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Literature summary for 2.4.1.376 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
Search for more literature for 2.4.1.376

Protein Variants

Protein Variants Comment Organism
G189E inactive Drosophila melanogaster

Localization

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Drosophila melanogaster
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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

Synonyms Comment Organism
Poglut
-
 Drosophila melanogaster
protein O-glycosyltransferase
-
 Drosophila melanogaster
Rumi
-
 Drosophila melanogaster

General Information

General Information Comment Organism
malfunction enzyme mutations cause a temperature-dependent loss of Notch signalling Drosophila melanogaster
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