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]].
","llm":false,"checked":false,"updated":false}],"wikipedia":[{"title":"N-glycosyltransferase","extract":"N-glycosyltransferase 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 N-glycosylating enzymes, 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.
","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"}}}