background:
The dynamic modification of cytoplasmic and nuclear proteins by O-linked N-acetylglucosamine (O-GlcNAc) addition and removal on serine and threonine residues is catalyzed by OGT (MIM 300255), which adds O-GlcNAc, and MGEA5, a glycosidase that removes O-GlcNAc modifications (Gao et al., 2001 [PubMed 11148210]).[supplied by OMIM, Mar 2008].
Function:
Cleaves GlcNAc but not GalNAc from glycopeptides. Can use p-nitrophenyl-beta-GlcNAc as substrate but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc. Possesses hyaluronidase activity. Acetylates 'Lys-8' of histone H4 and 'Lys-14' of histone H3 (By similarity).
Subunit:
Monomer. Binds both acetylated and unacetylated histone H4 tail but acetylation on 'Lys-8' of histone H4 abolishes binding (By similarity).
Subcellular Location:
Isoform 3: Nucleus.
Isoform 1: Cytoplasm.
Tissue Specificity:
Ubiquitous. Shows highest expression in the brain, placenta and pancreas. [PTM] Proteolytically cleaved by caspase-3.
Database links:
UniProtKB/Swiss-Prot: O60502.2
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
|
|