2.4.1.255	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	
2.4.1.255	additional information	dynamic modification of nuclear and cytoplasmic proteins with O-linked beta-N-acetylglucosamine	
2.4.1.255	additional information	enzyme for protein post-translational modifications	
2.4.1.255	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