate at these junctions. Implicated in basolateral spread in polarized cells (By similarity). In neuronal cells, gE/gI is essential for the anterograde spread of the infection throughout the host nervous system. Together with US9, the heterodimer gE/gI is involved in the sorting and transport of viral structural components toward axon tips", "gene_name": "gE", "glycan_count": 0, "glycosylation_sites": [ { "position": 124, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 243, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P04488", "name": "HSV glycoprotein D (gD)", "organism": "Human herpesvirus 1 (strain 17)", "uniprot_id": "P04488" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P0DTC2 (variant)", "name": "SARS-CoV-2 Spike Glycoprotein (Beta Variant, B.1.351)", "organism": "", "uniprot_id": "" }, { "function": "D-mannose specific lectin (PubMed:2792084). Displays antiviral activity and therefore may contribute to defense against infections (PubMed:7481093)", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [ { "position": 152, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P02866", "name": "ConA", "organism": "Canavalia ensiformis", "uniprot_id": "P02866" }, { "function": "Endoplasmic reticulum membrane sensor that translocates into the nucleus in response to various stresses to act as a transcription factor (PubMed:20932482, PubMed:24448410). Constitutes a precursor of the transcription factor NRF1 (By similarity). Able to detect various cellular stresses, such as cholesterol excess, oxidative stress or proteasome inhibition (PubMed:20932482). In response to stress, it is released from the endoplasmic reticulum membrane following cleavage by the protease DDI2 and translocates into the nucleus to form the transcription factor NRF1 (By similarity). Acts as a key sensor of cholesterol excess: in excess cholesterol conditions, the endoplasmic reticulum membrane form of the protein directly binds cholesterol via its CRAC motif, preventing cleavage and release of the transcription factor NRF1, thereby allowing expression of genes promoting cholesterol removal, such as CD36 (By similarity). Involved in proteasome homeostasis: in response to proteasome inhibition, it is released from the endoplasmic reticulum membrane, translocates to the nucleus and activates expression of genes encoding proteasome subunits (PubMed:20932482)", "gene_name": "NFE2L1", "glycan_count": 1, "glycosylation_sites": [ { "position": 348, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 360, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 412, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 423, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q14494", "name": "Nrf1 (Nuclear factor erythroid 2 related factor-1)", "organism": "Homo sapiens", "uniprot_id": "Q14494" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q66299", "name": "HCV E2 glycoprotein", "organism": "Norovirus isolates", "uniprot_id": "Q66299" }, { "function": "Nuclear receptor that exhibits a ligand-dependent transcriptional activation activity (PubMed:25661920). Binds preferentially to double-stranded oligonucleotide direct repeats having the consensus half-site sequence 5'-AGGTCA-3' and 4-nt spacing (DR-4). Regulates cholesterol uptake through MYLIP-dependent ubiquitination of LDLR, VLDLR and LRP8; DLDLR and LRP8. Interplays functionally with RORA for the regulation of genes involved in liver metabolism (By similarity). Induces LPCAT3-dependent phospholipid remodeling in endoplasmic reticulum (ER) membranes of hepatocytes, driving SREBF1 processing and lipogenesis (By similarity). Via LPCAT3, triggers the incorporation of arachidonate into phosphatidylcholines of ER membranes, increasing membrane dynamics and enabling triacylglycerols transfer to nascent very low-density lipoprotein (VLDL) particles (By similarity). Via LPCAT3 also counteracts lipid-induced ER stress response and inflammation, likely by modulating SRC kinase membrane compartmentalization and limiting the synthesis of lipid inflammatory mediators (By similarity). Plays an anti-inflammatory role during the hepatic acute phase response by acting as a corepressor: inhibits the hepatic acute phase response by preventing dissociation of the N-Cor corepressor complex (PubMed:20159957)", "gene_name": "NR1H2", "glycan_count": 1, "glycosylation_sites": [], "id": "P55055", "name": "LXR\u03b1 (Liver X receptor alpha)", "organism": "Homo sapiens", "uniprot_id": "P55055" }, { "function": "Aspartic protease that mediates the cleavage of NFE2L1/NRF1 at 'Leu-104', thereby promoting release of NFE2L1/NRF1 from the endoplasmic reticulum membrane (PubMed:27528193, PubMed:27676298). Ubiquitination of NFE2L1/NRF1 is a prerequisite for cleavage, suggesting that DDI2 specifically recognizes and binds ubiquitinated NFE2L1/NRF1 (PubMed:27528193). Seems to act as a proteasomal shuttle which links the proteasome and replication fork proteins like RTF2 (Probable). Required, with DDI1, for cellular survival following replication stress. Together or redudantly with DDI1, removes RTF2 from stalled forks to allow cell cycle progression after replication stress and maintains genome integrity (PubMed:29290612)", "gene_name": "DDI2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q5TDH0", "name": "DDI2 (DNA damage inducible 1 homolog 2)", "organism": "Homo sapiens", "uniprot_id": "Q5TDH0" }, { "function": "Cold-inducible mRNA binding protein that plays a protective role in the genotoxic stress response by stabilizing transcripts of genes involved in cell survival. Acts as a translational activator. Seems to play an essential role in cold-induced suppression of cell proliferation. Binds specifically to the 3'-untranslated regions (3'-UTRs) of stress-responsive transcripts RPA2 and TXN. Acts as a translational repressor (By similarity). Promotes assembly of stress granules (SGs), when overexpressed", "gene_name": "CIRBP", "glycan_count": 1, "glycosylation_sites": [], "id": "Q14011", "name": "CIRP", "organism": "Homo sapiens", "uniprot_id": "Q14011" }, { "function": "", "gene_name": "gag", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9QFQ2", "name": "GP64", "organism": "Human immunodeficiency virus type 1", "uniprot_id": "Q9QFQ2" }, { "function": "", "gene_name": "gag", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9QFQ1", "name": "F protein", "organism": "Human immunodeficiency virus type 1", "uniprot_id": "Q9QFQ1" }, { "function": "Sulfur-rich seed storage protein", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P06471", "name": "Polyhedrin", "organism": "Hordeum vulgare", "uniprot_id": "P06471" }, { "function": "", "gene_name": "gag", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9QFQ0", "name": "Granulin", "organism": "Human immunodeficiency virus type 1", "uniprot_id": "Q9QFQ0" }, { "function": "Multifunctional regulator of the expression of viral genes that contributes to the shutoff of host protein synthesis and mediates nuclear export of viral intronless mRNAs. Early in infection, this immediate early (EI) protein mediates the inhibition of cellular splicing. This results in the accumulation of unprocessed 3'end pre-mRNAs which can't be exported from the nucleus. Cellular protein synthesis is thereby shut off early after virus infection. Later in the infection, it helps recruit cellular RNA polymerase II to viral replication sites and promotes the nuclear export of viral intronless mRNAs by interacting with mRNAs and host NXF1/TAP. ICP27 binds to NUP62 which may provide facilitated viral mRNA export and may indirectly compete with some host cell transport receptors for binding and inhibit cellular nucleocytoplasmic transport pathways (PubMed:22334672). Also stimulates translation of viral transcripts. Repression of host gene expression blocks the cell cycle at the G1 phase and prevents apoptosis. Seems to silence the 3' splice site of the promyelocytic leukemia (PML) intron 7a, thereby switching PML isoforms from PML-II to PML-V. This could be linked to the accelerated mRNA export induced by ICP27 which might not provide sufficient time for PML pre-mRNA to be spliced in the nucleus", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P10238", "name": "ICP4", "organism": "Human herpesvirus 1 (strain 17)", "uniprot_id": "P10238" }, { "function": "Multifunctional serine/threonine kinase that plays a role in several processes including egress of virus particles from the nucleus, modulation of the actin cytoskeleton and inhibition of host immune response. Phosphorylates UL31 and UL34, two critical regulators of capsid budding from nucleus to endoplasmic reticulum, thereby facilitating virion egress. Modulates and redistributes host components of the nuclear envelope, including LMNA, emerin/EMD and the nuclear matrix protein MATR3. In turn, facilitates nuclear pore impairment and capsid release through impaired nuclear envelope. Phosphorylates envelope glycoprotein B (gB), probably to direct it to the cell surface. Promotes virus intracellular spread by restructuring host cell cytoskeleton. Blocks host apoptosis to extend cell survival and allow efficient viral replication. Promotes viral gene expression by phosphorylating host HDAC2 to reduce viral genome silencing. Strongly inhibits TCR-activated signal transduction in T-cells by reducing the ubiquitination of LAT and TRAF6, leading to a suboptimal activation of LAT. Subverts host antiviral innate immunity by inhibiting type I interferon production through hyperphosphorylation of beta-catenin/CTNNB1. In addition, phosphorylates the RNA sensor RIGI and the transcription factor IRF3 to prevent the RLR-mediated antiviral signaling pathway. Hyperphosphorylates host RELA and thereby dampens NF-kappa-B signaling. Acts as an immunoevasin partly responsible for inhibition of MR1 expression and antigen presentation in response to bacterial infection", "gene_name": "US3", "glycan_count": 0, "glycosylation_sites": [], "id": "P13287", "name": "\u03b334.5 (ICP34.5)", "organism": "Human herpesvirus 2 (strain HG52)", "uniprot_id": "P13287" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P05366 (SAA1)", "name": "Serum Amyloid A (SAA) protein family", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02671 (human, inferred)", "name": "Fibrinogen", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P07686 (HEXB_HUMAN)", "name": "\u03b2-hexosaminidase (Hex\u03b2)", "organism": "", "uniprot_id": "" }, { "function": "Member of the eIF2 complex that functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA (PubMed:16289705, PubMed:38340717). This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S pre-initiation complex (43S PIC) (PubMed:16289705). Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF2 and release of an eIF2-GDP binary complex (PubMed:16289705). In order for eIF2 to recycle and catalyze another round of initiation, the GDP bound to eIF2 must exchange with GTP by way of a reaction catalyzed by eIF2B (PubMed:16289705). EIF2S1/eIF2-alpha is a key component of the integrated stress response (ISR), required for adaptation to various stress: phosphorylation by metabolic-stress sensing protein kinases (EIF2AK1/HRI, EIF2AK2/PKR, EIF2AK3/PERK and EIF2AK4/GCN2) in response to stress converts EIF2S1/eIF2-alpha in a global protein synthesis inhibitor, leading to an attenuation of cap-dependent translation, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activators ATF4 and QRICH1, and hence allowing ATF4- and QRICH1-mediated reprogramming (PubMed:19131336, PubMed:33384352, PubMed:38340717). EIF2S1/eIF2-alpha also acts as an activator of mitophagy in response to mitochondrial damage: phosphorylation by EIF2AK1/HRI promotes relocalization to the mitochondrial surface, thereby triggering PRKN-independent mitophagy (PubMed:38340717)", "gene_name": "EIF2S1", "glycan_count": 1, "glycosylation_sites": [], "id": "P05198", "name": "eIF2\u03b1", "organism": "Homo sapiens", "uniprot_id": "P05198" }, { "function": "The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle", "gene_name": "PDHA1", "glycan_count": 1, "glycosylation_sites": [], "id": "P08559", "name": "Cleaved PARP", "organism": "Homo sapiens", "uniprot_id": "P08559" }, { "function": "Involved in calcium binding and microtubule stabilization (PubMed:12167714, PubMed:15162379, PubMed:15958728). Acts as a negative regulator of TSC22D1-mediated apoptosis, via interaction with and destabilization of TSC22D1 protein (PubMed:18325344)", "gene_name": "TPT1", "glycan_count": 1, "glycosylation_sites": [], "id": "P13693", "name": "TCTP (Translationally Controlled Tumor Protein)", "organism": "Homo sapiens", "uniprot_id": "P13693" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P38936, P46527", "name": "CDK inhibitors (p21, p27)", "organism": "", "uniprot_id": "" }, { "function": "Required for radial migration of cortical neurons in the superficial layer of the neocortex (By similarity). Plays a role in the formation or maintenance of inhibitory synapses. May function by inhibiting the activity of NLGN2", "gene_name": "MDGA1", "glycan_count": 3, "glycosylation_sites": [ { "position": 42, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 90, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 235, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 247, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 257, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 307, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 331, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 432, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 655, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 747, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 826, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8NFP4", "name": "EDEM3", "organism": "Homo sapiens", "uniprot_id": "Q8NFP4" }, { "function": "Transcription factor that plays an essential role in anti-viral immunity. It mediates signaling by type I IFNs (IFN-alpha and IFN-beta). Following type I IFN binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. IRF9/ISGF3G associates with the phosphorylated STAT1:STAT2 dimer to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state", "gene_name": "IRF9", "glycan_count": 0, "glycosylation_sites": [], "id": "Q00978", "name": "IRF9", "organism": "Homo sapiens", "uniprot_id": "Q00978" }, { "function": "Catalyzes the ATP-dependent transport of phospholipids such as phosphatidylcholine and phosphoglycerol from the cytoplasm into the lumen side of lamellar bodies, in turn participates in the lamellar bodies biogenesis and homeostasis of pulmonary surfactant (PubMed:16959783, PubMed:17574245, PubMed:27177387, PubMed:28887056, PubMed:31473345). Transports preferentially phosphatidylcholine containing short acyl chains (PubMed:27177387). In addition plays a role as an efflux transporter of miltefosine across macrophage membranes and free cholesterol (FC) through intralumenal vesicles by removing FC from the cell as a component of surfactant and protects cells from free cholesterol toxicity (PubMed:25817392, PubMed:26903515, PubMed:27177387)", "gene_name": "ABCA3", "glycan_count": 1, "glycosylation_sites": [ { "position": 14, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 53, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 124, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 140, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 620, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 783, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q99758", "name": "ABCA3", "organism": "Homo sapiens", "uniprot_id": "Q99758" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P35247/P34045", "name": "SFTPA1/SFTPA2", "organism": "", "uniprot_id": "" }, { "function": "Secreted signal that acts globally to regulate anterior/posterior axial patterning during development. May play critical roles in patterning both mesodermal and neural tissues (By similarity). It is required for proper vertebral patterning and orofacial development (PubMed:31215115). Signals through activin receptors type-2, ACVR2A and ACVR2B, and activin receptors type-1, ACVR1B, ACVR1C and TGFBR1 leading to the phosphorylation of SMAD2 and SMAD3 (PubMed:28257634)", "gene_name": "GDF11", "glycan_count": 2, "glycosylation_sites": [ { "position": 94, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O95390", "name": "Growth Differentiation Factor 11 (GDF11)", "organism": "Homo sapiens", "uniprot_id": "O95390" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "NPPB_HUMAN (P16860)", "name": "N-terminal pro\u2013B-type natriuretic peptide (NT-proBNP)", "organism": "", "uniprot_id": "" }, { "function": "Receptor for the atrial natriuretic peptide NPPA/ANP and the brain natriuretic peptide NPPB/BNP which are potent vasoactive hormones playing a key role in cardiovascular homeostasis (PubMed:39543315). Plays an essential role in the regulation of endothelial cell senescence and vascular aging (PubMed:36016499). Upon activation by ANP or BNP, stimulates the production of cyclic guanosine monophosphate (cGMP) that promotes vascular tone and volume homeostasis by activation of protein kinase cGMP-dependent 1/PRKG1 and subsequently PRKAA1, thereby controlling blood pressure and maintaining cardiovascular homeostasis (PubMed:36016499)", "gene_name": "NPR1", "glycan_count": 5, "glycosylation_sites": [ { "position": 34, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 45, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 212, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 338, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 379, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 386, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 427, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P16066", "name": "NPRA (Natriuretic Peptide Receptor A)", "organism": "Homo sapiens", "uniprot_id": "P16066" }, { "function": "Receptor for the C-type natriuretic peptide NPPC/CNP hormone. Has guanylate cyclase activity upon binding of its ligand. May play a role in the regulation of skeletal growth", "gene_name": "NPR2", "glycan_count": 0, "glycosylation_sites": [ { "position": 24, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 35, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 161, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 195, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 244, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 277, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 349, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P20594", "name": "NPRB (Natriuretic Peptide Receptor B)", "organism": "Homo sapiens", "uniprot_id": "P20594" }, { "function": "", "gene_name": "DNASE1L1", "glycan_count": 0, "glycosylation_sites": [ { "position": 261, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P49184", "name": "NPRC (Natriuretic Peptide Receptor C)", "organism": "Homo sapiens", "uniprot_id": "P49184" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P35968/P17948/P35916", "name": "VEGFR (Vascular Endothelial Growth Factor Receptor)", "organism": "", "uniprot_id": "" }, { "function": "Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity (PubMed:8666233). Inhibits HSP90AA1 ATPase activity (PubMed:23569206)", "gene_name": "CDC37", "glycan_count": 1, "glycosylation_sites": [], "id": "Q16543", "name": "Cell Division Cycle 37 (Cdc37)", "organism": "Homo sapiens", "uniprot_id": "Q16543" }, { "function": "Transcription factor that play a central role in proper axial mesendoderm morphogenesis and endoderm formation. Required for efficient differentiation of cells from the primitive streak stage to blood, by acting early in the recruitment and/or expansion of mesodermal progenitors to the hemangioblastic and hematopoietic lineages. Also involved in the morphogenesis of the heart and the gut during embryogenesis. Acts as a negative regulator of brachyury expression (By similarity)", "gene_name": "MIXL1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H2W2", "name": "MS4A6A", "organism": "Homo sapiens", "uniprot_id": "Q9H2W2" }, { "function": "", "gene_name": "RPS6KL1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6ZMQ6", "name": "FAM20A", "organism": "Homo sapiens", "uniprot_id": "Q9Y6S9" }, { "function": "3-alpha-hydroxysteroid dehydrogenase that converts 3-alpha-tetrahydroprogesterone (allopregnanolone) to dihydroxyprogesterone and 3-alpha-androstanediol to dihydroxyprogesterone (PubMed:11294878, PubMed:29541409). Also plays a role in the biosynthesis of retinoic acid from retinaldehyde (PubMed:11304534, PubMed:12618084). Can utilize both NADH and NADPH", "gene_name": "DHRS9", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9BPW9", "name": "DHRS9", "organism": "Homo sapiens", "uniprot_id": "Q9BPW9" }, { "function": "May play a role in reproduction", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [ { "position": 108, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 354, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9U6V9", "name": "GP60", "organism": "Polistes annularis", "uniprot_id": "Q9U6V9" }, { "function": "Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development (PubMed:10555141, PubMed:11399089, PubMed:11919202, PubMed:16567415, PubMed:17713477, PubMed:9662389). DNA methylation is coordinated with methylation of histones (PubMed:10555141, PubMed:11399089, PubMed:11919202, PubMed:16567415, PubMed:17713477, PubMed:9662389). It modifies DNA in a non-processive manner and also methylates non-CpG sites (PubMed:10555141, PubMed:11399089, PubMed:11919202, PubMed:16567415, PubMed:17713477, PubMed:9662389). May preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1 (PubMed:18823905). Plays a role in paternal and maternal imprinting (PubMed:15215868). Required for methylation of most imprinted loci in germ cells (PubMed:15215868). Acts as a transcriptional corepressor for ZBTB18 (PubMed:11350943). Recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites (PubMed:20547484). Can actively repress transcription through the recruitment of HDAC activity (PubMed:11350943). Also has weak auto-methylation activity on Cys-706 in absence of DNA (PubMed:21481189)", "gene_name": "Dnmt3a", "glycan_count": 0, "glycosylation_sites": [], "id": "O88508", "name": "Claudin-1", "organism": "Mus musculus", "uniprot_id": "O88508" }, { "function": "Membrane-cytoskeleton-associated protein that promotes the assembly of the spectrin-actin network. Binds to calmodulin", "gene_name": "Add1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9QYC0", "name": "Zo-1 (TJP1)", "organism": "Mus musculus", "uniprot_id": "Q9QYC0" }, { "function": "Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Acts as a suppressor of hepatic gluconeogenesis and glucose output by repressing PPARGC1A transcriptional activity on gluconeogenic genes via its phosphorylation. Phosphorylates PPP2R5B thereby stimulating the assembly of PP2A phosphatase with the PPP2R5B-AKT1 complex leading to dephosphorylation of AKT1. Phosphorylates: PTPN1, SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. Phosphorylates PAGE4 at several serine and threonine residues and this phosphorylation attenuates the ability of PAGE4 to potentiate the transcriptional activator activity of JUN (By similarity)", "gene_name": "Clk2", "glycan_count": 1, "glycosylation_sites": [], "id": "O35491", "name": "HSD11B1", "organism": "Mus musculus", "uniprot_id": "O35491" }, { "function": "Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(o) and JIP. Inhibits G(o)-alpha ATPase activity (By similarity). Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1 (By similarity). By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapses in axons (By similarity). May be involved in copper homeostasis/oxidative stress through copper ion reduction. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV (By similarity). The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons (By similarity). Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1", "gene_name": "App", "glycan_count": 2, "glycosylation_sites": [ { "position": 542, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 571, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P12023", "name": "APP", "organism": "Mus musculus", "uniprot_id": "P12023" }, { "function": "Multifunctional transcription factor that induces cell cycle arrest, DNA repair or apoptosis upon binding to its target DNA sequence (PubMed:19556538, PubMed:20673990, PubMed:22726440). Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Negatively regulates cell division by controlling expression of a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. Its pro-apoptotic activity is activated via its interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 (By similarity). However, this activity is inhibited when the interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 is displaced by PPP1R13L/iASPP (By similarity). In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression (By similarity). Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis, but seems to have to effect on cell-cycle regulation. Regulates the circadian clock by repressing CLOCK-BMAL1-mediated transcriptional activation of PER2 (PubMed:24051492)", "gene_name": "Tp53", "glycan_count": 1, "glycosylation_sites": [], "id": "P02340", "name": "P53", "organism": "Mus musculus", "uniprot_id": "P02340" }, { "function": "Nonheme diiron monooxygenase involved in the biosynthesis of xanthophylls. Specific for beta-ring hydroxylations of beta-carotene. Also has a low activity toward the beta- and epsilon-rings of alpha-carotene. No activity with acyclic carotenoids such as lycopene and neurosporene. Uses ferredoxin as an electron donor", "gene_name": "BETA-OHASE 1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9SZZ8", "name": "KIM-1", "organism": "Arabidopsis thaliana", "uniprot_id": "Q9SZZ8" }, { "function": "", "gene_name": "Ephb3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q60669", "name": "F4/80", "organism": "Mus musculus", "uniprot_id": "Q60669" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P28482/P27361", "name": "ERK1/2 (MAPK1/MAPK3)", "organism": "", "uniprot_id": "" }, { "function": "Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformation. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form of RAF1 (on residues Ser-338 and Ser-339, by PAK1) phosphorylates BAD/Bcl2-antagonist of cell death at 'Ser-75'. Phosphorylates adenylyl cyclases: ADCY2, ADCY5 and ADCY6, resulting in their activation. Phosphorylates PPP1R12A resulting in inhibition of the phosphatase activity. Phosphorylates TNNT2/cardiac muscle troponin T. Can promote NF-kB activation and inhibit signal transducers involved in motility (ROCK2), apoptosis (MAP3K5/ASK1 and STK3/MST2), proliferation and angiogenesis (RB1). Can protect cells from apoptosis also by translocating to the mitochondria where it binds BCL2 and displaces BAD/Bcl2-antagonist of cell death. Regulates Rho signaling and migration, and is required for normal wound healing. Plays a role in the oncogenic transformation of epithelial cells via repression of the TJ protein, occludin (OCLN) by inducing the up-regulation of a transcriptional repressor SNAI2/SLUG, which induces down-regulation of OCLN. Restricts caspase activation in response to selected stimuli, notably Fas stimulation, pathogen-mediated macrophage apoptosis, and erythroid differentiation", "gene_name": "RAF1", "glycan_count": 2, "glycosylation_sites": [], "id": "P04049", "name": "RAF1", "organism": "Homo sapiens", "uniprot_id": "P04049" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q02750/Q9Y243", "name": "MEK1/2", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9R0P9 (mouse)", "name": "ANGPTL2", "organism": "", "uniprot_id": "" }, { "function": "Plus end-directed microtubule-dependent motor protein involved in intracellular transport and regulating various processes such as mannose-6-phosphate receptor (M6PR) transport to the plasma membrane, endosomal sorting during melanosome biogenesis and cytokinesis. Mediates the transport of M6PR-containing vesicles from trans-Golgi network to the plasma membrane via direct interaction with the AP-1 complex. During melanosome maturation, required for delivering melanogenic enzymes from recycling endosomes to nascent melanosomes by creating peripheral recycling endosomal subdomains in melanocytes. Also required for the abscission step in cytokinesis: mediates translocation of ZFYVE26, and possibly TTC19, to the midbody during cytokinesis", "gene_name": "KIF13A", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H1H9", "name": "ITGBL1", "organism": "Homo sapiens", "uniprot_id": "Q9H1H9" }, { "function": "Immune regulatory cytokine that acts as a suppressor of innate inflammatory and immune responses involved in curbing excessive inflammation. Signaling can occur via two mechanisms, intracellularly through nuclear translocation with SMAD3 and extracellularly after secretion and binding to its receptor composed of IL18R1 and IL18RAP. Suppresses, or reduces, pro-inflammatory cytokine production, including IL1A and IL6, as well as CCL12, CSF1, CSF2, CXCL13, IL1B, IL23A and IL1RN, but spares anti-inflammatory cytokines. Inhibits dendritic cell activation", "gene_name": "IL37", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NZH6", "name": "IL-36\u03b3 (Interleukin-36 gamma)", "organism": "Homo sapiens", "uniprot_id": "Q9NZH6" }, { "function": "Modulator of T-cell signaling. Can be either a costimulator of T-cell function, or a coinhibitor, depending on the receptor it binds to. Upon binding to CD226, stimulates T-cell proliferation and cytokine production, including that of IL2, IL5, IL10, IL13, and IFNG. Upon interaction with PVRIG, inhibits T-cell proliferation. These interactions are competitive (PubMed:26755705). Probable cell adhesion protein (PubMed:9657005)", "gene_name": "NECTIN2", "glycan_count": 4, "glycosylation_sites": [ { "position": 137, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 324, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q92692", "name": "Nectin-2", "organism": "Homo sapiens", "uniprot_id": "Q92692" }, { "function": "Beta-1,4-glucuronyltransferase involved in O-mannosylation of alpha-dystroglycan (DAG1) (PubMed:19587235, PubMed:23359570, PubMed:25279697, PubMed:25279699). Transfers a glucuronic acid (GlcA) residue onto a xylose (Xyl) acceptor to produce the glucuronyl-beta-1,4-xylose-beta disaccharide primer, which is further elongated by LARGE1, during synthesis of phosphorylated O-mannosyl glycan (PubMed:25279697, PubMed:25279699). Phosphorylated O-mannosyl glycan is a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity (PubMed:25279697, PubMed:25279699). Required for axon guidance; via its function in O-mannosylation of alpha-dystroglycan (DAG1) (By similarity)", "gene_name": "B4GAT1", "glycan_count": 4, "glycosylation_sites": [ { "position": 204, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 300, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O43505", "name": "B3GAT1 (Beta-1,3-glucuronyltransferase 1)", "organism": "Homo sapiens", "uniprot_id": "O43505" }, { "function": "Receptor with a tyrosine-protein kinase activity (PubMed:10445845, PubMed:20548102, PubMed:30061385). Following activation by ALKAL1 or ALKAL2 ligands at the cell surface, transduces an extracellular signal into an intracellular response (PubMed:30061385, PubMed:34646012). Ligand-binding to the extracellular domain induces tyrosine kinase activation, leading to activation of the mitogen-activated protein kinase (MAPK) pathway (PubMed:20548102). Phosphorylates almost exclusively at the first tyrosine of the Y-x-x-x-Y-Y motif (By similarity). The exact function of this protein is not known; studies with chimeric proteins demonstrate its ability to promote growth and specifically neurite outgrowth, and cell survival (PubMed:18849880, PubMed:9223670). Involved in regulation of the secretory pathway involving endoplasmic reticulum (ER) export sites (ERESs) and ER to Golgi transport (PubMed:20548102)", "gene_name": "LTK", "glycan_count": 1, "glycosylation_sites": [ { "position": 257, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 380, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 412, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P29376", "name": "LTK (Leukocyte receptor tyrosine kinase)", "organism": "Homo sapiens", "uniprot_id": "P29376" }, { "function": "Catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine) (PubMed:11255023, PubMed:20354154, PubMed:34009357, PubMed:34241577). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming queuine, allowing a nucleophilic attack on the C1' of the ribose to form the product (By similarity). Modification of cytoplasmic tRNAs with queuosine controls the elongation speed of cognate codons, thereby ensuring the correct folding of nascent proteins to maintain proteome integrity (PubMed:30093495)", "gene_name": "QTRT1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9BXR0", "name": "NTAQ1 (N-terminal glutamine amidase 1)", "organism": "Homo sapiens", "uniprot_id": "Q9BXR0" }, { "function": "May act as a GTPase-activating protein for Rab family protein(s)", "gene_name": "TBC1D30", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y2I9", "name": "BCL7A (BAF Chromatin Remodelling Complex Subunit BCL7A)", "organism": "Homo sapiens", "uniprot_id": "Q9Y2I9" }, { "function": "Non-receptor protein tyrosine kinase that is involved in the regulation of cell growth and survival, apoptosis, cell-cell adhesion, cytoskeleton remodeling, and differentiation. Stimulation by receptor tyrosine kinases (RTKs) including EGFR, PDGFR, CSF1R and FGFR leads to recruitment of YES1 to the phosphorylated receptor, and activation and phosphorylation of downstream substrates. Upon EGFR activation, promotes the phosphorylation of PARD3 to favor epithelial tight junction assembly. Participates in the phosphorylation of specific junctional components such as CTNND1 by stimulating the FYN and FER tyrosine kinases at cell-cell contacts. Upon T-cell stimulation by CXCL12, phosphorylates collapsin response mediator protein 2/DPYSL2 and induces T-cell migration. Participates in CD95L/FASLG signaling pathway and mediates AKT-mediated cell migration. Plays a role in cell cycle progression by phosphorylating the cyclin-dependent kinase 4/CDK4 thus regulating the G1 phase. Also involved in G2/M progression and cytokinesis. Catalyzes phosphorylation of organic cation transporter OCT2 which induces its transport activity (PubMed:26979622)", "gene_name": "YES1", "glycan_count": 1, "glycosylation_sites": [], "id": "P07947", "name": "YES1", "organism": "Homo sapiens", "uniprot_id": "P07947" }, { "function": "Transcription factor (PubMed:10698492, PubMed:11909962). Directly controls the expression of cytokine and chemokine genes in a wide variety of different cellular contexts (PubMed:20378371). May control the differentiation, survival and proliferation of lymphoid cells (PubMed:20378371). May also regulate angiogenesis through regulation of expression of genes controlling endothelial cell migration and invasion (PubMed:15247905, PubMed:15592518)", "gene_name": "ETS1", "glycan_count": 1, "glycosylation_sites": [], "id": "P14921", "name": "ETS-1", "organism": "Homo sapiens", "uniprot_id": "P14921" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P48357/P80560", "name": "GABA-producing enzyme (GAD1/GAD2)", "organism": "", "uniprot_id": "" }, { "function": "E3 ubiquitin-protein ligase that acts as a negative regulator of many signaling pathways by mediating ubiquitination of cell surface receptors (PubMed:10514377, PubMed:11896602, PubMed:14661060, PubMed:14739300, PubMed:15190072, PubMed:17509076, PubMed:18374639, PubMed:19689429, PubMed:21596750, PubMed:28381567). Accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then transfers it to substrates promoting their degradation by the proteasome (PubMed:10514377, PubMed:14661060, PubMed:14739300, PubMed:17094949, PubMed:17509076, PubMed:17974561). Recognizes activated receptor tyrosine kinases, including KIT, FLT1, FGFR1, FGFR2, PDGFRA, PDGFRB, CSF1R, EPHA8 and KDR and mediates their ubiquitination to terminate signaling (PubMed:15190072, PubMed:18374639, PubMed:21596750). Recognizes membrane-bound HCK, SRC and other kinases of the SRC family and mediates their ubiquitination and degradation (PubMed:11896602). Ubiquitinates EGFR and SPRY2 (PubMed:17094949, PubMed:17974561). Ubiquitinates NECTIN1 following association between NECTIN1 and herpes simplex virus 1/HHV-1 envelope glycoprotein D, leading to NECTIN1 removal from cell surface (PubMed:28381567). Participates in signal transduction in hematopoietic cells. Plays an important role in the regulation of osteoblast differentiation and apoptosis (PubMed:15190072, PubMed:18374639). Essential for osteoclastic bone resorption (PubMed:14739300). The 'Tyr-731' phosphorylated form induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function (PubMed:14739300). May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3. In association with CBLB, required for proper feedback inhibition of ciliary platelet-derived growth factor receptor-alpha (PDGFRA) signaling pathway via ubiquitination and internalization of PDGFRA (By similarity)", "gene_name": "CBL", "glycan_count": 2, "glycosylation_sites": [], "id": "P22681", "name": "CBL", "organism": "Homo sapiens", "uniprot_id": "P22681" }, { "function": "", "gene_name": "MRPL1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9BYD6", "name": "MRPL12", "organism": "Homo sapiens", "uniprot_id": "Q9BYD6" }, { "function": "Hyperpolarization-activated ion channel that are permeable to sodium and potassium ions. Exhibits weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) and in neurons (Ih) (By similarity). Participates in cerebellar mechanisms of motor learning (By similarity). May mediate responses to sour stimuli (PubMed:11675786)", "gene_name": "Hcn1", "glycan_count": 1, "glycosylation_sites": [ { "position": 327, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9JKB0", "name": "Frizzled 2 (Fzd2)", "organism": "Rattus norvegicus", "uniprot_id": "Q9JKB0" }, { "function": "ATP-dependent transporter that catalyzes the transport of a broad-spectrum of porphyrins from the cytoplasm to the extracellular space through the plasma membrane or into the vesicle lumen (PubMed:17661442, PubMed:23792964, PubMed:27507172, PubMed:33007128). May also function as an ATP-dependent importer of porphyrins from the cytoplasm into the mitochondria, in turn may participate in the de novo heme biosynthesis regulation and in the coordination of heme and iron homeostasis during phenylhydrazine stress (PubMed:10837493, PubMed:17006453, PubMed:23792964, PubMed:33007128). May also play a key role in the early steps of melanogenesis producing PMEL amyloid fibrils (PubMed:29940187). In vitro, it confers to cells a resistance to toxic metal such as arsenic and cadmium and against chemotherapeutics agent such as 5-fluorouracil, SN-38 and vincristin (PubMed:21266531, PubMed:25202056, PubMed:31053883). In addition may play a role in the transition metal homeostasis (By similarity)", "gene_name": "ABCB6", "glycan_count": 1, "glycosylation_sites": [ { "position": 6, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NP58", "name": "ICG Transporter (OATP1B3)", "organism": "Homo sapiens", "uniprot_id": "Q9NP58" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P08514 (ITGA2B, CD41), P05106 (ITGB3, CD61)", "name": "CD41/CD61 complex (GPIIb/IIIa, integrin \u03b1IIb\u03b23)", "organism": "", "uniprot_id": "" }, { "function": "Catalytically inactive phosphatase (PubMed:20180778, PubMed:23163895). By binding to G3BP1, inhibits the formation of G3BP1-induced stress granules (PubMed:20180778, PubMed:23163895). Does not act by protecting the dephosphorylation of G3BP1 at 'Ser-149' (PubMed:23163895). Inhibits PTPMT1 phosphatase activity (PubMed:24709986). By inhibiting PTPMT1, positively regulates intrinsic apoptosis (PubMed:21262771). May play a role in the formation of neurites during neuronal development (PubMed:29250526)", "gene_name": "STYXL1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9Y6J8", "name": "AKAP13", "organism": "Homo sapiens", "uniprot_id": "Q9Y6J8" }, { "function": "Phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating protein that modulates actin cytoskeleton remodeling by regulating ARF and RHO family members. Is activated by phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) binding. Can be activated by phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding, albeit with lower efficiency. Acts on ARF6, RAC1, RHOA and CDC42. Plays a role in the internalization of anthrax toxin", "gene_name": "ARAP3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8WWN8", "name": "ARAP2", "organism": "Homo sapiens", "uniprot_id": "Q8WWN8" }, { "function": "Acts as an acyl-protein thioesterase hydrolyzing fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins, GSDMD, GAP43, ZDHHC6 or HRAS (PubMed:21152083, PubMed:28826475). Deacylates GAP43 (PubMed:21152083). Mediates depalmitoylation of ZDHHC6 (PubMed:28826475). Has lysophospholipase activity (PubMed:25301951). Hydrolyzes prostaglandin glycerol esters (PG-Gs) in the following order prostaglandin D2-glycerol ester (PGD2-G) > prostaglandin E2 glycerol ester (PGE2-G) > prostaglandin F2-alpha-glycerol ester (PGF2-alpha-G) (PubMed:25301951). Hydrolyzes 1-arachidonoylglycerol but not 2-arachidonoylglycerol or arachidonoylethanolamide (PubMed:25301951)", "gene_name": "LYPLA2", "glycan_count": 1, "glycosylation_sites": [], "id": "O95372", "name": "BCMA (TNFRSF17)", "organism": "Homo sapiens", "uniprot_id": "O95372" }, { "function": "May affect the movement of lipids in the cytoplasm or allow the binding of lipids to organelles", "gene_name": "APOL2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9BQE5", "name": "OPALIN", "organism": "Homo sapiens", "uniprot_id": "Q9BQE5" }, { "function": "Transcription factor. Binds to the oxygen responsive element of COX4I2 and activates its transcription under hypoxia conditions (4% oxygen), as well as normoxia conditions (20% oxygen) (PubMed:23303788)", "gene_name": "CHCHD2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y6H1", "name": "CHCHD2", "organism": "Homo sapiens", "uniprot_id": "Q9Y6H1" }, { "function": "Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone", "gene_name": "NDUFB6", "glycan_count": 1, "glycosylation_sites": [], "id": "O95139", "name": "NDUFA11", "organism": "Homo sapiens", "uniprot_id": "O95139" }, { "function": "Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules unsing 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix", "gene_name": "COX6A1", "glycan_count": 0, "glycosylation_sites": [], "id": "P12074", "name": "COX8A", "organism": "Homo sapiens", "uniprot_id": "P12074" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P0DTC2 (residues 319-541)", "name": "SARS-CoV-2 Spike RBD", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P59594 (residues 306-527)", "name": "SARS-CoV-1 Spike RBD", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01375/P05231", "name": "Inflammatory cytokines (e.g., TNF-\u03b1, IL-6)", "organism": "", "uniprot_id": "" }, { "function": "Cell surface receptor for the cytokine IL10 that participates in IL10-mediated anti-inflammatory functions, limiting excessive tissue disruption caused by inflammation. Upon binding to IL10, induces a conformational change in IL10RB, allowing IL10RB to bind IL10 as well (PubMed:16982608). In turn, the heterotetrameric assembly complex, composed of two subunits of IL10RA and IL10RB, activates the kinases JAK1 and TYK2 that are constitutively associated with IL10RA and IL10RB respectively (PubMed:12133952). These kinases then phosphorylate specific tyrosine residues in the intracellular domain in IL10RA leading to the recruitment and subsequent phosphorylation of STAT3. Once phosphorylated, STAT3 homodimerizes, translocates to the nucleus and activates the expression of anti-inflammatory genes. In addition, IL10RA-mediated activation of STAT3 inhibits starvation-induced autophagy (PubMed:26962683)", "gene_name": "IL10RA", "glycan_count": 0, "glycosylation_sites": [ { "position": 50, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 74, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 110, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 154, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 177, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 189, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13651", "name": "IL10RA", "organism": "Homo sapiens", "uniprot_id": "Q13651" }, { "function": "May play a role in B-lineage commitment and/or modulation of signaling through the B-cell receptor", "gene_name": "SLAMF8", "glycan_count": 1, "glycosylation_sites": [ { "position": 85, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9P0V8", "name": "SLAMF7", "organism": "Homo sapiens", "uniprot_id": "Q9P0V8" }, { "function": "Chemotactic for resting T-lymphocytes, and eosinophils (PubMed:9104803, PubMed:9365122). Has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes (PubMed:9104803, PubMed:9365122). Is a strong suppressor of colony formation by a multipotential hematopoietic progenitor cell line (PubMed:9104803, PubMed:9365122). Binds to CCR3 (PubMed:9104803, PubMed:9365122)", "gene_name": "CCL24", "glycan_count": 1, "glycosylation_sites": [ { "position": 115, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O00175", "name": "CCL13", "organism": "Homo sapiens", "uniprot_id": "O00175" }, { "function": "Cell surface receptor that plays an important role in the survival, differentiation, and chemotaxis of eosinophils (PubMed:9378992). Acts by forming a heterodimeric receptor with CSF2RB subunit and subsequently binding to interleukin-5 (PubMed:1495999, PubMed:22528658). In unstimulated conditions, interacts constitutively with JAK2. Heterodimeric receptor activation leads to JAK2 stimulation and subsequent activation of the JAK-STAT pathway (PubMed:9516124)", "gene_name": "IL5RA", "glycan_count": 0, "glycosylation_sites": [ { "position": 35, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 131, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 216, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 244, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q01344", "name": "IL5RA", "organism": "Homo sapiens", "uniprot_id": "Q01344" }, { "function": "Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint", "gene_name": "Smc1a", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Z1M9", "name": "NKG2D (KLRK1)", "organism": "Rattus norvegicus", "uniprot_id": "Q9Z1M9" }, { "function": "Phosphorylates specifically ribosomal protein S6. Seems to act downstream of mTOR signaling in response to growth factors and nutrients to promote cell proliferation, cell growth and cell cycle progression in an alternative pathway regulated by MEAK7", "gene_name": "Rps6kb2", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Z1M4", "name": "NKG2A (KLRC1)", "organism": "Mus musculus", "uniprot_id": "Q9Z1M4" }, { "function": "Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate, AA, C20:4(n-6)), with a particular role in the inflammatory response. The cyclooxygenase activity oxygenates AA to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide prostaglandin H2 (PGH2), the precursor of all 2-series prostaglandins and thromboxanes. This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons. Similarly catalyzes successive cyclooxygenation and peroxidation of dihomo-gamma-linoleate (DGLA, C20:3(n-6)) and eicosapentaenoate (EPA, C20:5(n-3)) to corresponding PGH1 and PGH3, the precursors of 1- and 3-series prostaglandins. In an alternative pathway of prostanoid biosynthesis, converts 2-arachidonoyl lysophopholipids to prostanoid lysophopholipids, which are then hydrolyzed by intracellular phospholipases to release free prostanoids. Metabolizes 2-arachidonoyl glycerol yielding the glyceryl ester of PGH2, a process that can contribute to pain response. Generates lipid mediators from n-3 and n-6 polyunsaturated fatty acids (PUFAs) via a lipoxygenase-type mechanism. Oxygenates PUFAs to hydroperoxy compounds and then reduces them to corresponding alcohols. Plays a role in the generation of resolution phase interaction products (resolvins) during both sterile and infectious inflammation. Metabolizes docosahexaenoate (DHA, C22:6(n-3)) to 17R-HDHA, a precursor of the D-series resolvins (RvDs). As a component of the biosynthetic pathway of E-series resolvins (RvEs), converts eicosapentaenoate (EPA, C20:5(n-3)) primarily to 18S-HEPE that is further metabolized by ALOX5 and LTA4H to generate 18S-RvE1 and 18S-RvE2. In vascular endothelial cells, converts docosapentaenoate (DPA, C22:5(n-3)) to 13R-HDPA, a precursor for 13-series resolvins (RvTs) shown to activate macrophage phagocytosis during bacterial infection. In activated leukocytes, contributes to oxygenation of hydroxyeicosatetraenoates (HETE) to diHETES (5,15-diHETE and 5,11-diHETE). Can also use linoleate (LA, (9Z,12Z)-octadecadienoate, C18:2(n-6)) as substrate and produce hydroxyoctadecadienoates (HODEs) in a regio- and stereospecific manner, being (9R)-HODE ((9R)-hydroxy-(10E,12Z)-octadecadienoate) and (13S)-HODE ((13S)-hydroxy-(9Z,11E)-octadecadienoate) its major products (By similarity). During neuroinflammation, plays a role in neuronal secretion of specialized preresolving mediators (SPMs) 15R-lipoxin A4 that regulates phagocytic microglia (By similarity)", "gene_name": "Ptgs2", "glycan_count": 0, "glycosylation_sites": [ { "position": 53, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 130, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 396, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 580, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P35355", "name": "COX-2", "organism": "Rattus norvegicus", "uniprot_id": "P35355" }, { "function": "Nucleolar protein that acts as a modulator of rRNA synthesis. Plays a central role during organogenesis (By similarity)", "gene_name": "WDR55", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H6Y2", "name": "IL-32", "organism": "Homo sapiens", "uniprot_id": "Q9H6Y2" }, { "function": "Low affinity receptor for granulocyte-macrophage colony-stimulating factor. Transduces a signal that results in the proliferation, differentiation, and functional activation of hematopoietic cells", "gene_name": "CSF2RA", "glycan_count": 9, "glycosylation_sites": [ { "position": 46, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 54, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 99, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 123, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 135, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 182, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 195, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 223, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 229, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 272, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 305, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P15509", "name": "CSF2RA", "organism": "Homo sapiens", "uniprot_id": "P15509" }, { "function": "Catalyzes the two-electron oxidation of bromide by hydrogen peroxide and generates hypobromite as a reactive intermediate which mediates the formation of sulfilimine cross-links between methionine and hydroxylysine residues within an uncross-linked collagen IV/COL4A1 NC1 hexamer (PubMed:18929642, PubMed:19590037, PubMed:22842973, PubMed:25708780, PubMed:25713063, PubMed:27697841, PubMed:28154175, PubMed:34679700). In turns, directly contributes to the collagen IV network-dependent fibronectin/FN and laminin assembly, which is required for full extracellular matrix (ECM)-mediated signaling (PubMed:19590037, PubMed:32543734, PubMed:34679700). Thus, sulfilimine cross-links are essential for growth factor-induced cell proliferation and survival in endothelial cells, an event essential to basement membrane integrity (PubMed:32543734). In addition, through the bromide oxidation, may promote tubulogenesis and induce angiogenesis through ERK1/2, Akt, and FAK pathways (PubMed:25713063). Moreover brominates alpha2 collagen IV chain/COL4A2 at 'Tyr-1485' and leads to bromine enrichment of the basement membranes (PubMed:32571911). In vitro, can also catalyze the two-electron oxidation of thiocyanate and iodide and these two substrates could effectively compete with bromide and thus inhibit the formation of sulfilimine bonds (PubMed:28154175). Binds laminins (PubMed:32485152). May play a role in the organization of eyeball structure and lens development during eye development (By similarity)", "gene_name": "PXDN", "glycan_count": 51, "glycosylation_sites": [ { "position": 640, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 699, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 719, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 731, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 865, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 964, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1178, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1280, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1368, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1425, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q92626", "name": "PXDN", "organism": "Homo sapiens", "uniprot_id": "Q92626" }, { "function": "Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins (PubMed:35145029). Ensures the regeneration of ubiquitin at the proteasome (PubMed:18162577, PubMed:28396413). Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell (PubMed:18162577). Required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis (PubMed:19106094). Also serves as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1 (PubMed:19135427). Indispensable for synaptic development and function at neuromuscular junctions (NMJs) (By similarity). Plays a role in the innate immune defense against viruses by stabilizing the viral DNA sensor CGAS and thus inhibiting its autophagic degradation (PubMed:27666593). Inhibits OPTN-mediated selective autophagic degradation of KDM4D and thereby negatively regulates H3K9me2 and H3K9me3 (PubMed:35145029)", "gene_name": "USP14", "glycan_count": 1, "glycosylation_sites": [], "id": "P54578", "name": "USP14", "organism": "Homo sapiens", "uniprot_id": "P54578" }, { "function": "Promotes a prolonged MAP-kinase signaling by neurotrophins through activation of a Rap1-dependent mechanism. Provides a docking site for the CRKL-C3G complex, resulting in Rap1-dependent sustained ERK activation. May play an important role in regulating postsynaptic signal transduction through the syntrophin-mediated localization of receptor tyrosine kinases such as EPHA4. In cooperation with SNTA1 can enhance EPHA4-induced JAK/STAT activation. Plays a role in nerve growth factor (NGF)-induced recruitment of RAPGEF2 to late endosomes and neurite outgrowth. May play a role in neurotrophin- and ephrin-mediated neuronal outgrowth and in axon guidance during neural development and in neuronal regeneration (By similarity). Modulates stress-induced apoptosis of melanoma cells via regulation of the MEK/ERK signaling pathway", "gene_name": "KIDINS220", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9ULH0", "name": "AFDN", "organism": "Homo sapiens", "uniprot_id": "Q9ULH0" }, { "function": "Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix", "gene_name": "MT-CO2", "glycan_count": 1, "glycosylation_sites": [], "id": "P00403", "name": "COXII", "organism": "Homo sapiens", "uniprot_id": "P00403" }, { "function": "Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP)", "gene_name": "PNPO", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NVS9", "name": "NFU1", "organism": "Homo sapiens", "uniprot_id": "Q9NVS9" }, { "function": "SOCS family proteins form part of a classical negative feedback system that regulates cytokine signal transduction. CIS is involved in the negative regulation of cytokines that signal through the JAK-STAT5 pathway such as erythropoietin, prolactin and interleukin 3 (IL3) receptor. Inhibits STAT5 trans-activation by suppressing its tyrosine phosphorylation. May be a substrate-recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity)", "gene_name": "CISH", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NSE2", "name": "MARS2", "organism": "Homo sapiens", "uniprot_id": "Q9NSE2" }, { "function": "This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5", "gene_name": "POR", "glycan_count": 3, "glycosylation_sites": [], "id": "P16435", "name": "Eosinophil peroxidase", "organism": "Homo sapiens", "uniprot_id": "P16435" }, { "function": "Catalyzes the hydrolysis of the 5-position phosphate of phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and phosphatidylinositol-3,4,5-bisphosphate (PtdIns(3,4,5)P3), with the greatest catalytic activity towards PtdIns(4,5)P2 (PubMed:10764818, PubMed:15474001, PubMed:7761412, PubMed:9430698). Able also to hydrolyze the 5-phosphate of inositol 1,4,5-trisphosphate and of inositol 1,3,4,5-tetrakisphosphate (PubMed:25869668, PubMed:7761412). Regulates traffic in the endosomal pathway by regulating the specific pool of phosphatidylinositol 4,5-bisphosphate that is associated with endosomes (PubMed:21971085). Involved in primary cilia assembly (PubMed:22228094, PubMed:22543976). Acts as a regulator of phagocytosis, hydrolyzing PtdIns(4,5)P2 to promote phagosome closure, through attenuation of PI3K signaling (PubMed:22072788)", "gene_name": "OCRL", "glycan_count": 1, "glycosylation_sites": [], "id": "Q01968", "name": "OCRL", "organism": "Homo sapiens", "uniprot_id": "Q01968" }, { "function": "Forms paracellular channels: coassembles with CLDN19 into tight junction strands with cation-selective channels through the strands, conveying epithelial permeability in a process known as paracellular tight junction permeability (PubMed:16234325, PubMed:18188451, PubMed:28028216). Involved in the maintenance of ion gradients along the nephron. In the thick ascending limb (TAL) of Henle's loop, facilitates sodium paracellular permeability from the interstitial compartment to the lumen, contributing to the lumen-positive transepithelial potential that drives paracellular magnesium and calcium reabsorption (PubMed:10390358, PubMed:11518780, PubMed:14628289, PubMed:16528408, PubMed:28028216)", "gene_name": "CLDN16", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y5I7", "name": "Claudin-10", "organism": "Homo sapiens", "uniprot_id": "Q9Y5I7" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NZQ6-2", "name": "Claudin-18.2", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "not assigned (hormonal fragment of FBN1)", "name": "Asprosin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P16599 (rat)", "name": "TNF-\u03b1", "organism": "", "uniprot_id": "" }, { "function": "Exhibits trypsin-like activity as defined by cleavage of synthetic substrates with Arg or Lys as the P1 site (PubMed:10373424). Involved in the terminal differentiation of keratinocytes through prostasin (PRSS8) activation and filaggrin (FLG) processing (PubMed:18843291). Proteolytically cleaves and therefore activates TMPRSS13 (PubMed:28710277)", "gene_name": "ST14", "glycan_count": 23, "glycosylation_sites": [ { "position": 109, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 302, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 485, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 772, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y5Y6", "name": "ST14", "organism": "Homo sapiens", "uniprot_id": "Q9Y5Y6" }, { "function": "Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient (PubMed:12369018, PubMed:14699049, PubMed:28512129). Essentially dedicated to O-mannosylation of alpha-DAG1 and few other proteins but not of cadherins and protocaherins (PubMed:28512129)", "gene_name": "POMT1", "glycan_count": 8, "glycosylation_sites": [ { "position": 435, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 471, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 539, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y6A1", "name": "TPST2", "organism": "Homo sapiens", "uniprot_id": "Q9Y6A1" }, { "function": "Implicated in chromosome condensation and DNA damage induced cellular responses. May play a role in neurogenesis and regulation of the size of the cerebral cortex", "gene_name": "MCPH1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8NEM0", "name": "MCPH1", "organism": "Homo sapiens", "uniprot_id": "Q8NEM0" }, { "function": "May play a role in the respiratory chain", "gene_name": "C2orf69", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8N8R5", "name": "PQLC3", "organism": "Homo sapiens", "uniprot_id": "Q8N8R5" }, { "function": "GTPase activator for RAN (PubMed:16428860, PubMed:8146159, PubMed:8896452). Converts cytoplasmic GTP-bound RAN to GDP-bound RAN, which is essential for RAN-mediated nuclear import and export (PubMed:27160050, PubMed:8896452). Mediates dissociation of cargo from nuclear export complexes containing XPO1, RAN and RANBP2 after nuclear export (PubMed:27160050)", "gene_name": "RANGAP1", "glycan_count": 2, "glycosylation_sites": [], "id": "P46060", "name": "RANGAP1", "organism": "Homo sapiens", "uniprot_id": "P46060" }, { "function": "Plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. Regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). Regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development", "gene_name": "KIF16B", "glycan_count": 0, "glycosylation_sites": [], "id": "Q96L93", "name": "KIF21B", "organism": "Homo sapiens", "uniprot_id": "Q96L93" }, { "function": "Microtubule-associated protein essential for correct brain development (PubMed:30449657). Appears to link the dystrophin/utrophin network with microtubule filaments via the syntrophins. Phosphorylation of DMD or UTRN may modulate their affinities for associated proteins (By similarity)", "gene_name": "MAST1", "glycan_count": 9, "glycosylation_sites": [], "id": "Q9Y2H9", "name": "MAST4", "organism": "Homo sapiens", "uniprot_id": "Q9Y2H9" }, { "function": "Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions (PubMed:22446626). Inhibits SIRT1 deacetylase activity leading to increasing levels of p53/TP53 acetylation and p53-mediated apoptosis (PubMed:18235501, PubMed:18235502, PubMed:23352644). Inhibits SUV39H1 methyltransferase activity (PubMed:19218236). Mediates ligand-dependent transcriptional activation by nuclear hormone receptors (PubMed:19131338). Plays a critical role in maintaining genomic stability and cellular integrity following UV-induced genotoxic stress (PubMed:23398316). Regulates the circadian expression of the core clock components NR1D1 and BMAL1 (PubMed:23398316). Enhances the transcriptional repressor activity of NR1D1 through stabilization of NR1D1 protein levels by preventing its ubiquitination and subsequent degradation (PubMed:23398316). Represses the ligand-dependent transcriptional activation function of ESR2 (PubMed:20074560). Acts as a regulator of PCK1 expression and gluconeogenesis by a mechanism that involves, at least in part, both NR1D1 and SIRT1 (PubMed:24415752). Negatively regulates the deacetylase activity of HDAC3 and can alter its subcellular localization (PubMed:21030595). Positively regulates the beta-catenin pathway (canonical Wnt signaling pathway) and is required for MCC-mediated repression of the beta-catenin pathway (PubMed:24824780). Represses ligand-dependent transcriptional activation function of NR1H2 and NR1H3 and inhibits the interaction of SIRT1 with NR1H3 (PubMed:25661920). Plays an important role in tumor suppression through p53/TP53 regulation; stabilizes p53/TP53 by affecting its interaction with ubiquitin ligase MDM2 (PubMed:25732823). Represses the transcriptional activator activity of BRCA1 (PubMed:20160719). Inhibits SIRT1 in a CHEK2 and PSEM3-dependent manner and inhibits the activity of CHEK2 in vitro (PubMed:25361978)", "gene_name": "CCAR2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8N163", "name": "Nectin1", "organism": "Homo sapiens", "uniprot_id": "Q8N163" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "GPR41: O14842, GPR43: O15552", "name": "GPR41/43", "organism": "", "uniprot_id": "" }, { "function": "Essential mediator of p53/TP53-dependent and p53/TP53-independent apoptosis (PubMed:11463391, PubMed:23340338). Promotes partial unfolding of BCL2L1 and dissociation of BCL2L1 from p53/TP53, releasing the bound p53/TP53 to induce apoptosis (PubMed:23340338). Regulates ER stress-induced neuronal apoptosis (By similarity)", "gene_name": "BBC3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9BXH1", "name": "PUMA (BBC3)", "organism": "Homo sapiens", "uniprot_id": "Q9BXH1" }, { "function": "Receptor for hyaluronate", "gene_name": "LAYN", "glycan_count": 2, "glycosylation_sites": [ { "position": 117, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q6UX15", "name": "Layilin", "organism": "Homo sapiens", "uniprot_id": "Q6UX15" }, { "function": "Receptor for gastrin-releasing peptide (GRP) (PubMed:1655761). Signals via association with G proteins that activate a phosphatidylinositol-calcium second messenger system, resulting in Akt phosphorylation. Contributes to the regulation of food intake. Contributes to the perception of prurient stimuli and transmission of itch signals in the spinal cord that promote scratching behavior, but does not play a role in the perception of pain. Contributes primarily to nonhistaminergic itch sensation. In one study, shown to act in the amygdala as part of an inhibitory network which inhibits memory specifically related to learned fear (By similarity). In another study, shown to contribute to disinhibition of glutamatergic cells in the auditory cortex via signaling on vasoactive intestinal peptide-expressing cells which leads to enhanced auditory fear memories (By similarity). Contributes to the induction of sighing through signaling in the pre-Botzinger complex, a cluster of several thousand neurons in the ventrolateral medulla responsible for inspiration during respiratory activity (By similarity)", "gene_name": "GRPR", "glycan_count": 0, "glycosylation_sites": [ { "position": 20, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P30550", "name": "GRPR (Gastrin-Releasing Peptide Receptor)", "organism": "Homo sapiens", "uniprot_id": "P30550" }, { "function": "", "gene_name": "US10", "glycan_count": 0, "glycosylation_sites": [], "id": "P06486", "name": "gC (glycoprotein C)", "organism": "Human herpesvirus 1 (strain 17)", "uniprot_id": "P06486" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "gH: P06485, gL: P06487", "name": "gH/gL (glycoprotein H/glycoprotein L complex)", "organism": "", "uniprot_id": "" }, { "function": "Cell surface receptor that plays a role in the regulation of IL-13-mediated responses (PubMed:11861389, PubMed:17030238). Functions as a decoy receptor that inhibits IL-13- and IL-4-mediated signal transduction via the JAK-STAT pathway and thereby modulates immune responses and inflammation (PubMed:11861389, PubMed:17030238). Serves as a functional signaling receptor for IL-13 in an alternative pathway involving AP-1 ultimately leading to the production of TGFB1 (PubMed:16327802)", "gene_name": "IL13RA2", "glycan_count": 0, "glycosylation_sites": [ { "position": 115, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 215, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 290, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 299, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q14627", "name": "IL-13R\u03b12", "organism": "Homo sapiens", "uniprot_id": "Q14627" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "various (e.g., P01892)", "name": "MHC-I", "organism": "", "uniprot_id": "" }, { "function": "Reversible hydration of carbon dioxide", "gene_name": "CA12", "glycan_count": 1, "glycosylation_sites": [ { "position": 28, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 80, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 162, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "O43570", "name": "Carbonic Anhydrase XII (CAXII)", "organism": "Homo sapiens", "uniprot_id": "O43570" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04578 (gp160 precursor)", "name": "HIV-1 gp140", "organism": "", "uniprot_id": "" }, { "function": "Pore-forming subunit of gustatory voltage-gated ion channels required for sensory perception of sweet, bitter and umami tastes (By similarity). With CALHM3 forms a fast-activating voltage-gated ATP-release channel in type II taste bud cells, ATP acting as a neurotransmitter to activate afferent neural gustatory pathways (By similarity) (PubMed:23467090). Acts both as a voltage-gated and calcium-activated ion channel: mediates neuronal excitability in response to membrane depolarization and low extracellular Ca(2+) concentration (PubMed:22711817, PubMed:23300080). Has poor ion selectivity and forms a wide pore (around 14 Angstroms) that mediates permeation of small ions including Ca(2+), Na(+), K(+) and Cl(-), as well as larger ions such as ATP(4-) (PubMed:22711817, PubMed:23300080, PubMed:32832629, PubMed:37380652). Mediates Ca(2+) influx and downstream activation of the ERK1 and ERK2 cascade in neurons (PubMed:23345406). Triggers endoplasmic reticulum stress by reducing the Ca(2+) content of the endoplasmic reticulum (PubMed:21574960). May indirectly control amyloid precursor protein (APP) proteolysis and aggregated amyloid-beta (Abeta) peptides levels in a Ca(2+)-dependent manner (PubMed:18585350)", "gene_name": "CALHM1", "glycan_count": 0, "glycosylation_sites": [ { "position": 140, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8IU99", "name": "CALHM1", "organism": "Homo sapiens", "uniprot_id": "Q8IU99" }, { "function": "Inactive tyrosine kinase involved in Wnt signaling pathway. Component of both the non-canonical (also known as the Wnt/planar cell polarity signaling) and the canonical Wnt signaling pathway. Functions in cell adhesion, cell migration, cell polarity, proliferation, actin cytoskeleton reorganization and apoptosis. Has a role in embryogenesis, epithelial tissue organization and angiogenesis", "gene_name": "PTK7", "glycan_count": 77, "glycosylation_sites": [ { "position": 116, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 175, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 184, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 214, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 268, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 283, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 405, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 463, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 567, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 646, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13308", "name": "Protein Tyrosine Kinase 7 (PTK7)", "organism": "Homo sapiens", "uniprot_id": "Q13308" }, { "function": "Functions as a cleaved signal peptide that is retained as the third component of the GP complex (GP-C). Helps to stabilize the spike complex in its native conformation. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of G1 and G2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion", "gene_name": "GPC", "glycan_count": 0, "glycosylation_sites": [ { "position": 85, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 95, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 114, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 124, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 171, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 232, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 371, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 396, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 401, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P07399", "name": "LCMV glycoprotein", "organism": "Lymphocytic choriomeningitis virus (strain WE)", "uniprot_id": "P07399" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O57650", "name": "Cyanovirin-N (CVN)", "organism": "Acanthurus chirurgus", "uniprot_id": "O57650" }, { "function": "Glycinin is the major seed storage protein of soybean (PubMed:2485233). Glycinin basic peptides (GBPs), and, to a lower extent, glycinin exhibit antibacterial activity against Gram-negative and Gram-positive bacteria (e.g. L.monocytogenes, B.subtilis, E.coli and S.enteritidis) by forming pores and aggregating in transmembranes, leading to membrane permeability and, eventually, cell death (PubMed:22236762, PubMed:28590128, Ref.17)", "gene_name": "GY4", "glycan_count": 0, "glycosylation_sites": [], "id": "P02858", "name": "glycinin", "organism": "Glycine max", "uniprot_id": "P02858" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P13916", "name": "\u03b2-conglycinin", "organism": "", "uniprot_id": "P13916" }, { "function": "In presence of calcium ions, it binds to surfactant phospholipids and contributes to lower the surface tension at the air-liquid interface in the alveoli of the mammalian lung and is essential for normal respiration. Enhances the expression of MYO18A/SP-R210 on alveolar macrophages (By similarity)", "gene_name": "SFTPA1", "glycan_count": 0, "glycosylation_sites": [ { "position": 207, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8IWL2", "name": "Surfactant Protein D (SP-D)", "organism": "Homo sapiens", "uniprot_id": "Q8IWL2" }, { "function": "Binds phosphatidylcholine, phosphatidylinositol, polychlorinated biphenyls (PCB) and weakly progesterone, potent inhibitor of phospholipase A2", "gene_name": "SCGB1A1", "glycan_count": 0, "glycosylation_sites": [], "id": "P11684", "name": "Club Cell Protein 16 (CC16)", "organism": "Homo sapiens", "uniprot_id": "P11684" }, { "function": "Has anti-angiogenic properties", "gene_name": "ADAMTS8", "glycan_count": 1, "glycosylation_sites": [ { "position": 344, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 400, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 465, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 490, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 599, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UP79", "name": "ADAM8", "organism": "Homo sapiens", "uniprot_id": "Q9UP79" }, { "function": "Seems to function as a Vpr-like protein, since it mediates host cell cycle arrest in G2 phase. Cell cycle arrest creates a favorable environment for maximizing viral expression and production (By similarity)", "gene_name": "tat", "glycan_count": 0, "glycosylation_sites": [], "id": "P03408", "name": "Nef", "organism": "Maedi visna virus (strain 1514)", "uniprot_id": "P03408" }, { "function": "DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single- or double-stranded RNA. Exhibits antiviral activity against simian immunodeficiency virus (SIV), hepatitis B virus (HBV), herpes simplex virus 1 (HHV-1) and Epstein-Barr virus (EBV) and may inhibit the mobility of LTR and non-LTR retrotransposons. May also play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation", "gene_name": "APOBEC3C", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NRW3", "name": "APOBEC3A", "organism": "Homo sapiens", "uniprot_id": "Q9NRW3" }, { "function": "Interferon-induced E3 ubiquitin ligase that plays important roles in innate and adaptive immunity (PubMed:25683609, PubMed:35777501). Restricts the replication of many viruses including HIV-1, encephalomyocarditis virus (EMCV), hepatitis B virus (HBV), hepatitis C virus (HCV) or Zika virus (ZIKV) (PubMed:25683609, PubMed:35777501, PubMed:36042495). Mechanistically, negatively regulates HCV replication by promoting ubiquitination and subsequent degradation of viral NS5A (PubMed:25683609). Also acts by promoting the degradation of Zika virus NS1 and NS3 proteins through proteasomal degradation (PubMed:36042495). Acts as a suppressor of basal HIV-1 LTR-driven transcription by preventing Sp1 binding to the HIV-1 promoter (PubMed:26683615). Also plays a role in antiviral immunity by co-regulating together with NT5C2 the RIGI/NF-kappa-B pathway by promoting 'Lys-63'-linked ubiquitination of RIGI, while NT5C2 is responsible for 'Lys-48'-linked ubiquitination of RIGI (PubMed:36159777). Participates in adaptive immunity by suppressing the amount of MHC class II protein in a negative feedback manner in order to limit the extent of MHC class II induction (PubMed:35777501)", "gene_name": "TRIM22", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8IYM9", "name": "TRIM22", "organism": "Homo sapiens", "uniprot_id": "Q8IYM9" }, { "function": "Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation", "gene_name": "PRDX4", "glycan_count": 1, "glycosylation_sites": [], "id": "Q13162", "name": "LEDGF/p75", "organism": "Homo sapiens", "uniprot_id": "Q13162" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04585-6", "name": "p6 (Gag p6 domain)", "organism": "", "uniprot_id": "" }, { "function": "Functions as an activating and costimulatory receptor involved in immunosurveillance upon binding to various cellular stress-inducible ligands displayed at the surface of autologous tumor cells and virus-infected cells. Provides both stimulatory and costimulatory innate immune responses on activated killer (NK) cells, leading to cytotoxic activity. Acts as a costimulatory receptor for T-cell receptor (TCR) in CD8(+) T-cell-mediated adaptive immune responses by amplifying T-cell activation. Stimulates perforin-mediated elimination of ligand-expressing tumor cells. Signaling involves calcium influx, culminating in the expression of TNF-alpha. Participates in NK cell-mediated bone marrow graft rejection. May play a regulatory role in differentiation and survival of NK cells. Binds to ligands belonging to various subfamilies of MHC class I-related glycoproteins including MICA, MICB, RAET1E, RAET1G, RAET1L/ULBP6, ULBP1, ULBP2, ULBP3 (ULBP2>ULBP1>ULBP3) and ULBP4", "gene_name": "KLRK1", "glycan_count": 0, "glycosylation_sites": [ { "position": 131, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 163, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 202, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P26718", "name": "NKG2D", "organism": "Homo sapiens", "uniprot_id": "P26718" }, { "function": "Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41", "gene_name": "env", "glycan_count": 0, "glycosylation_sites": [ { "position": 88, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 136, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 141, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 156, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 160, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 186, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 197, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 230, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 234, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 241, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 262, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 276, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 289, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 295, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 301, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 332, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 339, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 356, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 386, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 392, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 397, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 406, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 448, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 463, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 611, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 616, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 625, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 637, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 674, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P03376", "name": "HIV-2 Envelope glycoprotein (Env)", "organism": "Human immunodeficiency virus type 1 group M subtype B (isolate BH10)", "uniprot_id": "P03375" }, { "function": "Chemotactic activity for resting CD4, CD8 T-cells and eosinophils. Binds to CCR3 and CCR10 and induces calcium mobilization in a dose-dependent manner", "gene_name": "CCL28", "glycan_count": 0, "glycosylation_sites": [ { "position": 78, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NRJ3", "name": "CCL28", "organism": "Homo sapiens", "uniprot_id": "Q9NRJ3" }, { "function": "Serine-type endopeptidase involved in atrial natriuretic peptide (NPPA) and brain natriuretic peptide (NPPB) processing (PubMed:10880574, PubMed:20489134, PubMed:21288900, PubMed:21763278). Converts through proteolytic cleavage the non-functional propeptides NPPA and NPPB into their active hormones, ANP and BNP(1-32) respectively, thereby regulating blood pressure in the heart and promoting natriuresis, diuresis and vasodilation (PubMed:10880574, PubMed:20489134, PubMed:21288900, PubMed:21763278). Proteolytic cleavage of pro-NPPA also plays a role in female pregnancy by promoting trophoblast invasion and spiral artery remodeling in uterus (PubMed:22437503). Also acts as a regulator of sodium reabsorption in kidney (By similarity)", "gene_name": "CORIN", "glycan_count": 1, "glycosylation_sites": [ { "position": 80, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 104, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 135, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 141, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 231, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 245, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 251, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 305, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 320, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 376, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 413, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 446, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 451, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 469, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 567, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 651, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 697, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 761, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1022, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9Y5Q5", "name": "Corin", "organism": "Homo sapiens", "uniprot_id": "Q9Y5Q5" }, { "function": "Plays an important role in the regulation of interdigestive gastrointestinal motility and indirectly causes rhythmic contraction of duodenal and colonic smooth muscle", "gene_name": "MLN", "glycan_count": 0, "glycosylation_sites": [], "id": "P12872", "name": "Motilin", "organism": "Homo sapiens", "uniprot_id": "P12872" }, { "function": "", "gene_name": "hdcA", "glycan_count": 0, "glycosylation_sites": [], "id": "P00862", "name": "Catalase", "organism": "Lactobacillus sp. (strain 30a)", "uniprot_id": "P00862" }, { "function": "Plays a role in the mitochondrial apoptotic process. Upon arrival of cell death signals, promotes mitochondrial outer membrane (MOM) permeabilization by oligomerizing to form pores within the MOM. This releases apoptogenic factors into the cytosol, including cytochrome c, promoting the activation of caspase 9 which in turn processes and activates the effector caspases", "gene_name": "BAK1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q16611", "name": "Bak (Bcl-2 homologous antagonist/killer)", "organism": "Homo sapiens", "uniprot_id": "Q16611" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P07204 (human)", "name": "Thrombomodulin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9UQB3 (canine)", "name": "Alpha-catenin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P35222 (canine)", "name": "Beta-catenin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P08253 (human)", "name": "Matrix Metalloproteinase-2 (MMP-2)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P16035 (human)", "name": "Tissue Inhibitor of Metalloproteinase-2 (TIMP-2)", "organism": "", "uniprot_id": "" }, { "function": "This is an intracellular thiol proteinase inhibitor. Tightly binding reversible inhibitor of cathepsins L, H and B", "gene_name": "CSTB", "glycan_count": 1, "glycosylation_sites": [], "id": "P04080", "name": "Cystatin B", "organism": "Homo sapiens", "uniprot_id": "P04080" }, { "function": "The large binding pocket can accommodate several single chain phospholipids and fatty acids, GM2A also exhibits some calcium-independent phospholipase activity (By similarity). Binds gangliosides and stimulates ganglioside GM2 degradation. It stimulates only the breakdown of ganglioside GM2 and glycolipid GA2 by beta-hexosaminidase A. It extracts single GM2 molecules from membranes and presents them in soluble form to beta-hexosaminidase A for cleavage of N-acetyl-D-galactosamine and conversion to GM3 (By similarity). Has cholesterol transfer activity (PubMed:17552909)", "gene_name": "GM2A", "glycan_count": 0, "glycosylation_sites": [ { "position": 63, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P17900", "name": "GM2 activator protein", "organism": "Homo sapiens", "uniprot_id": "P17900" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02452, P08123", "name": "Type I Collagen (Col1a1, Col1a2)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P06756 (ITGAV), P05556 (ITGB3)", "name": "\u03b1v\u03b23 integrin", "organism": "", "uniprot_id": "" }, { "function": "Receptor for neuropeptide Y and peptide YY. The rank order of affinity of this receptor for pancreatic polypeptides is NPY > [Pro-34] PYY, PYY and [Leu-31, Pro-34] NPY > NPY (2-36) > [Ile-31, Gln-34] PP and PYY (3-36) > PP > NPY free acid", "gene_name": "NPY1R", "glycan_count": 0, "glycosylation_sites": [ { "position": 2, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 11, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 17, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P25929", "name": "NPY-Y1 receptor", "organism": "Homo sapiens", "uniprot_id": "P25929" }, { "function": "Component of the membrane attack complex (MAC), a multiprotein complex activated by the complement cascade, which inserts into a target cell membrane and forms a pore, leading to target cell membrane rupture and cell lysis (PubMed:22267737, PubMed:22832194, PubMed:26841837, PubMed:27052168, PubMed:30552328). The MAC is initiated by proteolytic cleavage of C5 into complement C5b in response to the classical, alternative, lectin and GZMK complement pathways (PubMed:30552328). The complement pathways consist in a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system (PubMed:30552328). Together with component C5b, involved in MAC complex assembly: complement C5b and C6 associate with the outer leaflet of target cell membrane, reducing the energy for membrane bending (PubMed:30552328, PubMed:32569291)", "gene_name": "C6", "glycan_count": 29, "glycosylation_sites": [ { "position": 29, "type": "C-linked (Man) tryptophan" }, { "position": 32, "type": "C-linked (Man) tryptophan; partial" }, { "position": 38, "type": "O-linked (Fuc...) threonine" }, { "position": 90, "type": "C-linked (Man) tryptophan; partial" }, { "position": 324, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 392, "type": "O-linked (Fuc...) threonine" }, { "position": 568, "type": "C-linked (Man) tryptophan; partial" }, { "position": 571, "type": "C-linked (Man) tryptophan; partial" }, { "position": 574, "type": "C-linked (Man) tryptophan; partial" }, { "position": 855, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P13671", "name": "Complement Component C6 (C6)", "organism": "Homo sapiens", "uniprot_id": "P13671" }, { "function": "Probable hormone that may attenuate cell proliferation and induce senescence of oligodendrocyte and neural precursor cells in the central nervous system (By similarity). ECRG4-induced senescence is characterized by G1 arrest, RB1 dephosphorylation and accelerated CCND1 and CCND3 proteasomal degradation (By similarity)", "gene_name": "ECRG4", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H1Z8", "name": "Thrombospondin-5", "organism": "Homo sapiens", "uniprot_id": "Q9H1Z8" }, { "function": "Multifunctional protein that plays a critical role in regulating the availability of IGFs to their receptors and thereby regulates IGF-mediated cellular processes including proliferation, differentiation, and apoptosis in a cell-type specific manner (PubMed:18930415, PubMed:7683690). Increases the cell proliferation of osteoblasts, intestinal smooth muscle cells and neuroblastoma cells. Enhances adhesion and survival of epithelial cells but decreases adhesion of mesenchymal cells (By similarity). Once secreted, acts as a major mediator of mTORC1-dependent feedback inhibition of IGF1 signaling (By similarity). Also plays a role in the induction of extracellular matrix (ECM) production and deposition independently of its nuclear translocation and binding to IGFs (PubMed:20345844, PubMed:26103640). Acts itself as a growth factor that can act independently of IGFs to regulate bone formation. Acts as a ligand for the ROR1 receptor which triggers formation of ROR1/HER2 heterodimer to enhance CREB oncogenic signaling (PubMed:36949068)", "gene_name": "IGFBP5", "glycan_count": 3, "glycosylation_sites": [ { "position": 172, "type": "O-linked (HexNAc...) threonine" } ], "id": "P24593", "name": "IGFBP5", "organism": "Homo sapiens", "uniprot_id": "P24593" }, { "function": "Involved in the mineralization and structural organization of enamel", "gene_name": "AMBN", "glycan_count": 0, "glycosylation_sites": [ { "position": 112, "type": "O-linked (GalNAc...) serine" } ], "id": "Q9H2X1", "name": "PEAR1", "organism": "Homo sapiens", "uniprot_id": "Q9NP70" }, { "function": "Heterogenous nuclear ribonucleoprotein (hnRNP) implicated in mRNA processing mechanisms. Component of the CRD-mediated complex that promotes MYC mRNA stability. Isoform 1, isoform 2 and isoform 3 are associated in vitro with pre-mRNA, splicing intermediates and mature mRNA protein complexes. Isoform 1 binds to apoB mRNA AU-rich sequences. Isoform 1 is part of the APOB mRNA editosome complex and may modulate the postranscriptional C to U RNA-editing of the APOB mRNA through either by binding to A1CF (APOBEC1 complementation factor), to APOBEC1 or to RNA itself. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Interacts in vitro preferentially with poly(A) and poly(U) RNA sequences. Isoform 3 may be involved in cytoplasmic vesicle-based mRNA transport through interaction with synaptotagmins. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation; seems not to be essential for GAIT complex function", "gene_name": "SYNCRIP", "glycan_count": 3, "glycosylation_sites": [], "id": "O60506", "name": "Nucleoporin Nup153", "organism": "Homo sapiens", "uniprot_id": "O60506" }, { "function": "Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs (PubMed:14690600, PubMed:29276085, PubMed:8626397, PubMed:9659921). CFIm contributes to the recruitment of multiprotein complexes on specific sequences on the pre-mRNA 3'-end, so called cleavage and polyadenylation signals (pA signals) (PubMed:14690600, PubMed:8626397, PubMed:9659921). Most pre-mRNAs contain multiple pA signals, resulting in alternative cleavage and polyadenylation (APA) producing mRNAs with variable 3'-end formation (PubMed:23187700, PubMed:29276085). The CFIm complex acts as a key regulator of cleavage and polyadenylation site choice during APA through its binding to 5'-UGUA-3' elements localized in the 3'-untranslated region (UTR) for a huge number of pre-mRNAs (PubMed:20695905, PubMed:29276085). CPSF6 enhances NUDT21/CPSF5 binding to 5'-UGUA-3' elements localized upstream of pA signals and promotes RNA looping, and hence activates directly the mRNA 3'-processing machinery (PubMed:15169763, PubMed:21295486, PubMed:29276085). Plays a role in mRNA export (PubMed:19864460)", "gene_name": "CPSF6", "glycan_count": 1, "glycosylation_sites": [], "id": "Q16630", "name": "CPSF6", "organism": "Homo sapiens", "uniprot_id": "Q16630" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P12497-2", "name": "HIV-1 Matrix protein (MA)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P09012 (U1 snRNP 70 kDa)", "name": "U1 small nuclear ribonucleoprotein (U1-snRNP)", "organism": "", "uniprot_id": "" }, { "function": "Binds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation", "gene_name": "Hpx", "glycan_count": 4, "glycosylation_sites": [ { "position": 38, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 64, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 186, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 240, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 246, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 419, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q91X72", "name": "Serpina3n", "organism": "Mus musculus", "uniprot_id": "Q91X72" }, { "function": "Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex (phycobilisome, PBS). Phycocyanin is the major phycobiliprotein in the PBS rod", "gene_name": "cpcB2", "glycan_count": 0, "glycosylation_sites": [], "id": "P08039", "name": "Glutathione peroxidase", "organism": "Microchaete diplosiphon", "uniprot_id": "P08039" }, { "function": "Protects virus-infected cells from TNF-induced cytolysis", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04493", "name": "Glycoprotein D (gD)", "organism": "Human adenovirus C serotype 5", "uniprot_id": "P04493" }, { "function": "Binds and retains class I heavy chains in the endoplasmic reticulum during the early period of virus infection, thereby impairing their transport to the cell surface. Also delays the expression of class I alleles that it cannot affect by direct retention. Binds transporters associated with antigen processing (TAP) and acts as a tapasin inhibitor, preventing class I/TAP association. In consequence, infected cells are masked for immune recognition by cytotoxic T-lymphocytes", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [ { "position": 30, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 79, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P04494", "name": "Glycoprotein E (gE)", "organism": "Human adenovirus C serotype 5", "uniprot_id": "P04494" }, { "function": "Participates in the last steps of viral maturation and release. Associates with nuclear capsids prior to DNA encapsidation and later preserves the integrity of nucleocapsids through secondary envelopment at the assembly compartment. Interacts with host CCNA2 and thereby blocks the onset of lytic gene expression to promote establishment of a quiescent state of infection in undifferentiated cells", "gene_name": "UL32", "glycan_count": 0, "glycosylation_sites": [ { "position": 921, "type": "O-linked (GlcNAc) serine; by host" }, { "position": 952, "type": "O-linked (GlcNAc) serine; by host" } ], "id": "P08318", "name": "Glycoprotein G", "organism": "Human cytomegalovirus (strain AD169)", "uniprot_id": "P08318" }, { "function": "In epithelial cells, the heterodimer gE/gI is required for the cell-to-cell spread of the virus, by sorting nascent virions to cell junctions. Once the virus reaches the cell junctions, virus particles can spread to adjacent cells extremely rapidly through interactions with cellular receptors that accumulate at these junctions. Implicated in basolateral spread in polarized cells. In neuronal cells, gE/gI is essential for the anterograde spread of the infection throughout the host nervous system. Together with US9, the heterodimer gE/gI is involved in the sorting and transport of viral structural components toward axon tips", "gene_name": "gI", "glycan_count": 0, "glycosylation_sites": [ { "position": 156, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 169, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 175, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 243, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P13291", "name": "Glycoprotein M", "organism": "Human herpesvirus 2 (strain HG52)", "uniprot_id": "P13291" }, { "function": "Envelope glycoprotein that forms spikes at the surface of virion envelope and binds to the host cell entry receptors MYH9/NMMHC-IIA and MYH10/NMMHC-IIB, promoting the virus entry into host cells. Essential for the initial attachment to heparan sulfate moieties of the host cell surface proteoglycans. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell: following initial binding to its host cell entry receptors, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May be involved in the fusion between the virion envelope and the outer nuclear membrane during virion egress. Also plays a role, together with gK, in virus-induced cell-to-cell fusion (syncytia formation)", "gene_name": "gB", "glycan_count": 0, "glycosylation_sites": [ { "position": 86, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 140, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 397, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 429, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 488, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 673, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P06436", "name": "Glycoprotein C", "organism": "Human herpesvirus 1 (strain F)", "uniprot_id": "P06436" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04156-variant", "name": "Prion protein Q227X mutant", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P21447 (canine)", "name": "P-Glycoprotein", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04183 (human)", "name": "Thymidine Kinase 1", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q04609 (human)", "name": "Prostate Specific Membrane Antigen", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Y6Y9 (human)", "name": "Apoptosis Inhibitor of Macrophage", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02778 (human)", "name": "CXCL10", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P80188 (human)", "name": "Heparin Binding Protein", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01034 (human)", "name": "Cystatin C", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P05107/P06756", "name": "Integrin Mac-1 (CD11b/CD18)", "organism": "", "uniprot_id": "" }, { "function": "Melittin: Main toxin of bee venom with strong antimicrobial activity and hemolytic activity (PubMed:24512991, PubMed:4057243, PubMed:5139482, PubMed:5794226). It has enhancing effects on bee venom phospholipase A2 activity (PubMed:4371280). This amphipathic toxin binds to negatively charged membrane surface and forms pore by inserting into lipid bilayers inducing the leakage of ions and molecules and the enhancement of permeability that ultimately leads to cell lysis (PubMed:3666135, PubMed:4057243, PubMed:6830776). It acts as a voltage-gated pore with higher selectivity for anions over cations (PubMed:6269667). The ion conductance has been shown to be voltage-dependent (PubMed:7061434). Self-association of melittin in membranes is promoted by high ionic strength, but not by the presence of negatively charged lipids (PubMed:3443079). In vivo, intradermal injection into healthy human volunteers produce sharp pain sensation and an inflammatory response (PubMed:26983715). It produces pain by activating primary nociceptor cells directly and indirectly due to its ability to activate plasma membrane phospholipase A2 and its pore-forming activity (PubMed:26983715). In the context of inflammation and cancer tests, is highly cytotoxic to normal cells, highly induces calcium signaling and almost completely prevents cAMP production (PubMed:36548715). In addition, prevents LPS-induced nitric oxid (NO) synthesis but does not affect the IP3 signaling and pro-inflammatory activation of endothelial cells (PubMed:36548715). Also shows significant antiproliferative activity on the breast cancer cell line MDA-MB-231 (PubMed:36548715)", "gene_name": "MELT", "glycan_count": 0, "glycosylation_sites": [], "id": "P01501", "name": "Apamin", "organism": "Apis mellifera", "uniprot_id": "P01501" }, { "function": "Morphine modulating peptides. Have wide-ranging physiologic effects, including the modulation of morphine-induced analgesia, elevation of arterial blood pressure, and increased somatostatin secretion from the pancreas. Neuropeptide FF potentiates and sensitizes ASIC1 and ASIC3 channels", "gene_name": "NPFF", "glycan_count": 0, "glycosylation_sites": [], "id": "O15130", "name": "SCAMP (Secretory Carrier Membrane Protein)", "organism": "Homo sapiens", "uniprot_id": "O15130" }, { "function": "Key regulator of striated muscle performance by acting as the major Ca(2+) ATPase responsible for the reuptake of cytosolic Ca(2+) into the sarcoplasmic reticulum. Catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen (PubMed:10914677, PubMed:11438520, PubMed:15189864, PubMed:18075584, PubMed:23996003, PubMed:24270570, PubMed:29081402). Contributes to calcium sequestration involved in muscular excitation/contraction", "gene_name": "ATP2A1", "glycan_count": 0, "glycosylation_sites": [], "id": "P04191", "name": "SERCA (Sarcoplasmic Reticulum Ca2+ ATPase)", "organism": "Oryctolagus cuniculus", "uniprot_id": "P04191" }, { "function": "This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The exact function of the beta-3 subunit is not known", "gene_name": "ATP1B3", "glycan_count": 32, "glycosylation_sites": [ { "position": 124, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 240, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P54709", "name": "FXYD2 (\u03b3-subunit of Na+/K+ ATPase)", "organism": "Homo sapiens", "uniprot_id": "P54709" }, { "function": "Rod linker protein, associated with phycocyanin (PC). Linker polypeptides determine the state of aggregation and the location of the disk-shaped phycobiliprotein units within the phycobilisome (PBS) and modulate their spectroscopic properties in order to mediate a directed and optimal energy transfer. Forms a supercomplex with tetrameric photosystem I (PSI) and PC that allows efficient energy transfer from PC to PSI. This protein seems to be in the middle of the PC hexameric rod and may anchor the PC rods at the periphery of PSI tetramers. May be involved in the cyclic electron transport around PSI that provides ATP needed for N(2) fixation in heterocysts (PubMed:24550276)", "gene_name": "cpcL", "glycan_count": 0, "glycosylation_sites": [], "id": "P29988", "name": "Dengue virus Precursor membrane glycoprotein (prM)", "organism": "Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)", "uniprot_id": "P29988" }, { "function": "Component of the signaling pathway of IL-1 and Toll-like receptors (PubMed:10854325, PubMed:11751856). Inhibits cell activation by microbial products. Recruits IRAK1 to the IL-1 receptor complex (PubMed:10854325). Inhibits IRAK1 phosphorylation and kinase activity (PubMed:11751856). Connects the ubiquitin pathway to autophagy by functioning as a ubiquitin-ATG8 family adapter and thus mediating autophagic clearance of ubiquitin conjugates (PubMed:25042851). The TOLLIP-dependent selective autophagy pathway plays an important role in clearance of cytotoxic polyQ proteins aggregates (PubMed:25042851). In a complex with TOM1, recruits ubiquitin-conjugated proteins onto early endosomes (PubMed:15047686). Binds to phosphatidylinositol 3-phosphate (PtdIns(3)P) (PubMed:26320582)", "gene_name": "TOLLIP", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9H0E2", "name": "TOLLIP", "organism": "Homo sapiens", "uniprot_id": "Q9H0E2" }, { "function": "Neuronal cell surface protein that may be involved in cell recognition and cell adhesion. May mediate intracellular signaling", "gene_name": "NRXN2", "glycan_count": 5, "glycosylation_sites": [ { "position": 60, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 338, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 841, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1236, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1400, "type": "O-linked (Xyl...) (heparan sulfate) serine" } ], "id": "Q9P2S2", "name": "Neurexin 2 (NRXN2)", "organism": "Homo sapiens", "uniprot_id": "Q9P2S2" }, { "function": "Neuronal cell surface protein that may be involved in cell recognition and cell adhesion. May mediate intracellular signaling (By similarity)", "gene_name": "NRXN3", "glycan_count": 1, "glycosylation_sites": [ { "position": 58, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 105, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 757, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1189, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1257, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1301, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1317, "type": "O-linked (Xyl...) (heparan sulfate) serine" } ], "id": "Q9Y4C0", "name": "Neurexin 3 (NRXN3)", "organism": "Homo sapiens", "uniprot_id": "Q9Y4C0" }, { "function": "Major scaffold postsynaptic density protein which interacts with multiple proteins and complexes to orchestrate the dendritic spine and synapse formation, maturation and maintenance. Interconnects receptors of the postsynaptic membrane including NMDA-type and metabotropic glutamate receptors via complexes with GKAP/PSD-95 and HOMER, respectively, and the actin-based cytoskeleton. Plays a role in the structural and functional organization of the dendritic spine and synaptic junction through the interaction with Arp2/3 and WAVE1 complex as well as the promotion of the F-actin clusters. By way of this control of actin dynamics, participates in the regulation of developing neurons growth cone motility and the NMDA receptor-signaling. Also modulates GRIA1 exocytosis and GRM5/MGLUR5 expression and signaling to control the AMPA and metabotropic glutamate receptor-mediated synaptic transmission and plasticity. May be required at an early stage of synapse formation and be inhibited by IGF1 to promote synapse maturation", "gene_name": "SHANK3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9BYB0", "name": "SHANK3", "organism": "Homo sapiens", "uniprot_id": "Q9BYB0" }, { "function": "Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Acts as a scaffold regulating CPC localization and activity. The C-terminus associates with AURKB or AURKC, the N-terminus associated with BIRC5/survivin and CDCA8/borealin tethers the CPC to the inner centromere, and the microtubule binding activity within the central SAH domain directs AURKB/C toward substrates near microtubules (PubMed:12925766, PubMed:15316025, PubMed:27332895). The flexibility of the SAH domain is proposed to allow AURKB/C to follow substrates on dynamic microtubules while ensuring CPC docking to static chromatin (By similarity). Activates AURKB and AURKC (PubMed:27332895). Required for localization of CBX5 to mitotic centromeres (PubMed:21346195). Controls the kinetochore localization of BUB1 (PubMed:16760428)", "gene_name": "INCENP", "glycan_count": 2, "glycosylation_sites": [], "id": "Q9NQS7", "name": "Nectin 1", "organism": "Homo sapiens", "uniprot_id": "Q9NQS7" }, { "function": "Involved in the regulation of innate immunity and the inflammatory response in response to IFNG/IFN-gamma (PubMed:10807793, PubMed:11468188, PubMed:16037825, PubMed:16785446, PubMed:17431422, PubMed:17964261, PubMed:18577712, PubMed:19109554, PubMed:19584923, PubMed:26347139, PubMed:27030597, PubMed:28835462). Organizes autophagic machinery by serving as a platform for the assembly of ULK1, Beclin 1/BECN1, ATG16L1, and ATG8 family members and recognizes specific autophagy targets, thus coordinating target recognition with assembly of the autophagic apparatus and initiation of autophagy (PubMed:16785446, PubMed:17431422, PubMed:26347139). Acts as an autophagy receptor for the degradation of several inflammasome components, including CASP1, NLRP1 and NLRP3, hence preventing excessive IL1B- and IL18-mediated inflammation (PubMed:16785446, PubMed:17431422, PubMed:26347139). However, it can also have a positive effect in the inflammatory pathway, acting as an innate immune sensor that triggers PYCARD/ASC specks formation, caspase-1 activation, and IL1B and IL18 production (PubMed:16037825, PubMed:27030597, PubMed:28835462). Together with AIM2, also acts as a mediator of pyroptosis, necroptosis and apoptosis (PANoptosis), an integral part of host defense against pathogens, in response to bacterial infection (By similarity). It is required for PSTPIP1-induced PYCARD/ASC oligomerization and inflammasome formation (PubMed:10807793, PubMed:11468188, PubMed:17964261, PubMed:18577712, PubMed:19109554, PubMed:19584923). Recruits PSTPIP1 to inflammasomes, and is required for PSTPIP1 oligomerization (PubMed:10807793, PubMed:11468188, PubMed:17964261, PubMed:18577712, PubMed:19109554, PubMed:19584923)", "gene_name": "MEFV", "glycan_count": 1, "glycosylation_sites": [], "id": "O15553", "name": "Pyrin", "organism": "Homo sapiens", "uniprot_id": "O15553" }, { "function": "The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products", "gene_name": "rep", "glycan_count": 0, "glycosylation_sites": [], "id": "P0C6X6", "name": "Spike (S) glycoprotein", "organism": "Human coronavirus OC43", "uniprot_id": "P0C6X6" }, { "function": "The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products", "gene_name": "rep", "glycan_count": 0, "glycosylation_sites": [], "id": "P0C6X6-1", "name": "S1 subunit of Spike glycoprotein", "organism": "Human coronavirus OC43", "uniprot_id": "P0C6X6" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P0C6X6-2", "name": "S2 subunit of Spike glycoprotein", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "Knop1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8BJI0", "name": "Human Metapneumovirus Fusion Glycoprotein (F)", "organism": "Mus musculus", "uniprot_id": "Q9Z2Q2" }, { "function": "Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8Y6X6", "name": "ActA", "organism": "Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)", "uniprot_id": "Q8Y6X6" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8I4C6", "name": "Circumsporozoite protein (CSP)", "organism": "Caenorhabditis elegans", "uniprot_id": "Q8I4C6" }, { "function": "Forms an icosahedral capsid with a T=7 symmetry and a 50 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with L2 proteins. Binds to heparan sulfate proteoglycans on cell surface of basal layer keratinocytes to provide initial virion attachment. This binding mediates a conformational change in the virus capsid that facilitates efficient infection. The virion enters the host cell via endocytosis. During virus trafficking, L1 protein dissociates from the viral DNA and the genomic DNA is released to the host nucleus. The virion assembly takes place within the cell nucleus. Encapsulates the genomic DNA together with protein L2", "gene_name": "L1", "glycan_count": 0, "glycosylation_sites": [], "id": "P03101", "name": "L1 (HPV)", "organism": "Human papillomavirus type 16", "uniprot_id": "P03101" }, { "function": "", "gene_name": "unc-61", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8I4C9", "name": "VAR2CSA", "organism": "Caenorhabditis elegans", "uniprot_id": "Q8I4C9" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P06473 (CMV)", "name": "Glycoprotein B (gB)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P16716 (CMV)", "name": "Glycoprotein H (gH)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "various (IAV)", "name": "Hemagglutinin (HA)", "organism": "", "uniprot_id": "" }, { "function": "Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41", "gene_name": "env", "glycan_count": 0, "glycosylation_sites": [ { "position": 88, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 136, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 141, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 156, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 160, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 186, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 197, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 230, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 234, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 241, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 262, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 276, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 289, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 295, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 301, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 332, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 339, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 356, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 386, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 392, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 397, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 406, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 448, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 463, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 611, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 616, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 624, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 637, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 674, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P04578-1", "name": "HIV-1 gp120", "organism": "Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)", "uniprot_id": "P04578" }, { "function": "Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity", "gene_name": "CLDN11", "glycan_count": 1, "glycosylation_sites": [], "id": "O75508", "name": "Oligodendrocyte-specific protein (OSP/Claudin-11)", "organism": "Homo sapiens", "uniprot_id": "O75508" }, { "function": "Enhances virion budding by targeting host CD4 and Tetherin/BST2 to proteasome degradation. Degradation of CD4 prevents any unwanted premature interactions between viral Env and its host receptor CD4 in the endoplasmic reticulum. Degradation of antiretroviral protein Tetherin/BST2 is important for virion budding, as BST2 tethers new viral particles to the host cell membrane. Mechanistically, Vpu bridges either CD4 or BST2 to BTRC, a substrate recognition subunit of the Skp1/Cullin/F-box protein E3 ubiquitin ligase, induces their ubiquitination and subsequent proteasomal degradation. The alteration of the E3 ligase specificity by Vpu seems to promote the degradation of host IKBKB, leading to NF-kappa-B down-regulation and subsequent apoptosis. Acts as a viroporin that forms an oligomeric ion channel in membranes. Modulates the host DNA repair mechanisms to promote degradation of nuclear viral cDNA in cells that are already productively infected in order to suppress immune sensing and proviral hyper-integration (superinfection). Manipulates PML-NBs and modulates SUMOylation of host BLM protein thereby enhancing its DNA-end processing activity toward viral unintegrated linear DNA. Also inhibits RAD52-mediated homologous repair of viral cDNA, preventing the generation of dead-end circular forms of single copies of the long terminal repeat and permitting sustained nucleolytic attack", "gene_name": "vpu", "glycan_count": 0, "glycosylation_sites": [], "id": "P05919", "name": "Vpu", "organism": "Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)", "uniprot_id": "P05919" }, { "function": "A cytochrome P450 monooxygenase with a key role in vitamin D catabolism and calcium homeostasis. Via C24- and C23-oxidation pathways, catalyzes the inactivation of both the vitamin D precursor calcidiol (25-hydroxyvitamin D(3)) and the active hormone calcitriol (1-alpha,25-dihydroxyvitamin D(3)) (PubMed:11012668, PubMed:15574355, PubMed:16617161, PubMed:24893882, PubMed:29461981, PubMed:8679605). With initial hydroxylation at C-24 (via C24-oxidation pathway), performs a sequential 6-step oxidation of calcitriol leading to the formation of the biliary metabolite calcitroic acid (PubMed:15574355, PubMed:24893882). With initial hydroxylation at C-23 (via C23-oxidation pathway), catalyzes sequential oxidation of calcidiol leading to the formation of 25(OH)D3-26,23-lactone as end product (PubMed:11012668, PubMed:8679605). Preferentially hydroxylates at C-25 other vitamin D active metabolites, such as CYP11A1-derived secosteroids 20S-hydroxycholecalciferol and 20S,23-dihydroxycholecalciferol (PubMed:25727742). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via FDXR/adrenodoxin reductase and FDX1/adrenodoxin (PubMed:8679605)", "gene_name": "CYP24A1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q07973", "name": "CYP24A1", "organism": "Homo sapiens", "uniprot_id": "Q07973" }, { "function": "Serine protease that cleaves after hydrophobic or small residues, provided that Arg or Lys is in position P4: known substrates include SREBF1/SREBP1, SREBF2/SREBP2, BDNF, GNPTAB, ATF6, ATF6B and FAM20C (PubMed:10644685, PubMed:12782636, PubMed:21719679, PubMed:34349020). Cleaves substrates after Arg-Ser-Val-Leu (SREBP2), Arg-His-Leu-Leu (ATF6), Arg-Gly-Leu-Thr (BDNF) and its own propeptide after Arg-Arg-Leu-Leu (PubMed:10644685, PubMed:21719679). Catalyzes the first step in the proteolytic activation of the sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2 (PubMed:12782636). Also mediates the first step in the proteolytic activation of the cyclic AMP-dependent transcription factor ATF-6 (ATF6 and ATF6B) (PubMed:12782636). Mediates the protein cleavage of GNPTAB into subunit alpha and beta, thereby participating in biogenesis of lysosomes (PubMed:21719679). Cleaves the propeptide from FAM20C which is required for FAM20C secretion from the Golgi apparatus membrane and for enhancement of FAM20C kinase activity, promoting osteoblast differentiation and biomineralization (PubMed:34349020). Involved in the regulation of M6P-dependent Golgi-to-lysosome trafficking of lysosomal enzymes (PubMed:21719679, PubMed:30046013). It is required for the activation of CREB3L2/BBF2H7, a transcriptional activator of MIA3/TANGO and other genes controlling mega vesicle formation (PubMed:30046013). Therefore, it plays a key role in the regulation of mega vesicle-mediated collagen trafficking (PubMed:30046013). In astrocytes and osteoblasts, upon DNA damage and ER stress, mediates the first step of the regulated intramembrane proteolytic activation of the transcription factor CREB3L1, leading to the inhibition of cell-cycle progression (PubMed:16417584)", "gene_name": "MBTPS1", "glycan_count": 10, "glycosylation_sites": [ { "position": 236, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 305, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 515, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 728, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 939, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q14703", "name": "SKI-1/S1P (Site-1 Protease)", "organism": "Homo sapiens", "uniprot_id": "Q14703" }, { "function": "Catalyzes the formation of mannose 6-phosphate (M6P) markers on high mannose type oligosaccharides in the Golgi apparatus. M6P residues are required to bind to the M6P receptors (MPR), which mediate the vesicular transport of lysosomal enzymes to the endosomal/prelysosomal compartment", "gene_name": "GNPTAB", "glycan_count": 24, "glycosylation_sites": [ { "position": 83, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 114, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 148, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 179, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 250, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 614, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 699, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 729, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 829, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1009, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1129, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q3T906", "name": "GNPTAB (N-acetylglucosamine-1-phosphotransferase)", "organism": "Homo sapiens", "uniprot_id": "Q3T906" }, { "function": "Acts as a cofactor for the NS3 protease activity", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q65815", "name": "BVDV E2", "organism": "Bovine viral diarrhea virus 1-Osloss", "uniprot_id": "Q65815" }, { "function": "Serine endopeptidase which is involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. Responsible for the release of glucagon from proglucagon in pancreatic A cells", "gene_name": "PCSK2", "glycan_count": 3, "glycosylation_sites": [ { "position": 375, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 514, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 524, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P16519", "name": "Prohormone convertase 2 (PC2)", "organism": "Homo sapiens", "uniprot_id": "P16519" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q4W9A7", "name": "Anthrax Toxin Protective Antigen", "organism": "Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)", "uniprot_id": "Q4W9A7" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03437 (Influenza A H1N1)", "name": "Hemagglutinin (HA)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03468 (Influenza A H1N1)", "name": "Neuraminidase (NA)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P27395 (Japanese Encephalitis Virus)", "name": "Envelope glycoprotein E", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8JUX6/Q8JUX7 (Rift Valley Fever Virus)", "name": "Envelope glycoprotein GN/GC", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03485 (Influenza A)", "name": "Matrix protein", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6V1X1 (Enterovirus 71)", "name": "VP3 protein", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9QJY0 (Duck Plague Virus)", "name": "UL6 protein", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P59595 (SARS-CoV)", "name": "Nucleocapsid protein", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9YFA9 (Porcine Circovirus 2)", "name": "ORF2 Rep protein", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P06935 (West Nile Virus)", "name": "Envelope glycoprotein", "organism": "", "uniprot_id": "" }, { "function": "Serine endoprotease that processes various proproteins by cleavage at paired basic amino acids, recognizing the RXXX[KR]R consensus motif. Likely functions in the constitutive and regulated secretory pathways. Plays an essential role in pregnancy establishment by proteolytic activation of a number of important factors such as BMP2, CALD1 and alpha-integrins", "gene_name": "PCSK5", "glycan_count": 2, "glycosylation_sites": [ { "position": 225, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 381, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 665, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 752, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 802, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 852, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1014, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1191, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1290, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1497, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1685, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1707, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q92824", "name": "PC5", "organism": "Homo sapiens", "uniprot_id": "Q92824" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "varies by virus (e.g., P59594 for SARS-CoV)", "name": "Spike glycoprotein (S)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "varies", "name": "Hemagglutinin-esterase (HE)", "organism": "", "uniprot_id": "" }, { "function": "May play a role in hearing", "gene_name": "TMPRSS5", "glycan_count": 0, "glycosylation_sites": [ { "position": 163, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 170, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 195, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 319, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 375, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9H3S3", "name": "DESC1 (TMPRSS11E)", "organism": "Homo sapiens", "uniprot_id": "Q9H3S3" }, { "function": "Plasma membrane-anchored serine protease that directly induces processing of pro-uPA/PLAU into the active form through proteolytic activity (PubMed:24434139). Seems to be capable of activating ENaC (By similarity)", "gene_name": "TMPRSS4", "glycan_count": 0, "glycosylation_sites": [ { "position": 130, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 178, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NRS4", "name": "TMPRSS3", "organism": "Homo sapiens", "uniprot_id": "Q9NRS4" }, { "function": "Serine protease that cleaves extracellular substrates, and contributes to the proteolytic processing of growth factors, such as HGF and MST1/HGFL (PubMed:15839837, PubMed:21875933). Plays a role in cell growth and maintenance of cell morphology (PubMed:21875933, PubMed:8346233). Plays a role in the proteolytic processing of ACE2 (PubMed:24227843). Mediates the proteolytic cleavage of urinary UMOD that is required for UMOD polymerization (PubMed:26673890)", "gene_name": "HPN", "glycan_count": 13, "glycosylation_sites": [ { "position": 112, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P05981", "name": "Hepsin (TMPRSS1)", "organism": "Homo sapiens", "uniprot_id": "P05981" }, { "function": "Regulatory light chain of myosin. Does not bind calcium", "gene_name": "MYL3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NRS8", "name": "TMPRSS4", "organism": "Homo sapiens", "uniprot_id": "P08590" }, { "function": "Membrane-bound serine protease (PubMed:18976966, PubMed:20518742, PubMed:25156943, PubMed:25588876). Through the cleavage of cell surface hemojuvelin (HJV), a regulator of the expression of the iron absorption-regulating hormone hepicidin/HAMP, plays a role in iron homeostasis (PubMed:18408718, PubMed:18976966, PubMed:25156943)", "gene_name": "TMPRSS6", "glycan_count": 0, "glycosylation_sites": [ { "position": 136, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 184, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 216, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 338, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 433, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 453, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 518, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8IU80", "name": "Matriptase-2 (TMPRSS6)", "organism": "Homo sapiens", "uniprot_id": "Q8IU80" }, { "function": "RNA-directed RNA polymerase that catalyzes the transcription of viral mRNAs, their capping and polyadenylation. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). The viral polymerase binds to the genomic RNA at the 3' leader promoter, and transcribes subsequently all viral mRNAs with a decreasing efficiency. The first gene is the most transcribed, and the last the least transcribed. The viral phosphoprotein acts as a processivity factor. Capping is concomitant with initiation of mRNA transcription. Indeed, a GDP polyribonucleotidyl transferase (PRNTase) adds the cap structure when the nascent RNA chain length has reached few nucleotides. Ribose 2'-O methylation of viral mRNA cap precedes and facilitates subsequent guanine-N-7 methylation, both activities being carried by the viral polymerase. Polyadenylation of mRNAs occur by a stuttering mechanism at a slipery stop site present at the end viral genes. After finishing transcription of a mRNA, the polymerase can resume transcription of the downstream gene", "gene_name": "L", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9QJT4", "name": "Influenza B matrix protein 2 (BM2)", "organism": "Snakehead rhabdovirus", "uniprot_id": "Q9QJT4" }, { "function": "Sodium:iodide symporter that mediates the transport of iodide into the thyroid gland (PubMed:12488351, PubMed:18372236, PubMed:18708479, PubMed:20797386, PubMed:31310151, PubMed:32084174, PubMed:8806637, PubMed:9329364). Can also mediate the transport of chlorate, thiocynate, nitrate and selenocynate (PubMed:12488351)", "gene_name": "SLC5A5", "glycan_count": 0, "glycosylation_sites": [ { "position": 489, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 502, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q92911", "name": "SLC5A5 (sodium/iodide symporter)", "organism": "Homo sapiens", "uniprot_id": "Q92911" }, { "function": "Forms an icosahedral capsid with a T=7 symmetry and a 40 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with VP2 or VP3 proteins. Interacts with a N-linked glycoprotein containing terminal alpha(2-6)-linked sialic acids on the cell surface to provide virion attachment to target cell. The serotonergic receptor 5HT2AR also acts as a cellular receptor for JCV on human glial cells. Once attached, the virions enter predominantly by a ligand-inducible clathrin-dependent pathway and traffic to the ER. Inside the endoplasmic reticulum, the protein folding machinery isomerizes VP1 interpentamer disulfide bonds, thereby triggering initial uncoating. Next, the virion uses the endoplasmic reticulum-associated degradation machinery to probably translocate in the cytosol before reaching the nucleus. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2/Vp3 nuclear localization signal. In late phase of infection, neo-synthesized VP1 encapsulates replicated genomic DNA at nuclear domains called promyelocytic leukemia (PML) bodies, and participates in rearranging nucleosomes around the viral DNA", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03089", "name": "JC Virus VP1", "organism": "JC polyomavirus", "uniprot_id": "P03089" }, { "function": "Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag-Pol, or to Gag-Pol binding host factors. Interaction with HECT ubiquitin ligases probably link the viral protein to the host ESCRT pathway and facilitates release", "gene_name": "pol", "glycan_count": 0, "glycosylation_sites": [], "id": "P03357", "name": "HTLV-I Envelope Glycoprotein", "organism": "AKV murine leukemia virus", "uniprot_id": "P03356" }, { "function": "Attaches the virus to the human SLAMF1/CD150 receptor for entry into host dendritic cells, macrophages, activated memory T cells and naive or memory B cells, thereby explaining the long immunosuppression that follows infection (PubMed:10972291). In the respiratory airways, binds to the NECTIN4 receptor for entry into the host cell. Binding of H protein to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion (By similarity). The vaccine and laboratory-adapted strains use host CD46 as an alternate receptor (Probable). The high degree of interaction between H and CD46 results in down-regulation of the latter from the surface of infected cells, rendering them more sensitive to c3b-mediated complement lysis (PubMed:9811778)", "gene_name": "H", "glycan_count": 0, "glycosylation_sites": [ { "position": 168, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 187, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 200, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 215, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 238, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P08362", "name": "Measles Virus Hemagglutinin", "organism": "Measles virus (strain Edmonston)", "uniprot_id": "P08362" }, { "function": "Effector molecule of the innate immune system that acts via antibiotic-like properties against a broad array of infectious agents including bacteria, fungi, and viruses or by promoting the activation and maturation of some APCs (PubMed:15616305, PubMed:17142766, PubMed:20220136, PubMed:24236072). Interacts with the essential precursor of cell wall synthesis lipid II to inhibit bacterial cell wall synthesis (PubMed:20214904). Inhibits adenovirus infection via inhibition of viral disassembly at the vertex region, thereby restricting the release of internal capsid protein pVI, which is required for endosomal membrane penetration during cell entry (PubMed:18191790). In addition, interaction with adenovirus capsid leads to the redirection of viral particles to TLR4 thereby promoting a NLRP3-mediated inflammasome response and interleukin 1-beta (IL-1beta) release (PubMed:35080426). Induces the production of proinflammatory cytokines including type I interferon (IFN) in plasmacytoid dendritic cells (pDCs) by triggering the degradation of NFKBIA and nuclear translocation of IRF1, both of which are required for activation of pDCs (PubMed:27031443)", "gene_name": "DEFA1", "glycan_count": 0, "glycosylation_sites": [], "id": "P59665", "name": "HNP-1", "organism": "Homo sapiens", "uniprot_id": "P59665" }, { "function": "", "gene_name": "DEFB103A", "glycan_count": 0, "glycosylation_sites": [], "id": "Q5U7J2", "name": "hBD3", "organism": "Homo sapiens", "uniprot_id": "Q5U7J2" }, { "function": "Component of the viral envelope that plays a central role in virus morphogenesis and assembly via its interactions with other viral proteins", "gene_name": "M", "glycan_count": 0, "glycosylation_sites": [ { "position": 4, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P59596", "name": "SARS-CoV Membrane (M) glycoprotein", "organism": "Severe acute respiratory syndrome coronavirus", "uniprot_id": "P59596" }, { "function": "Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication (PubMed:17210170). May modulate transforming growth factor-beta signaling by binding host SMAD3 (PubMed:18055455)", "gene_name": "N", "glycan_count": 0, "glycosylation_sites": [], "id": "P59595", "name": "SARS-CoV Nucleocapsid (N) protein", "organism": "Severe acute respiratory syndrome coronavirus", "uniprot_id": "P59595" }, { "function": "May regulate immune response to the intracellular capsid in acting as a T-cell tolerogen, by having an immunoregulatory effect which prevents destruction of infected cells by cytotoxic T-cells", "gene_name": "C", "glycan_count": 0, "glycosylation_sites": [], "id": "P03154", "name": "HPV16 L2 protein", "organism": "Duck hepatitis B virus (strain United States/DHBV-16)", "uniprot_id": "P03154" }, { "function": "Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [ { "position": 183, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 347, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 433, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 903, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 980, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1132, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1188, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 2300, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 2304, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 2456, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P27915", "name": "NS1", "organism": "Dengue virus type 3 (strain Philippines/H87/1956)", "uniprot_id": "P27915" }, { "function": "Cytoplasmic adapter regulating receptors of the signaling lymphocytic activation molecule (SLAM) family such as SLAMF1, CD244, LY9, CD84, SLAMF6 and SLAMF7. In SLAM signaling seems to cooperate with SH2D1B/EAT-2. Initially it has been proposed that association with SLAMF1 prevents SLAMF1 binding to inhibitory effectors including INPP5D/SHIP1 and PTPN11/SHP-2 (PubMed:11806999). However, by simultaneous interactions, recruits FYN which subsequently phosphorylates and activates SLAMF1 (PubMed:12458214). Positively regulates CD244/2B4- and CD84-mediated natural killer (NK) cell functions. Can also promote CD48-, SLAMF6 -, LY9-, and SLAMF7-mediated NK cell activation. In the context of NK cell-mediated cytotoxicity enhances conjugate formation with target cells (By similarity). May also regulate the activity of the neurotrophin receptors NTRK1, NTRK2 and NTRK3", "gene_name": "SH2D1A", "glycan_count": 1, "glycosylation_sites": [], "id": "O60880", "name": "SAP (SLAM-associated protein)", "organism": "Homo sapiens", "uniprot_id": "O60880" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Fragment of P02671", "name": "Fibrinogen \u03b1 C-chain 5.9 kDa fragment", "organism": "", "uniprot_id": "" }, { "function": "Catalyzes the post-translational addition of a tyrosine to the C-terminal end of detyrosinated alpha-tubulin", "gene_name": "Ttl", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9QXJ0", "name": "VP7", "organism": "Rattus norvegicus", "uniprot_id": "Q9QXJ0" }, { "function": "Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication", "gene_name": "N", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6Q1R8", "name": "E1 glycoprotein", "organism": "Human coronavirus NL63", "uniprot_id": "Q6Q1R8" }, { "function": "Component of the viral envelope that plays a central role in virus morphogenesis and assembly via its interactions with other viral proteins", "gene_name": "M", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6Q1R9", "name": "E2 glycoprotein", "organism": "Human coronavirus NL63", "uniprot_id": "Q6Q1R9" }, { "function": "Plays critical roles in regulating RNA replication and transcription through its interactions with multiple proteins (PubMed:25568210, PubMed:26474524). Tethers the RNA-directed RNA polymerase L to the nucleoprotein-RNA complex (PubMed:26474524). Recruits the M2-1 protein, a processivity factor that is required for efficient transcription of viral RNA (PubMed:26474524). Acts as a chaperone for neo-synthesized nucleoprotein by forming an N-P complex that preserves N in a monomeric and RNA-free state and prevents the association of nascent N with host cell RNAs (PubMed:25568210). Recruits the host phosphatase PP1 to inclusion bodies to regulate viral transcription (PubMed:29489893). Together with the nucleoprotein, sequesters host NF-kappa-B in inclusion bodies (IBs) thereby inhibiting this host defense pathway (By similarity)", "gene_name": "P", "glycan_count": 0, "glycosylation_sites": [], "id": "P03421", "name": "Nucleoprotein (N)", "organism": "Human respiratory syncytial virus A (strain A2)", "uniprot_id": "P03421" }, { "function": "Together with its co-chaperonin GroES, plays an essential role in assisting protein folding (PubMed:10532860, PubMed:16751100, PubMed:1676490, PubMed:18418386, PubMed:18987317, PubMed:20603018, PubMed:24816391, PubMed:2573517, PubMed:2897629, PubMed:8104102, PubMed:9285593). The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding, probably by preventing aggregation and by entropically destabilizing folding intermediates (PubMed:16751100, PubMed:18418386, PubMed:18987317, PubMed:20603018, PubMed:24816391). Rapid binding of ATP, followed by slower binding of the non-native substrate protein and GroES to the cis open ring of GroEL initiates productive folding of the non-native protein inside a highly stable GroEL-ATP-GroES complex (PubMed:19915138, PubMed:22445172, PubMed:9285585, PubMed:9285593). Binding of ATP and GroES induces conformational changes that result in the release of the substrate protein into a nano-cage compartment, within the GroEL central cavity, for folding in isolation (PubMed:16684774, PubMed:22445172, PubMed:8861908, PubMed:9285585). To discharge GroES and substrate protein, ATP hydrolysis in the cis ring is required to form a GroEL-ADP-GroES complex with decreased stability (PubMed:9285593). Finally, binding of ATP to the opposite trans ring of GroEL results in disassembly of the cis-ternary complex, which opens the cage and allows release of the folded protein (PubMed:9285585, PubMed:9285593). Proteins released in non-native form may be rapidly rebound by another GroEL complex until all of the initially bound polypeptide reaches native form (PubMed:7867798, PubMed:7915201). Can rescue kinetically trapped intermediates (PubMed:20603018). GroEL shows ATPase activity (PubMed:1676490, PubMed:379350, PubMed:9285593). ATP hydrolysis moves the reaction cycle forward but is not required for substrate folding (PubMed:9285593)", "gene_name": "groEL", "glycan_count": 0, "glycosylation_sites": [], "id": "P0A6F5", "name": "GroEL", "organism": "Escherichia coli (strain K12)", "uniprot_id": "P0A6F5" }, { "function": "Together with the chaperonin GroEL, plays an essential role in assisting protein folding (PubMed:10532860, PubMed:16751100, PubMed:1676490, PubMed:18418386, PubMed:18987317, PubMed:20603018, PubMed:24816391, PubMed:2573517, PubMed:2897629). The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding, probably by preventing aggregation and by entropically destabilizing folding intermediates (PubMed:16751100, PubMed:18418386, PubMed:18987317, PubMed:20603018, PubMed:24816391). GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel (PubMed:9285585). Regulates the ATPase activity of GroEL (PubMed:1361169, PubMed:1676490)", "gene_name": "groES", "glycan_count": 0, "glycosylation_sites": [], "id": "P0A6F9", "name": "GroES", "organism": "Escherichia coli (strain K12)", "uniprot_id": "P0A6F9" }, { "function": "The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (PubMed:33795473). TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (PubMed:2194289, PubMed:2363050, PubMed:2374612, PubMed:27193682, PubMed:33795473). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:27007846, PubMed:33795473). The TFIID complex structure can be divided into 3 modules TFIID-A, TFIID-B, and TFIID-C (PubMed:33795473). TBP forms the TFIID-A module together with TAF3 and TAF5 (PubMed:33795473). TBP is a general transcription factor that functions at the core of the TFIID complex (PubMed:2194289, PubMed:2363050, PubMed:2374612, PubMed:27193682, PubMed:33795473, PubMed:9836642). During assembly of the core PIC on the promoter, as part of TFIID, TBP binds to and also bends promoter DNA, irrespective of whether the promoter contains a TATA box (PubMed:33795473). Component of a BRF2-containing transcription factor complex that regulates transcription mediated by RNA polymerase III (PubMed:26638071). Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC during RNA polymerase I-dependent transcription (PubMed:15970593). The rate of PIC formation probably is primarily dependent on the rate of association of SL1 with the rDNA promoter (PubMed:15970593). SL1 is involved in stabilization of nucleolar transcription factor 1/UBTF on rDNA (PubMed:15970593)", "gene_name": "TBP", "glycan_count": 1, "glycosylation_sites": [], "id": "P20226", "name": "TATA-box binding protein (TBP)", "organism": "Homo sapiens", "uniprot_id": "P20226" }, { "function": "Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. It is subsequently lost, together with VP7, following virus entry into the host cell. Following entry into the host cell, low intracellular or intravesicular Ca(2+) concentration probably causes the calcium-stabilized VP7 trimers to dissociate from the virion. This step is probably necessary for the membrane-disrupting entry step and the release of VP4, which is locked onto the virion by VP7. During the virus exit from the host cell, VP4 seems to be required to target the newly formed virions to the host cell lipid rafts", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P11194", "name": "NSP4", "organism": "Rotavirus A (isolate RVA/Human/Italy/VA70/1975/G4P1A[8])", "uniprot_id": "P11194" }, { "function": "The B subunit is responsible for the binding of the holotoxin to specific receptors on the target cell surface, such as globotriaosylceramide (Gb3) in human intestinal microvilli", "gene_name": "stxB2", "glycan_count": 0, "glycosylation_sites": [], "id": "P09386", "name": "Shiga toxin", "organism": "Escherichia phage 933W", "uniprot_id": "P09386" }, { "function": "Accumulates harmlessly in the cytoplasmic membrane until it reaches a critical concentration that triggers the formation of micron-scale pores (holes) causing host cell membrane disruption and endolysin escape into the periplasmic space (Probable). Determines the precise timing of host cell lysis (By similarity). Participates with the endolysin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles from the host cell (By similarity)", "gene_name": "14", "glycan_count": 0, "glycosylation_sites": [], "id": "P11188", "name": "Rotavirus VP7", "organism": "Bacillus phage phi29", "uniprot_id": "P11188" }, { "function": "Capsid protein self assembles to form an icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and consisting of 180 capsid proteins (PubMed:10514371). A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry (PubMed:31182604, PubMed:9311906). The capsid encapsulates the genomic RNA and is decorated with VP2 proteins. Attaches virion to target cells by binding histo-blood group antigens (HBGAs) present on gastroduodenal epithelial cells (PubMed:12055602, PubMed:12825167, PubMed:16840313)", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q83884", "name": "Norwalk virus capsid protein", "organism": "Norovirus (strain Human/NoV/United States/Norwalk/1968/GI)", "uniprot_id": "Q83884" }, { "function": "The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase", "gene_name": "eltB", "glycan_count": 0, "glycosylation_sites": [], "id": "P32890", "name": "E. coli heat-labile enterotoxin B subunit (LT-B)", "organism": "Escherichia coli", "uniprot_id": "P32890" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q548U0", "name": "Mouse glutamate decarboxylase", "organism": "", "uniprot_id": "" }, { "function": "Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP1 mainly forms the vertices of the capsid (By similarity). Capsid protein VP1 interacts with host cell receptor PVR to provide virion attachment to target host cells (By similarity). This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis in Hela cells and through caveolin-mediated endocytosis in brain microvascular endothelial cells (By similarity). Tyrosine kinases are probably involved in the entry process (By similarity). Virus binding to PVR induces increased junctional permeability and rearrangement of junctional proteins (By similarity). Modulation of endothelial tight junctions, as well as cytolytic infection of endothelial cells themselves, may result in loss of endothelial integrity which may help the virus to reach the CNS (By similarity). After binding to its receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized (By similarity). Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm (By similarity)", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03302", "name": "VPI protein of foot and mouth disease virus", "organism": "Poliovirus type 3 (strains P3/Leon/37 and P3/Leon 12A[1]B)", "uniprot_id": "P03302" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03176", "name": "Herpesvirus thymidine kinase", "organism": "", "uniprot_id": "P03176" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04578 (gp120)", "name": "HIV-1 envelope glycoprotein (gp120/gp41)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01730 (human)", "name": "CD4", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01732 (human)", "name": "CD8", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P08637 (human)", "name": "CD16 (Fc\u03b3RIII)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P05362 (human)", "name": "ICAM-1", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04233 (human)", "name": "Invariant chain (CD74)", "organism": "", "uniprot_id": "" }, { "function": "Pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. Has bactericidal activity towards Gram-positive bacteria. May kill Gram-positive bacteria by interfering with peptidoglycan biosynthesis. Also binds to Gram-negative bacteria, and has bacteriostatic activity towards Gram-negative bacteria. Plays a role in innate immunity", "gene_name": "PGLYRP4", "glycan_count": 0, "glycosylation_sites": [ { "position": 22, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 39, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 109, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 145, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 247, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q96LB8", "name": "PGLRP-1 (Peptidoglycan recognition protein 1)", "organism": "Homo sapiens", "uniprot_id": "Q96LB8" }, { "function": "The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products", "gene_name": "rep", "glycan_count": 0, "glycosylation_sites": [], "id": "P0C6X8", "name": "Envelope protein (E)", "organism": "Murine coronavirus (strain 2)", "uniprot_id": "P0C6X8" }, { "function": "The replicase polyprotein of coronaviruses is a multifunctional protein: it contains the activities necessary for the transcription of negative stranded RNA, leader RNA, subgenomic mRNAs and progeny virion RNA as well as proteinases responsible for the cleavage of the polyprotein into functional products", "gene_name": "rep", "glycan_count": 0, "glycosylation_sites": [], "id": "P0C6X9", "name": "Nucleocapsid protein (N)", "organism": "Murine coronavirus (strain A59)", "uniprot_id": "P0C6X9" }, { "function": "Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors. It is subsequently lost, together with VP7, following virus entry into the host cell. Following entry into the host cell, low intracellular or intravesicular Ca(2+) concentration probably causes the calcium-stabilized VP7 trimers to dissociate from the virion. This step is probably necessary for the membrane-disrupting entry step and the release of VP4, which is locked onto the virion by VP7. During the virus exit from the host cell, VP4 seems to be required to target the newly formed virions to the host cell lipid rafts", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P13842", "name": "RSV G protein", "organism": "Rotavirus A (strain RVA/Human/Japan/KU/1995/G1P1A[8])", "uniprot_id": "P13842" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q0ZME7 (OC43)", "name": "Coronavirus HE protein", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P59596 (SARS-CoV)", "name": "Coronavirus M protein", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P29990 (DENV-2)", "name": "Envelope protein (E)", "organism": "", "uniprot_id": "" }, { "function": "Putative oxidoreductase. Acts as a tumor suppressor and plays a role in apoptosis. Required for normal bone development (By similarity). May function synergistically with p53/TP53 to control genotoxic stress-induced cell death. Plays a role in TGFB1 signaling and TGFB1-mediated cell death. May also play a role in tumor necrosis factor (TNF)-mediated cell death. Inhibits Wnt signaling, probably by sequestering DVL2 in the cytoplasm", "gene_name": "WWOX", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NZC7", "name": "C-type lectin domain family 5, member A (CLEC5A)", "organism": "Homo sapiens", "uniprot_id": "Q9NZC7" }, { "function": "", "gene_name": "env", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9QF73", "name": "US28", "organism": "Human immunodeficiency virus type 1", "uniprot_id": "Q9QF73" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03437 (H1N1 HA)", "name": "Influenza Hemagglutinin (HA)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03101 (HPV16)", "name": "HPV L1 Protein (VLP component)", "organism": "", "uniprot_id": "" }, { "function": "Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P08562", "name": "Rubella Virus E1 Glycoprotein", "organism": "Trypanosoma cruzi", "uniprot_id": "P08562" }, { "function": "The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II ManXYZ PTS system is involved in mannose transport", "gene_name": "manX", "glycan_count": 0, "glycosylation_sites": [], "id": "P69798", "name": "HBV e Antigen (HBeAg)", "organism": "Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)", "uniprot_id": "P69798" }, { "function": "Innate immune receptor that senses cytoplasmic viral nucleic acids and activates a downstream signaling cascade leading to the production of type I interferons and pro-inflammatory cytokines (PubMed:15208624, PubMed:15708988, PubMed:16125763, PubMed:16127453, PubMed:16153868, PubMed:17190814, PubMed:18636086, PubMed:19122199, PubMed:19211564, PubMed:24366338, PubMed:28469175, PubMed:29117565, PubMed:31006531, PubMed:34935440, PubMed:35263596, PubMed:36793726). Forms a ribonucleoprotein complex with viral RNAs on which it homooligomerizes to form filaments (PubMed:15208624, PubMed:15708988). The homooligomerization allows the recruitment of RNF135 an E3 ubiquitin-protein ligase that activates and amplifies the RIG-I-mediated antiviral signaling in an RNA length-dependent manner through ubiquitination-dependent and -independent mechanisms (PubMed:28469175, PubMed:31006531). Upon activation, associates with mitochondria antiviral signaling protein (MAVS/IPS1) that activates the IKK-related kinases TBK1 and IKBKE which in turn phosphorylate the interferon regulatory factors IRF3 and IRF7, activating transcription of antiviral immunological genes including the IFN-alpha and IFN-beta interferons (PubMed:28469175, PubMed:31006531). Ligands include 5'-triphosphorylated ssRNAs and dsRNAs but also short dsRNAs (<1 kb in length) (PubMed:15208624, PubMed:15708988, PubMed:19576794, PubMed:19609254, PubMed:21742966). In addition to the 5'-triphosphate moiety, blunt-end base pairing at the 5'-end of the RNA is very essential (PubMed:15208624, PubMed:15708988, PubMed:19576794, PubMed:19609254, PubMed:21742966). Overhangs at the non-triphosphorylated end of the dsRNA RNA have no major impact on its activity (PubMed:15208624, PubMed:15708988, PubMed:19576794, PubMed:19609254, PubMed:21742966). A 3'overhang at the 5'triphosphate end decreases and any 5'overhang at the 5' triphosphate end abolishes its activity (PubMed:15208624, PubMed:15708988, PubMed:19576794, PubMed:19609254, PubMed:21742966). Detects both positive and negative strand RNA viruses including members of the families Paramyxoviridae: Human respiratory syncytial virus and measles virus (MeV), Rhabdoviridae: vesicular stomatitis virus (VSV), Orthomyxoviridae: influenza A and B virus, Flaviviridae: Japanese encephalitis virus (JEV), hepatitis C virus (HCV), dengue virus (DENV) and west Nile virus (WNV) (PubMed:21616437, PubMed:21884169). It also detects rotaviruses and reoviruses (PubMed:21616437, PubMed:21884169). Detects and binds to SARS-CoV-2 RNAs which is inhibited by m6A RNA modifications (Ref.74). Also involved in antiviral signaling in response to viruses containing a dsDNA genome such as Epstein-Barr virus (EBV) (PubMed:19631370). Detects dsRNA produced from non-self dsDNA by RNA polymerase III, such as Epstein-Barr virus-encoded RNAs (EBERs). May play important roles in granulocyte production and differentiation, bacterial phagocytosis and in the regulation of cell migration", "gene_name": "RIGI", "glycan_count": 2, "glycosylation_sites": [], "id": "O95786", "name": "RIG-I (DDX58)", "organism": "Homo sapiens", "uniprot_id": "O95786" }, { "function": "Acts as a regulator of RIGI and IFIH1/MDA5 mediated antiviral signaling. Cannot initiate antiviral signaling as it lacks the CARD domain required for activating MAVS/IPS1-dependent signaling events. Can have both negative and positive regulatory functions related to RIGI and IFIH1/MDA5 signaling and this role in regulating signaling may be complex and could probably depend on characteristics of the infecting virus or target cells, or both. Its inhibitory action on RIG-I signaling may involve the following mechanisms: competition with RIGI for binding to the viral RNA, binding to RIGI and inhibiting its dimerization and interaction with MAVS/IPS1, competing with IKBKE in its binding to MAVS/IPS1 thereby inhibiting activation of interferon regulatory factor 3 (IRF3). Its positive regulatory role may involve unwinding or stripping nucleoproteins of viral RNA thereby facilitating their recognition by RIGI and IFIH1/MDA5. Involved in the innate immune response to various RNA viruses and some DNA viruses such as poxviruses and coronavirus SARS-CoV-2, and also to the bacterial pathogen Listeria monocytogenes (PubMed:31256877). Can bind both ssRNA and dsRNA, with a higher affinity for dsRNA. Shows a preference to 5'-triphosphorylated RNA, although it can recognize RNA lacking a 5'-triphosphate", "gene_name": "DHX58", "glycan_count": 0, "glycosylation_sites": [], "id": "Q96C10", "name": "LGP2 (DHX58)", "organism": "Homo sapiens", "uniprot_id": "Q96C10" }, { "function": "E3 ubiquitin-protein ligase (PubMed:26656854). Required for mesoderm patterning during embryonic development (By similarity). Acts as an enhancer of the transcriptional responses of the SMAD2/SMAD3 effectors, which are activated downstream of BMP (PubMed:14657019, PubMed:16601693). Acts by mediating ubiquitination and degradation of SMAD inhibitors such as SMAD7, inducing their proteasomal degradation and thereby enhancing the transcriptional activity of TGF-beta and BMP (PubMed:14657019, PubMed:16601693). In addition to enhance transcription of SMAD2/SMAD3 effectors, also regulates their turnover by mediating their ubiquitination and subsequent degradation, coupling their activation with degradation, thereby ensuring that only effectors 'in use' are degraded (By similarity). Activates SMAD3/SMAD4-dependent transcription by triggering signal-induced degradation of SNON isoform of SKIL (PubMed:17591695). Associates with UBE2D2 as an E2 enzyme (PubMed:22411132). Specifically binds polysumoylated chains via SUMO interaction motifs (SIMs) and mediates ubiquitination of sumoylated substrates (PubMed:23751493). Catalyzes 'Lys-63'-linked ubiquitination of sumoylated XPC in response to UV irradiation, promoting nucleotide excision repair (PubMed:23751493). Mediates ubiquitination and degradation of sumoylated PML (By similarity). The regulation of the BMP-SMAD signaling is however independent of sumoylation and is not dependent of SUMO interaction motifs (SIMs) (By similarity)", "gene_name": "RNF111", "glycan_count": 1, "glycosylation_sites": [], "id": "Q6ZNA4", "name": "Riplet (RNF135)", "organism": "Homo sapiens", "uniprot_id": "Q6ZNA4" }, { "function": "IFN-induced dsRNA-dependent serine/threonine-protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) and plays a key role in the innate immune response to viral infection (PubMed:18835251, PubMed:19189853, PubMed:19507191, PubMed:21072047, PubMed:21123651, PubMed:22381929, PubMed:22948139, PubMed:23229543). Inhibits viral replication via the integrated stress response (ISR): EIF2S1/eIF-2-alpha phosphorylation in response to viral infection converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, resulting to a shutdown of cellular and viral protein synthesis, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4 (PubMed:19189853, PubMed:21123651, PubMed:22948139, PubMed:23229543). Exerts its antiviral activity on a wide range of DNA and RNA viruses including hepatitis C virus (HCV), hepatitis B virus (HBV), measles virus (MV) and herpes simplex virus 1 (HHV-1) (PubMed:11836380, PubMed:19189853, PubMed:19840259, PubMed:20171114, PubMed:21710204, PubMed:23115276, PubMed:23399035). Also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation: phosphorylates other substrates including p53/TP53, PPP2R5A, DHX9, ILF3, IRS1 and the HHV-1 viral protein US11 (PubMed:11836380, PubMed:19229320, PubMed:22214662). In addition to serine/threonine-protein kinase activity, also has tyrosine-protein kinase activity and phosphorylates CDK1 at 'Tyr-4' upon DNA damage, facilitating its ubiquitination and proteasomal degradation (PubMed:20395957). Either as an adapter protein and/or via its kinase activity, can regulate various signaling pathways (p38 MAP kinase, NF-kappa-B and insulin signaling pathways) and transcription factors (JUN, STAT1, STAT3, IRF1, ATF3) involved in the expression of genes encoding pro-inflammatory cytokines and IFNs (PubMed:22948139, PubMed:23084476, PubMed:23372823). Activates the NF-kappa-B pathway via interaction with IKBKB and TRAF family of proteins and activates the p38 MAP kinase pathway via interaction with MAP2K6 (PubMed:10848580, PubMed:15121867, PubMed:15229216). Can act as both a positive and negative regulator of the insulin signaling pathway (ISP) (PubMed:20685959). Negatively regulates ISP by inducing the inhibitory phosphorylation of insulin receptor substrate 1 (IRS1) at 'Ser-312' and positively regulates ISP via phosphorylation of PPP2R5A which activates FOXO1, which in turn up-regulates the expression of insulin receptor substrate 2 (IRS2) (PubMed:20685959). Can regulate NLRP3 inflammasome assembly and the activation of NLRP3, NLRP1, AIM2 and NLRC4 inflammasomes (PubMed:22801494). Plays a role in the regulation of the cytoskeleton by binding to gelsolin (GSN), sequestering the protein in an inactive conformation away from actin (By similarity)", "gene_name": "EIF2AK2", "glycan_count": 2, "glycosylation_sites": [], "id": "P19525", "name": "PKR (EIF2AK2)", "organism": "Homo sapiens", "uniprot_id": "P19525" }, { "function": "This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly", "gene_name": "rplM", "glycan_count": 0, "glycosylation_sites": [], "id": "P0AA10", "name": "ClyA", "organism": "Escherichia coli (strain K12)", "uniprot_id": "P0AA10" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04489 (HSV-1)", "name": "Glycoprotein D (gD)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P26664 (HCV)", "name": "Envelope glycoprotein (E2)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q706L7 (EBV)", "name": "gp42", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P06437 (HSV-1)", "name": "Glycoprotein B (gB)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P11194 (Rotavirus)", "name": "VP4", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04578/P04585", "name": "HIV envelope glycoprotein (gp120/gp41)", "organism": "", "uniprot_id": "" }, { "function": "Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) interacts with HN tetramer at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis", "gene_name": "F", "glycan_count": 0, "glycosylation_sites": [ { "position": 104, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 245, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 449, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P04854", "name": "Measles Virus Hemagglutinin", "organism": "Sendai virus (strain Z)", "uniprot_id": "P04855" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8K3Z0 (mouse)", "name": "Siglec-E", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P11224 (MHV S)", "name": "Spike glycoprotein (S)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P11225 (MHV M)", "name": "Transmembrane glycoprotein (M)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9D8S9 (MHV HE)", "name": "Hemagglutinin-esterase (HE)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P11226 (MHV E)", "name": "Envelope protein (E)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q61549 (mouse)", "name": "Carcinoembryonic antigen cell adhesion molecule 1a (CEACAM-1a)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P11223 (MHV N)", "name": "Nucleocapsid protein (N)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P28862 (mouse)", "name": "Matrix metalloproteinase 3 (MMP3)", "organism": "", "uniprot_id": "" }, { "function": "Modulates host cell cycle progression and apoptotic signaling pathways by acting as a cyclin. Forms an active kinase complex with cellular CDK6 kinase. Promotes host S-phase entry of quiescent cells and activates host cyclin A. Triggers host apoptosis by inactivating host BCL2", "gene_name": "ORF72", "glycan_count": 0, "glycosylation_sites": [], "id": "Q77Q36", "name": "HHV-8 K5", "organism": "Human herpesvirus 8 type P (isolate GK18)", "uniprot_id": "Q77Q36" }, { "function": "Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication", "gene_name": "N", "glycan_count": 0, "glycosylation_sites": [], "id": "K9N4V7", "name": "Nucleocapsid (N) protein", "organism": "Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012)", "uniprot_id": "K9N4V7" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P27915 (DENV2)", "name": "NS1", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04489 (HSV1)", "name": "Glycoprotein G (gG)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q67175 (EV71)", "name": "VP1", "organism": "", "uniprot_id": "" }, { "function": "Is, with PLP, the most abundant protein component of the myelin membrane in the CNS. Has a role in both the formation and stabilization of this compact multilayer arrangement of bilayers. Each splice variant and charge isomer may have a specialized function in the assembly of an optimized, biochemically functional myelin membrane (By similarity)", "gene_name": "Mbp", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Z1J6", "name": "Ionized Calcium Binding Adapter Molecule 1 (Iba1)", "organism": "Rattus norvegicus", "uniprot_id": "P02688" }, { "function": "Required for oligodendrocyte and motor neuron specification in the spinal cord, as well as for the development of somatic motor neurons in the hindbrain. Functions together with ZNF488 to promote oligodendrocyte differentiation. Cooperates with OLIG1 to establish the pMN domain of the embryonic neural tube. Antagonist of V2 interneuron and of NKX2-2-induced V3 interneuron development", "gene_name": "OLIG2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q13516", "name": "Oligodendrocyte Transcription Factor 2 (Olig2)", "organism": "Homo sapiens", "uniprot_id": "Q13516" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02708 (alpha subunit, human)", "name": "Acetylcholine receptor", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O14793 (human)", "name": "Myostatin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01876 (human)", "name": "Immunoglobulin A (IgA)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q04446 (human)", "name": "Glycogen branching enzyme (GBE)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P13807 (human)", "name": "Glycogen synthase 1 (GYS1)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P06732 (human, muscle type)", "name": "Creatine kinase (CK)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P05413 (human, muscle type)", "name": "Fatty acid binding protein", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P07451 (human)", "name": "Carbonic anhydrase III", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P08605", "name": "CD45", "organism": "", "uniprot_id": "" }, { "function": "Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress", "gene_name": "prx26", "glycan_count": 0, "glycosylation_sites": [], "id": "Q5U1R7", "name": "CD31 (PECAM-1)", "organism": "Oryza sativa subsp. japonica", "uniprot_id": "Q5U1R7" }, { "function": "High affinity receptor for the C-C type chemokines CCL17/TARC and CCL22/MDC. The activity of this receptor is mediated by G(i) proteins which activate a phosphatidylinositol-calcium second messenger system. Could play a role in lipopolysaccharide (LPS)-induced endotoxic shock. In the CNS, could mediate hippocampal-neuron survival (By similarity)", "gene_name": "CCR4", "glycan_count": 0, "glycosylation_sites": [ { "position": 183, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 194, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8MJW8", "name": "CD34", "organism": "Canis lupus familiaris", "uniprot_id": "Q8MJW8" }, { "function": "Chaperone protein which promotes assembly of the 20S proteasome. May cooperate with PSMG1-PSMG2 heterodimers to orchestrate the correct assembly of proteasomes", "gene_name": "PSMG3", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9BT73", "name": "Uroplakin III", "organism": "Homo sapiens", "uniprot_id": "Q9BT73" }, { "function": "Tubulin is the major constituent of microtubules, protein filaments consisting of alpha- and beta-tubulin heterodimers (PubMed:38305685, PubMed:34996871, PubMed:38609661). Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms (PubMed:38305685, PubMed:34996871, PubMed:38609661). Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin (PubMed:34996871, PubMed:38609661)", "gene_name": "TUBA1B", "glycan_count": 2, "glycosylation_sites": [], "id": "P68363", "name": "Tubulin", "organism": "Homo sapiens", "uniprot_id": "P68363" }, { "function": "Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue", "gene_name": "PRXC1A", "glycan_count": 0, "glycosylation_sites": [ { "position": 43, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 87, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 188, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 216, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 228, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 244, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 285, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 298, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P00433", "name": "Horseradish peroxidase", "organism": "Armoracia rusticana", "uniprot_id": "P00433" }, { "function": "Monomeric heme protein which primary function is to store oxygen and facilitate its diffusion within muscle tissues. Reversibly binds oxygen through a pentacoordinated heme iron and enables its timely and efficient release as needed during periods of heightened demand. Depending on the oxidative conditions of tissues and cells, and in addition to its ability to bind oxygen, it also has a nitrite reductase activity whereby it regulates the production of bioactive nitric oxide. Under stress conditions, like hypoxia and anoxia, it also protects cells against reactive oxygen species thanks to its pseudoperoxidase activity", "gene_name": "MB", "glycan_count": 0, "glycosylation_sites": [], "id": "P02185", "name": "Hemoglobin", "organism": "Physeter macrocephalus", "uniprot_id": "P02185" }, { "function": "Chromatin-associated factor that regulates transcription (PubMed:29065309). Regulates Pol I-mediated rRNA biogenesis and, probably, Pol III-mediated transcription (PubMed:29065309). Regulates the epigenetic status of rDNA (PubMed:29065309)", "gene_name": "PWP1", "glycan_count": 1, "glycosylation_sites": [], "id": "Q13610", "name": "Reelin", "organism": "Homo sapiens", "uniprot_id": "Q13610" }, { "function": "Cytokine with antiviral, antitumour and immunomodulatory activities. Plays a critical role in the antiviral host defense, predominantly in the epithelial tissues. Acts as a ligand for the heterodimeric class II cytokine receptor composed of IL10RB and IFNLR1, and receptor engagement leads to the activation of the JAK/STAT signaling pathway resulting in the expression of IFN-stimulated genes (ISG), which mediate the antiviral state. Has a restricted receptor distribution and therefore restricted targets: is primarily active in epithelial cells and this cell type-selective action is because of the epithelial cell-specific expression of its receptor IFNLR1. Exerts an immunomodulatory effect by up-regulating MHC class I antigen expression", "gene_name": "IFNL1", "glycan_count": 0, "glycosylation_sites": [ { "position": 65, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q8IU54", "name": "IFN-\u03bb4", "organism": "Homo sapiens", "uniprot_id": "Q8IU54" }, { "function": "Involved in the binding of tRNA to the ribosomes", "gene_name": "rps10", "glycan_count": 0, "glycosylation_sites": [], "id": "P19460", "name": "Troponin-I", "organism": "Guillardia theta", "uniprot_id": "P19460" }, { "function": "Induces vacuolation of eukaryotic cells. Causes ulceration and gastric lesions", "gene_name": "vacA", "glycan_count": 0, "glycosylation_sites": [], "id": "Q48245", "name": "CagA", "organism": "Helicobacter pylori", "uniprot_id": "Q48245" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O25831", "name": "BabA2", "organism": "Helicobacter pylori (strain ATCC 700392 / 26695)", "uniprot_id": "O25831" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P56112", "name": "VacA", "organism": "Helicobacter pylori (strain ATCC 700392 / 26695)", "uniprot_id": "P56112" }, { "function": "Cleaves host elastin, collagen, IgG, and several complement components as well as endogenous pro-aminopeptidase (PubMed:11533066). Autocatalyses processing of its pro-peptide (PubMed:1744034, PubMed:9642203). Processes the pro-peptide of pro-chitin-binding protein (cbpD) (PubMed:9642203). Involved in the pathogenesis of P.aeruginosa infections", "gene_name": "lasB", "glycan_count": 0, "glycosylation_sites": [], "id": "P14756", "name": "Elastase", "organism": "Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)", "uniprot_id": "P14756" }, { "function": "Hydrolyzes a wide range of dipeptides including the conversion of leukotriene D4 to leukotriene E4 (PubMed:2303490, PubMed:31442408, PubMed:32325220, PubMed:6334084). Hydrolyzes cystinyl-bis-glycine (cys-bis-gly) formed during glutathione degradation (PubMed:32325220). Also possesses beta lactamase activity and can hydrolyze the beta-lactam antibiotic imipenem (PubMed:32325220, PubMed:6334084)", "gene_name": "DPEP1", "glycan_count": 141, "glycosylation_sites": [ { "position": 57, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 279, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 332, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 358, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P16444", "name": "Cysteinylglycine dipeptidase (Renal dipeptidase, DPEP1)", "organism": "Homo sapiens", "uniprot_id": "P16444" }, { "function": "Sodium channel mediating the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which sodium ions may pass in accordance with their electrochemical gradient (PubMed:10580103, PubMed:12384689, PubMed:24036948, PubMed:24776970, PubMed:25791876, PubMed:26645915). Involved in membrane depolarization during action potential in nociceptors which function as key relay stations for the electrical transmission of pain signals from the periphery to the central nervous system (PubMed:24036948, PubMed:24776970, PubMed:25791876, PubMed:26645915). Also involved in rapid BDNF-evoked neuronal depolarization (PubMed:12384689)", "gene_name": "SCN11A", "glycan_count": 1, "glycosylation_sites": [ { "position": 290, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 338, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 781, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1209, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1216, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1222, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1230, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 1568, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9UI33", "name": "Leucyl aminopeptidase (LAP3)", "organism": "Homo sapiens", "uniprot_id": "Q9UI33" }, { "function": "", "gene_name": "UL4", "glycan_count": 0, "glycosylation_sites": [ { "position": 46, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 51, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 59, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 67, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 105, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 109, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 119, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 136, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 145, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "Q6SWC6", "name": "UL97", "organism": "Human cytomegalovirus (strain Merlin)", "uniprot_id": "Q6SWC6" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P51681/P61073", "name": "Chemokine receptors (e.g., CCR5, CXCR4)", "organism": "", "uniprot_id": "" }, { "function": "Structural component of specialized membrane microdomains known as tetraspanin-enriched microdomains (TERMs), which act as platforms for receptor clustering and signaling (PubMed:28487417). Participates thereby in diverse biological functions such as cell signal transduction, adhesion, migration and protein trafficking (PubMed:32974937, PubMed:35767951). Plays a role in the activation of monocytes and B-cells (PubMed:8335905). Acts as an essential regulator of B-cell development by promoting interleukin-7 receptor/IL7R signaling (By similarity). Also promotes, in B-cells, the BCR signaling by recruiting PKC to the plasma membrane in order to phosphorylate its substrates (PubMed:28487417). Plays an essential role in B- and T-cells homing to lymph nodes by stabilizing L-selectin/SELL cell surface expression (By similarity). Also mediates metabolic and inflammatory functions in hepatocytes and adipose tissue by promoting TNF-alpha and LPS signaling independent of the immune compartment (By similarity)", "gene_name": "CD53", "glycan_count": 4, "glycosylation_sites": [ { "position": 129, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 148, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P19397", "name": "CD53 glycoprotein", "organism": "Homo sapiens", "uniprot_id": "P19397" }, { "function": "Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy (PubMed:29895852). The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP2 may act as a secondary sperm receptor (PubMed:29895852)", "gene_name": "ZP2", "glycan_count": 0, "glycosylation_sites": [ { "position": 105, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 122, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 462, "type": "O-linked (GalNAc...) threonine" } ], "id": "Q05996", "name": "Zona pellucida glycoprotein 2", "organism": "Homo sapiens", "uniprot_id": "Q05996" }, { "function": "Involved in the mineralization and structural organization of enamel", "gene_name": "AMBN", "glycan_count": 0, "glycosylation_sites": [ { "position": 112, "type": "O-linked (GalNAc...) serine" } ], "id": "Q9NP70", "name": "Scavenger receptor class A, member 3", "organism": "Homo sapiens", "uniprot_id": "Q9NP70" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P01137/P61812", "name": "TGF\u03b21/2", "organism": "", "uniprot_id": "" }, { "function": "Self-ligand receptor of the signaling lymphocytic activation molecule (SLAM) family. SLAM receptors triggered by homo- or heterotypic cell-cell interactions are modulating the activation and differentiation of a wide variety of immune cells and thus are involved in the regulation and interconnection of both innate and adaptive immune response. Activities are controlled by presence or absence of small cytoplasmic adapter proteins, SH2D1A/SAP and/or SH2D1B/EAT-2. SLAMF1-induced signal-transduction events in T-lymphocytes are different from those in B-cells. Two modes of SLAMF1 signaling seem to exist: one depending on SH2D1A (and perhaps SH2D1B) and another in which protein-tyrosine phosphatase 2C (PTPN11)-dependent signal transduction operates. Initially it has been proposed that association with SH2D1A prevents binding to inhibitory effectors including INPP5D/SHIP1 and PTPN11/SHP-2 (PubMed:11806999). However, signaling is also regulated by SH2D1A which can simultaneously interact with and recruit FYN which subsequently phosphorylates and activates SLAMF1 (PubMed:12458214). Mediates IL-2-independent proliferation of activated T-cells during immune responses and induces IFN-gamma production (By similarity). Downstreaming signaling involves INPP5D, DOK1 and DOK2 leading to inhibited IFN-gamma production in T-cells, and PRKCQ, BCL10 and NFKB1 leading to increased T-cell activation and Th2 cytokine production (By similarity). Promotes T-cell receptor-induced IL-4 secretion by CD4(+) cells (By similarity). Inhibits antigen receptor-mediated production of IFN-gamma, but not IL-2, in CD4(-)/CD8(-) T-cells (By similarity). Required for IL-4 production by germinal centers T follicular helper (T(Fh))cells (By similarity). May inhibit CD40-induced signal transduction in monocyte-derived dendritic cells (PubMed:16317102). May play a role in allergic responses and may regulate allergen-induced Th2 cytokine and Th1 cytokine secretion (By similarity). In conjunction with SLAMF6 controls the transition between positive selection and the subsequent expansion and differentiation of the thymocytic natural killer T (NKT) cell lineage. Involved in the peripheral differentiation of indifferent natural killer T (iNKT) cells toward a regulatory NKT2 type (By similarity). In macrophages involved in down-regulation of IL-12, TNF-alpha and nitric oxide in response to lipopolysaccharide (LPS) (By similarity). In B-cells activates the ERK signaling pathway independently of SH2D1A but implicating both, SYK and INPP5D, and activates Akt signaling dependent on SYK and SH2D1A (By similarity). In B-cells also activates p38 MAPK and JNK1 and JNK2 (PubMed:20231852). In conjunction with CD84/SLAMF5 and SLAMF6 may be a negative regulator of the humoral immune response (By similarity). Involved in innate immune response against Gram-negative bacteria in macrophages; probably recognizes OmpC and/or OmpF on the bacterial surface, regulates phagosome maturation and recruitment of the PI3K complex II (PI3KC3-C2) leading to accumulation of PdtIns(3)P and NOX2 activity in the phagosomes (PubMed:20818396)", "gene_name": "SLAMF1", "glycan_count": 0, "glycosylation_sites": [ { "position": 53, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 57, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 102, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 125, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 150, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 155, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 189, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 217, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q13291", "name": "SR-A (Scavenger Receptor A)", "organism": "Homo sapiens", "uniprot_id": "Q13291" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P33400/P11247", "name": "Measles virus H/F glycoprotein complex", "organism": "", "uniprot_id": "" }, { "function": "Antigen-presenting major histocompatibility complex class I (MHCI) molecule with an important role in reproduction and antiviral immunity (PubMed:11172028, PubMed:20104487, PubMed:20439706, PubMed:20972337, PubMed:24091323, PubMed:28649982, PubMed:29312307). In complex with B2M/beta 2 microglobulin displays a restricted repertoire of self and viral peptides and acts as a dominant ligand for inhibitory and activating killer immunoglobulin receptors (KIRs) expressed on NK cells (PubMed:16141329). In an allogeneic setting, such as during pregnancy, mediates interaction of extravillous trophoblasts with KIR on uterine NK cells and regulate trophoblast invasion necessary for placentation and overall fetal growth (PubMed:20972337, PubMed:24091323). During viral infection, may present viral peptides with low affinity for KIRs, impeding KIR-mediated inhibition through peptide antagonism and favoring lysis of infected cells (PubMed:20439706). Presents a restricted repertoire of viral peptides on antigen-presenting cells for recognition by alpha-beta T cell receptor (TCR) on HLA-C-restricted CD8-positive T cells, guiding antigen-specific T cell immune response to eliminate infected cells, particularly in chronic viral infection settings such as HIV-1 or CMV infection (PubMed:11172028, PubMed:20104487, PubMed:28649982). Both the peptide and the MHC molecule are recognized by TCR, the peptide is responsible for the fine specificity of antigen recognition and MHC residues account for the MHC restriction of T cells (By similarity). Typically presents intracellular peptide antigens of 9 amino acids that arise from cytosolic proteolysis via proteasome. Can bind different peptides containing allele-specific binding motifs, which are mainly defined by anchor residues at position 2 and 9. Preferentially displays peptides having a restricted repertoire of hydrophobic or aromatic amino acids (Phe, Ile, Leu, Met, Val and Tyr) at the C-terminal anchor (PubMed:25311805, PubMed:8265661)", "gene_name": "HLA-C", "glycan_count": 0, "glycosylation_sites": [ { "position": 110, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P04222", "name": "HLA-C", "organism": "Homo sapiens", "uniprot_id": "P10321" }, { "function": "S1 is an NAD-dependent ADP-ribosyltransferase, which plays a crucial role in the pathogenesis of B.pertussis causing disruption of normal host cellular regulation. It catalyzes the ADP-ribosylation of a cysteine in the alpha subunit of host heterotrimeric G proteins. In the absence of G proteins it also catalyzes the cleavage of NAD(+) into ADP-ribose and nicotinamide. It irreversibly uncouples the G-alpha GTP-binding proteins from their membrane receptors", "gene_name": "ptxA", "glycan_count": 0, "glycosylation_sites": [], "id": "P04977", "name": "Filamentous hemagglutinin (B. pertussis)", "organism": "Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)", "uniprot_id": "P04977" }, { "function": "Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or both. The LMAN1-MCFD2 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins", "gene_name": "LMAN1", "glycan_count": 5, "glycosylation_sites": [], "id": "P49257", "name": "p58/ERGIC-53", "organism": "Homo sapiens", "uniprot_id": "P49257" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "O35111 (mouse)", "name": "Nephrin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02468 (human LAMA1)", "name": "Laminin", "organism": "", "uniprot_id": "" }, { "function": "The restriction (R) subunit of a type I restriction enzyme that recognizes 5'-GAAN(6)RTCG-3' (for EcoR124I) and 5'-GAAN(7)RTCG-3' (for EcoR124II) and cleaves a random distance away (PubMed:2784505). Subunit R is required for both nuclease and ATPase activities, but not for modification (Probable) (PubMed:12654995). After locating an unmethylated recognition site, the enzyme complex serves as a molecular motor that translocates DNA in an ATP-dependent manner until a collision occurs that triggers cleavage (PubMed:15300241). The enzyme undergoes major structural changes to bring the motor domains into contact with DNA, allowing DNA translocation. This prevents DNA access to the catalytic domains of both the R and M subunits, preventing both restriction and methylation (PubMed:32483229). The R(1)M(2)S(1) complex translocates an average of 555 bp/second on nicked DNA; the R(2)M(2)S(1) complex translocates at double that speed (PubMed:15300241). The 2 R subunit motors are independent and track along the helical pitch of the DNA, inducing positive supercoiling ahead of themselves (PubMed:15300241)", "gene_name": "hsdR", "glycan_count": 0, "glycosylation_sites": [], "id": "P10486", "name": "Entactin (nidogen)", "organism": "Escherichia coli", "uniprot_id": "P10486" }, { "function": "Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen cell proliferative response in vitro, contributing significantly to the immunostimulatory activity of S.aureus", "gene_name": "clfA", "glycan_count": 0, "glycosylation_sites": [], "id": "Q53653", "name": "Streptococcal C5a peptidase", "organism": "Staphylococcus aureus (strain Newman)", "uniprot_id": "Q53653" }, { "function": "Diphtheria toxin, produced by a phage infecting Corynebacterium diphtheriae, is a proenzyme that, after activation, catalyzes the covalent attachment of the ADP ribose moiety of NAD to elongation factor 2. Fragment A is responsible for enzymatic ADP-ribosylation of elongation factor 2, while fragment B is responsible for binding of toxin to cell receptors and entry of fragment A", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P00587", "name": "Diphtheria toxoid", "organism": "Corynephage omega", "uniprot_id": "P00587" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02949", "name": "Group A Streptococcus M protein", "organism": "", "uniprot_id": "P02949" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04085 (human)", "name": "PDGF (platelet-derived growth factor)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02340 (cat)", "name": "p53", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q04206 (cat)", "name": "NF-\u03baB", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P19751 (CSFV)", "name": "Envelope glycoprotein E2", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Q879 (PEDV)", "name": "Spike (S) protein", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P10213 (SuHV-1)", "name": "Glycoprotein E (gE)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P10214 (SuHV-1)", "name": "Glycoprotein I (gI)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9YFA3 (PCV2)", "name": "Capsid protein", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03452 (Influenza A)", "name": "Hemagglutinin (HA)", "organism": "", "uniprot_id": "" }, { "function": "Metalloprotease, specifically cleaves on the N-terminal side of aspartyl, glutamyl and cysteic acid residues", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9R4J4", "name": "P. multocida toxin", "organism": "Pseudomonas fragi", "uniprot_id": "Q9R4J4" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P07359/P14770/P13224", "name": "Platelet glycoprotein GPIb-IX complex", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9Q6Q1", "name": "West Nile virus envelope glycoprotein", "organism": "Grapevine leafroll-associated virus 1", "uniprot_id": "Q9Q6Q1" }, { "function": "Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migrate to the cell nucleus where it modulates host functions. Overcomes the anti-viral effects of host EXOC1 by sequestering and degrading the latter through the proteasome degradation pathway", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [ { "position": 142, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 448, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 924, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1001, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "P27395", "name": "Japanese encephalitis virus envelope glycoprotein", "organism": "Japanese encephalitis virus (strain SA-14)", "uniprot_id": "P27395" }, { "function": "As part of the pyruvate dehydrogenase complex, catalyzes the transfers of an acetyl group to a lipoic acid moiety (PubMed:3117054). The pyruvate dehydrogenase complex, catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links cytoplasmic glycolysis and the mitochondrial tricarboxylic acid (TCA) cycle (Probable)", "gene_name": "DLAT", "glycan_count": 0, "glycosylation_sites": [], "id": "P11180", "name": "VP7", "organism": "Bos taurus", "uniprot_id": "P11180" }, { "function": "Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling (PubMed:19029295, PubMed:2022671, PubMed:2472670, PubMed:8119955). Mediates responses to increased cellular Ca(2+)/calmodulin levels (PubMed:19029295, PubMed:2022671). May be involved in regulatory processes in the central nervous system. May play a role in memory and learning. Plays a role in the regulation of the circadian rhythm of daytime contrast sensitivity probably by modulating the rhythmic synthesis of cyclic AMP in the retina (By similarity)", "gene_name": "ADCY1", "glycan_count": 0, "glycosylation_sites": [ { "position": 706, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P19754", "name": "NSP4", "organism": "Bos taurus", "uniprot_id": "P19754" }, { "function": "The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). Within this complex, the catalytic function of this enzyme is to accept, and to transfer to coenzyme A, acyl groups that are generated by the branched-chain alpha-keto acid decarboxylase component", "gene_name": "DBT", "glycan_count": 0, "glycosylation_sites": [], "id": "P11181", "name": "VP4", "organism": "Bos taurus", "uniprot_id": "P11181" }, { "function": "Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P21895", "name": "Mast cell tryptase (alpha-tryptase)", "organism": "Chironomus thummi thummi", "uniprot_id": "P21895" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "varies by strain (e.g., P03437 for H1N1)", "name": "Hemagglutinin (HA)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "varies by strain (e.g., P03468 for H1N1)", "name": "Neuraminidase (NA)", "organism": "", "uniprot_id": "" }, { "function": "Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi)", "gene_name": "gag", "glycan_count": 0, "glycosylation_sites": [], "id": "P12493", "name": "HIV-1 p24", "organism": "Human immunodeficiency virus type 1 group M subtype B (isolate NY5)", "uniprot_id": "P12493" }, { "function": "Lipid-binding protein which shows high specificity for the surfactant phospholipid dipalmitoylphosphatidylcholine (DPPC) (PubMed:25223608). Plays a role in the innate immune responses of the upper airways (PubMed:23132494, PubMed:23499554). Reduces the surface tension in secretions from airway epithelia and inhibits the formation of biofilm by pathogenic Gram-negative bacteria, such as P.aeruginosa and K.pneumoniae (PubMed:23132494, PubMed:23499554, PubMed:27145151). Negatively regulates proteolytic cleavage of SCNN1G, an event that is required for activation of the epithelial sodium channel (ENaC), and thereby contributes to airway surface liquid homeostasis and proper clearance of mucus (PubMed:24043776, PubMed:24124190). Plays a role in the airway inflammatory response after exposure to irritants (PubMed:11425234). May attract macrophages and neutrophils (PubMed:23132494)", "gene_name": "BPIFA1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NP55", "name": "SPLUNC1 (Short-palate-lung and nasal-epithelial clone 1)", "organism": "Homo sapiens", "uniprot_id": "Q9NP55" }, { "function": "", "gene_name": "IFNW1", "glycan_count": 4, "glycosylation_sites": [ { "position": 101, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P05000", "name": "Interferon-\u03c9 (IFN-\u03c9)", "organism": "Homo sapiens", "uniprot_id": "P05000" }, { "function": "Catalyzes the phosphorylation of hexose, such as D-glucose, D-fructose and D-mannose, to hexose 6-phosphate (D-glucose 6-phosphate, D-fructose 6-phosphate and D-mannose 6-phosphate, respectively) (PubMed:11916951, PubMed:15277402, PubMed:17082186, PubMed:18322640, PubMed:19146401, PubMed:25015100, PubMed:7742312, PubMed:8325892). Compared to other hexokinases, has a weak affinity for D-glucose, and is effective only when glucose is abundant (By similarity). Mainly expressed in pancreatic beta cells and the liver and constitutes a rate-limiting step in glucose metabolism in these tissues (PubMed:11916951, PubMed:15277402, PubMed:18322640, PubMed:25015100, PubMed:8325892). Since insulin secretion parallels glucose metabolism and the low glucose affinity of GCK ensures that it can change its enzymatic activity within the physiological range of glucose concentrations, GCK acts as a glucose sensor in the pancreatic beta cell (By similarity). In pancreas, plays an important role in modulating insulin secretion (By similarity). In liver, helps to facilitate the uptake and conversion of glucose by acting as an insulin-sensitive determinant of hepatic glucose usage (By similarity). Required to provide D-glucose 6-phosphate for the synthesis of glycogen (PubMed:8878425). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate (PubMed:7742312)", "gene_name": "GCK", "glycan_count": 0, "glycosylation_sites": [], "id": "P35557", "name": "Glucokinase (GCK)", "organism": "Homo sapiens", "uniprot_id": "P35557" }, { "function": "Transcriptional activator that regulates the tissue specific expression of multiple genes, especially in pancreatic islet cells and in liver (By similarity). Binds to the inverted palindrome 5'-GTTAATNATTAAC-3' (PubMed:10966642, PubMed:12453420). Activates the transcription of CYP1A2, CYP2E1 and CYP3A11 (By similarity)", "gene_name": "HNF1A", "glycan_count": 1, "glycosylation_sites": [], "id": "P20823", "name": "Hepatocyte nuclear factor 1-alpha (HNF1A)", "organism": "Homo sapiens", "uniprot_id": "P20823" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "varies by virus (e.g., P59596 for SARS-CoV)", "name": "Membrane protein (M)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "varies by virus (e.g., P59637 for SARS-CoV)", "name": "Envelope protein (E)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "varies by virus (e.g., P59595 for SARS-CoV)", "name": "Nucleocapsid protein (N)", "organism": "", "uniprot_id": "" }, { "function": "Probably involved in connections of major cytoskeletal structures to the plasma membrane. In epithelial cells, required for the formation of microvilli and membrane ruffles on the apical pole. Along with PLEKHG6, required for normal macropinocytosis", "gene_name": "EZR", "glycan_count": 1, "glycosylation_sites": [], "id": "P15311", "name": "Ezrin", "organism": "Homo sapiens", "uniprot_id": "P15311" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Complex", "name": "Complement C5b-9 (Membrane Attack Complex)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P20916 (human)", "name": "Myelin-associated glycoprotein (MAG)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P60201 (human)", "name": "Proteolipid protein (PLP)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02686 (human)", "name": "Myelin basic protein (MBP)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P25189 (human)", "name": "Po protein", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "ITGA2B/ITGB3", "name": "Integrin \u03b1IIb\u03b23", "organism": "", "uniprot_id": "" }, { "function": "Inhibitory regulator of the Ras-cyclic AMP pathway. Binds inositol tetrakisphosphate (IP4) with high affinity. Might be a specific IP4 receptor", "gene_name": "RASA3", "glycan_count": 0, "glycosylation_sites": [], "id": "Q14644", "name": "Rasa3", "organism": "Homo sapiens", "uniprot_id": "Q14644" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P00747 (Fibrinogen alpha chain, precursor)", "name": "D-dimer", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04578 (gp160 precursor, HIV-1)", "name": "HIV Env glycoprotein (gp160/gp120/gp41)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q8Z4F3", "name": "PgtE protease", "organism": "Salmonella typhi", "uniprot_id": "Q8Z4F3" }, { "function": "Glycosylphosphatidylinositol (GPI)-anchored cell surface glycoprotein that interacts via its N-terminal immunoglobulin domain with cell surface receptors including 2B4/CD244 or CD2 to regulate immune cell function and activation. Participates in T-cell signaling transduction by associating with CD2 and efficiently bringing the Src family protein kinase LCK and LAT to the TCR/CD3 complex. In turn, promotes LCK phosphorylation and subsequent activation. Induces the phosphorylation of the cytoplasmic immunoreceptortyrosine switch motifs (ITSMs) of CD244 initiating a series of signaling events that leads to the generation of the immunological synapse and the directed release of cytolytic granules containing perforin and granzymes by T-lymphocytes and NK-cells", "gene_name": "Cd48", "glycan_count": 34, "glycosylation_sites": [ { "position": 38, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 97, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 140, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 186, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 203, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P10252", "name": "Urtica dioica agglutinin (UDA)", "organism": "Rattus norvegicus", "uniprot_id": "P10252" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q2G2D7", "name": "VraS", "organism": "Staphylococcus aureus (strain NCTC 8325 / PS 47)", "uniprot_id": "Q2G2D7" }, { "function": "Chemotactic factor that attracts monocytes and eosinophils, but not neutrophils. Augments monocyte anti-tumor activity. Also induces the release of gelatinase B. This protein can bind heparin. Binds to CCR1, CCR2 and CCR3", "gene_name": "CCL7", "glycan_count": 0, "glycosylation_sites": [ { "position": 29, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P80098", "name": "MCP-3 (CCL7)", "organism": "Homo sapiens", "uniprot_id": "P80098" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9D8E0 (mouse)", "name": "Erythroferrone (ERFE)", "organism": "", "uniprot_id": "" }, { "function": "Attaches the virion to the host cell membrane by interacting with heparan sulfate, initiating the infection. Unlike the other paramyxovirus attachment proteins, lacks both neuraminidase and hemagglutinating activities", "gene_name": "G", "glycan_count": 0, "glycosylation_sites": [ { "position": 72, "type": "O-linked (GalNAc...) threonine; by host" }, { "position": 80, "type": "O-linked (GalNAc...) threonine; by host" }, { "position": 85, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 87, "type": "O-linked (GalNAc...) threonine; by host" }, { "position": 92, "type": "O-linked (GalNAc...) threonine; by host" }, { "position": 105, "type": "O-linked (GalNAc...) serine; by host" }, { "position": 139, "type": "O-linked (GalNAc...) threonine; by host" }, { "position": 163, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 199, "type": "O-linked (GalNAc...) threonine; by host" }, { "position": 215, "type": "O-linked (GalNAc...) threonine; by host" }, { "position": 233, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 251, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 253, "type": "O-linked (GalNAc...) serine; by host" } ], "id": "P69351", "name": "Measles Hemagglutinin", "organism": "Bovine respiratory syncytial virus (strain 220-69)", "uniprot_id": "P69351" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P00338 (LDHA)", "name": "Lactate dehydrogenase (LDH)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q05320 (Zaire ebolavirus GP)", "name": "Ebolavirus glycoprotein (GP)", "organism": "", "uniprot_id": "" }, { "function": "Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. The major receptor is host ACE2 (PubMed:32142651, PubMed:32155444, PubMed:33607086). When S2/S2' has been cleaved, binding to the receptor triggers direct fusion at the cell membrane (PubMed:34561887). When S2/S2' has not been cleaved, binding to the receptor results in internalization of the virus by endocytosis using host TFRC and GRM2 and leading to fusion of the virion membrane with the host endosomal membrane (PubMed:32075877, PubMed:32221306, PubMed:34903715, PubMed:36779763). Alternatively, may use NRP1/NRP2 (PubMed:33082294, PubMed:33082293) and integrin as entry receptors (PubMed:35150743). The use of NRP1/NRP2 receptors may explain the tropism of the virus in human olfactory epithelial cells, which express these molecules at high levels but ACE2 at low levels (PubMed:33082293). The stalk domain of S contains three hinges, giving the head unexpected orientational freedom (PubMed:32817270)", "gene_name": "S", "glycan_count": 379, "glycosylation_sites": [ { "position": 17, "type": "N-linked (GlcNAc...) (complex) asparagine; by host" }, { "position": 61, "type": "N-linked (GlcNAc...) (hybrid) asparagine; by host" }, { "position": 74, "type": "N-linked (GlcNAc...) (complex) asparagine; by host" }, { "position": 122, "type": "N-linked (GlcNAc...) (hybrid) asparagine; by host" }, { "position": 149, "type": "N-linked (GlcNAc...) (complex) asparagine; by host" }, { "position": 165, "type": "N-linked (GlcNAc...) (complex) asparagine; by host" }, { "position": 234, "type": "N-linked (GlcNAc...) (high mannose) asparagine; by host" }, { "position": 282, "type": "N-linked (GlcNAc...) (complex) asparagine; by host" }, { "position": 323, "type": "O-linked (GalNAc) threonine; by host" }, { "position": 325, "type": "O-linked (HexNAc...) serine; by host" }, { "position": 331, "type": "N-linked (GlcNAc...) (complex) asparagine; by host" }, { "position": 343, "type": "N-linked (GlcNAc...) (complex) asparagine; by host" }, { "position": 603, "type": "N-linked (GlcNAc...) (hybrid) asparagine; by host" }, { "position": 616, "type": "N-linked (GlcNAc...) (complex) asparagine; by host" }, { "position": 657, "type": "N-linked (GlcNAc...) (complex) asparagine; by host" }, { "position": 676, "type": "O-linked (GlcNAc...) threonine; by host GALNT1" }, { "position": 678, "type": "O-linked (GlcNAc...) threonine; by host GALNT1" }, { "position": 709, "type": "N-linked (GlcNAc...) (high mannose) asparagine; by host" }, { "position": 717, "type": "N-linked (GlcNAc...) (hybrid) asparagine; by host" }, { "position": 801, "type": "N-linked (GlcNAc...) (hybrid) asparagine; by host" }, { "position": 1074, "type": "N-linked (GlcNAc...) (hybrid) asparagine; by host" }, { "position": 1098, "type": "N-linked (GlcNAc...) (complex) asparagine; by host" }, { "position": 1134, "type": "N-linked (GlcNAc...) (complex) asparagine; by host" }, { "position": 1158, "type": "N-linked (GlcNAc...) (complex) asparagine; by host" }, { "position": 1173, "type": "N-linked (GlcNAc...) (complex) asparagine; by host" }, { "position": 1194, "type": "N-linked (GlcNAc...) (complex) asparagine; by host" } ], "id": "P0DTC2-1", "name": "S1 subunit of S protein", "organism": "Severe acute respiratory syndrome coronavirus 2", "uniprot_id": "P0DTC2" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q6YMS4 (DENV-2)", "name": "Nonstructural protein 1 (NS1)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "Q32ZE1 (ZIKV)", "name": "Nonstructural protein 1 (ns1)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P06821 (Influenza A)", "name": "Matrix protein 2", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P03301 (Enterovirus 71)", "name": "Major capsid protein VP1", "organism": "", "uniprot_id": "" }, { "function": "Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection", "gene_name": "S", "glycan_count": 0, "glycosylation_sites": [ { "position": 19, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 29, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 58, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 114, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 132, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 171, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 188, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 192, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 251, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 335, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 355, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 433, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 454, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 561, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 664, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 684, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 703, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 725, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 771, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 776, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 793, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 924, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1181, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1211, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1221, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1226, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1240, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1247, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1255, "type": "N-linked (GlcNAc...) asparagine; by host" }, { "position": 1276, "type": "N-linked (GlcNAc...) asparagine; by host" } ], "id": "Q14EB0", "name": "Hemagglutinin-esterase dimer (HE)", "organism": "Human coronavirus HKU1 (isolate N2)", "uniprot_id": "Q14EB0" }, { "function": "DNA-binding protein that binds to the 5'GGGAATRCC-3' Ikaros-binding sequence. Transcriptional repressor. Interacts with SPI1 and MITF to repress transcription of the CTSK and ACP5 promoters via recruitment of corepressors SIN3A and CTBP2. May be involved in the development of central and peripheral nervous systems. Essential for the inhibitory function of regulatory T-cells (Treg). Mediates FOXP3-mediated gene silencing in regulatory T-cells (Treg) via recruitment of corepressor CTBP1 (By similarity)", "gene_name": "IKZF4", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9H2S9", "name": "IKZF2 (Helios)", "organism": "Homo sapiens", "uniprot_id": "Q9H2S9" }, { "function": "Calmodulin-binding scaffolding protein which is the center of the striatin-interacting phosphatase and kinase (STRIPAK) complexes (PubMed:18782753, PubMed:32640226). STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling (PubMed:32640226). Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation (Probable). Key regulator of the expanded Hippo signaling pathway by interacting and allowing the inhibition of MAP4K kinases by the STRIPAK complex (PubMed:32640226)", "gene_name": "STRN4", "glycan_count": 1, "glycosylation_sites": [], "id": "Q9NRL3", "name": "Regulator of Calcineurin 1 (RCAN1)", "organism": "Homo sapiens", "uniprot_id": "Q9NRL3" }, { "function": "Acts as a molecular chaperone for mitochondrial complex I assembly (PubMed:16200211, PubMed:19384974). Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (PubMed:16200211, PubMed:27626371). Is involved in the initial steps of cilia formation, including removal of CP110 from the mother centrioles, docking of membrane vesicles to the mother centrioles, and establishment of the transition zone (PubMed:38949024)", "gene_name": "NDUFAF2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q8N183", "name": "DCAF17", "organism": "Homo sapiens", "uniprot_id": "Q8N183" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P59637 (SARS-CoV)", "name": "Envelope (E) protein", "organism": "", "uniprot_id": "" }, { "function": "May play a role in CNS development by interacting with growth factors implicated in motor neuron differentiation and survival. May play a role in capillary formation and maintenance during angiogenesis. Modulates BMP activity by affecting its processing and delivery to the cell surface", "gene_name": "CRIM1", "glycan_count": 5, "glycosylation_sites": [ { "position": 71, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 113, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 330, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 474, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 746, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "Q9NZV1", "name": "C3AR1", "organism": "Homo sapiens", "uniprot_id": "Q9NZV1" }, { "function": "Probable adapter protein that bind to and organize the subcellular localization of a variety of membrane proteins containing some PDZ recognition sequence. Involved in the clustering of various receptors, possibly by acting at the receptor internalization level. Plays a role in synaptic plasticity by regulating the trafficking and internalization of AMPA receptors. May be regulated upon PRKCA activation. May regulate ASIC1/ASIC3 channel. Regulates actin polymerization by inhibiting the actin-nucleating activity of the Arp2/3 complex; the function is competitive with nucleation promoting factors and is linked to neuronal morphology regulation and AMPA receptor (AMPAR) endocytosis. Via interaction with the Arp2/3 complex involved in regulation of synaptic plasicity of excitatory synapses and required for spine shrinkage during long-term depression (LTD). Involved in regulation of astrocyte morphology, antagonistic to Arp2/3 complex activator WASL/N-WASP function", "gene_name": "PICK1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NRD5", "name": "PICK1", "organism": "Homo sapiens", "uniprot_id": "Q9NRD5" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P07359/P14770", "name": "Platelet GP-Ib/IX", "organism": "", "uniprot_id": "" }, { "function": "Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen", "gene_name": "COL4A5", "glycan_count": 1, "glycosylation_sites": [ { "position": 125, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P29400", "name": "COL4A5", "organism": "Homo sapiens", "uniprot_id": "P29400" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P07335 (rat, muscle type)", "name": "creatine kinase (CK)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P15289 (rat, tissue-nonspecific)", "name": "alkaline phosphatase (AP)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04785 (rat)", "name": "alanine aminotransferase (ALT)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04642 (rat, LDHA)", "name": "lactate dehydrogenase (LDH)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P19440 (rat)", "name": "gamma glutamyl transferase (rGT)", "organism": "", "uniprot_id": "" }, { "function": "Plays a role in inhibiting the host innate immune response by targeting the mitochondrial-associated innate immune response. Acts by binding to host TOMM70, inhibiting its binding to HSP90AB1 thereby disrupting the interferon activation pathway", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P0DTD2", "name": "SARS-CoV-2 Helicase (NSP13)", "organism": "Severe acute respiratory syndrome coronavirus 2", "uniprot_id": "P0DTD2" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "not present in SARS-CoV-2", "name": "Hemagglutinin-esterase (HE)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04746 (rat)", "name": "Alanine aminotransferase (ALT)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02454 (rat, COL1A1)", "name": "Type I Collagen", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02461 (rat, COL3A1)", "name": "Type III Collagen", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P62738 (rat, ACTA2)", "name": "\u03b1-Smooth Muscle Actin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P05182 (rat)", "name": "Cytochrome P450 2E1", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P0DMV8 (rat)", "name": "Heat Shock Protein 70 (HSP70)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P29477 (rat)", "name": "Inducible Nitric Oxide Synthase (iNOS)", "organism": "", "uniprot_id": "" }, { "function": "Component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF) (PubMed:11741539, PubMed:9230079). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (PubMed:11741539, PubMed:9230079). In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA (PubMed:29925947). The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs) (PubMed:29925947)", "gene_name": "ARPC1B", "glycan_count": 1, "glycosylation_sites": [], "id": "O15143", "name": "Thrombopoietin", "organism": "Homo sapiens", "uniprot_id": "O15143" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P0DTD1 (residues 3264-3569)", "name": "3CL pro (Main Protease, Mpro)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P0DTD1 (residues 6453-6798)", "name": "Nsp15 (Endoribonuclease)", "organism": "", "uniprot_id": "" }, { "function": "Transcriptional coregulator of NF-kappa-B which facilitates binding of NF-kappa-B proteins to target kappa-B genes in a redox-state-dependent manner. May be required for efficient terminal myeloid maturation of hematopoietic cells. Has quercetin 2,3-dioxygenase activity (in vitro)", "gene_name": "PIR", "glycan_count": 0, "glycosylation_sites": [], "id": "O00625", "name": "Pirin", "organism": "Homo sapiens", "uniprot_id": "O00625" }, { "function": "Protein insertase that mediates insertion of transmembrane proteins into the mitochondrial outer membrane (PubMed:36264797). Catalyzes insertion of proteins with alpha-helical transmembrane regions, such as signal-anchored, tail-anchored and multi-pass membrane proteins (By similarity). Does not mediate insertion of beta-barrel transmembrane proteins (By similarity). May play a role in apoptosis (PubMed:12377771)", "gene_name": "MTCH1", "glycan_count": 0, "glycosylation_sites": [], "id": "Q9NZJ7", "name": "BCMA", "organism": "Homo sapiens", "uniprot_id": "Q9NZJ7" }, { "function": "Ligand of the T-lymphocyte CD2 glycoprotein. This interaction is important in mediating thymocyte interactions with thymic epithelial cells, antigen-independent and -dependent interactions of T-lymphocytes with target cells and antigen-presenting cells and the T-lymphocyte rosetting with erythrocytes. In addition, the LFA-3/CD2 interaction may prime response by both the CD2+ and LFA-3+ cells", "gene_name": "CD58", "glycan_count": 8, "glycosylation_sites": [ { "position": 40, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 94, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 109, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 135, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 169, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 195, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P19256", "name": "CD58", "organism": "Homo sapiens", "uniprot_id": "P19256" }, { "function": "Essential negative regulator of type I and type II interferon (IFN) signaling, as well as that of other cytokines, including IL2, IL4, IL6 and leukemia inhibitory factor (LIF) (PubMed:32499645, PubMed:33087723). Downregulates cytokine signaling by inhibiting the JAK/STAT signaling pathway. Acts by binding to JAK proteins and to IFNGR1 and inhibiting their kinase activity. In vitro, suppresses Tec protein-tyrosine activity (PubMed:9341160). Regulates IFN-gamma (IFNG)-mediated sensory neuron survival (By similarity). Probable substrate recognition component of an ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:11278610, PubMed:11313480)", "gene_name": "SOCS1", "glycan_count": 0, "glycosylation_sites": [], "id": "O15524", "name": "SOCS1", "organism": "Homo sapiens", "uniprot_id": "O15524" }, { "function": "One of the major pre-mRNA-binding proteins. Binds tenaciously to poly(C) sequences. Likely to play a role in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. Can also bind poly(C) single-stranded DNA. Plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. When sumoylated, acts as a transcriptional coactivator of p53/TP53, playing a role in p21/CDKN1A and 14-3-3 sigma/SFN induction (By similarity). As far as transcription repression is concerned, acts by interacting with long intergenic RNA p21 (lincRNA-p21), a non-coding RNA induced by p53/TP53. This interaction is necessary for the induction of apoptosis, but not cell cycle arrest. As part of a ribonucleoprotein complex composed at least of ZNF827, HNRNPL and the circular RNA circZNF827 that nucleates the complex on chromatin, may negatively regulate the transcription of genes involved in neuronal differentiation (PubMed:33174841)", "gene_name": "HNRNPK", "glycan_count": 2, "glycosylation_sites": [], "id": "P61978", "name": "hnRNP K", "organism": "Homo sapiens", "uniprot_id": "P61978" }, { "function": "Involved in DNA nucleotide excision repair (NER). Initiates repair by binding to damaged sites with various affinities, depending on the photoproduct and the transcriptional state of the region. Required for UV-induced CHEK1 phosphorylation and the recruitment of CEP164 to cyclobutane pyrimidine dimmers (CPD), sites of DNA damage after UV irradiation (PubMed:19197159). During NER stimulates the 5'-3' helicase activity of XPD/ERCC2 and the DNA translocase activity of XPB/ERCC3 (PubMed:31253769). Connects XPD/ERCC2 and XPB/ERCC3 during NER, retaining DNA near the XPB/ERCC3 active site, and stabilizing the complex in a different conformation than in transcribing TFIIH (PubMed:31253769)", "gene_name": "XPA", "glycan_count": 1, "glycosylation_sites": [], "id": "P23025", "name": "Dengue virus NS1", "organism": "Homo sapiens", "uniprot_id": "P23025" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P0DTD1 (nsp3 region)", "name": "Papain-like protease (PLpro)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P0DTD1 (nsp5 region)", "name": "3-chymotrypsin-like protease (3CLpro, Mpro)", "organism": "", "uniprot_id": "" }, { "function": "Leu-enkephalins compete with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress (By similarity)", "gene_name": "PDYN", "glycan_count": 0, "glycosylation_sites": [], "id": "P01213", "name": "Prodynorphin (PDYN)", "organism": "Homo sapiens", "uniprot_id": "P01213" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P31946/P62258", "name": "14-3-3 protein", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P0DTC1-5", "name": "NSP5 (Main viral protease, 3CLpro)", "organism": "", "uniprot_id": "" }, { "function": "Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, BMAL1, BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and BMAL1 or BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-BMAL1|BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress BMAL1 transcription, respectively. Regulates the circadian expression of ICAM1, VCAM1, CCL2, THPO and MPL and also acts as an enhancer of the transactivation potential of NF-kappaB. Plays an important role in the homeostatic regulation of sleep. The CLOCK-BMAL1 heterodimer regulates the circadian expression of SERPINE1/PAI1, VWF, B3, CCRN4L/NOC, NAMPT, DBP, MYOD1, PPARGC1A, PPARGC1B, SIRT1, GYS2, F7, NGFR, GNRHR, BHLHE40/DEC1, ATF4, MTA1, KLF10 and also genes implicated in glucose and lipid metabolism. Promotes rhythmic chromatin opening, regulating the DNA accessibility of other transcription factors. The CLOCK-BMAL2 heterodimer activates the transcription of SERPINE1/PAI1 and BHLHE40/DEC1. The preferred binding motif for the CLOCK-BMAL1 heterodimer is 5'-CACGTGA-3', which contains a flanking adenine nucleotide at the 3-prime end of the canonical 6-nucleotide E-box sequence (PubMed:23229515). CLOCK specifically binds to the half-site 5'-CAC-3', while BMAL1 binds to the half-site 5'-GTGA-3' (PubMed:23229515). The CLOCK-BMAL1 heterodimer also recognizes the non-canonical E-box motifs 5'-AACGTGA-3' and 5'-CATGTGA-3' (PubMed:23229515). CLOCK has an intrinsic acetyltransferase activity, which enables circadian chromatin remodeling by acetylating histones and nonhistone proteins, including its own partner BMAL1. Represses glucocorticoid receptor NR3C1/GR-induced transcriptional activity by reducing the association of NR3C1/GR to glucocorticoid response elements (GREs) via the acetylation of multiple lysine residues located in its hinge region (PubMed:21980503). The acetyltransferase activity of CLOCK is as important as its transcription activity in circadian control. Acetylates metabolic enzymes IMPDH2 and NDUFA9 in a circadian manner. Facilitated by BMAL1, rhythmically interacts and acetylates argininosuccinate synthase 1 (ASS1) leading to enzymatic inhibition of ASS1 as well as the circadian oscillation of arginine biosynthesis and subsequent ureagenesis (PubMed:28985504). Drives the circadian rhythm of blood pressure through transcriptional activation of ATP1B1 (By similarity)", "gene_name": "CLOCK", "glycan_count": 1, "glycosylation_sites": [], "id": "O15516", "name": "Melanoma Differentiation Associated Gene 5 (MDA5)", "organism": "Homo sapiens", "uniprot_id": "O15516" }, { "function": "Promotes cell proliferation, chemotaxis, angiogenesis and cell adhesion. Appears to play a role in wound healing by up-regulating, in skin fibroblasts, the expression of a number of genes involved in angiogenesis, inflammation and matrix remodeling including VEGA-A, VEGA-C, MMP1, MMP3, TIMP1, uPA, PAI-1 and integrins alpha-3 and alpha-5. CCN1-mediated gene regulation is dependent on heparin-binding. Down-regulates the expression of alpha-1 and alpha-2 subunits of collagen type-1. Promotes cell adhesion and adhesive signaling through integrin alpha-6/beta-1, cell migration through integrin alpha-v/beta-5 and cell proliferation through integrin alpha-v/beta-3", "gene_name": "CCN1", "glycan_count": 1, "glycosylation_sites": [], "id": "O00622", "name": "Cysteine rich protein 61 (CYR61)", "organism": "Homo sapiens", "uniprot_id": "O00622" }, { "function": "Plays an important role in fat metabolism. It preferentially splits the esters of long-chain fatty acids at positions 1 and 3, producing mainly 2-monoacylglycerol and free fatty acids, and shows considerably higher activity against insoluble emulsified substrates than against soluble ones", "gene_name": "PNLIP", "glycan_count": 0, "glycosylation_sites": [ { "position": 183, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P16233", "name": "Pancreatic lipase", "organism": "Homo sapiens", "uniprot_id": "P16233" }, { "function": "Cytokine secreted predominantly by activated T-lymphocytes as well as mast cells and osteoblastic cells that controls the production and differentiation of hematopoietic progenitor cells into lineage-restricted cells (PubMed:2556442). Also stimulates mature basophils, eosinophils, and monocytes to become functionally activated (PubMed:10779277, PubMed:32889153). In addition, plays an important role in neural cell proliferation and survival (PubMed:23226269). Participates as well in bone homeostasis and inhibits osteoclast differentiation by preventing NF-kappa-B nuclear translocation and activation (PubMed:12816992). Mechanistically, exerts its biological effects through a receptor composed of IL3RA subunit and a signal transducing subunit IL3RB (PubMed:29374162). Receptor stimulation results in the rapid activation of JAK2 kinase activity leading to STAT5-mediated transcriptional program (By similarity). Alternatively, contributes to cell survival under oxidative stress in non-hematopoietic systems by activating pathways mediated by PI3K/AKT and ERK (PubMed:27862234)", "gene_name": "IL3", "glycan_count": 0, "glycosylation_sites": [ { "position": 34, "type": "N-linked (GlcNAc...) asparagine" }, { "position": 89, "type": "N-linked (GlcNAc...) asparagine" } ], "id": "P08700", "name": "IL-3", "organism": "Homo sapiens", "uniprot_id": "P08700" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P24941 (human CDK2, as used in docking)", "name": "Herpesvirus cyclin-dependent kinase complex (CDK2)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P04275 (human)", "name": "von Willebrand factor", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P16581 (human)", "name": "E-selectin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P16109 (human)", "name": "P-selectin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P19320 (human)", "name": "Vascular cell adhesion molecule-1 (VCAM-1)", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P05107 (human, ITGB2)", "name": "\u03b22-integrin", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P0DJI8 (human)", "name": "Serum amyloid A", "organism": "", "uniprot_id": "" }, { "function": "", "gene_name": "", "glycan_count": 0, "glycosylation_sites": [], "id": "P02671 (human, FGA)", "name": "Fibrinogen", "organism": "", "uniprot_id": "" }, { "function": "The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (PubMed:33795473). TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (PubMed:33795473). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:33795473, PubMed:9418870, PubMed:9774672). TAF2 forms a promoter DNA binding subcomplex of TFIID, together with TAF7 and TAF1 (PubMed:33795473, PubMed:9774672)", "gene_name": "TAF2", "glycan_count": 1, "glycosylation_sites": [], "id": "Q6P1X5", "name": "Debrancher enzyme", "organism": "Homo sapiens", "uniprot_id": "Q6P1X5" }, { "function": "Transcription factor playing an essential role to promote self-tolerance in the thymus by regulating the expression of a wide array of self-antigens that have the commonality of being tissue-restricted in their expression pattern in the periphery, called tissue restricted antigens (TRA) (PubMed:26084028). Binds to G-doublets in an A/T-rich environment; the preferred motif is a tandem repeat of 5'-ATTGGTTA-3' combined with a 5'-TTATTA-3' box. Binds to nucleosomes (By similarity). Binds to chromatin and interacts selectively with histone H3 that is not methylated at 'Lys-4', not phosphorylated at 'Thr-3' and not methylated at 'Arg-2'. Functions as a sensor of histone H3 modifications that are important for the epigenetic regulation of gene expression. Mainly expressed by medullary thymic epithelial cells (mTECs), induces the expression of thousands of tissue-restricted proteins, which are presented on major histocompatibility complex class I (MHC-I) and MHC-II molecules to developing T-cells percolating through the thymic medulla (PubMed:26084028). Also induces self-tolerance through other mechanisms such as the regulation of the mTEC differentiation program. Controls the medullary accumulation of thymic dendritic cells and the development of regulatory T-cell through the regulation of XCL1 expression. Regulates the production of CCR4 and CCR7 ligands in medullary thymic epithelial cells and alters the coordinated maturation and migration of thymocytes. In thimic B-cells, allows the presentation of licensing-dependent endogenous self-anitgen for negative selection. In secondary lymphoid organs, induces functional inactivation of CD4(+) T-cells. Expressed by a distinct bone marrow-derived population, induces self-tolerance through a mechanism that does not require regulatory T-cells and is resitant to innate inflammatory stimuli (By similarity)", "gene_name": "AIRE", "glycan_count": 0, "glycosylation_sites": [], "id": "O43918", "name": "Autoimmune Regulator (AIRE)", "organism": "Homo sapiens", "uniprot_id": "O43918" }, { "function": "Associated with ribosomes but is not required for canonical ribosome function and has extra-ribosomal functions. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the ribosome and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation. In the GAIT complex interacts with m7G cap-bound eIF4G at or near the eIF3-binding site and blocks the recruitment of the 43S ribosomal complex. Involved in methylation of rRNA", "gene_name": "Rpl13a", "glycan_count": 0, "glycosylation_sites": [], "id": "P35427", "name": "Mucin 2 (Muc2)", "organism": "Rattus norvegicus", "uniprot_id": "P35427" } ], "total_proteins": 4952, "version": "1.0" }