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Information on EC 2.4.1.221 - peptide-O-fucosyltransferase
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EC Tree
2.4.1.221 peptide-O-fucosyltransferaseIUBMB Comments
The enzyme, found in animals and plants, is involved in the biosynthesis of O-fucosylated proteins. In EGF domains, the attachment of O-linked fucose to serine or threonine occurs within the sequence Cys-Xaa-Xaa-Gly-Gly-Ser/Thr-Cys.
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Word Map
- 2.4.1.221
- notch
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o-fucosylation
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o-fucose
-
factor-like
-
o-linked
- thrombospondin
-
fringe
-
dowling-degos
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egf-like
- poglut1
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notch-ligand
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lunatic
-
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
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
+
=
+
+
[protein]-(L-serine/L-threonine)
=
+
[protein]-3-O-(alpha-L-fucosyl)-(L-serine/L-threonine)
Synonyms
pofut1, protein o-fucosyltransferase 1, pofut2, o-fucosyltransferase, ofut1, protein o-fucosyltransferase 2, o-fut1, o-fuct-1, o-fucosyltransferase 1, alpha-6-fucosyltransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-6-fucosyltransferase
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core alpha6FucT
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fucosyltransferase, guanosine diphosphofucose-glycoprotein
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FUT2
GDP-fucose glycoprotein fucosyltransferase
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GDP-fucose protein O-fucosyltransferase
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GDP-fucose protein O-fucosyltransferase 1
GDP-fucose:polypeptide fucosyltransferase
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GDP-L-fucose-glycoprotein fucosyltransferase
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GDP-L-fucose:polypeptide fucosyltransferase
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glycoprotein fucosyltransferase
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guanosine diphosphofucose-glycoprotein fucosyltransferase
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N-acetyl-beta-D-glucosaminide alpha1-->6-fucosyltransferase
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N-glycan alpha-6-fucosyltransferase
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O-fucosyltransferase 1
O-fucT-1
OFUT1
Pofut1
POFUT2
protein O-fucosyltransferase 1
protein O-fucosyltransferase 2
protein O-fucosyltransferases 1
protein O-fucosyltransferases 2
TGGT1_273550
O-fucT-1
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Pofut1
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Pofut1
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POFUT2
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GDP-beta-L-fucose + PCQNGGSCKDQL = PCQNGGS(O-beta-L-fucosyl)-CKDQL + GDP
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GDP-beta-L-fucose + PCQNGGSCKDQL = PCQNGGS(O-beta-L-fucosyl)-CKDQL + GDP
catalytic mechanism and substrate specificity, overview
GDP-beta-L-fucose + PCQNGGSCKDQL = PCQNGGS(O-beta-L-fucosyl)-CKDQL + GDP
catalytic mechanism of isozyme POFUT2 and its preference for threonine over serine residues
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycosyl group transfer
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transglycosylation
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
GDP-beta-L-fucose:protein-(L-serine/L-threonine) O-alpha-L-fucosyltransferase (configuration-inverting)
The enzyme, found in animals and plants, is involved in the biosynthesis of O-fucosylated proteins. In EGF domains, the attachment of O-linked fucose to serine or threonine occurs within the sequence Cys-Xaa-Xaa-Gly-Gly-Ser/Thr-Cys.
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CAS REGISTRY NUMBER
COMMENTARY
9033-08-3
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SUBSTRATE
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-6-alkynyl fucose + protein
?
-
6-alkynyl fucose is efficiently incorporated onto EGF repeats, TSRs, and N-glycan on Lfng and N-glycans on a number of proteins in crude lysates of CHO cells, e.g. the O-fucosylation site in EGF3 of mouse Notch1 and elongated by Lfng, mass spectrometry analysis, overview. Using the Cu(I)-catalyzed azide-alkyne cycloaddition (CuAAC), or click reaction, azido-biotin allows tagging and detection of 6AF-modified proteins
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?
GDP-Fuc + biotin-DHPCTQALGNPCLNGGSCVPREATYECLCPGGFSGLHCEKG
?
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peptide of the fourth EGF domain of agrin (EGF4) is used as an acceptor substrate with biotin conjugated at the N-terminus
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?
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
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 + ?
SN1-like mechanism. 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 + ?
SN2-like mechanism. 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 + ?
SN1-like mechanism. 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 + ?
SN2-like mechanism. 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 + ?
SN1-like mechanism. 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-fucose + TSR4
GDP + fucosyl-TSR4
GDP-fucose binding mode, overview. Activity with recombinant TSR4 mutants expressed in HEK293Tcells
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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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?
GDP-L-fucose + Notch
?
Drosophila sp. (in: flies)
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O-fucosylation of Notch, catalytic and non-catalytic activities
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?
GDP-L-fucose + Notch
?
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Pofut1 transfers fucose in the endoplasmic reticulum, transfers fucose to Ser or Thr residues of epidermal growth factor-like repeats
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?
GDP-L-fucose + transcription regulators DELLA
GDP + fucosylated transcription regulators DELLA
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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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?
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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enzyme POFUT2 fucosylates threonine preferentially over serine and relies on folded TSRs containing the minimal consensus sequence C-X-X-S/T-, substrate specificity, overview
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?
additional information
?
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enzyme POFUT2 fucosylates threonine preferentially over serine and relies on folded TSRs containing the minimal consensus sequence C-X-X-S/T-, substrate specificity, overview
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?
additional information
?
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fucosylates various synthetic peptides of EGF-1 domain of human factor VII, GDP-mannose, UDP-glucose, UDP-N-acetylglucosamine, UDP-galactose, UDP-H-acetylgalactosamine and UDP-xylose can replace GDP-fucose
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?
additional information
?
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links fucose through an O-glycosidic linkage to a conserved serine or threonine residue in of the EGF-1 domain of human factor VII, various synthetic peptides serve as substrates
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?
additional information
?
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essential for Notch signaling
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?
additional information
?
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Drosophila sp. (in: flies)
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enzyme that glycosylates epidermal growth factorlike domains of Notch, also has a distinct Notch chaperone activity
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?
additional information
?
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O-fucosylation of thrombospondin-1 at Ser 377, Thr 432 and Thr 489
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?
additional information
?
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adds o-fucose to epidermal growth factor-like repeats
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?
additional information
?
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adds o-fucose to epidermal growth factor-like repeats
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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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fucose is added exclusively to properly folded Epidermal Growth Factor-like (EGF) repeats and Thrombospondin Type 1 Repeats (TSRs)
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additional information
?
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fucose is added exclusively to properly folded Epidermal Growth Factor-like (EGF) repeats and Thrombospondin Type 1 Repeats (TSRs)
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additional information
?
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fucose is added exclusively to properly folded Epidermal Growth Factor-like (EGF) repeats and Thrombospondin Type 1 Repeats (TSRs). The O-linked fucose can also be elongated with other sugars
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additional information
?
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fucose is added exclusively to properly folded Epidermal Growth Factor-like (EGF) repeats and Thrombospondin Type 1 Repeats (TSRs). The O-linked fucose can also be elongated with other sugars
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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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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.
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?
additional information
?
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protein O-fucosyltransferase 1 and protein O-fucosyltransferase 2 add O-linked fucose at distinct consensus sequences in properly folded epidermal growth factor (EGF)-like repeats and thrombospondin type-1 (TSR) repeats, respectively
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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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?
additional information
?
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links fucose through an O-glycosidic linkage to a conserved serine or threonine residue in of the EGF-1 domain of human factor VII, various synthetic peptides serve as substrates
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?
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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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
GDP-L-fucose + micronemal protein 2
GDP + fucosylated micronemal protein 2
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-
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?
GDP-L-fucose + micronemal protein 2
GDP + fucosylated micronemal protein 2
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-
-
?
additional information
?
-
POFUT1s bind GDP-fucose and EGF repeats, and transfer this monosaccharide into small EGF repeats producing GDP during the reaction
-
-
?
additional information
?
-
essential for Notch signaling
-
-
?
additional information
?
-
-
may be involved in intracellular quality control
-
-
?
additional information
?
-
the enzyme catalyzes the addition of O-linked fucose to the epidermal growth factor-like repeats of Notch
-
-
?
additional information
?
-
-
the enzyme catalyzes the addition of O-linked fucose to the epidermal growth factor-like repeats of Notch
-
-
?
additional information
?
-
-
enzyme is an essential core member of Notch signaling pathways in mammals
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mn2+
additional information
Mg2+ is not required for catalytic activity by POFUT1, glycosyltransferases adopting GT-B folds are metal-independent
Mn2+
activates transfer of fucose from DP-fucose to small EGF repeats
Mn2+
activates wild-type and mutant enzymes, but has a nonessential role in catalysis. Residue R290 replaces Mn2+ function by establishing electrostatic and hydrogen bond interactions with beta-phosphate
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Abortion, Spontaneous
poFUT1 promotes endometrial decidualization by enhancing the O-fucosylation of Notch1.
Abortion, Spontaneous
poFUT1 promotes uterine angiogenesis and vascular remodeling via enhancing the O-fucosylation on uPA.
Abortion, Spontaneous
Progesterone promotes embryo adhesion by upregulating c-Fos/c-Jun transcription factor-mediate poFUT1 expression.
Abortion, Threatened
LIF upregulates poFUT1 expression and promotes trophoblast cell migration and invasion at the fetal-maternal interface.
Adenoma
Molecular characterization of colorectal adenomas reveals POFUT1 as a candidate driver of tumor progression.
Breast Neoplasms
Overexpression of Pofut1 and activated Notch1 may be associated with poor prognosis in breast cancer.
Carcinogenesis
PLAGL2 and POFUT1 are regulated by an evolutionarily conserved bidirectional promoter and are collaboratively involved in colorectal cancer by maintaining stemness.
Carcinoma
Bioinformatics insight into glycosyltransferase gene expression in gastric cancer: POFUT1 is a potential biomarker.
Carcinoma
Protein O-fucosyltransferase 1: A potential diagnostic marker and therapeutic target for human oral cancer.
Carcinoma, Ductal
Overexpression of Pofut1 and activated Notch1 may be associated with poor prognosis in breast cancer.
Carcinoma, Hepatocellular
Author Correction: Caveolin-1 promotes invasion and metastasis by upregulating Pofut1 expression in mouse hepatocellular carcinoma.
Carcinoma, Hepatocellular
Caveolin-1 promotes invasion and metastasis by upregulating Pofut1 expression in mouse hepatocellular carcinoma.
Carcinoma, Hepatocellular
Overexpression of protein O-fucosyltransferase 1 accelerates hepatocellular carcinoma progression via the Notch signaling pathway.
Colorectal Neoplasms
Functional Characterization of POFUT1 Variants Associated with Colorectal Cancer.
Colorectal Neoplasms
PLAGL2 and POFUT1 are regulated by an evolutionarily conserved bidirectional promoter and are collaboratively involved in colorectal cancer by maintaining stemness.
Colorectal Neoplasms
POFUT1 promotes colorectal cancer development through the activation of Notch1 signaling.
Colorectal Neoplasms
Weighted gene coexpression analysis indicates that PLAGL2 and POFUT1 are related to the differential features of proximal and distal colorectal cancer.
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
Analyzing the Effects of O-Fucosylation on Secretion of ADAMTS Proteins Using Cell-Based Assays.
Enterocolitis
Intestinal deletion of Pofut1 in the mouse inactivates notch signaling and causes enterocolitis.
Esophageal Neoplasms
Upregulation of Fucosyltransferase 3, 8 and protein O-Fucosyltransferase 1, 2 genes in esophageal cancer stem-like cells (CSLCs).
Glioblastoma
Histology-based expression profiling yields novel prognostic markers in human glioblastoma.
Glioblastoma
POFUT1 acts as a tumor promoter in glioblastoma by enhancing the activation of Notch signaling.
Heart Failure
Uncontrolled angiogenic precursor expansion causes coronary artery anomalies in mice lacking Pofut1.
Hidradenitis
Novel POFUT1 mutation associated with hidradenitis suppurativa-Dowling-Degos disease firm up a role for Notch signalling in the pathogenesis of this disorder.
Hidradenitis
Novel POFUT1 mutation associated with hidradenitis suppurativa-Dowling-Degos disease firm up a role for Notch signalling in the pathogenesis of this disorder: reply from the authors.
Hidradenitis Suppurativa
A new nonsense mutation in the POGLUT1 gene in two sisters with Dowling-Degos disease.
Hidradenitis Suppurativa
A novel mutation in POFUT1 gene associated with Dowling-Degos disease and hidradenitis suppurativa.
Hyperpigmentation
Phenotypic expansion of POFUT1 loss of function mutations in a disorder featuring segmental dyspigmentation with eczematous and folliculo-centric lesions.
Hyperpigmentation
Variant in human POFUT1 reduces enzymatic activity and likely causes a recessive microcephaly, global developmental delay with cardiac and vascular features.
Hypopigmentation
Mutations in POFUT1, Encoding Protein O-fucosyltransferase 1, Cause Generalized Dowling-Degos Disease.
Infections
Protein O-fucosylation in Plasmodium falciparum ensures efficient infection of mosquito and vertebrate hosts.
Infections
Protein O-Fucosyltransferase 2 Is Not Essential for Plasmodium berghei Development.
Infections
Protein O-fucosyltransferase 2-mediated O-glycosylation of the adhesin MIC2 is dispensable for Toxoplasma gondii tachyzoite infection.
Keratosis, Seborrheic
Novel deletion of the POFUT1 gene associated with multiple seborrheic keratosis Dowling-Degos disease.
Liver Diseases
Variant in human POFUT1 reduces enzymatic activity and likely causes a recessive microcephaly, global developmental delay with cardiac and vascular features.
Lymphatic Metastasis
Overexpression of Pofut1 and activated Notch1 may be associated with poor prognosis in breast cancer.
Lymphatic Metastasis
POFUT1 mRNA expression as an independent prognostic parameter in muscle-invasive bladder cancer.
Malaria
Protein O-fucosylation in Plasmodium falciparum ensures efficient infection of mosquito and vertebrate hosts.
Malaria
Protein O-Fucosyltransferase 2 Is Not Essential for Plasmodium berghei Development.
Malignant Atrophic Papulosis
Variant in human POFUT1 reduces enzymatic activity and likely causes a recessive microcephaly, global developmental delay with cardiac and vascular features.
Microcephaly
Variant in human POFUT1 reduces enzymatic activity and likely causes a recessive microcephaly, global developmental delay with cardiac and vascular features.
Mouth Neoplasms
Protein O-fucosyltransferase 1: A potential diagnostic marker and therapeutic target for human oral cancer.
Myocardial Infarction
Uncontrolled angiogenic precursor expansion causes coronary artery anomalies in mice lacking Pofut1.
Neoplasm Metastasis
Author Correction: Caveolin-1 promotes invasion and metastasis by upregulating Pofut1 expression in mouse hepatocellular carcinoma.
Neoplasm Metastasis
Caveolin-1 promotes invasion and metastasis by upregulating Pofut1 expression in mouse hepatocellular carcinoma.
Neoplasm Metastasis
Overexpression of Pofut1 and activated Notch1 may be associated with poor prognosis in breast cancer.
Neoplasm Metastasis
POFUT1 mRNA expression as an independent prognostic parameter in muscle-invasive bladder cancer.
Neoplasms
Bioinformatics insight into glycosyltransferase gene expression in gastric cancer: POFUT1 is a potential biomarker.
Neoplasms
Caveolin-1 promotes invasion and metastasis by upregulating Pofut1 expression in mouse hepatocellular carcinoma.
Neoplasms
Downregulated protein O-fucosyl transferase 1 (Pofut1) expression exerts antiproliferative and antiadhesive effects on hepatocytes by inhibiting Notch signalling.
Neoplasms
Functional Characterization of POFUT1 Variants Associated with Colorectal Cancer.
Neoplasms
Integrated analysis of genome-wide copy number alterations and gene expression in microsatellite stable, CpG island methylator phenotype-negative colon cancer.
Neoplasms
Molecular characterization of colorectal adenomas reveals POFUT1 as a candidate driver of tumor progression.
Neoplasms
Overexpression of Pofut1 and activated Notch1 may be associated with poor prognosis in breast cancer.
Neoplasms
PLAGL2 and POFUT1 are regulated by an evolutionarily conserved bidirectional promoter and are collaboratively involved in colorectal cancer by maintaining stemness.
Neoplasms
POFUT1 acts as a tumor promoter in glioblastoma by enhancing the activation of Notch signaling.
Neoplasms
POFUT1 and PLAGL2 gene pair linked by a bidirectional promoter: the two in one of tumour progression in colorectal cancer?
Neoplasms
POFUT1 mRNA expression as an independent prognostic parameter in muscle-invasive bladder cancer.
Neoplasms
POFUT1 promotes colorectal cancer development through the activation of Notch1 signaling.
Neoplasms
Protein O-fucosyltransferase 1: A potential diagnostic marker and therapeutic target for human oral cancer.
Neoplasms
Structure of human POFUT1, its requirement in ligand-independent oncogenic Notch signaling, and functional effects of Dowling-Degos mutations.
Neoplasms
Upregulation of Fucosyltransferase 3, 8 and protein O-Fucosyltransferase 1, 2 genes in esophageal cancer stem-like cells (CSLCs).
Neoplasms
Weighted gene coexpression analysis indicates that PLAGL2 and POFUT1 are related to the differential features of proximal and distal colorectal cancer.
peptide-o-fucosyltransferase deficiency
POFUT1 is dispensable for structure, function and survival of mouse podocytes.
peptide-o-fucosyltransferase deficiency
Protein O-fucosyltransferase 1 (Pofut1) regulates lymphoid and myeloid homeostasis through modulation of notch receptor ligand interactions.
peptide-o-fucosyltransferase deficiency
Recognition of EGF-like domains by the Notch-modifying O-fucosyltransferase POFUT1.
Psoriasis
Genetic diagnosis history and osteoarticular phenotype of a non-transfusion secondary hemochromatosis.
Skin Diseases
Phenotypic expansion of POFUT1 loss of function mutations in a disorder featuring segmental dyspigmentation with eczematous and folliculo-centric lesions.
Squamous Cell Carcinoma of Head and Neck
Protein O-fucosyltransferase 1: A potential diagnostic marker and therapeutic target for human oral cancer.
Stomach Neoplasms
Bioinformatics insight into glycosyltransferase gene expression in gastric cancer: POFUT1 is a potential biomarker.
Teratoma
O-fucosylation of thrombospondin type 1 repeats restricts epithelial to mesenchymal transition (EMT) and maintains epiblast pluripotency during mouse gastrulation.
Urinary Bladder Neoplasms
POFUT1 mRNA expression as an independent prognostic parameter in muscle-invasive bladder cancer.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
steady-state kinetic measurements of wild-type and mutant POFUT2
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additional information
additional information
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steady-state kinetic measurements of wild-type and mutant POFUT2
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
