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{
"metadata": {
"accession": "PF13844",
"entry_id": null,
"type": "family",
"go_terms": null,
"source_database": "pfam",
"member_databases": null,
"integrated": "IPR029489",
"hierarchy": null,
"name": {
"name": "Glycosyl transferase family 41",
"short": "Glyco_transf_41"
},
"description": [
{
"text": "<p>This family of glycosyltransferases includes O-linked beta-N-acetylglucosamine (O-GlcNAc) transferase, an enzyme which catalyses the addition of O-GlcNAc to serine and threonine residues [[cite:PUB00047969],[cite:PUB00049883]]. In addition to its function as an O-GlcNAc transferase, human OGT, [swissprot:O15294], also appears to proteolytically cleave the epigenetic cell-cycle regulator HCF-1 [[cite:PUB00070115]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": [
{
"title": "N-glycosyltransferase",
"extract": "<p><b><i>N</i>-glycosyltransferase</b> is an enzyme in prokaryotes which transfers individual hexoses onto asparagine sidechains in substrate proteins, using a nucleotide-bound intermediary, within the cytoplasm. They are distinct from regular <span><i>N</i>-glycosylating enzymes</span>, which are oligosaccharyltransferases that transfer pre-assembled oligosaccharides. Both enzyme families however target a shared amino acid sequence asparagine—-any amino acid except proline—serine or threonine (N–x–S/T), with some variations.</p>",
"thumbnail": null
}
],
"literature": {
"PUB00049883": {
"PMID": 18536723,
"ISBN": null,
"volume": "15",
"issue": "7",
"year": 2008,
"title": "Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation.",
"URL": null,
"raw_pages": "764-5",
"medline_journal": "Nat Struct Mol Biol",
"ISO_journal": "Nat. Struct. Mol. Biol.",
"authors": [
"Martinez-Fleites C",
"Macauley MS",
"He Y",
"Shen DL",
"Vocadlo DJ",
"Davies GJ."
],
"DOI_URL": "http://dx.doi.org/10.1038/nsmb.1443"
},
"PUB00070115": {
"PMID": 21295698,
"ISBN": null,
"volume": "144",
"issue": "3",
"year": 2011,
"title": "O-GlcNAc transferase catalyzes site-specific proteolysis of HCF-1.",
"URL": null,
"raw_pages": "376-88",
"medline_journal": "Cell",
"ISO_journal": "Cell",
"authors": [
"Capotosti F",
"Guernier S",
"Lammers F",
"Waridel P",
"Cai Y",
"Jin J",
"Conaway JW",
"Conaway RC",
"Herr W."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.cell.2010.12.030"
},
"PUB00047969": {
"PMID": 18818698,
"ISBN": null,
"volume": "27",
"issue": "20",
"year": 2008,
"title": "Structural insights into mechanism and specificity of O-GlcNAc transferase.",
"URL": null,
"raw_pages": "2780-8",
"medline_journal": "EMBO J",
"ISO_journal": "EMBO J.",
"authors": [
"Clarke AJ",
"Hurtado-Guerrero R",
"Pathak S",
"Schuttelkopf AW",
"Borodkin V",
"Shepherd SM",
"Ibrahim AF",
"van Aalten DM."
],
"DOI_URL": "http://dx.doi.org/10.1038/emboj.2008.186"
}
},
"set_info": {
"accession": "CL0113",
"name": "GT-B"
},
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 2863,
"interactions": 0,
"matches": 23550,
"pathways": 0,
"proteins": 13844,
"proteomes": 4945,
"sets": 1,
"structural_models": {
"alphafold": 10349,
"bfvd": 0
},
"structures": 55,
"taxa": 13916
},
"entry_annotations": {
"hmm": 0,
"logo": 0,
"alignment:seed": 12,
"alignment:full": 11610
},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "5npr",
"name": "The human O-GlcNAc transferase in complex with a thiol-linked bisubstrate inhibitor"
}
}
}
