2.4.1.255: protein O-GlcNAc transferase
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For detailed information about protein O-GlcNAc transferase, go to the full flat file.
Word Map on EC 2.4.1.255
Reaction
Synonyms
beta-N-acetylglucosaminidase, EGF domain-specific O-GlcNAc transferase, EGF domain-specific O-linked N-acetylglucosamine transferase, EOGT, EOGT1, epidermal growth factor domain-specific O-GlcNAc transferase, glycosyltransferase OGT, Gtf1, GtfA, hOGT, HsOGT, human OGT, mammalian OGT, mOGT, More, N-acetylglucosamine transferase, N-acetylglucosamine-peptide N-acetylglucosaminyltransferase, N-acetylglucosaminyltransferase, ncOGT, nuclear cytoplasmic OGT, nucleocytoplasmic glycosyltransferase, nucleocytoplasmic OGT, O-GlcNAc protein, O-GlcNAc transferase, O-GlcNAc transferase OGT, O-GlcNAc-transferase, O-GlcNAcase, O-glycosylated protein p135, O-linked beta-N-acetylglucosamine transferase, O-linked beta-N-acetylglucosaminyltransferase, O-linked GlcNAc transferase, O-linked N-acetylglucosamine transferase, O-linked N-acetylglucosaminyltransferase, O-N-acetylglucosamine (O-GlcNAc) transferase, OGT, OGT p110, OGT protein, ogta, OGTase, OGTase protein, ogtb, p135, Protein SECRET AGENT, SEC, SECRET AGENT, sOGT, spindly, SPY, super sex combs, Sxc, Synpcc7942_0051, transferase OGT, UDP-GlcNAc: polypeptide O-N-acetylglucosaminyltransferase, UDP-GlcNAc:polypeptidyl transferase, UDP-N-acetylglucosaminyl transferase, uridine diphosphate-N-acetyl-D-glucosamine:polypeptidyltransferase, uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylaminyltransferase, uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyltransferase, XcOGT, XcOGT protein
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2.4.1.255 protein O-GlcNAc transferaseAdvanced search results
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results (Posttranslational Modification
Posttranslational Modification on EC 2.4.1.255 - protein O-GlcNAc transferase
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POSTTRANSLATIONAL MODIFICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glycoprotein
O-GlcNAcylation of Ser389 in nucleocytoplasmic O-GlcNAc transferase affects its nuclear translocation in HeLa cells. Six O-GlcNAc sites are identified in the tetratricopeptide repeat domain in short-form of O-GlcNAc transferase, with Thr12 and Ser56 being two key sites. Thr12 is a dominant O-GlcNAcylation site. The modification of Ser56 plays a role in regulating short-form of O-GlcNAc transferase. O-GlcNAcylation does not affect activity of O-GlcNAc transferase but alters its substrate selectivity
proteolytic modification
N-glycosylation sites Asn-263 and Asn-354, but not Asn-493, are modified with N-glycans. Both residues are modified with oligomannose N-glycans. Loss of an individual N-glycan does not affect endoplasmic reticulum localization of the enzyme (EOGT), enzyme activity, and ability to O-GlcNAcylate Notch1 in HEK-293T cells. Simultaneous substitution of both N-glycosylation sites affects both enzyme maturation and expression levels without an apparent change in enzymatic activity, suggesting that N-glycosylation at a single site is sufficient for enzyme maturation and expression
additional information
additional information
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dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine
