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Information on EC 2.4.1.214 - glycoprotein 3-alpha-L-fucosyltransferase and Organism(s) Homo sapiens and UniProt Accession Q11130
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2.4.1.214 glycoprotein 3-alpha-L-fucosyltransferaseIUBMB Comments
Requires Mn2+. The enzyme transfers to N-linked oligosaccharide structures (N-glycans), generally with a specificity for N-glycans with one unsubstituted non-reducing terminal GlcNAc residue. This enzyme catalyses a reaction similar to that of EC 2.4.1.68, glycoprotein 6-alpha-L-fucosyltransferase, but transferring the L-fucosyl group from GDP-beta-L-fucose to form an alpha1,3-linkage rather than an alpha1,6-linkage. The {iupac/misc/glycp#3.5::N-glycan} products of this enzyme are present in plants, insects and some other invertebrates (e.g., Schistosoma, Haemonchus, Lymnaea).
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Word Map
- 2.4.1.214
-
lewis
-
sialylated
-
fucosylated
- selectins
-
p-selectin
-
fucts
-
alpha1,3-fucosylated
- psgl-1
-
fuc-tiv
- ligand-1
-
alpha1,3fucosyltransferases
- n-acetyllactosamine
-
polylactosamine
-
sialyl-lewis
-
alpha2,3-sialylated
-
anti-horseradish
- beta1,2-xylosyltransferase
-
selectin-dependent
-
skin-homing
- lacto-n-neotetraose
- st3gal
-
alpha2,3-sialyltransferase
-
counterreceptors
- lacto-n-tetraose
-
sialyl-lex
-
lewis-type
-
meca-79
-
alpha1,3-fucose
- fuct-iii
- alpha1,3/4-fucosyltransferases
- synthesis
- drug development
- pharmacology
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
+
=
+
+
=
+
Synonyms
fuct-vii, fuc-tvii, alpha1,3-fucosyltransferase, fuct-iv, fucosyltransferase vii, fut11, alpha(1,3)fucosyltransferase, fucta, alpha3-fucosyltransferase, fuct vii, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AtFUT11
-
-
-
-
core alpha-(1,3)-fucosyltransferase
-
-
-
-
Fuc-T C3
-
-
-
-
FucT1
-
-
-
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FucTA
-
-
-
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GDP-fucose:beta-N-acetylglucosamine (Fuc to (Fuca1-6GlcNAc)-Asn-peptide) alpha1-3-fucosyltransferase
-
-
-
-
GDP-L-fuc:Asn-linked GlcNAc alpha1,3-fucosyltransferase
-
-
-
-
GDP-L-fuc:N-acetyl-beta-D-glucosaminide alpha1,3-fucosyltransferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GDP-beta-L-fucose + N4-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc]-L-asparaginyl-[protein] = GDP + N4-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc]-L-asparaginyl-[protein]
the enzyme contains the conserved alpha 1,3 FucT motif, which is crucial for activity and nucleotide sugar binding
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
GDP-beta-L-fucose:glycoprotein (L-fucose to asparagine-linked N-acetylglucosamine of N4-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl}asparagine) 3-alpha-L-fucosyl-transferase
Requires Mn2+. The enzyme transfers to N-linked oligosaccharide structures (N-glycans), generally with a specificity for N-glycans with one unsubstituted non-reducing terminal GlcNAc residue. This enzyme catalyses a reaction similar to that of EC 2.4.1.68, glycoprotein 6-alpha-L-fucosyltransferase, but transferring the L-fucosyl group from GDP-beta-L-fucose to form an alpha1,3-linkage rather than an alpha1,6-linkage. The {iupac/misc/glycp#3.5::N-glycan} products of this enzyme are present in plants, insects and some other invertebrates (e.g., Schistosoma, Haemonchus, Lymnaea).
CAS REGISTRY NUMBER
COMMENTARY
68247-53-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GDP-alpha-L-fucose + Galbeta1-4GlcNAc-R
GDP + Galbeta1-4[Fucalpha1-3]GlcNAc-R
-
-
-
-
ir
GDP-alpha-L-fucose + NeuAcalpha2-3Galbeta1-3GlcNAcbeta-R
GDP + NeuAcalpha2-3Galbeta1-3[Fucalpha1-3]GlcNAcbeta-R
-
4% of the activity with NeuAcalpha2-3Galbeta1-4GlcNAc-R
-
-
?
GDP-alpha-L-fucose + NeuAcalpha2-3Galbeta1-4GlcNAc
GDP + NeuAcalpha2-3Galbeta1-4[Fucalpha1-3]GlcNAc
-
28% of the activity with NeuAcalpha2-3Galbeta1-4GlcNAc-R
-
-
?
GDP-alpha-L-fucose + NeuAcalpha2-3Galbeta1-4GlcNAcbeta-R
GDP + NeuAcalpha2-3Galbeta1-4[Fucalpha1-3]GlcNAcbeta-R
-
best substrate
-
-
?
GDP-L-fucose + N4-[N-acetyl-beta-D-glucosaminyl-(1-2)-alpha-D-mannosyl-(1-3)-[N-acetyl-beta-D-glucosaminyl-(1-2)-alpha-D-mannosyl-(1-6)]-beta-D-mannosyl-(1-4)-N-acetyl-beta-D-glucosaminyl-(1-4)-N-acetyl-beta-D-glucosaminyl]asparagine
GDP + N4-[N-acetyl-beta-D-glucosaminyl-(1-2)-alpha-D-mannosyl-(1-3)-[N-acetyl-beta-D-glucosaminyl-(1-2)-alpha-D-mannosyl-(1-6)]-beta-D-mannosyl-(1-4)-N-acetyl-beta-D-glucosaminyl-(1-4)-[alpha-L-fucosyl-(1-3)]-N-acetyl-beta-D-glucosaminyl]asparagine
-
-
-
?
additional information
?
-
-
alpha1,3-fucosylation by FucT-VII is a step in the biosynthesis of Lewis X antigen, FucT-VII stimulates the growth of hepatocarcinoma cells via the cyclin-dependent kinase inhibitor p27Kip1, phosphorylation of the Rb protein is involved, signaling pathway overview
-
-
?
additional information
?
-
-
FucT-IV and FucT-VII are responsible for generation of sialylated Lewis X, i.e. sLex, FucT-VII being the major enzyme form in selectin ligand activity regulating leukocyte recruitment and lymphocyte homing into lymph nodes, FucT-IV and FucT-VII are both involved in conferring L-, P- and E-selectin binding activities to P-selectin glycoprotein ligand-1, i.e. PSGL-1, in humans, overview, FucT-IV and FucT-VII show cooperation in recruitment of selectin-expressing cells on PSGL-1 and in regulating cell rolling velocity and stability
-
-
?
additional information
?
-
-
FucT-VII is essential for biosynthesis of selectin binding ligands in T-cells, H-Ras and phosphoinositide 3-kinase cooperate to induce alpha(1,3)-fucosyltransferase VII expression in Jurkat T cells via the Raf-MEK-ERK pathway, but induction of FucT-VII requires the concomitant activation of at least 3 different signaling pathways, overview
-
-
?
additional information
?
-
-
sialyl Lewis X biosynthesis is mediated by alpha1-3 fucosyltransferase-VIIS, the enzyme is essential for biosynthesis of P- and E-selectin binding ligands in T-cells
-
-
?
additional information
?
-
-
the enzyme is essential for biosynthesis of selectin binding ligands in T-cells
-
-
?
additional information
?
-
-
the enzyme is responsible for the generation of functional P- and E-selectin ligands
-
-
?
additional information
?
-
-
the enzyme synthesizes functional selectin ligands on the surface of leukocytes
-
-
?
additional information
?
-
-
development of a sensitive cell-based assay system to monitor FucT-VII mediated sialyl Lewis biosynthesis
-
-
?
additional information
?
-
-
poorly active with Galbeta1-4GlcNAc-O-(CH2)8-COOCH3, Fucalpha1-2Galbeta1-4GlcNAcbeta-R, Galbeta1-3GlcNAcbeta-R, and Fucalpha1-2Galbeta1-3GlcNAcbeta-R
-
-
?
additional information
?
-
-
substrate specificities of wild-type and alpha 1,3 FucT motif mutants, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GDP-alpha-L-fucose + Galbeta1-4GlcNAc-R
GDP + Galbeta1-4[Fucalpha1-3]GlcNAc-R
-
-
-
-
ir
GDP-L-fucose + N4-[N-acetyl-beta-D-glucosaminyl-(1-2)-alpha-D-mannosyl-(1-3)-[N-acetyl-beta-D-glucosaminyl-(1-2)-alpha-D-mannosyl-(1-6)]-beta-D-mannosyl-(1-4)-N-acetyl-beta-D-glucosaminyl-(1-4)-N-acetyl-beta-D-glucosaminyl]asparagine
GDP + N4-[N-acetyl-beta-D-glucosaminyl-(1-2)-alpha-D-mannosyl-(1-3)-[N-acetyl-beta-D-glucosaminyl-(1-2)-alpha-D-mannosyl-(1-6)]-beta-D-mannosyl-(1-4)-N-acetyl-beta-D-glucosaminyl-(1-4)-[alpha-L-fucosyl-(1-3)]-N-acetyl-beta-D-glucosaminyl]asparagine
-
-
-
?
additional information
?
-
-
alpha1,3-fucosylation by FucT-VII is a step in the biosynthesis of Lewis X antigen, FucT-VII stimulates the growth of hepatocarcinoma cells via the cyclin-dependent kinase inhibitor p27Kip1, phosphorylation of the Rb protein is involved, signaling pathway overview
-
-
?
additional information
?
-
-
FucT-IV and FucT-VII are responsible for generation of sialylated Lewis X, i.e. sLex, FucT-VII being the major enzyme form in selectin ligand activity regulating leukocyte recruitment and lymphocyte homing into lymph nodes, FucT-IV and FucT-VII are both involved in conferring L-, P- and E-selectin binding activities to P-selectin glycoprotein ligand-1, i.e. PSGL-1, in humans, overview, FucT-IV and FucT-VII show cooperation in recruitment of selectin-expressing cells on PSGL-1 and in regulating cell rolling velocity and stability
-
-
?
additional information
?
-
-
FucT-VII is essential for biosynthesis of selectin binding ligands in T-cells, H-Ras and phosphoinositide 3-kinase cooperate to induce alpha(1,3)-fucosyltransferase VII expression in Jurkat T cells via the Raf-MEK-ERK pathway, but induction of FucT-VII requires the concomitant activation of at least 3 different signaling pathways, overview
-
-
?
additional information
?
-
-
sialyl Lewis X biosynthesis is mediated by alpha1-3 fucosyltransferase-VIIS, the enzyme is essential for biosynthesis of P- and E-selectin binding ligands in T-cells
-
-
?
additional information
?
-
-
the enzyme is essential for biosynthesis of selectin binding ligands in T-cells
-
-
?
additional information
?
-
-
the enzyme is responsible for the generation of functional P- and E-selectin ligands
-
-
?
additional information
?
-
-
the enzyme synthesizes functional selectin ligands on the surface of leukocytes
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
additional information
-
activation by divalent cations in descending order: Mn2+, Mg2+, Ca2+, Co2+, while Ni2+ has no effect on the enzyme activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
p-chloromercuribenzoate
-
at 0.05 mM: almost 30% of the original enzyme activity remains
additional information
-
no inhibition of the recombinant soluble enzyme by NEM
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
enzyme is induced by interleukin 12Rbeta2 and interferon-gamma
-
additional information
-
H-Ras and phosphoinositide 3-kinase cooperate to induce alpha(1,3)-fucosyltransferase VII expression in Jurkat T cellsvia the Raf-MEK-ERK pathway, but induction of FucT-VII requires the concomitant activation of at least 3 different signaling pathways, overview
-
additional information
-
interleukin-12 i.e. IL-12, and TGF-beta1 strongly induce the enzyme in activated T-cells, IL-12 and TGF-beta1 are important for homing of the T-cells to inflammation sites in the skin and gut, respectively, via selectins, which are bound by ligands expressed by the T-cells involving the enzyme, induction by TGF-beta1 can be blocked by p38 mitogen-activated protein kinase, but is unaffected by mitogen-activated protein/extracellular signal-related kinase kinase inhibitor, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetics of wild-type and alpha 1,3 FucT motif mutants
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
FucT-IV and FucT-VII regulated E-, L-, and P-selectin-dependent rolling of cells, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 11
-
enzyme is not affected by high pH but shows no activity at pH below pH 5.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
IL-12 and TGF-beta1 are important for homing of the T-cells to inflammation sites in the skin and gut, respectively, via selectins, which are bound by ligands expressed by the T-cells involving the enzyme
-
Th1 cells, of peripheral blood and synovial fluid from juveniles with idiopathic arthritis
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
overexpression of FUT7 up-regulates sLeX synthesis and enhances sLeX-mediated embryo implantation. FUT7 overexpression enhances JAR cell adhesion to RL95-2 cells
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
49000
-
x * 49000, recombinant enzyme glycoform 1, SDS-PAGE, x * 55000, recombinant enzyme glycoform 1, SDS-PAGE
55000
-
x * 49000, recombinant enzyme glycoform 1, SDS-PAGE, x * 55000, recombinant enzyme glycoform 1, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 49000, recombinant enzyme glycoform 1, SDS-PAGE, x * 55000, recombinant enzyme glycoform 1, SDS-PAGE
additional information
-
6 neighboring cysteine residues in the enzyme, Cys68-Cys76 at the N-terminus, Cys211-Cys214 in the middle, and Cys318-Cys321 at the C-terminus, are engaged in disulfide bridges, forming small loop structures, enzyme structure modeling using sequnce analysis, mass spectrometry, fold recognition and homology modeling
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
monosaccharide composition analysis of recombinant enzyme expressed in CHO cells
glycoprotein
-
the recombinant enzyme exists in 2 glycoprotein forms of 55 and 49 kDa, cleaving by PNGaseF
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E247A
-
site-directed mutagenesis of a residue from the conserved alpha 1,3 FucT motif, below 1% activity compared to the wild-type FucT VI
E257A
-
site-directed mutagenesis of a residue from the conserved alpha 1,3 FucT motif, below 1% activity compared to the wild-type FucT VI
F242A
-
site-directed mutagenesis of a residue from the conserved alpha 1,3 FucT motif, below 1% activity compared to the wild-type FucT VI
F246A
-
site-directed mutagenesis of a residue from the conserved alpha 1,3 FucT motif, 7% activity compared to the wild-type FucT VI
K241A
-
site-directed mutagenesis of a residue from the conserved alpha 1,3 FucT motif, low expression level in COS-7 cells, below 1% activity compared to the wild-type FucT VI
K258A
-
site-directed mutagenesis of a residue from the conserved alpha 1,3 FucT motif, inactive mutant
L244A
-
site-directed mutagenesis of a residue from the conserved alpha 1,3 FucT motif, 7% activity compared to the wild-type FucT VI
N248A
-
site-directed mutagenesis of a residue from the conserved alpha 1,3 FucT motif, below 1% activity compared to the wild-type FucT VI
S249A
-
site-directed mutagenesis of a residue from the conserved alpha 1,3 FucT motif, 57% activity compared to the wild-type FucT VI
T256A
-
site-directed mutagenesis of a residue from the conserved alpha 1,3 FucT motif, below 1% activity compared to the wild-type FucT VI
Y240A
-
site-directed mutagenesis of a residue from the conserved alpha 1,3 FucT motif, 14% activity compared to the wild-type FucT VI
Y254A
-
site-directed mutagenesis of a residue from the conserved alpha 1,3 FucT motif, inactive mutant
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant soluble enzyme from CHO cells by GDP-hexanolamine affinity chromatography to homogeneity
-
recombinant soluble protein A-fusion wild-type and mutant FucT VIs from COS-7 cells by IgG affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
1121-bp PCR product of cDNA containing the full length of the FUT7 gene ligated into the pM.D.18-T cloning vector, propagation in Escherichia coli DH5alpha. Full coding sequence of FUT7 subcloned into pIRES2-EGFP expression vector and transiently transfected into RL95-2 cells or injected into the uteri of early pregnant mice
the complex of the FUT7-cytoplasmic tail and bovine UDP-galactose:beta-N-acetylglucosaminide: beta1,4-galactosyltransferase 1 is expressed in Sf9 insect cells
expression of the soluble enzyme, by constructing a fusion enzyme amino acid residues 1-63 of a mammalian enzyme fused to the stem and the catalytic region of residues 39-342 of the enzyme, in CHO cells
-
expression of wild-type and mutant FucT VIs in COS-7 cells as soluble N-terminal protein A-fusion proteins, mutant K241A shows a low expression level
-
gene FUT7, stable expression in MOLT-4 8H cells being induced by the recombinant enzyme in presence of mifepristone to produce sL2x epitopes, expression of Staphylococcus aureus protein A-human FucT-VII fusion protein in Spodoptera frugiperda Sf21 insect cells via the baculovirus infection system
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of FUT7 and sLeX is significantly increased after transfection of pIRES2-EGFP-FUT7 into RL95-2 cells compared with the parental control and mock vector transfectants
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
-
the enzyme is a target for rational inhibitor design for medication in the treatment of rheumatoid arthritis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Scudder, P.R.; Chantler, E.N.
Glycosyltransferases of the human cervical epithelium. I. Characterization of a beta-galactoside alpha-2-L-fucosyltransferase and the identification of a beta-N-acetylglucosaminide alpha-3-L-fucosyltransferase
Biochim. Biophys. Acta
660
128-135
1981
Homo sapiens
Miyashiro, M.; Furuya, S.; Fujishige, K.; Sugita, T.
Highly sensitive cell-based assay system to monitor the sialyl Lewis X biosynthesis mediated by alpha1-3 fucosyltransferase-VII
Biochem. Biophys. Res. Commun.
324
98-107
2004
Homo sapiens
Wang, Q.Y.; Guo, P.; Duan, L.L.; Shen, Z.H.; Chen, H.L.
alpha-1,3-Fucosyltransferase-VII stimulates the growth of hepatocarcinoma cells via the cyclin-dependent kinase inhibitor p27Kip1
Cell. Mol. Life Sci.
62
171-178
2005
Homo sapiens
De Vries, T.; Yen, T.Y.; Joshi, R.K.; Storm, J.; Van den Eijnden, D.H.; Knegtel, R.M.A.; Bunschoten, H.; Joziasse, D.H.; Macher, B.A.
Neighboring cysteine residues in human fucosyltransferase VII are engaged in disulfide bridges, forming small loop structures
Glycobiology
11
423-432
2001
Homo sapiens
De Vries, T.; Storm, J.; Rotteveel, F.; Verdonk, G.; Van Duin, M.; Van den Eijnden, D.H.; Joziasse, D.H.; Bunschoten, H.
Production of soluble human alpha3-fucosyltransferase (FucT VII) by membrane targeting and in vivo proteolysis
Glycobiology
11
711-717
2001
Homo sapiens
Jost, F.; de Vries, T.; Knegtel, R.M.; Macher, B.A.
Mutation of amino acids in the alpha 1,3-fucosyltransferase motif affects enzyme activity and Km for donor and acceptor substrates
Glycobiology
15
165-175
2005
Homo sapiens
Zisoulis, D.G.; Kansas, G.S.
H-Ras and phosphoinositide 3-kinase cooperate to induce alpha(1,3)-fucosyltransferase VII expression in Jurkat T cells
J. Biol. Chem.
279
39495-39504
2004
Homo sapiens
Martinez, M.; Joffraud, M.; Giraud, S.; Baisse, B.; Bernimoulin, M.P.; Schapira, M.; Spertini, O.
Regulation of PSGL-1 interactions with L-selectin, P-selectin, and E-selectin: role of human fucosyltransferase-IV and -VII
J. Biol. Chem.
280
5378-5390
2005
Homo sapiens
Wagers, A.J.; Kansas, G.S.
Potent induction of alpha(1,3)-fucosyltransferase VII in activated CD4+ T cells by TGF-beta1 through a p38 mitogen-activated protein kinase-dependent pathway
J. Immunol.
165
5011-5016
2000
Homo sapiens
De Benedetti, F.; Pignatti, P.; Biffi, M.; Bono, E.; Wahid, S.; Ingegnoli, F.; Chang, S.Y.; Alexander, H.; Massa, M.; Pistorio, A.; Martini, A.; Pitzalis, C.; Sinigaglia, F.; Rogge, L.
Increased expression of alpha(1,3)-fucosyltransferase-VII and P-selectin binding of synovial fluid T cells in juvenile idiopathic arthritis
J. Rheumatol.
30
1611-1615
2003
Homo sapiens
Zhang, Y.; Liu, S.; Liu, Y.; Wang, Z.; Wang, X.; Yan, Q.
Overexpression of fucosyltransferase VII (FUT7) promotes embryo adhesion and implantation
Fertil. Steril.
91
908-914
2009
Homo sapiens (Q11130), Homo sapiens
Liu, T.W.; Kaji, H.; Togayachi, A.; Ito, H.; Sato, T.; Narimatsu, H.
A chemoenzymatic approach toward the identification of fucosylated glycoproteins and mapping of N-glycan sites
Glycobiology
22
630-637
2012
Homo sapiens
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