Protein Variants | Comment | Organism |
---|---|---|
N263Q/N354Q | a decrease in O-GlcNAc stoichiometry is observed in Notch1 co-expressed with an N263Q/N354Q variant compared with wild-type enzyme. The N263Q/N354Q variant exhibits altered subcellular distribution within the endoplasmic reticulum in HEK293T cells, indicating that N-glycosylation of EOGT is required for its localization in the endoplasmic reticulum at the cell periphery | Mus musculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | Q8BYW9 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
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 | Mus musculus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
HEK-293T cell | - |
Mus musculus | - |
Synonyms | Comment | Organism |
---|---|---|
EGF domain-specific O-GlcNAc transferase | - |
Mus musculus |
EOGT | - |
Mus musculus |
epidermal growth factor domain-specific O-GlcNAc transferase | - |
Mus musculus |
General Information | Comment | Organism |
---|---|---|
malfunction | several EOGT mutations that may affect putative N-glycosylation consensus sites are recorded in the cancer database | Mus musculus |