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Literature summary for 2.4.1.221 extracted from

  • Rana, N.A.; Haltiwanger, R.S.
    Fringe benefits: functional and structural impacts of O-glycosylation on the extracellular domain of Notch receptors (2011), Curr. Opin. Struct. Biol., 21, 583-589.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.4.1.221

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum lumen
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 Mus musculus 5788
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soluble
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 Mus musculus
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-

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster
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-
-
Mus musculus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information Pofut1 adds fucose to Ser or Thr in the C2-x-x-x-x-(S/T)-C3 consensus sequence. Eliminating any of three highly conserved O-fucose sites at EGF 12, 26, or 27 within mouse Notch1 alters activity. Mus musculus ?
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 ?

Synonyms

Synonyms Comment Organism
O-fucosyltransferase 1
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 Drosophila melanogaster
OFUT1
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 Drosophila melanogaster
Pofut1
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 Mus musculus
protein O-fucosyltransferase 1
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 Mus musculus

General Information

General Information Comment Organism
malfunction elimination of Pofut1 in mice has a profound effect on ligand binding in both embryonic stem cells and lymphoid cells. A small decrease in cell surface expression of Notch proteins is seen in embryonic stem cells lacking Pofut1 and in somites from mice with a hypomorphic allele of Pofut1, cax Mus musculus
additional information O-glycome of Drosophila melanogaster by mass spectrometry, using beta-elimination to release the O-linked sugar modifications from total protein extracts of fly embryos, overview Drosophila melanogaster
physiological function O-fucosylation is universally required for all Notch signaling. O-Fucose and O-glucose glycans on Notch occur at specific consensus sequences within the context of EGF repeats, which make up the majority of the Notch extracellular domain. Molecular mechanisms by which O-fucose and O-glucose glycans affect Notch function Mus musculus
physiological function O-fucosylation is universally required for all Notch signaling. O-Fucose and O-glucose glycans on Notch occur at specific consensus sequences within the context of EGF repeats, which make up the majority of the Notch extracellular domain. Ofut1 might have a chaperone-like activity in Drosophila that is required for cell-surface expression of Notch in flies. Molecular mechanisms by which O-fucose and O-glucose glycans affect Notch function, overview Drosophila melanogaster