2.4.1.221: peptide-O-fucosyltransferase
This is an abbreviated version!
For detailed information about peptide-O-fucosyltransferase, go to the full flat file.
Word Map on EC 2.4.1.221
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2.4.1.221
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notch
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o-fucosylation
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o-fucose
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factor-like
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o-linked
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thrombospondin
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fringe
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dowling-degos
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egf-like
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poglut1
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notch-ligand
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lunatic
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plagl2
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somitogenesis
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dll1
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genodermatosis
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hidradenitis
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o-glucosyltransferase
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drug development
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medicine
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molecular biology
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diagnostics
- 2.4.1.221
- notch
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o-fucosylation
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o-fucose
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factor-like
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o-linked
- thrombospondin
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fringe
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dowling-degos
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egf-like
- poglut1
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notch-ligand
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lunatic
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plagl2
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somitogenesis
- dll1
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genodermatosis
- hidradenitis
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o-glucosyltransferase
- drug development
- medicine
- molecular biology
- diagnostics
Reaction
Synonyms
alpha-6-fucosyltransferase, At3g05320, AtOFT1, core alpha6FucT, fucosyltransferase, guanosine diphosphofucose-glycoprotein, FUT2, GDP-fucose glycoprotein fucosyltransferase, GDP-fucose protein O-fucosyltransferase, GDP-fucose protein O-fucosyltransferase 1, GDP-fucose protein O-fucosyltransferase 2, GDP-fucose:polypeptide fucosyltransferase, GDP-L-fucose-glycoprotein fucosyltransferase, GDP-L-fucose:polypeptide fucosyltransferase, glycoprotein fucosyltransferase, guanosine diphosphofucose-glycoprotein fucosyltransferase, N-acetyl-beta-D-glucosaminide alpha1-->6-fucosyltransferase, N-glycan alpha-6-fucosyltransferase, O-fucosyltransferase, O-fucosyltransferase 1, O-fucosyltransferase O-fut 1, O-fucosyltransferase SPINDLY, O-fucT-1, O-fut1, OFUT1, OFUTI, Pofut1, POFUT2, protein O-fucosyltransferase 1, protein O-fucosyltransferase 2, protein O-fucosyltransferases 1, protein O-fucosyltransferases 2, SPY, TGGT1_273550
ECTree
2.4.1.221 peptide-O-fucosyltransferaseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 2.4.1.221 - peptide-O-fucosyltransferase
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GDP-L-fucose + Notch protein
GDP + fucosylated Notch protein
the enzyme fucosylates the epidermal growth factor (EGF)-like domains found in cell-surface and secreted glycoproteins including Notch and its ligands
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?
GDP-L-fucose + transcription regulators DELLA
GDP + fucosylated transcription regulators DELLA
O-fucosylation activates DELLA by promoting its interaction with key regulators in brassinosteroid- and light-signaling pathways, including BRASSINAZOLE-RESISTANT1 (BZR1), PHYTOCHROME-INTERACTING-FACTOR3 (PIF3), and PIF4
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?
GDP-beta-L-fucose + protein
GDP + ?
protein O-fucosyltransferases 1 and 2 (PoFUT1 and PoFUT2) are the enzymes responsible for this protein O-fucosylation and selectively glycosylate specific residues in epidermal growth factor-like (EGF) repeats and thrombospondin type I repeats (TSRs). PoFUT1 glycosylates epidermal growth factor-like (EGF) repeats within the consensus sequence C2-X-X-X-X-S/T-C3
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?
GDP-beta-L-fucose + protein
GDP + ?
protein O-fucosyltransferases 1 and 2 (PoFUT1 and PoFUT2) are the enzymes responsible for this protein O-fucosylation and selectively glycosylate specific residues in epidermal growth factor-like (EGF) repeats and thrombospondin type I repeats (TSRs). PoFUT2 glycosylates thrombospondin type I repeats (TSRs) containing Ser/Thr residues located in the consensus sequences C1-X-X-S/T-C2 or C2-X-X-S/T-C3 of TSRs of groups 1 and 2
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?
GDP-beta-L-fucose + protein
GDP + ?
protein O-fucosyltransferases 1 and 2 (PoFUT1 and PoFUT2) are the enzymes responsible for this protein O-fucosylation and selectively glycosylate specific residues in epidermal growth factor-like (EGF) repeats and thrombospondin type I repeats (TSRs). PoFUT1 glycosylates epidermal growth factor-like (EGF) repeats within the consensus sequence C2-X-X-X-X-S/T-C3
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?
GDP-beta-L-fucose + protein
GDP + ?
protein O-fucosyltransferases 1 and 2 (PoFUT1 and PoFUT2) are the enzymes responsible for this protein O-fucosylation and selectively glycosylate specific residues in epidermal growth factor-like (EGF) repeats and thrombospondin type I repeats (TSRs). PoFUT2 glycosylates thrombospondin type I repeats (TSRs) containing Ser/Thr residues located in the consensus sequences C1-X-X-S/T-C2 or C2-X-X-S/T-C3 of TSRs of groups 1 and 2
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?
GDP-beta-L-fucose + protein
GDP + ?
protein O-fucosyltransferases 1 and 2 (PoFUT1 and PoFUT2) are the enzymes responsible for this protein O-fucosylation and selectively glycosylate specific residues in epidermal growth factor-like (EGF) repeats and thrombospondin type I repeats (TSRs). PoFUT1 glycosylates epidermal growth factor-like (EGF) repeats within the consensus sequence C2-X-X-X-X-S/T-C3
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?
GDP-L-fucose + micronemal protein 2
GDP + fucosylated micronemal protein 2
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?
GDP-L-fucose + micronemal protein 2
GDP + fucosylated micronemal protein 2
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?
additional information
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POFUT1s bind GDP-fucose and EGF repeats, and transfer this monosaccharide into small EGF repeats producing GDP during the reaction
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?
additional information
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essential for Notch signaling
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?
additional information
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may be involved in intracellular quality control
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additional information
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the enzyme catalyzes the addition of O-linked fucose to the epidermal growth factor-like repeats of Notch
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additional information
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the enzyme catalyzes the addition of O-linked fucose to the epidermal growth factor-like repeats of Notch
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?
additional information
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enzyme is an essential core member of Notch signaling pathways in mammals
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additional information
?
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the enzyme catalyzes O-fucosylation of Notch proteins, twenty potential O-fucosylation sites on EGF-like repeats are present on mouse Notch1, and 13 are known to be modified by O-fucose. Notch2 and Notch3 receptors have 21 and 15 potential O-fucosylation sites, respectively, and are probably predominantly O-fucosylated
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?
additional information
?
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the enzyme catalyzes O-fucosylation of Notch proteins, twenty potential O-fucosylation sites on EGF-like repeats are present on mouse Notch1, and 13 are known to be modified by O-fucose. Notch2 and Notch3 receptors have 21 and 15 potential O-fucosylation sites, respectively, and are probably predominantly O-fucosylated
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?
