Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.4.1.255 extracted from

  • Alam, S.M.D.; Tsukamoto, Y.; Ogawa, M.; Senoo, Y.; Ikeda, K.; Tashima, Y.; Takeuchi, H.; Okajima, T.
    N-Glycans on EGF domain-specific O-GlcNAc transferase (EOGT) facilitate EOGT maturation and peripheral endoplasmic reticulum localization (2020), J. Biol. Chem., 295, 8560-8574 .
    View publication on PubMedView publication on EuropePMC

Protein Variants

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

Organism UniProt Comment Textmining
Mus musculus Q8BYW9
-
-

Posttranslational Modification

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

Source Tissue Comment Organism Textmining
HEK-293T cell
-
Mus musculus
-

Synonyms

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

General Information Comment Organism
malfunction several EOGT mutations that may affect putative N-glycosylation consensus sites are recorded in the cancer database Mus musculus