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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR005331",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0008146",
"name": "sulfotransferase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0016020",
"name": "membrane",
"category": {
"code": "C",
"name": "cellular_component"
}
}
],
"source_database": "interpro",
"member_databases": {
"pfam": {
"PF03567": "Sulfotransferase family"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR005331",
"name": "Sulfotransferase",
"type": "Family",
"children": [
{
"accession": "IPR007669",
"name": "Carbohydrate sulfotransferase Chst-1-like",
"type": "Family",
"children": []
},
{
"accession": "IPR007734",
"name": "Heparan sulphate 2-O-sulfotransferase",
"type": "Family",
"children": []
},
{
"accession": "IPR010635",
"name": "Heparan sulphate 6-sulfotransferase/Protein-tyrosine sulfotransferase",
"type": "Family",
"children": []
},
{
"accession": "IPR018011",
"name": "Carbohydrate sulfotransferase 8-10",
"type": "Family",
"children": []
}
]
},
"name": {
"name": "Sulfotransferase",
"short": "Sulfotransferase"
},
"description": [
{
"text": "<p>This entry consists of a number of carbohydrate sulphotransferases that transfer sulphate to carbohydrate groups in glycoproteins and glycolipids. These include:</p>\r\n\r\n\n<ul><li>Carbohydrate sulphotransferases 8 and 9, which transfer sulphate to position 4 of non-reducing N-acetylgalactosamine (GalNAc) residues in both N-glycans and O-glycans [[cite:PUB00033954]]. They function in the biosynthesis of glycoprotein hormones lutropin and thyrotropin, by mediating sulphation of their carbohydrate structures.</li></ul>\r\n\n<ul><li>Carbohydrate sulphotransferase 10, which transfers sulphate to position 3 of the terminal glucuronic acid in both protein- and lipid-linked oligosaccharides [[cite:PUB00033955]]. It directs the biosynthesis of the HNK-1 carbohydrate structure, a sulphated glucuronyl-lactosaminyl residue carried by many neural recognition molecules, which is involved in cell interactions during ontogenetic development and in synaptic plasticity in the adult.</li></ul>\r\n\n<ul><li>Carbohydrate sulphotransferases 11 - 13, which catalyze the transfer of sulphate to position 4 of the GalNAc residue of chondroitin [[cite:PUB00033956]]. The orthologue in<i>Caenorhabditis elegans</i>is known as carbohydrate sulfotransferase chst-1 [[cite:PUB00085650]]. Chondroitin sulphate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Some, thought not all, of these enzymes also transfer sulphate to dermatan.</li></ul>\r\n\n<ul><li>Carbohydrate sulphotransferase D4ST1, which transfers sulphate to position 4 of the GalNAc residue of dermatan sulphate [[cite:PUB00033957]].</li></ul>\r\n\n<ul><li>Heparan sulphate 2-O-sulphotransferase (HS2ST). Heparan sulphate (HS) is a co-receptor for a number of growth factors, morphogens, and adhesion proteins. HS biosynthetic modifications may determine the strength and outcome of HS-ligand interactions. Mice that lack HS2ST undergo developmental failure only after midgestation,the most dramatic effect being the complete failure of kidney development [[cite:PUB00010170]].</li></ul>\r\n\n<ul><li>Heparan-sulphate 6-O-sulphotransferase (HS6ST), which catalyses the transfer of sulphate from adenosine 3'-phosphate, 5'-phosphosulphate to the 6th position of the N -sulphoglucosamine residue in heparan sulphate [[cite:PUB00012826]].</li></ul>\r\n\n<ul><li>Chondroitin 6-sulphotransferase catalyses the transfer of sulphate to position 6 of the N-acetylgalactosamine residue of chondroitin [[cite:PUB00053392]].</li></ul>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00012826": {
"PMID": 12492399,
"ISBN": null,
"volume": "371",
"issue": "Pt 1",
"year": 2003,
"title": "Biosynthesis of heparan sulphate with diverse structures and functions: two alternatively spliced forms of human heparan sulphate 6-O-sulphotransferase-2 having different expression patterns and properties.",
"URL": null,
"raw_pages": "131-42",
"medline_journal": "Biochem J",
"ISO_journal": "Biochem. J.",
"authors": [
"Habuchi H",
"Miyake G",
"Nogami K",
"Kuroiwa A",
"Matsuda Y",
"Kusche-Gullberg M",
"Habuchi O",
"Tanaka M",
"Kimata K."
],
"DOI_URL": "http://dx.doi.org/10.1042/BJ20021259"
},
"PUB00010170": {
"PMID": 11956326,
"ISBN": null,
"volume": "115",
"issue": "Pt 9",
"year": 2002,
"title": "Increased responsiveness of hypoxic endothelial cells to FGF2 is mediated by HIF-1alpha-dependent regulation of enzymes involved in synthesis of heparan sulfate FGF2-binding sites.",
"URL": null,
"raw_pages": "1951-9",
"medline_journal": "J Cell Sci",
"ISO_journal": "J. Cell. Sci.",
"authors": [
"Li J",
"Shworak NW",
"Simons M."
],
"DOI_URL": "http://jcs.biologists.org/cgi/content/abstract/115/9/1951"
},
"PUB00033954": {
"PMID": 11445554,
"ISBN": null,
"volume": "11",
"issue": "6",
"year": 2001,
"title": "Molecular cloning and expression of two distinct human N-acetylgalactosamine 4-O-sulfotransferases that transfer sulfate to GalNAc beta 1-->4GlcNAc beta 1-->R in both N- and O-glycans.",
"URL": null,
"raw_pages": "495-504",
"medline_journal": "Glycobiology",
"ISO_journal": "Glycobiology",
"authors": [
"Hiraoka N",
"Misra A",
"Belot F",
"Hindsgaul O",
"Fukuda M."
],
"DOI_URL": "http://dx.doi.org/10.1093/glycob/11.6.495"
},
"PUB00033955": {
"PMID": 9478973,
"ISBN": null,
"volume": "273",
"issue": "9",
"year": 1998,
"title": "Expression cloning of a human sulfotransferase that directs the synthesis of the HNK-1 glycan on the neural cell adhesion molecule and glycolipids.",
"URL": null,
"raw_pages": "5190-5",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Ong E",
"Yeh JC",
"Ding Y",
"Hindsgaul O",
"Fukuda M."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.273.9.5190"
},
"PUB00033956": {
"PMID": 10781601,
"ISBN": null,
"volume": "275",
"issue": "26",
"year": 2000,
"title": "Molecular cloning and expression of two distinct human chondroitin 4-O-sulfotransferases that belong to the HNK-1 sulfotransferase gene family.",
"URL": null,
"raw_pages": "20188-96",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Hiraoka N",
"Nakagawa H",
"Ong E",
"Akama TO",
"Fukuda MN",
"Fukuda M."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M002443200"
},
"PUB00033957": {
"PMID": 11470797,
"ISBN": null,
"volume": "276",
"issue": "39",
"year": 2001,
"title": "Molecular cloning and characterization of a dermatan-specific N-acetylgalactosamine 4-O-sulfotransferase.",
"URL": null,
"raw_pages": "36344-53",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Evers MR",
"Xia G",
"Kang HG",
"Schachner M",
"Baenziger JU."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M105848200"
},
"PUB00053392": {
"PMID": 18697746,
"ISBN": null,
"volume": "283",
"issue": "41",
"year": 2008,
"title": "Sulfation of the galactose residues in the glycosaminoglycan-protein linkage region by recombinant human chondroitin 6-O-sulfotransferase-1.",
"URL": null,
"raw_pages": "27438-43",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Kitagawa H",
"Tsutsumi K",
"Ikegami-Kuzuhara A",
"Nadanaka S",
"Goto F",
"Ogawa T",
"Sugahara K."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M803279200"
},
"PUB00085650": {
"PMID": 27645998,
"ISBN": null,
"volume": "291",
"issue": "44",
"year": 2016,
"title": "Chondroitin 4-O-Sulfotransferase Is Indispensable for Sulfation of Chondroitin and Plays an Important Role in Maintaining Normal Life Span and Oxidative Stress Responses in Nematodes.",
"URL": null,
"raw_pages": "23294-23304",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Izumikawa T",
"Dejima K",
"Watamoto Y",
"Nomura KH",
"Kanaki N",
"Rikitake M",
"Tou M",
"Murata D",
"Yanagita E",
"Kano A",
"Mitani S",
"Nomura K",
"Kitagawa H."
],
"DOI_URL": "https://doi.org/10.1074/jbc.M116.757328"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 320,
"interactions": 0,
"matches": 27662,
"pathways": 32,
"proteins": 27355,
"proteomes": 3420,
"sets": 0,
"structural_models": {
"alphafold": 24060,
"bfvd": 16
},
"structures": 5,
"taxa": 9000
},
"entry_annotations": {
"alignment:seed": 60,
"alignment:full": 18129
},
"cross_references": {
"ec": {
"displayName": "ENZYME",
"description": "ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.",
"rank": 19,
"accessions": [
{
"accession": "2.8.2.-",
"url": "https://enzyme.expasy.org/EC/2.8.2.-"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
