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Information on EC 2.4.1.221 - peptide-O-fucosyltransferase
for references in articles please use BRENDA:EC2.4.1.221
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EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.1 Hexosyltransferases
2.4.1.221 peptide-O-fucosyltransferase
IUBMB 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. The POFUT3 and POFUT4 proteins modify EMI domains.
The enzyme appears in viruses and cellular organisms
- 2.4.1.221
- notch
-
o-fucosylation
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o-fucose
-
factor-like
-
o-linked
- thrombospondin
-
fringe
-
dowling-degos
-
egf-like
- poglut1
-
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 Schemes
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[protein]-(L-serine/L-threonine)
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[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, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-6-fucosyltransferase
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alpha1,3-fucosyltransferase
core alpha6FucT
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fucosyltransferase, guanosine diphosphofucose-glycoprotein
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FUT10
FUT11
FUT2
GDP-fucose glycoprotein fucosyltransferase
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-
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GDP-fucose protein O-fucosyltransferase
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-
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GDP-fucose protein O-fucosyltransferase 1
GDP-fucose:polypeptide fucosyltransferase
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-
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GDP-L-fucose-glycoprotein fucosyltransferase
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-
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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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-
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N-acetyl-beta-D-glucosaminide alpha1-->6-fucosyltransferase
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-
-
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N-glycan alpha-6-fucosyltransferase
-
-
-
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O-fucosyltransferase 1
O-fucT-1
OFUT1
Pofut1
POFUT2
POFUT3
POFUT4
protein O-fucosyltransferase 1
protein O-fucosyltransferase 2
protein O-fucosyltransferases 1
protein O-fucosyltransferases 2
spindly
TGGT1_273500
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 + [protein]-(L-serine/L-threonine) = GDP + [protein]-3-O-(alpha-L-fucosyl)-(L-serine/L-threonine)
GDP-beta-L-fucose + [protein]-(L-serine/L-threonine) = GDP + [protein]-3-O-(alpha-L-fucosyl)-(L-serine/L-threonine)
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GDP-beta-L-fucose + [protein]-(L-serine/L-threonine) = GDP + [protein]-3-O-(alpha-L-fucosyl)-(L-serine/L-threonine)
catalytic mechanism and substrate specificity, overview
GDP-beta-L-fucose + [protein]-(L-serine/L-threonine) = GDP + [protein]-3-O-(alpha-L-fucosyl)-(L-serine/L-threonine)
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. The POFUT3 and POFUT4 proteins modify EMI domains.
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CAS REGISTRY NUMBER
COMMENTARY
9033-08-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GDP-6-alkynyl fucose + protein
?
-
Substrates: 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-beta-L-fucose + N-acetyl-D-lactosamine
GDP + L-Fuc-alpha-(1->3)-[D-Gal-beta(1->4)]-D-GlcNac
-
Substrates: -
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?
GDP-beta-L-fucose + NeuAcalpha(2,3)-Galbeta(1,4)-GlcNAc-R
GDP + NeuAcalpha(2,3)-Galbeta(1,4)[Fucalpha1-3]-GlcNAc-R
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Substrates: sialyl-Lewisx terminal structure
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?
GDP-beta-L-fucose + NeuAcalpha(2,3)-Galbeta(1,4)[SO3H-6]-GlcNAc-R
GDP + NeuAcalpha(2,3)-Galbeta(1,4)[Fucalpha1-3][SO3H-6]-GlcNAc-R
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Substrates: sialyl-Lewisx terminal structure
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?
GDP-beta-L-fucose + [DELLA]]-(L-serine/L-threonine)
GDP + [DELLA]-3-O-(alpha-L-fucosyl)-(L-serine/L-threonine)
Substrates: -
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?
GDP-beta-L-fucose + [human MMRN1 protein EMI domain]-(L-serine/L-threonine)
GDP + [human MMRN1 protein EMI domain]-3-O-(alpha-L-fucosyl)-(L-serine/L-threonine)
Substrates: an MMRN1 T216A mutant protein displays a reduced fucosylation level at the T265 site, indicating that the presence of the T216 fucose facilitates the addition of the T265 fucose
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?
GDP-beta-L-fucose + [Multimerin-1]-(L-serine/L-threonine)
GDP + [Multimerin-1]-3-O-(alpha-L-fucosyl)-(L-serine/L-threonine)
Substrates: the enzyme adds O-fucose to Multimerin-1 elastin microfibril interface domain in vitro
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?
GDP-beta-L-fucose + [SPINDLY]]-(L-serine/L-threonine)
GDP + [SPINDLY]-3-O-(alpha-L-fucosyl)-(L-serine/L-threonine)
GDP-beta-L-fucose + [SSSSSASSSSSSFPSSSSSDSVPPR]]-(L-serine/L-threonine)
GDP + [SSSSSASSSSSSFPSSSSSDSVPPR]-3-O-(alpha-L-fucosyl)-(L-serine/L-threonine)
GDP-Fuc + biotin-DHPCTQALGNPCLNGGSCVPREATYECLCPGGFSGLHCEKG
?
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Substrates: 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
Substrates: 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 + protein
GDP + fucosylated protein
Substrates: -
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?
GDP-L-fucose + transcription regulators DELLA
GDP + fucosylated transcription regulators DELLA
GlcNAcbeta(1-2)Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-)(CH2)3-NHCO-(CH2)5-NH-biotin + GDP-L-fucose
GlcNAcbeta(1-2)Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)[Fucalpha(1-3)]GlcNAcbeta(1-)(CH2)3-NHCO-(CH2)5-NH-biotin + GDP
GlcNAcbeta(1-2)Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-)AspNHCO-biotin + GDP-L-fucose
GlcNAcbeta(1-2)Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)[Fucalpha(1-3)]GlcNAcbeta(1-)AspNHCO-biotin + GDP
Substrates: -
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?
GDP-beta-L-fucose + H2O
GDP + L-fucose
Substrates: -
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?
GDP-beta-L-fucose + protein
GDP + ?
Substrates: 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 + ?
Substrates: 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 + ?
Substrates: 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 + ?
Substrates: 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 + ?
Substrates: 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 + ?
Substrates: 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 + ?
Substrates: 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 + ?
Substrates: 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 + ?
Substrates: 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 + ?
Substrates: 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 + [SPINDLY]]-(L-serine/L-threonine)
GDP + [SPINDLY]-3-O-(alpha-L-fucosyl)-(L-serine/L-threonine)
Substrates: -
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?
GDP-beta-L-fucose + [SPINDLY]]-(L-serine/L-threonine)
GDP + [SPINDLY]-3-O-(alpha-L-fucosyl)-(L-serine/L-threonine)
Substrates: i.e. autofucosylation
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?
GDP-beta-L-fucose + [SPINDLY]]-(L-serine/L-threonine)
GDP + [SPINDLY]-3-O-(alpha-L-fucosyl)-(L-serine/L-threonine)
Substrates: i.e. autofucosylation
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?
GDP-beta-L-fucose + [SSSSSASSSSSSFPSSSSSDSVPPR]]-(L-serine/L-threonine)
GDP + [SSSSSASSSSSSFPSSSSSDSVPPR]-3-O-(alpha-L-fucosyl)-(L-serine/L-threonine)
Substrates: SSSSSASSSSSSFPSSSSSDSVPPR i.e. tryptic peptide ZN190 derived from RINGF1
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GDP-beta-L-fucose + [SSSSSASSSSSSFPSSSSSDSVPPR]]-(L-serine/L-threonine)
GDP + [SSSSSASSSSSSFPSSSSSDSVPPR]-3-O-(alpha-L-fucosyl)-(L-serine/L-threonine)
Substrates: SSSSSASSSSSSFPSSSSSDSVPPR i.e. tryptic peptide ZN190 derived from RINGF1
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?
GDP-fucose + TSR4
GDP + fucosyl-TSR4
Substrates: 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
Substrates: -
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?
GDP-L-fucose + micronemal protein 2
GDP + fucosylated micronemal protein 2
Substrates: -
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?
GDP-L-fucose + Notch
?
-
Substrates: O-fucosylation of Notch, catalytic and non-catalytic activities
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?
GDP-L-fucose + Notch
?
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Substrates: 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
Substrates: 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-L-fucose + transcription regulators DELLA
GDP + fucosylated transcription regulators DELLA
Substrates: -
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?
GlcNAcbeta(1-2)Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-)(CH2)3-NHCO-(CH2)5-NH-biotin + GDP-L-fucose
GlcNAcbeta(1-2)Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)[Fucalpha(1-3)]GlcNAcbeta(1-)(CH2)3-NHCO-(CH2)5-NH-biotin + GDP
Substrates: FUT10 activity toward the acceptor 0989-BM is increased by about 50% compared with those observed using BGA-biotin
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GlcNAcbeta(1-2)Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-)(CH2)3-NHCO-(CH2)5-NH-biotin + GDP-L-fucose
GlcNAcbeta(1-2)Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)[Fucalpha(1-3)]GlcNAcbeta(1-)(CH2)3-NHCO-(CH2)5-NH-biotin + GDP
Substrates: -
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?
additional information
?
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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: enzyme recognizes similarly the 3D structure of thrombospondin repeats from both groups 1 and 2 to fucosylate them. Its active site is highly exposed to the solvent
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additional information
?
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Substrates: 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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Substrates: 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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Substrates: essential for Notch signaling
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additional information
?
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Substrates: 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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Substrates: O-fucosylation of thrombospondin-1 at Ser 377, Thr 432 and Thr 489
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additional information
?
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Substrates: adds o-fucose to epidermal growth factor-like repeats
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additional information
?
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Substrates: adds o-fucose to epidermal growth factor-like repeats
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additional information
?
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Substrates: may be involved in intracellular quality control
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additional information
?
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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: PoFUT2 follows a pure SN2 mechanism. The enzyme recognizes similarly the 3D structure of thrombospondin repeats (TSRs) from both groups 1 and 2 to fucosylate them. Water molecules interacting directly with the diphosphate contribute to stabilizing the leaving group GDP. The acceptor TSR substrate protects the area around the anomeric carbon of GDP-Fuc from bulk water and hinders hydrolysis
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additional information
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Substrates: enzyme is an essential core member of Notch signaling pathways in mammals
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additional information
?
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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: in the absence of an acceptor substrate, SPINDLY hydrolyses GDP-Fuc but not UDP-GlcNAc, GDP-Man, or UDP-Gal
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additional information
?
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Substrates: in the absence of an acceptor substrate, SPINDLY hydrolyses GDP-Fuc but not UDP-GlcNAc, GDP-Man, or UDP-Gal
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GDP-beta-L-fucose + NeuAcalpha(2,3)-Galbeta(1,4)-GlcNAc-R
GDP + NeuAcalpha(2,3)-Galbeta(1,4)[Fucalpha1-3]-GlcNAc-R
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Substrates: sialyl-Lewisx terminal structure
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GDP-beta-L-fucose + NeuAcalpha(2,3)-Galbeta(1,4)[SO3H-6]-GlcNAc-R
GDP + NeuAcalpha(2,3)-Galbeta(1,4)[Fucalpha1-3][SO3H-6]-GlcNAc-R
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Substrates: sialyl-Lewisx terminal structure
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GDP-L-fucose + Notch protein
GDP + fucosylated Notch protein
Substrates: 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
Substrates: 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 + ?
Substrates: 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 + ?
Substrates: 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 + ?
Substrates: 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 + ?
Substrates: 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 + ?
Substrates: 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
Substrates: -
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GDP-L-fucose + micronemal protein 2
GDP + fucosylated micronemal protein 2
Substrates: -
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additional information
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Substrates: 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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Substrates: essential for Notch signaling
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additional information
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Substrates: may be involved in intracellular quality control
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additional information
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Substrates: 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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Substrates: 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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Substrates: enzyme is an essential core member of Notch signaling pathways in mammals
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additional information
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Substrates: 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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Substrates: 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
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
additional information
Mg2+ is not required for catalytic activity by POFUT1, glycosyltransferases adopting GT-B folds are metal-independent
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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interleukin-6 or interleukin-8 significantly induce the expression of alpha1,3/4-fucosyltransferases, the amounts of sialyl-Lewisx and 6-sulfo-sialyl-Lewisx epitopes at the periphery of high molecular-mass proteins, including MUC4, are increased
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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
0.15 - 0.154
GlcNAcbeta(1-2)Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-)AspNHCO-biotin
0.000999
GDP-beta-L-fucose
pH 7.0, 37°C, T265 O-fucosylation site
0.006738
GDP-beta-L-fucose
pH 7.0, 37°C, T216 O-fucosylation site
0.15
GlcNAcbeta(1-2)Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-)AspNHCO-biotin
FUT10-479
0.154
GlcNAcbeta(1-2)Manalpha(1-6)[GlcNAcbeta(1-2)Manalpha(1-3)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAcbeta(1-)AspNHCO-biotin
FUT10-391
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
enzyme has a distinct chaperone activity for Notch proteins independent of its enzymic activity
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brenda
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brenda
floxed Pofut1 (Pofut1F/F) mice and Pofut1 heterozygous mice (Pofut1+/-)
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brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
upregulated in esophageal cancer stem-like cell in comparison to adherent cells
brenda
analysis of enzyme expression in 8 HCC cell lines and 253 human HCC tissues, overview
brenda
fetal tissue with weak level, adult tissue with moderate level
brenda
oral squamous cell carcinoma cell-derived cell lines and primary oral squamous cell carcinoma cells, increased enzyme expression
brenda
fetal tissue, intensity similar to in the embryos
brenda
additional information
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fucosylation-deficient Lec13 chinese hamster ovary cells have wild-type levels of Pofut1 and cell surface Notch receptors
brenda
additional information
adult spleen, heart, muscle, liver, and pancreas do not express any of the FUT10 transcripts
brenda
additional information
adult spleen, heart, muscle, liver, and pancreas do not express any of the FUT10 transcripts
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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OFUT1 promotes transcytosis of Notch from the apical plasma membrane to the adherens junctions
brenda
additional information
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cell surface accumulation of Notch in ofut1 mutant cells
brenda
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OFUT1 may be a chaperone of Notch that is necessary for retaining Notch at the cell surface once it has traversed the secretory pathway
brenda
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OFUT1 associates with Notch at the cell surface and promotes the constitutive endocytosis of Notch receptors
brenda
Spindly mediates assembly of O-Fuc on numerous proteins that accumulate in the cytoplasm
brenda
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retention in the ER is required for normal OFUT1 function in vivo
brenda
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Ofut1 acts as a chaperone in the endoplasmic reticulum to promote the proper folding of the epidermal growth factor-like repeats of Notch, thereby ensuring its correct cell-surface localization and ligand-binding activity
brenda
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OFUT1 may be a chaperone of Notch that is necessary for escorting Notch out of the endoplasmic reticulum
brenda
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OFUT1 is required for the correct folding of Notch receptors in the endoplasmic reticulum and their subsequent trafficking to the cell surface
brenda
FUT10-419 and FUT10-479, FUT10-479 has the same trans-membrane domain and NH2-terminal endoplasmic reticulum membrane retention signal found in the FUT10-419 splice variant plus a new endoplasmic reticulum membrane retention signal in the COOH terminus
brenda
FUT11-476 has no endoplasmic reticulum membrane retention signal, but the FUT11-492 variant has a KKXX-like motif in its COOH terminus that can retain it in the endoplasmic reticulum
brenda
Pofut1 mainly colocalizes with GRP94, an endoplasmic reticulum chaperone
brenda
FUT10-391 is a soluble protein without a transmembrane domain or endoplasmic reticulum retention signal that transiently localizes to the Golgi and then is routed to the lysosome
brenda
FUT10-419 and FUT10-479 have a type II trans-membrane topology. FUT10-479 has, in addition, a COOH-endoplasmic reticulum membrane retention signal
brenda
additional information
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Ofut1 is required for the proper distribution of Notch at adherens junction
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brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
evolution
CePOFUT1 is a member of the GT65 family and contains four conserved disulfide bridges through the GT65 family
evolution
POFUT2 belongs to the classical GT-B fold family of glycosyltransferases with two closely interacting Rossmann-like domains. POFUT2 shows a variation of the classical GT-B fold
evolution
the highly correlated presence of POFUT1 and fucosylatable hEGFs has accompanied animal evolution
malfunction
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embryonic stem cells lacking Pofut1 are deficient in Notch ligand binding, have wild-type levels of cell surface Notch receptors. Pofut1-/- embryonic stem cells do not bind Notch ligands or exhibit Notch signaling. Overexpression of fucosyltransferase-defective Pofut1 R245A in Pofut1-/- cells partially rescues ligand binding and Notch signaling, but this effect is not specific. Under certain conditions, mammalian Notch receptors can bind Notch ligands and transduce a Notch signal in the absence of Pofut1 and O-fucose
malfunction
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Pofut1-null mouse shows a similar phenotype to the RBP-Jk null mouse. Cardiac development in the Pofut1-/- mice is severely affected in valve formation, which is characterized in the lack of mesenchymal cells as seen in RBP-Jk null embryos and embryonic development is arrested at E9.0. Pofut1-null cells do not possess normally localized Notch1 receptors. Abnormal accumulation of the Notch1 receptor in the endoplasmic reticulum and cytoplasm in Pofut1-null mouse embryos
malfunction
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Pofut1 deletion inactivates Notch signaling, giving rise to smaller but viable mice. Dysplastic foci in Pofut1-deficient small intestine with occasional progression to tumor formation. Inactivation of Pofut1 leads to intestinal inflammation. Mucus hypersecretion upon Pofut1 inactivation is accompanied by alteration of the mucus-associated flora, which likely contributes to the development of enterocolitis
malfunction
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in ofut1 mutant cells, Notch goes to the membrane, is internalized and accumulates in an uncharacterized endocytic compartment. Knockdown of Ofut1 using doublestranded RNA in cultured cells inhibits the secretion of a soluble version of the Notch extracellular domain. In ofut1 mutant cells, Notch does not accumulate at adherens junctions but instead accumulates into intracellular dots. A low level of Notch is also present at the surface of ofut1 mutant cells
malfunction
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neural crest cell-specific Pofut1-knockout mice die within 1 day of birth, accompanied by a defect of enteric nervous system development. Sox10 expression is decreased in Pofut1-null enteric neural crest cells, whereas the number of enteric neural crest cells that express Mash1, a potent repressor of Sox10, is increased in the Pofut1-null mouse. Enteric neural crest cells lacking Pofut1 show premature neurogenesis and a decrease in the number of glial progenitors
malfunction
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deletion of Pofut1 leads to global defects in Notch signaling and death of mice at E9.5, with a phenotype consistent with inactivation of signaling by the four Notch receptors. Embryonic stem cells lacking Pofut1 express Notch receptors on the cell surface at similar levels to wild-type cells. In mouse somites, there is evidence of altered Notch trafficking in the absence of Pofut1, consistent with reduced cell surface expression
malfunction
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CHO cells lacking Pofut1 express Notch receptors on the cell surface at similar levels to wild-type cells
malfunction
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loss of OFUT1 results in the phenotype that is characteristic of Notch loss of function. Loss of OFUT1 leads to the loss of cell surface expression and the intracellular accumulation of Notch receptors. Secretion of Notch is impaired in OFUT1-depleted S2 cells and the abnormal endoplasmic reticulum accumulation of Notch receptors is observed in Ofut1 mutant clones in Drosophila wing imaginal discs
malfunction
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loss of Pofut1 results in the phenotype that is characteristic of Notch loss of function
malfunction
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siRNAs eliminating Pofut1 transcripts in CHO cells. CHO cells deficient in Pofut1 have reduced Notch signaling and ligand binding. Under certain conditions, mammalian Notch receptors can bind Notch ligands and transduce a Notch signal in the absence of Pofut1 and O-fucose
malfunction
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mice lacking Pofut1 show myeloid hyperplasia and impaired lymphopoiesis. Mx-Cre/Pofut1F/F mice splenomegaly show in the bone marrow a decrease in T and B lymphocytes and an expansion of mature granulocytes and myeloid progenitors, mutant mice phenotypes, detailed overview. Mx-Cre/Pofut1F/F marrow progenitors have defective T lymphopoiesis and enhanced myeloid development in vitro that is correlated with decreased Notch ligand binding.. Defective T-cell development and myeloid hyperplasia are rescued by reinstating Notch1 signaling. Heterozygosity of Pofut1 affects rescue of FX-/- mice myeloid hyperplasia by exogenous fucose
malfunction
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elimination of Pofut1 in mice causes embryonic lethality with Notch-like phenotypes, elimination of Pofut2 results in an early embryonic lethal phenotype in mice
malfunction
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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
malfunction
knockdown and overexpression of Pofut1 inhibits and accelerates the growth, migration and invasion of hepatocellular carcinoma cells, respectively
malfunction
cell proliferation of POFUT1 knockdown cells is significantly inhibited compared with that of control cells, phenotypes, overview
malfunction
phenotype of Pofut1-/- mouse embryos resembles embryos lacking downstream components of Notch signaling, like CBF1/RBP-Jkappa. Mutation on the O-fucosylation site in mouse Notch1 EGF12 results in a hypomorphic allele affecting the Notch-ligand interaction. Pofut1 knockdown decreases Pax7 and disrupts the expression of myogenic markers. Downregulation of gene Pofut1 significantly lowers the quantity of cleaved Notch intracellular domain and the expression levels of genes Rbpj and Hes1 but without modification of the cell surface expression pattern of Notch1, phenotype, overview
malfunction
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suppression of isoform Fut10 expression induces the differentiation of neural stem cells and embryonic stem cells. In addition, knockdown of Fut10 expression in the cortical ventricular zone of the embryonic brain impairs the radial migration of neural precursor cells
malfunction
genetic disruption of POFUT2 in Plasmodium falciparum results in ookinetes that are attenuated for colonizing the mosquito midgut, an essential step in malaria transmission. Some POFUT2-deficient parasites mature into salivary gland sporozoites although they are impaired for gliding motility, cell traversal, hepatocyte invasion, and production of exoerythrocytic forms in humanized chimeric liver mice
malfunction
heterozygous mutations in POFUT1 are linked to a rare skin condition, Dowling-Degos Disease. Amplification of POFUT1 is associated with several types of cancer
malfunction
CRISPR-mediated knockout of POFUT1 in U2OS cells suppresses both normal Notch1 signaling, and the ligand-independent signaling associated with leukemogenic mutations of Notch1. Normal and oncogenic signaling are rescued by wild-type POFUT1 but rescue is impaired by an active-site R240A mutation
malfunction
loss-of-function mutants display impaired sexual reproduction that is linked to a defective male gamete. oft1 Mutant pollen tubes are ineffective at penetrating the stigma-style interface leading to a drastic reduction in seed set and a nearly 2000-fold reduction in pollen transmission
physiological function
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Notch receptors require Pofut1 for the generation of optimally functional Notch receptors, but Pofut1 is not required for stable cell surface expression of Notch
physiological function
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Pofut1 is required for Notch signaling upstream of NICD1
physiological function
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roles in the folding of Notch in the endoplasmic reticulum, in Notch-ligand binding and in endocytic trafficking of Notch. The carboxy-terminal extremity of Ofut1 contains a Lys-Asp-Glu-Leu (KDEL)-like motif that is dispensable for its catalytic activity but is required for both endoplasmic reticulum retention and function. Ofut1 is required only for Fringe-dependent signaling events
physiological function
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is essential for Notch signalling. Ability of OFUT1 to promote Notch secretion does not depend on its enzyme activity, suggesting the chaperon-like role of OFUT1
physiological function
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Notch receptors require Pofut1 for the generation of optimally functional Notch receptors, but Pofut1 is not required for stable cell surface expression of Notch
physiological function
protein O-fucosyltransferase 2 catalyzes the protein O-fucosylation, a post-translational modification found on serine/threonine residues of thrombospondin type 1 repeats
physiological function
-
Notch is a transmembrane receptor that shares homology with proteins containing epidermal growth factor-like repeats and mediates the cell-cell interactions necessary for many cell fate decisions. O-fucosyltransferase 1 catalyzes the O-fucosylation of these epidermal growth factor-like repeats. This O-fucose elongates, resulting in an O-linked tetrasaccharide that regulates the signaling activities of Notch. Fucosylation occurs in the lumen of the endoplasmicreticulum and Golgi. GDP-fucose uptake into the ER and Golgi is essential for fucosylation, Efr, a multifunctional nucleotide sugar transporter, and Golgi GDP-fucose transporter Gfr are involved in the biosynthesis of heparan sulfate-glycosaminoglycan chains and the O-fucosylation of Notch. Gfr but not Efr is crucial for the fucosylation of N-glycans, overview
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
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
physiological function
the enzyme catalyzes the addition of O-linked fucose to the epidermal growth factor-like repeats of Notch. Pofut1 overexpression accelerates cell proliferation and migration in hepatocellular carcinoma cells and it promotes the binding of Notch ligand Dll1 to Notch receptor, and hence activates Notch signaling pathway in hepatocellular carcinoma cells
physiological function
the enzyme adds O-fucose through O-glycosidic linkage to conserved serine or threonine residues in the epidermal growth factor-like repeats of a number of cellular surface and secreted proteins. ENzyme POFUT1 expression can contribute to cancer progression
physiological function
critical role of Pofut1 on Notch pathway activation during myogenic differentiation, overview. Both active Pofut1 and O-fucosylation of Notch are required for the canonical Notch signaling by Delta1 or Jagged1
physiological function
protein O-fucosyltransferase 2 is an essential enzyme that fucosylates serine and threonine residues of folded thrombospondin type 1 repeats
physiological function
-
overexpression of isoform Fut10 enhances the self-renewal of neural stem cells
physiological function
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
physiological function
the enzyme is responsible for O-glycosylating of the sporozoite surface proteins CSP and TRAP. The enzyme (POFUT2) ensures the trafficking of Plasmodium thrombospondin repeat proteins as part of a non-canonical glycosylation-dependent endoplasmic reticulum protein quality control mechanism
physiological function
the enzyme (Pofut1), which transfers O-fucose to the EGF domains of the Notch1 receptor, is indispensable for Notch signaling activation
physiological function
protein O-fucosylation is an important glycosylation modification and plays an important role in embryonic development. Protein O-fucosyltransferase 1 promotes trophoblast cell proliferation through activation of MAPK and PI3K/Akt signaling pathways
physiological function
both POFUT1 and POFUT2 are proposed to participate in non-canonical endoplasmic reticulum quality control pathways for the folding of Epidermal Growth Factor-like (EGF) repeats and Thrombospondin Type 1 Repeats (TSRs), respectively
physiological function
the enzyme O-glycosylates micronemal protein 2 (MIC2). This glycan is dispensable in Toxoplasma gondii tachyzoites and for Toxoplasma gondii infectivity
physiological function
the enzyme activates nuclear growth repressor DELLA. SPY-dependent protein O-fucosylation plays a key role in regulating plant development
physiological function
AtOFT1 plays a critical role in pollen tube penetration through the stigma/style in Arabidopsis
physiological function
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
physiological function
both POFUT1 and POFUT2 participate in non-canonical endoplasmic reticulum quality control pathways for the folding of Epidermal Growth Factor-like (EGF) repeats and Thrombospondin Type 1 Repeats (TSRs), respectively
physiological function
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
physiological function
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
physiological function
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
physiological function
the enzyme requires folded domain structures for adding O-fucose to elastin microfibril interface (EMI) domains and participates in a non-canonical endoplasmic reticulum quality control pathway for elastin microfibril interface domain-containing protein secretion. FUT10 and FUT11 are independently capable of adding O-fucose to EMI domains in cells and are the sole enzymes responsible for this modification
physiological function
the enzyme functions in the endoplasmic reticulum, requires folded domain structures for modification and participate in a non-canonical endoplasmic reticulum quality control pathway for EMI domain-containing protein secretion
physiological function
a loss-of-function mutant has larger root apical meristems and ectopic root hairs. Gibberellin or ethylene do not influence the epidermal patterns
physiological function
SPINDLY is the nucleocytoplasmic O-fucosyltransferase and is able to fucosylate itself. Growth of tachyzoites lacking SPINDLY in fibroblasts is modestly affected, tachyzoites show marked reductions in the levels of ectopically expressed proteins normally modified with O-fucose. Infection kinetics in mice are similar to wild-type, but mutant tachozytes display increased persistence in the chronic brain phase
physiological function
disruption of Spindly abloishes the occurence of alpha-L-fucosylated nucleocytoplasmic proteins
physiological function
-
the enzyme O-glycosylates micronemal protein 2 (MIC2). This glycan is dispensable in Toxoplasma gondii tachyzoites and for Toxoplasma gondii infectivity
-
physiological function
-
SPINDLY is the nucleocytoplasmic O-fucosyltransferase and is able to fucosylate itself. Growth of tachyzoites lacking SPINDLY in fibroblasts is modestly affected, tachyzoites show marked reductions in the levels of ectopically expressed proteins normally modified with O-fucose. Infection kinetics in mice are similar to wild-type, but mutant tachozytes display increased persistence in the chronic brain phase
-
additional information
GDP-fucose is bound in a conserved cavity formed mainly by amino acids from the C-terminal domain, it is localised in the interface where the two domains face each other, localisation of EGF repeat binding site in CePOFUT1, active site and ligand binding structure analysis, detailed overview
additional information
recognition of a small conserved 3D structural motif and mechanism of enzyme-protein substrate specificity. POFUT2 features a unique loop, residues 265-285, located on the opposite side of the large cleft, which protrudes from the C-terminal domain and which is attached to the N-terminal domain via a completely conserved tryptophan residue, W273 is involved in controlling movements of the N- and C-terminal domain relative to each other during the catalytic cycle, and 90% activity is lost in mutant W273A. Structure-function analysis of POFUT2 and comparison to POFUT1
additional information
-
recognition of a small conserved 3D structural motif and mechanism of enzyme-protein substrate specificity. POFUT2 features a unique loop, residues 265-285, located on the opposite side of the large cleft, which protrudes from the C-terminal domain and which is attached to the N-terminal domain via a completely conserved tryptophan residue, W273 is involved in controlling movements of the N- and C-terminal domain relative to each other during the catalytic cycle, and 90% activity is lost in mutant W273A. Structure-function analysis of POFUT2 and comparison to POFUT1
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
additional information
enzyme in complex with GDP and human thrombospondin type 1 repeat shows an inverting mechanism for fucose transfer assisted by a catalytic base and shows that nearly half of the thrombospondin type 1 repeat is embraced by CePOFUT2. A small number of direct interactions and a large network of water molecules maintain the complex, role of interstitial water in the complex interface, water-mediated interactions, overview
additional information
-
enzyme in complex with GDP and human thrombospondin type 1 repeat shows an inverting mechanism for fucose transfer assisted by a catalytic base and shows that nearly half of the thrombospondin type 1 repeat is embraced by CePOFUT2. A small number of direct interactions and a large network of water molecules maintain the complex, role of interstitial water in the complex interface, water-mediated interactions, overview
Show AA Sequence and Transmembrane Helices (3699 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the N- and the C-terminal domains adopt Rossmann-like folds, which are formed by a central beta-sheet surrounded by alpha-helices on both sides and these constitute the typical signature of a GT-B fold. The donor sugar, GDP-fucose, is localised in the interface where the two domains face each other
additional information
enzyme shows a highly dynamic behaviour in solution and adopts mainly compact conformations and to a lesser extend a highly dynamic population that oscillates between compact and highly extended conformations
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
glycoprotein with more than one high mannose type oligosaccharide chain
additional information
-
contains a KDEL-like sequence at the C-terminus for retention in the endoplasmic reticulum
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cryo-electron microscopy structure of SPY and its complex with GDP-fucose, 3.6 to 3.9 A resolution. SPY forms an antiparallel dimer and its catalytic domain interconverts among multiple conformations. The N-terminal disordered peptide in SPY contains trans autofucosylation sites and inhibits the POFUT activity. Tetratricopeptide repeats TPRs 1-5 dynamically regulate SPY activity by interfering with protein substrate binding
structure of mutant C645S, to 2.85 A resolution. Two SPYmolecules interact with each other in a head-to-tail manner, forming a symmetrical dimer
crystal structures of the enzyme in the unliganded form and in complex with GDP and GDP-fucose
crystal structures of the ternary complex between the enzyme and the human TSR1 repeat
crystals of the complex between PoFUT2 mutant A418C and Rattus norvegicus TSR4 mutant E10C, at 2.13 A
purified recombinant enzyme CePOFUT2 in complex with GDP and human TSR1, X-ray diffraction structure determination and analysis
purified recombinant truncated enzyme in apoform or complex with GDP-fucose, or GDP, or GDP and Mn2+, sitting drop method, 0.001 ml of 30 mg/ml protein is mixed with 0.001 ml of precipitant solution containing 100 mM HEPES, 100 mM MgCl2, 20% PEG 3350, pH 7.5, with or without 5 mM GDP, or 100 mM HEPES, 2% PEG 400, 1.8 M ammonium sulfate, pH 6.5, or 100 mM BIS-TRIS, 2 M ammonium sulfate, pH 6.0, 18°C, two crystals forms, X-ray diffraction structure determination and analysis at 1.54-2.60 A resolution
crystals of the complex between PoFUT2 mutant A418C and Rattus norvegicus TSR4 mutant E10C, at 2.13 A
the crystal structure is reported in the free form and in the presence of GDP-fucose
vapor diffusion using the hanging drop method. Structures of the enzyme (POFUT1) in free and GDP-fucose bound states
crystal structures of Mus musculus PoFUT1 in complex with different EGF repeats
X-ray crystal structure the enzyme (POFUT1) in complex with several EGF-like domains, including EGF12 and EGF26 of Notch
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C645S
mutation intruduced to allow crystallisation of protein, mutation has little impact on activity
D266A
mutation does not affect the self-fucosylation but increases the fucosylation of DELLA1
H728A
mutation slightly impairs the self-fucosylation of SPY and hardly affects the enzyme activity towards DELLA
K231A
mutation does not affect the self-fucosylation but decreases the fucosylation of DELLA1
K231A/D266A
mutation does not affect the self-fucosylation but decreases the fucosylation of DELLA1
N300A/N334A/N367A/N368A/N402A
mutation of tetratricopeptide repeat (TPR) domain, complete loss of autofucosylation and fucosylation of substrate DELLA
N300A/N334A/N367A/N368A/N402A/R408A/N436A
mutation of TPR domain, complete loss of autofucosylation and fucosylation of substrate DELLA
N661A
mutation slightly impairs the self-fucosylation of SPY and hardly affects the enzyme activity towards DELLA
S21A
mutation of autofucosylation site, does not affect SPY's fucosylation activity
S24A
mutation of autofucosylation site, does not affect SPY's fucosylation activity
A418C
mutation introduced to form a disulfide bridge with Rattus norvegicus TSR4 mutant E10C
D242A
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, the mutant shows about 10% increased activity compared to the wild-type enzyme
D244A
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, the mutant shows reduced activity compared to the wild-type enzyme
D309N
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, the mutant shows reduced activity compared to the wild-type enzyme
F199A
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, the mutant shows reduced activity compared to the wild-type enzyme
F261A
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, the mutant shows reduced activity compared to the wild-type enzyme
F357A
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, the mutant shows reduced activity compared to the wild-type enzyme
G19Q
site-directed mutagenesis, the mutation affects both secretion and fucosylation
G19R
site-directed mutagenesis, the mutation affects both secretion and fucosylation
G20H
site-directed mutagenesis, the mutation affects both secretion and fucosylation
N43A
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, the mutant shows highly reduced activity compared to the wild-type enzyme
R240A
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, inactive mutant
R240K
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, inactive mutant
R298K/R299K
site-directed mutagenesis, the mutant enzyme is stable against proteolysis and similarly active as the wild-type. The mutant enzymes is capable of fucosylating TSRs not only of group 1 but also of group 2, it not only recognizes and reacts with TSRs showing slightly different structures but also accepts TSRs with very low sequence identity. Residue Glu52 of mutant CePOFUT is the catalytic base
R40A
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, the mutant shows reduced activity compared to the wild-type enzyme
S15D
site-directed mutagenesis, the mutant shows increased secretion, but a significant reduction in fucosylation, suggesting that HsPOFUT2 is highly selective for amino acids in the Xa position
S15Q
site-directed mutagenesis, the mutant shows increased secretion, but a significant reduction in fucosylation, suggesting that HsPOFUT2 is highly selective for amino acids in the Xa position
V16H
site-directed mutagenesis, the mutation affects both secretion and fucosylation
W245A
site-directed mutagenessis, altered mutant temperature dependence and GDP-fucose/GDP dissociation constants compared to the wild-type, the mutant shows reduced activity compared to the wild-type enzyme
R254A
-
expression of a mutant, Ofut1R245A, lacking fucosyltransferase activity, rescues the requirement for Ofut1 in embryonic neurogenesis. Lack of requirement for O-fucosylation is further supported by the absence of embryonic phenotypes in Gmd mutants, which lack all forms of fucosylation. Requirements for O-fucose during imaginal development are evaluated by characterizing clones of cells expressing only Ofut1R245A. These clones phenocopy fringe mutant clones, indicating that the absence of O-fucose is functionally equivalent to the absence of elongated O-fucose
R275A
-
is catalytically dead. Ofut1 and mutant both bind the Notch extracellular domain, and expression of the mutant in cultured cells can increase both the amount and the ligand-binding activity of secreted Notch extracellular domain. Complete loss of ofut1 activity results in a strong phenotype mimicking a loss of Notch activity that is rescued to larval viability by the expression of mutant R275A, it rescues Notch receptor activity in these ofut1 mutant cells and leads to phenotypes mimicking a loss of fringe activity
A418C
mutation introduced to form a disulfide bridge with Rattus norvegicus TSR4 mutant E10C
D297A
site-directed mutagenesis, the mutant shows 15% activity compared to the wild-type enzyme
E396A
site-directed mutagenesis, the mutant shows 8% activity compared to the wild-type enzyme
W273a
site-directed mutagenesis, W273 is involved in controlling movements of the N- and C-terminal domain relative to each other during the catalytic cycle, and 90% activity is lost in mutant W273A
R245A
S1726A
-
mutant protein shows no activity, loss of O-fucosylation causes a gain of function for muscle agrin such that it stimulates acetylcholine receptors, clustering and MuSK phosphorylation in cultured myotubes at levels normally only found with the neural splice form
E692K
reduced expression compared to wild-type, less than 10% of wild-type activity
G695D
reduced expression compared to wild-type, less than 10% of wild-type activity
K793A
reduced expression compared to wild-type, less than 10% of wild-type activity
E692K
-
reduced expression compared to wild-type, less than 10% of wild-type activity
-
G695D
-
reduced expression compared to wild-type, less than 10% of wild-type activity
-
K793A
-
reduced expression compared to wild-type, less than 10% of wild-type activity
-
additional information
R245A
-
is fucosylation-defective, has a dominant negative effect on wild-type Pofut1, since Pofut1 activity in Pofut1-/- cells expressing Pofut1 R245A is markedly reduced in the in vitro assay
R245A
mutation disrupts O-fucosyltransferase activity destabilizes the protein and abolishes Notch1 signaling during mouse somitogenesis
additional information
mutants R40A, N43A and R240A/K are more stable while F199A, D309N, D242A, D244A, W245A, F261A and F357A are less stable than the wild-type. Mutants R40A, R240A/K, W245A and F357A show a decrease in binding to GDP, from this group, R40A and W245A bind better to GDP than F357A, R240K and R240A, with the latter being impaired in binding
additional information
-
down-regulation of enzyme by RNA interference in Notch-secreting cells inhibits both Delta-Notch and Serrate-Notch binding. Overexpression of enzyme in cultured cells increases Serrate-Notch binding but inhibits Delta-Notch binding
additional information
enzyme disruption mutant, enzyme is essential for Notch signaling, Fringe function, for physical interaction of Notch with its ligand Delta, and lateral inhibition during neuroblast segregation
additional information
-
analysis of O-fut 1 homozygous mutant cells shows that O-fut1 is required for the endocytic transportation of Notch to the early endosome which is shown to be independent of the O-fucosyltransferase activity of O-fut1
additional information
-
O-fut 1 overexpression and analysis of O-fut 1 homozygous mutant cells indicates that O-fut 1 promotes the turnover of Notch, which consequently downregulates Notch signaling
additional information
-
O-fut1 protein added to conditioned medium and endocytosed is sufficient to rescue normal Notch transportation to the early endosome in O-fut1 knockdown cells
additional information
-
using O-fut I knock out mutants it is shown that the localization of Notch in the region from the subapical complex (SAC) to the apical portion of the adherens junctions (AJs) depends on its O-fucosylation
additional information
-
an artificial O-glycosylation pathway to produce an O-fucosylated epidermal growth factor (EGF) domain in Saccharomyces cerevisiae is generated. The in vivo O-fucosylation system is constructed via expression of genes that encode protein O-fut1 and the EGF domain, along with genes whose protein products convert cytoplasmic GDP-mannose to GDP-fucose
additional information
-
enzyme deletion mutant, mouse embryose lacking enzyme die at midgestation with severe defects in somitogenesis, vasculinogenesis, cardiogenesis, and neurogenesis
additional information
-
deletion of Pofut1 in cultured primary myotubes and in adult skeletal muscle increases acetylcholine receptor aggregation
additional information
generation of murine myoblastic Pofut1 knockdown C2C12 cell line, and analysis of the C2C12 cell line downregulated for Pofut1 expression by short hairpin RNA (shRNA) inhibition during the time course of differentiation. Knockdown of Pofut1 affects the signaling pathway activation by a reduction of the amount of cleaved Notch intracellular domain and a decrease in downstream Notch target gene expression. Depletion in Pax7/MyoD- cells and earlier myogenic program entrance are observed, leading to an increase in myotube quantity with a small number of nuclei, reflecting fusion defects. The rescue of Pofut1 expression in knockdown cells, by generation of Pofut1 knockdown C2C12 cell lines reexpressing shRNA-resistant Pofut1, restores Notch signaling activation and a normal course in C2C12 differentiation. Downregulation of gene Pofut1 significantly lowers the quantity of cleaved Notch intracellular domain and the expression levels of genes Rbpj and Hes1 but without modification of the cell surface expression pattern of Notch1, phenotype, overview
additional information
-
generation of murine myoblastic Pofut1 knockdown C2C12 cell line, and analysis of the C2C12 cell line downregulated for Pofut1 expression by short hairpin RNA (shRNA) inhibition during the time course of differentiation. Knockdown of Pofut1 affects the signaling pathway activation by a reduction of the amount of cleaved Notch intracellular domain and a decrease in downstream Notch target gene expression. Depletion in Pax7/MyoD- cells and earlier myogenic program entrance are observed, leading to an increase in myotube quantity with a small number of nuclei, reflecting fusion defects. The rescue of Pofut1 expression in knockdown cells, by generation of Pofut1 knockdown C2C12 cell lines reexpressing shRNA-resistant Pofut1, restores Notch signaling activation and a normal course in C2C12 differentiation. Downregulation of gene Pofut1 significantly lowers the quantity of cleaved Notch intracellular domain and the expression levels of genes Rbpj and Hes1 but without modification of the cell surface expression pattern of Notch1, phenotype, overview
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50 - 55
dependent on ligands present, Mn2+ shifts the optimum to 50°C, GDP to 55°C, overview
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme CePOFUT2 in complex with GDP and human TSR1 by gel filtration
recombinant truncated POFUT1_26-382 from Pichia pastoris by affinity and ion exchange chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of a truncated form of CePOFUT1, comprising amino acids 26-382, excluding the signal sequence and the retention endoplasmic reticulum localisation sequence, as a secreted protein in Pichia pastoris
gene FUT11, expression analysis in bronchial mucosa of cystic fibrosis patients
-
gene Pofut1, semiquantitative real-time RT-PCR enzyme expression analysis
gene profut2, recombinant expression in Pichia pastoris and secretion to the medium, partially degradation of the protein
transient expression of cDNA splice variants FUT10-391, FUT10-419, and FUT10-479, and GFP-tagged-FUT10 cDNA constructs from vector PCR3.1 in COS-7 Cells
transient expression of cDNA splice variants FUT11-476 and FUT11-492 from vector PCR3.1 in COS-7 Cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression in tumorsphere is significantly higher than in parental adherent cells. Upregulated in esophageal cancer stem-like cell in comparison to adherent cells
POFUT1 mRNA expression is upregulated in oral squamous cell carcinoma cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
drug development
POFUT1 is a potential target for cancers driven by Notch1 mutations
medicine
an aberrant activated Pofut1-Notch pathway is involved in hepatocellular carcinoma progression, and blockage of this pathway can be a promising strategy for the therapy of hepatocellular carcinomas
molecular biology
diagnostics
Pofut1 overexpression clinically correlates with the unfavorable survival and high disease recurrence in hepatocellular carcinoma
diagnostics
enzyme POFUT1 may serve as a diagnostic marker and a therapeutic target for oral squamous cell carcinoma cells
molecular biology
-
O-fucosylation is dispensable for many Notch signaling events during Drosophila development
molecular biology
-
engineering of an O-fucosylation system in yeast provides a powerful tool for producing proteins with homogenous carbohydrate chains. Such proteins can be used for the analysis of substrate specificity and the production of antibodies that recognize O-glycosylated EGF domains
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hofsteenge, J.; Huwiler, K.G.; Bacik B.; Hess, D.; Lawler, J.; Mosher, D.F.; Peter-Katalinic, J.
C-mannosylation and o-fuxosylation of the thrombospondin type 1 module
J. Biol. Chem.
276
6485-6498
2001
Homo sapiens
brenda
Wang, Y.; Lee, G.F.; Kelley, R.F.; Spellman, M.W.
Identification of a GDP-L-fucose:polypeptide fucosyltransferase and enzymic addition of O-linked fucose to EGF domains
Glycobiology
6
837-842
1996
Cricetulus griseus, Rattus norvegicus
brenda
ang, Y.; Shao, L.; Shi, S.; Harris, R.J.; Spellman, M.W.; Stanley, P.; Haltiwanger, R.S.
Modification of epidermal growth factor-like repeats with O-fucose. Molecular cloning and expression of a novel GDP-fucose protein O-fucosyltransferase
J. Biol. Chem.
276
40338-40345
2001
Candida elegans, Drosophila melanogaster, Homo sapiens (Q9H488), Homo sapiens, Mus musculus (Q91ZW2), Mus musculus
brenda
Wang, Y.; Spellman, M.W.
Purification and characterization of a GDP-fucose:polypeptide fucosyltransferase from Chinese hamster ovary cells
J. Biol. Chem.
273
8112-8118
1998
Cricetulus griseus
brenda
Okajima, T.; Xu, A.; Irvine, K.D.
Modulation of notch-ligand binding by protein O-fucosyltransferase 1 and fringe
J. Biol. Chem.
278
42340-42345
2003
Drosophila melanogaster
brenda
Luo, Y.; Haltiwanger, R.S.
O-fucosylation of notch occurs in the endoplasmic reticulum
J. Biol. Chem.
280
11289-11294
2005
Homo sapiens
brenda
Shi, S.; Stanley, P.
Protein O-fucosyltransferase 1 is an essential component of Notch signaling pathways
Proc. Natl. Acad. Sci. USA
100
5234-5239
2003
Mus musculus
brenda
Okajima, T.; Xu, A.; Lei, L.; Irvine, K.D.
Chaperone activity of protein O-fucosyltransferase 1 promotes notch receptor folding
Science
307
1599-1603
2005
Drosophila melanogaster
brenda
Sasamura, T.; Sasaki, N.; Miyashita, F.; Nakao, S.; Ishikawa, H.O.; Ito, M.; Kitagawa, M.; Harigaya, K.; Spana, E.; Bilder, D.; Perrimon, N.; Matsuno, K.
neurotic, a novel maternal neurogenic gene, encodes an O-fucosyltransferase that is essential for Notch-Delta interactions
Development
130
4785-4795
2003
Drosophila melanogaster (Q9V6X7)
brenda
Speer, N.J.; Tang, S.J.; Miller, T.; Chiang, T.C.
Coherent electronic fringe structure in incommensurate silver-silicon quantum wells
Science
314
804-806
2006
Drosophila sp. (in: flies)
brenda
Groux-Degroote, S.; Krzewinski-Recchi, M.A.; Cazet, A.; Vincent, A.; Lehoux, S.; Lafitte, J.J.; Van Seuningen, I.; Delannoy, P.
IL-6 and IL-8 increase the expression of glycosyltransferases and sulfotransferases involved in the biosynthesis of sialylated and/or sulfated Lewisx epitopes in the human bronchial mucosa
Biochem. J.
410
213-223
2008
Homo sapiens
brenda
Okajima, T.; Reddy, B.; Matsuda, T.; Irvine, K.D.
Contributions of chaperone and glycosyltransferase activities of O-fucosyltransferase 1 to Notch signaling
BMC Biol.
6
1-10
2008
Drosophila melanogaster
brenda
Sasamura, T.; Ishikawa, H.O.; Sasaki, N.; Higashi, S.; Kanai, M.; Nakao, S.; Ayukawa, T.; Aigaki, T.; Noda, K.; Miyoshi, E.; Taniguchi, N.; Matsuno, K.
The O-fucosyltransferase O-fut1 is an extracellular component that is essential for the constitutive endocytic trafficking of Notch in Drosophila
Development
134
1347-1356
2007
Drosophila melanogaster
brenda
Sasaki, N.; Sasamura, T.; Ishikawa, H.O.; Kanai, M.; Ueda, R.; Saigo, K.; Matsuno, K.
Polarized exocytosis and transcytosis of Notch during its apical localization in Drosophila epithelial cells
Genes Cells
12
89-103
2007
Drosophila melanogaster
brenda
Chigira, Y.; Oka, T.; Okajima, T.; Jigami, Y.
Engineering of a mammalian O-glycosylation pathway in the yeast Saccharomyces cerevisiae: production of O-fucosylated epidermal growth factor domains
Glycobiology
18
303-314
2008
Homo sapiens
brenda
Kim, M.L.; Chandrasekharan, K.; Glass, M.; Shi, S.; Stahl, M.C.; Kaspar, B.; Stanley, P.; Martin, P.T.
O-fucosylation of muscle agrin determines its ability to cluster acetylcholine receptors
Mol. Cell. Neurosci.
39
452-464
2008
Mus musculus
brenda
Okamura, Y.; Saga, Y.
Notch signaling is required for the maintenance of enteric neural crest progenitors
Development
135
3555-3565
2008
Mus musculus
brenda
Guilmeau, S.; Flandez, M.; Bancroft, L.; Sellers, R.; Tear, B.; Stanley, P.; Augenlicht, L.
Intestinal deletion of Pofut1 in the mouse inactivates notch signaling and causes enterocolitis
Gastroenterology
135
849-860
2008
Mus musculus
brenda
Stanley, P.; Guidos, C.J.
Regulation of Notch signaling during T- and B-cell development by O-fucose glycans
Immunol. Rev.
230
201-215
2009
Mus musculus, Cricetulus griseus, Drosophila sp. (in: flies)
brenda
Carvalho, A.; Harduin-Lepers, A.; Magalhaes, A.; Machado, E.; Mendes, N.; Costa, L.; Matthiesen, R.; Almeida, R.; Costa, J.; Reis, C.
Differential expression of alpha-2,3-sialyltransferases and alpha-1,3/4-fucosyltransferases regulates the levels of sialyl Lewis a and sialyl Lewis x in gastrointestinal carcinoma cells
Int. J. Biochem. Cell Biol.
42
80-89
2010
Homo sapiens (Q495W5), Homo sapiens (Q6P4F1)
brenda
Okajima, T.; Matsuura, A.; Matsuda, T.
Biological functions of glycosyltransferase genes involved in O-fucose glycan synthesis
J. Biochem.
144
1-6
2008
Drosophila sp. (in: flies), Mus musculus
brenda
Stahl, M.; Uemura, K.; Ge, C.; Shi, S.; Tashima, Y.; Stanley, P.
Roles of Pofut1 and O-fucose in mammalian Notch signaling
J. Biol. Chem.
283
13638-13651
2008
Cricetulus griseus, Mus musculus
brenda
Mollicone, R.; Moore, S.E.; Bovin, N.; Garcia-Rosasco, M.; Candelier, J.J.; Martinez-Duncker, I.; Oriol, R.
Activity, splice variants, conserved peptide motifs, and phylogeny of two new alpha1,3-fucosyltransferase families (FUT10 and FUT11)
J. Biol. Chem.
284
4723-4738
2009
Homo sapiens (Q495W5), Homo sapiens (Q6P4F1)
brenda
Vodovar, N.; Schweisguth, F.
Functions of O-fucosyltransferase in Notch trafficking and signaling: Towards the end of a controversy?
J. Biol.
7
7-7
2008
Drosophila sp. (in: flies)
brenda
Okamura, Y.; Saga, Y.
Pofut1 is required for the proper localization of the Notch receptor during mouse development
Mech. Dev.
125
663-673
2008
Mus musculus
brenda
Yao, D.; Huang, Y.; Huang, X.; Wang, W.; Yan, Q.; Wei, L.; Xin, W.; Gerson, S.; Stanley, P.; Lowe, J.B.; Zhou, L.
Protein O-fucosyltransferase 1 (Pofut1) regulates lymphoid and myeloid homeostasis through modulation of Notch receptor ligand interactions
Blood
117
5652-5662
2011
Mus musculus
brenda
Rana, N.A.; Haltiwanger, R.S.
Fringe benefits: functional and structural impacts of O-glycosylation on the extracellular domain of Notch receptors
Curr. Opin. Struct. Biol.
21
583-589
2011
Drosophila melanogaster, Mus musculus
brenda
Chen, C.I.; Keusch, J.J.; Klein, D.; Hess, D.; Hofsteenge, J.; Gut, H.
Structure of human POFUT2: insights into thrombospondin type 1 repeat fold and O-fucosylation
EMBO J.
31
3183-3197
2012
Homo sapiens (Q9Y2G5), Homo sapiens
brenda
Al-Shareffi, E.; Chaubard, J.L.; Leonhard-Melief, C.; Wang, S.K.; Wong, C.H.; Haltiwanger, R.S.
6-Alkynyl fucose is a bioorthogonal analog for O-fucosylation of epidermal growth factor-like repeats and thrombospondin type-1 repeats by protein O-fucosyltransferases 1 and 2
Glycobiology
23
188-198
2013
Mus musculus
brenda
Ishikawa, H.; Ayukawa, T.; Nakayama, M.; Higashi, S.; Kamiyama, S.; Nishihara, S.; Aoki, K.; Ishida, N.; Sanai, Y.; Matsuno, K.
Two pathways for importing GDP-fucose into the endoplasmic reticulum lumen function redundantly in the O-fucosylation of notch in Drosophila
J. Biol. Chem.
285
4122-4129
2010
Drosophila melanogaster
brenda
Lira-Navarrete, E.; Valero-Gonzalez, J.; Villanueva, R.; Martinez-Julvez, M.; Tejero, T.; Merino, P.; Panjikar, S.; Hurtado-Guerrero, R.
Structural insights into the mechanism of protein O-fucosylation
PLoS ONE
6
e25365
2011
Caenorhabditis elegans (Q18014)
brenda
Ma, L.; Dong, P.; Liu, L.; Gao, Q.; Duan, M.; Zhang, S.; Chen, S.; Xue, R.; Wang, X.
Overexpression of protein O-fucosyltransferase 1 accelerates hepatocellular carcinoma progression via the Notch signaling pathway
Biochem. Biophys. Res. Commun.
473
503-510
2016
Homo sapiens (Q9H488), Homo sapiens
brenda
Yokota, S.; Ogawara, K.; Kimura, R.; Shimizu, F.; Baba, T.; Minakawa, Y.; Higo, M.; Kasamatsu, A.; Endo-Sakamoto, Y.; Shiiba, M.; Tanzawa, H.; Uzawa, K.
Protein O-fucosyltransferase 1: a potential diagnostic marker and therapeutic target for human oral cancer
Int. J. Oncol.
43
1864-1870
2013
Homo sapiens (Q9H488), Homo sapiens
brenda
Kumar, A.; Torii, T.; Ishino, Y.; Muraoka, D.; Yoshimura, T.; Togayachi, A.; Narimatsu, H.; Ikenaka, K.; Hitoshi, S.
The Lewis X-related alpha1,3-fucosyltransferase, Fut10, is required for the maintenance of stem cell populations
J. Biol. Chem.
288
28859-28868
2013
Mus musculus
brenda
Der Vartanian, A.; Audfray, A.; Al Jaam, B.; Janot, M.; Legardinier, S.; Maftah, A.; Germot, A.
Protein O-fucosyltransferase 1 expression impacts myogenic C2C12 cell commitment via the Notch signaling pathway
Mol. Cell. Biol.
35
391-405
2015
Mus musculus (Q91ZW2), Mus musculus
brenda
Valero-Gonzalez, J.; Leonhard-Melief, C.; Lira-Navarrete, E.; Jimenez-Oses, G.; Hernandez-Ruiz, C.; Pallares, M.C.; Yruela, I.; Vasudevan, D.; Lostao, A.; Corzana, F.; Takeuchi, H.; Haltiwanger, R.S.; Hurtado-Guerrero, R.
A proactive role of water molecules in acceptor recognition by protein O-fucosyltransferase 2
Nat. Chem. Biol.
12
240-246
2016
Caenorhabditis elegans (Q8WR51), Caenorhabditis elegans
brenda
Lira-Navarrete, E.; Hurtado-Guerrero, R.
A perspective on structural and mechanistic aspects of protein O-fucosylation
Acta Crystallogr. Sect. F
74
443-450
2018
Caenorhabditis elegans (Q18014), Caenorhabditis elegans (Q8WR51), Homo sapiens (Q9H488), Homo sapiens (Q9Y2G5), Mus musculus (Q91ZW2)
brenda
Liu, C.; Liang, X.; Wang, J.; Zheng, Q.; Zhao, Y.; Khan, M.N.; Liu, S.; Yan, Q.
Protein O-fucosyltransferase 1 promotes trophoblast cell proliferation through activation of MAPK and PI3K/Akt signaling athways
Biomed. Pharmacother.
88
95-101
2017
Homo sapiens (Q9H488), Homo sapiens
brenda
Holdener, B.C.; Haltiwanger, R.S.
Protein O-fucosylation structure and function
Curr. Opin. Struct. Biol.
56
78-86
2019
Homo sapiens (Q9H488), Homo sapiens (Q9Y2G5)
brenda
Sanz, S.; Aquilini, E.; Tweedell, R.E.; Verma, G.; Hamerly, T.; Hritzo, B.; Tripathi, A.; Machado, M.; Churcher, T.S.; Rodrigues, J.A.; Izquierdo, L.; Dinglasan, R.R.
Protein O-fucosyltransferase 2 is not essential for Plasmodium berghei development
Front. Cell. Infect. Microbiol.
9
238
2019
Homo sapiens (Q9H488), Homo sapiens
brenda
McMillan, B.J.; Zimmerman, B.; Egan, E.D.; Lofgren, M.; Xu, X.; Hesser, A.; Blacklow, S.C.
Structure of human POFUT1, its requirement in ligand-independent oncogenic Notch signaling, and functional effects of Dowling-Degos mutations
Glycobiology
27
777-786
2017
Homo sapiens (Q9H488), Homo sapiens
brenda
Sadeghzadeh, Z.; Khosravi, A.; Jazi, M.S.; Asadi, J.
Upregulation of fucosyltransferase 3, 8 and protein O-fucosyltransferase 1, 2 genes in esophageal cancer stem-like cells (CSLCs)
Glycoconj. J.
37
319-327
2020
Homo sapiens (Q9H488), Homo sapiens (Q9Y2G5)
brenda
Khurana, S.; Coffey, M.J.; John, A.; Uboldi, A.D.; Huynh, M.H.; Stewart, R.J.; Carruthers, V.B.; Tonkin, C.J.; Goddard-Borger, E.D.; Scott, N.E.
Protein O-fucosyltransferase 2-mediated O-glycosylation of the adhesin MIC2 is dispensable for Toxoplasma gondii tachyzoite infection
J. Biol. Chem.
294
1541-1553
2019
Toxoplasma gondii (S7WCF5), Toxoplasma gondii, Toxoplasma gondii ATCC 50853 (S7WCF5)
brenda
Zentella, R.; Sui, N.; Barnhill, B.; Hsieh, W.; Hu, J.; Shabanowitz, J.; Boyce, M.; Olszewski, N.; Zhou, P.; Hunt, D.; Sun, T.
The Arabidopsis O-fucosyltransferase SPINDLY activates nuclear growth repressor della
Nat. Chem. Biol.
13
479-485
2017
Arabidopsis thaliana (Q96301), Arabidopsis thaliana
brenda
Li, Z.; Han, K.; Pak, J.E.; Satkunarajah, M.; Zhou, D.; Rini, J.M.
Recognition of EGF-like domains by the Notch-modifying O-fucosyltransferase POFUT1
Nat. Chem. Biol.
13
757-763
2017
Mus musculus (Q91ZW2), Mus musculus
brenda
Lopaticki, S.; Yang, A.S.P.; John, A.; Scott, N.E.; Lingford, J.P.; ONeill, M.T.; Erickson, S.M.; McKenzie, N.C.; Jennison, C.; Whitehead, L.W.; Douglas, D.N.; Kneteman, N.M.; Goddard-Borger, E.D.; Boddey, J.A.
Protein O-fucosylation in Plasmodium falciparum ensures efficient infection of mosquito and vertebrate hosts
Nat. Commun.
8
561
2017
Plasmodium falciparum (Q8I360), Plasmodium falciparum
brenda
Smith, D.; Harper, J.; Wallace, I.
A potential role for protein O-fucosylation during pollen-pistil interactions
Plant Signal. Behav.
13
e1467687
2018
Arabidopsis thaliana (Q9MA87), Arabidopsis thaliana
brenda
Ajima, R.; Suzuki, E.; Saga, Y.
Pofut1 point-mutations that disrupt O-fucosyltransferase activity destabilize the protein and abolish Notch1 signaling during mouse somitogenesis
PLoS ONE
12
e0187248
2017
Mus musculus (Q91ZW2), Mus musculus
brenda
Hao, H.; Yuan, Y.; Ito, A.; Eberand, B.M.; Tjondro, H.; Cielesh, M.; Norris, N.; Moreno, C.L.; Maxwell, J.W.C.; Neely, G.G.; Payne, R.J.; Kebede, M.A.; Bieber Urbauer, R.J.; Passam, F.H.; Larance, M.; Haltiwanger, R.S.
FUT10 and FUT11 are protein O-fucosyltransferases that modify protein EMI domains
Nat. Chem. Biol.
FEHLT
0000
2025
Homo sapiens (Q495W5), Homo sapiens (Q6P4F1)
brenda
Sanz-Martinez, I.; Garcia-Garcia, A.; Tejero, T.; Hurtado-Guerrero, R.; Merino, P.
The essential role of water molecules in the reaction mechanism of protein O-fucosyltransferase 2
Angew. Chem. Int. Ed. Engl.
61
e202213610
2022
Caenorhabditis elegans (Q8WR51), Homo sapiens (Q9Y2G5)
brenda
Mutanwad, K.V.; Zangl, I.; Lucyshyn, D.
The Arabidopsis O-fucosyltransferase SPINDLY regulates root hair patterning independently of gibberellin signaling
Development
147
dev192039
2020
Arabidopsis thaliana (Q96301)
brenda
van der Wel, H.; Garcia, A.M.; Gas-Pascual, E.; Willis, M.M.; Kim, H.W.; Bandini, G.; Gaye, M.M.; Costello, C.E.; Samuelson, J.; West, C.M.
Spindly is a nucleocytosolic O-fucosyltransferase in Dictyostelium and related proteins are widespread in protists and bacteria
Glycobiology
33
225-244
2023
Dictyostelium discoideum (Q54NH1)
brenda
Bandini, G.; Agop-Nersesian, C.; van der Wel, H.; Mandalasi, M.; Kim, H.W.; West, C.M.; Samuelson, J.
The nucleocytosolic O-fucosyltransferase SPINDLY affects protein expression and virulence in Toxoplasma gondii
J. Biol. Chem.
296
100039
2021
Toxoplasma gondii (S7WCF1), Toxoplasma gondii GT1 (S7WCF1)
brenda
Lira-Navarrete, E.; Pallares, M.C.; Castello, F.; Ruedas-Rama, M.J.; Orte, A.; Lostao, A.; Hurtado-Guerrero, R.
Protein O-fucosyltransferase 1 undergoes interdomain flexibility in solution
Molecules
26
2105
2021
Caenorhabditis elegans (Q18014)
brenda
Hao, H.; Yuan, Y.; Ito, A.; Eberand, B.M.; Tjondro, H.; Cielesh, M.; Norris, N.; Moreno, C.L.; Maxwell, J.W.C.; Neely, G.G.; Payne, R.J.; Kebede, M.A.; Urbauer, R.J.B.; Passam, F.H.; Larance, M.; Haltiwanger, R.S.
FUT10 and FUT11 are protein O-fucosyltransferases that modify protein EMI domains
Nat. Chem. Biol.
21
598-610
2025
Mus musculus (Q5F2L2), Mus musculus (Q8BHC9)
brenda
Zhu, L.; Wei, X.; Cong, J.; Zou, J.; Wan, L.; Xu, S.
Structural insights into mechanism and specificity of the plant protein O-fucosyltransferase SPINDLY
Nat. Commun.
13
7424
2022
Arabidopsis thaliana (Q96301)
brenda
Kumar, S.; Wang, Y.; Zhou, Y.; Dillard, L.; Li, F.; Sciandra, C.; Sui, N.; Zentella, R.; Zahn, E.; Shabanowitz, J.; Hunt, D.; Borgnia, M.; Bartesaghi, A.; Sun, T.; Zhou, P.
Structure and dynamics of the Arabidopsis O-fucosyltransferase SPINDLY
Nat. Commun.
14
1538
2023
Arabidopsis thaliana (Q96301)
brenda
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