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Literature summary extracted from

  • Takeuchi, H.; Haltiwanger, R.
    The role of O-glucosylation in Notch signaling (2008), Trends Glycosci. Glycotechnol., 20, 159-170 .
No PubMed abstract available

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.376 G189E inactive Drosophila melanogaster

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.4.1.376 endoplasmic reticulum
-
 Drosophila melanogaster 5783
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.1.376 UDP-alpha-D-glucose + [Notch protein with EGF-like domain]-L-serine Drosophila melanogaster
-
 UDP + [Notch protein with EGF-like domain]-3-O-(beta-D-glucosyl)-L-serine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.376 Drosophila melanogaster
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.376 UDP-alpha-D-glucose + [Notch protein with EGF-like domain]-L-serine
-
 Drosophila melanogaster UDP + [Notch protein with EGF-like domain]-3-O-(beta-D-glucosyl)-L-serine
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.376 Poglut
-
 Drosophila melanogaster
2.4.1.376 protein O-glycosyltransferase
-
 Drosophila melanogaster
2.4.1.376 Rumi
-
 Drosophila melanogaster

General Information

EC Number General Information Comment Organism
2.4.1.376 malfunction enzyme mutations cause a temperature-dependent loss of Notch signalling Drosophila melanogaster
2.4.1.376 metabolism the enzyme regulates Notch protein folding and/or trafficking and allows signalling at the cell membrane by O-glycosylation of Notch in the endoplasmic reticulum Drosophila melanogaster