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alpha-1-antitrypsin precursor + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
angiotensinogen preproprotein + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
beta-N-acetylhexosaminidase A + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
cathepsin D preproprotein + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
cathepsin X precursor + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
DDR1 variant protein + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
dipeptidyl peptidase 7 preproprotein + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
discoidin receptor tyrosine kinase + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
dystroglycan 1 precursor + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
galectin 3 binding protein + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
granulin isoform 1 precursor + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
heat shock protein 70 kDa protein 8 isoform 1 + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
heat shock protein gp96 precursor + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
heparan sulfate proteoglycan perlecan + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
hexosaminidase B preproprotein + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
human Fc binding protein + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
Ig kappa chain V-III + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
laminin gamma1 precursor + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
legumain preproprotein + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
lysosomal-associated membrane protein-1 + UDP-N-acetyl-D-glucosamine
?
-
LAMP-1
-
-
?
lysosome-associated membrane protein-1 + UDP-N-acetyl-D-glucosamine
?
-
LAMP-1
-
-
?
met proto-oncogene + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
N-acetylgalactosamine-6-sulfatase + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
N-acetylglucosamine-6-sulfatase + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
prosaposin + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
protective protein for beta-galactosidase + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
protein tyrosine phosphatase kappa + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
protein-tyrosine kinase-related receptor PTK7 + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
ribonuclease T2 precursor + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
TDP-glucose + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
TDP + ?
-
-
-
-
?
tissue inhibitor of metalloproteinase-1 + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
tumor-associated calcium signal transducer 1 + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
tyrosinase + UDP-N-acetyl-D-glucosamine
?
-
-
-
-
?
tyrosinase-related protein-1 + UDP-N-acetyl-D-glucosamine
?
-
TYRP-1
-
-
?
tyrosinase-related protein-2 + UDP-N-acetyl-D-glucosamine
?
-
TYRP-2
-
-
?
UDP-GlcNAc + GlcNAc-beta(1-2)Man-alpha(1-3)(GlcNAc-beta(1-2)Man-alpha(1-4))Man-beta(1-4)GlcNAc-2-amino pyridine
?
-
-
-
-
?
UDP-glucose + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + ?
-
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-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-N-Asn-[protein]
UDP + beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-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-N-Asn-[TIMP-1]
UDP + beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[TIMP-1]
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + GlcNAcbeta(1->2)Manalpha(1->3)-[GlcNAcbeta(1->2)Manalpha(1->6)]-Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc-pyridylamine
?
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 6-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 6-(2,6-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP-N-acetyl-D-glucosamine + Ac-Val-Glu-Pro-(GlcNAcbeta(1-2)Manalpha1-O-)Thr-Ala-Val-NH2
UDP + Ac-Val-Glu-Pro-(GlcNAcbeta(1-2)[GlcNAcbeta(1-6)]Manalpha1-O-)Thr-Ala-Val-NH2
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + epidermal growth factor receptor
UDP + N-acetylglucosamine-beta-1,6-mannose-alpha-1,3-branch of epidermal growth factor receptor
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta(1-2)Manalpha(1-2)Glc-O-octyl
UDP + GlcNAcbeta(1-2)[GlcNAcbeta(1-6)]Manalpha(1-2)Glc-O-octyl
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta(1-2)Manalpha(1-3)[GlcNAcbeta(1-2)Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc
UDP + GlcNAcbeta(1-2)[GlcNAcbeta(1-6)]Manalpha(1-3)[GlcNACbeta(1-2)Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta(1-2)Manalpha1-O-benzyl
UDP + GlcNAcbeta(1-2)[GlcNAcbeta(1-6)]Manalpha1-O-benzyl
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-4-deoxy-mannosyl-1,6-beta-glucosyl-O-(CH2)7-CH3
UDP + N-acetyl-D-glucosaminyl-1,6-(N-acetyl-D-glucosaminyl-1,2)-alpha-4-deoxy-mannosyl-1,6-beta-D-mannosyl-O-(CH2)7-CH3
-
good substrate
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-L-Asn
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-L-Asn
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-mannosyl-1,6-beta-glucosyl-O-R
UDP + N-acetyl-D-glucosaminyl-1,6-(N-acetyl-D-glucosaminyl-1,2)-alpha-mannosyl-1,6-beta-D-glucosyl-O-R
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-mannosyl-1,6-beta-mannosyl-O-(CH2)8COOCH3
UDP + N-acetyl-D-glucosaminyl-1,6-(N-acetyl-D-glucosaminyl-1,2)-alpha-mannosyl-1,6-beta-D-mannosyl-O-(CH2)8COOCH3
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-mannosyl-1,6-beta-mannosyl-O-R
UDP + N-acetyl-D-glucosaminyl-1,6-(N-acetyl-D-glucosaminyl-1,2)-alpha-mannosyl-1,6-beta-D-mannosyl-O-R
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,6-beta-glucosaminyl-O-(CH2)7-CH3
UDP + ?
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + octyl 6-O-[2-O-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-alpha-D-mannopyranosyl]-beta-D-glucopyranoside
UDP + ?
UDP-N-acetyl-D-glucosamine + [GlcNAcbeta(1-2)][GlcNAcbeta(1-6)]Manalpha(1-3)[GlcNAcbeta(1-2)Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc
UDP + [GlcNAcbeta(1-2)][GlcNAcbeta(1-6)]Manalpha(1-3)[[GlcNAcbeta(1-2)][GlcNAcbeta(1-6)]Manalpha(1-6)]Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc
-
-
-
-
?
Zn-alpha-2-glycoprotein + UDP-N-acetyl-D-glucosamine
?
-
identified target protein for GnT-V in human colon cancer cell WiDr
-
-
?
additional information
?
-
UDP-N-acetyl-D-glucosamine + 6-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 6-(2,6-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 6-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 6-(2,6-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
-
-
-
?
UDP-N-acetyl-D-glucosamine + 6-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 6-(2,6-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 6-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 6-(2,6-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
-
-
-
?
UDP-N-acetyl-D-glucosamine + 6-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 6-(2,6-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
-
catalyzes the formation of beta-1-6 GlcNAc branches on asparagine-linked oligosaccharides, which is directly linked to tumorigenesis
-
-
?
UDP-N-acetyl-D-glucosamine + 6-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 6-(2,6-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
-
GnTIII competes with GnT-V for the modification of integrin alpha3 subunit in living cells. This competition results in the inhibition of alpha3beta1 integrin-mediated cell migration induced by GnT-V
-
-
?
UDP-N-acetyl-D-glucosamine + 6-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 6-(2,6-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
no substrates are bisected N-glycans
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
enzyme requires prior action of N-acetylglucosaminyltransferase II which requires prior action of N-acetylglucosaminyltransferase I
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
best substrates are bi- and tri-antennary acceptors
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
most active towards biantennary sugars
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
enzyme also uses bisected oligosaccharides
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
glycopeptides with sialic acid or galactose at non-reducing terminal
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
specificity study with various pyridylaminated sugar chains
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
acceptor substrates are only branched mannose glycopeptides with non-reducing N-acetylglucosamine terminal residues
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
no substrates are bisected N-glycans
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
enzyme requires prior action of N-acetylglucosaminyltransferase II which requires prior action of N-acetylglucosaminyltransferase I
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
promotes angiogenesis in vitro and in vivo at physiological concentrations
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
involved in biosynthesis of branched N-glycopeptides
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
synthetic acceptor substrates
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
no substrates are bisected N-glycans
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
enzyme requires prior action of N-acetylglucosaminyltransferase II which requires prior action of N-acetylglucosaminyltransferase I
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
involved in biosynthesis of branched N-glycopeptides
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
biosynthesis of cell-surface ASSN-linked oligosaccharides
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
glycopeptides with sialic acid
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
glycopeptides with sialic acid or galactose at non-reducing terminal
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
transfers N-acetylglucosamine to C-6 of alpha-linked mannose residue with inversion of configuration at its anomeric center
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
acceptor substrates are only branched mannose glycopeptides with non-reducing N-acetylglucosamine terminal residues
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
acceptors are bi-antennary Asn-linked asialo-or agalacto-oligosaccharides containing N-acetylglucosamine at the non-reducing terminal
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
no substrates are bisected N-glycans
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
enzyme requires prior action of N-acetylglucosaminyltransferase II which requires prior action of N-acetylglucosaminyltransferase I
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
involved in biosynthesis of branched N-glycopeptides
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
synthetic acceptor substrates
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-mannosyl-1,6-beta-glucosyl-O-R
UDP + N-acetyl-D-glucosaminyl-1,6-(N-acetyl-D-glucosaminyl-1,2)-alpha-mannosyl-1,6-beta-D-glucosyl-O-R
-
best substrate
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-mannosyl-1,6-beta-glucosyl-O-R
UDP + N-acetyl-D-glucosaminyl-1,6-(N-acetyl-D-glucosaminyl-1,2)-alpha-mannosyl-1,6-beta-D-glucosyl-O-R
-
R: hydrophobic group, e.g. (CH2)7-CH3 or (CH2)8-COOCH3
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-mannosyl-1,6-beta-glucosyl-O-R
UDP + N-acetyl-D-glucosaminyl-1,6-(N-acetyl-D-glucosaminyl-1,2)-alpha-mannosyl-1,6-beta-D-glucosyl-O-R
-
R: hydrophobic group, e.g. (CH2)7-CH3
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-mannosyl-1,6-beta-glucosyl-O-R
UDP + N-acetyl-D-glucosaminyl-1,6-(N-acetyl-D-glucosaminyl-1,2)-alpha-mannosyl-1,6-beta-D-glucosyl-O-R
-
R: hydrophobic group, e.g. (CH2)7-CH3
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-mannosyl-1,6-beta-glucosyl-O-R
UDP + N-acetyl-D-glucosaminyl-1,6-(N-acetyl-D-glucosaminyl-1,2)-alpha-mannosyl-1,6-beta-D-glucosyl-O-R
-
R: hydrophobic group, e.g. (CH2)7-CH3 or (CH2)8-COOCH3
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-mannosyl-1,6-beta-mannosyl-O-R
UDP + N-acetyl-D-glucosaminyl-1,6-(N-acetyl-D-glucosaminyl-1,2)-alpha-mannosyl-1,6-beta-D-mannosyl-O-R
-
R: hydrophobic group, e.g. (CH2)8-COOCH3
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-mannosyl-1,6-beta-mannosyl-O-R
UDP + N-acetyl-D-glucosaminyl-1,6-(N-acetyl-D-glucosaminyl-1,2)-alpha-mannosyl-1,6-beta-D-mannosyl-O-R
-
R: hydrophobic group, e.g. (CH2)8-COOCH3
-
?
UDP-N-acetyl-D-glucosamine + octyl 6-O-[2-O-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-alpha-D-mannopyranosyl]-beta-D-glucopyranoside
UDP + ?
a synthetic trisaccharide acceptor
-
-
?
UDP-N-acetyl-D-glucosamine + octyl 6-O-[2-O-(2-acetamido-2-deoxy-beta-D-glucopyranosyl)-alpha-D-mannopyranosyl]-beta-D-glucopyranoside
UDP + ?
a synthetic trisaccharide acceptor
-
-
?
additional information
?
-
-
ADP-glucose, CDP-glucose and GDP-glucose do not act as glycosyl donor
-
-
?
additional information
?
-
synthesis of N-linked beta(1,6)-branched glykans
-
-
?
additional information
?
-
-
synthesis of N-linked beta(1,6)-branched glykans
-
-
?
additional information
?
-
-
down regulation of N-acetylglucosaminyltransferase V facilitates all-transretinoic acid to induce apoptosis of human hepatocarcinoma cells
-
-
?
additional information
?
-
-
GnT-V is cleaved at the transmembrane region by gamma-secretase, and this might control tumor angiogenesis
-
-
?
additional information
?
-
-
N-acetylglucosaminyltransferase V is a key enzyme in the formation of branching of asparagine-linked oligosaccharides and is strongly linked to tumor invasion and metastasis. Blocking of GnT-V expression impairs functions of chaperones and N-glycan-synthesizing enzymes, which causes unfolded protein response in vivo
-
-
?
additional information
?
-
-
NMR structural characterization of substrates bound to N-acetylglucosaminyltransferase V
-
-
?
additional information
?
-
the MCAM glycoprotein, which is a biomarker of cutaneous melanoma, as a potential target for overexpressed glycosyltransferases
-
-
?
additional information
?
-
-
the MCAM glycoprotein, which is a biomarker of cutaneous melanoma, as a potential target for overexpressed glycosyltransferases
-
-
?
additional information
?
-
branched N-glycans modified by GnT-V are evaluated by lectin blot analysis. The reactivities with Datura stramonium lectin (DSA) or leuko-agglutinating phytohemagglutinin (L4-PHA lectin), which specifically recognize, that branched N-glycans are clearly increased in the GnT-V transfectants compared to the control cells
-
-
-
additional information
?
-
-
GnT-V can partially compensate for GnT-Vb(IX) activity in vivo
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-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-N-Asn-[protein]
UDP + beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[protein]
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-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-N-Asn-[TIMP-1]
UDP + beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc-N-Asn-[TIMP-1]
-
-
-
?
UDP-N-acetyl-D-glucosamine + 6-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 6-(2,6-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP-N-acetyl-D-glucosamine + epidermal growth factor receptor
UDP + N-acetylglucosamine-beta-1,6-mannose-alpha-1,3-branch of epidermal growth factor receptor
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-L-Asn
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-L-Asn
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
additional information
?
-
UDP-N-acetyl-D-glucosamine + 6-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 6-(2,6-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 6-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 6-(2,6-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
-
-
-
?
UDP-N-acetyl-D-glucosamine + 6-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 6-(2,6-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 6-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 6-(2,6-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
-
-
-
?
UDP-N-acetyl-D-glucosamine + 6-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 6-(2,6-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
-
catalyzes the formation of beta-1-6 GlcNAc branches on asparagine-linked oligosaccharides, which is directly linked to tumorigenesis
-
-
?
UDP-N-acetyl-D-glucosamine + 6-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 6-(2,6-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
-
GnTIII competes with GnT-V for the modification of integrin alpha3 subunit in living cells. This competition results in the inhibition of alpha3beta1 integrin-mediated cell migration induced by GnT-V
-
-
?
UDP-N-acetyl-D-glucosamine + 6-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
UDP + 6-(2,6-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
enzyme requires prior action of N-acetylglucosaminyltransferase II which requires prior action of N-acetylglucosaminyltransferase I
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
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enzyme requires prior action of N-acetylglucosaminyltransferase II which requires prior action of N-acetylglucosaminyltransferase I
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-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
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promotes angiogenesis in vitro and in vivo at physiological concentrations
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-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
involved in biosynthesis of branched N-glycopeptides
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
enzyme requires prior action of N-acetylglucosaminyltransferase II which requires prior action of N-acetylglucosaminyltransferase I
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
involved in biosynthesis of branched N-glycopeptides
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
biosynthesis of cell-surface ASSN-linked oligosaccharides
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
enzyme requires prior action of N-acetylglucosaminyltransferase II which requires prior action of N-acetylglucosaminyltransferase I
-
-
?
UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
UDP + N-acetyl-D-glucosaminyl-1,2-(N-acetyl-D-glucosaminyl-1,6)-1,2-alpha-D-mannosyl-1,3(6)-(N-acetyl-D-glucosaminyl-1,2-alpha-D-mannosyl-1,6(3))-beta-D-mannosyl-1,4-N-acetyl-D-glucosaminyl-R
-
involved in biosynthesis of branched N-glycopeptides
-
-
?
additional information
?
-
-
down regulation of N-acetylglucosaminyltransferase V facilitates all-transretinoic acid to induce apoptosis of human hepatocarcinoma cells
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-
?
additional information
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-
-
GnT-V is cleaved at the transmembrane region by gamma-secretase, and this might control tumor angiogenesis
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-
?
additional information
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N-acetylglucosaminyltransferase V is a key enzyme in the formation of branching of asparagine-linked oligosaccharides and is strongly linked to tumor invasion and metastasis. Blocking of GnT-V expression impairs functions of chaperones and N-glycan-synthesizing enzymes, which causes unfolded protein response in vivo
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-
?
additional information
?
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the MCAM glycoprotein, which is a biomarker of cutaneous melanoma, as a potential target for overexpressed glycosyltransferases
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-
?
additional information
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-
the MCAM glycoprotein, which is a biomarker of cutaneous melanoma, as a potential target for overexpressed glycosyltransferases
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?
additional information
?
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GnT-V can partially compensate for GnT-Vb(IX) activity in vivo
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?
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additional information
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beta1,6-N-acetylglucosaminyltransferase V (GnT-V) is encoded by ets-1, a transcriptional factor which also regulates several enzymes associated with cell invasion and metastasis
malfunction
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associated with increase metastasis
malfunction
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Mgat5 knockout mice, change in depression-like behaviour, decrease in immobility time in the forced swim test and the tail suspension test, no response to antidepressant treatment, altered social behavior in males
malfunction
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N-acetylglucosaminyltransferase Va knockout mice, aberrant expression of several N-glycan structures, decrease in tumor progression
malfunction
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overexpressed in malignant tumors
malfunction
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decreased enzyme activity due to inflammatory cytokine induction in human monocytes results in enhancement of integrin alpha5beta1-dependent monocyte-vascular endothelium adhesion and transmigration
malfunction
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enzyme down-regulation inhibits the proliferation, migration and invasion of the Hep-G2 cells
malfunction
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GnT-V null brains lack N-linked, beta(1,6)-glycans but have normal levels of O-Manbeta(1,6)-branched structures
malfunction
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Mgat5-deficient mouse skin is resistant to 12-O-tetradecanoyl phorbol-13-acetate-induced epidermal thickening. Cell surface epidermal growth factor receptor expression is decreased in Mgat5-deficient mouse keratinocytes
malfunction
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N-acetylglucosaminyltransferase-V-deficient mice are born healthy and lack beta1,6GlcNAc branches on N-glycans, but develop immunological disorders due to T-cell dysfunction at 12-20 months of age
malfunction
absense of the enzyme is due to a base insertion at nucleotide 822 of the Magt5 gene that shifts the open reading frame. A 155 amino acid truncated GlcNAcT-V (instead of a full length 740 amino acid enzyme) may be synthesized, which consists of the cytosolic and transmembrane domains and a short piece of the stem region, the truncated enzyme is degenerated. Lack of the enzyme protein causes a reduction in Golgi volume density in Lec4A cells, this can be reversed by stable transfection of Lec4A cells with a cDNA encoding Mgat5. No effect on Golgi volume density is observed in CHO Lec1 cells that contain enzymatically active GlcNAcT-V, but cannot synthesize beta1,6-branched glycans due to an inactive GlcNAcT-I in their Golgi apparatus. The structure of the Golgi apparatus in cells stably transfected and therefore overexpressing different glycosyltransferases appears normal
malfunction
absense of the enzyme is due to a base insertion at nucleotide 822 of the Magt5 gene that shifts the open reading frame. A 155 amino acid truncated GlcNAcT-V (instead of a full length 740 amino acid enzyme) may be synthesized, which consists of the cytosolic and transmembrane domains and a short piece of the stem region, the truncated enzyme is degenerated. Lack of the enzyme protein causes a reduction in Golgi volume density in Lec4A cells, this can be reversed by stable transfection of Lec4A cells with a cDNA encoding Mgat5. No effect on Golgi volume density is observed in CHO Lec1 cells that contain enzymatically active GlcNAcT-V, but cannot synthesize beta1,6-branched glycans due to an inactive GlcNAcT-I in their Golgi apparatus. The structure of the Golgi apparatus in cells stably transfected and therefore overexpressing different glycosyltransferases appears normal
malfunction
GnT-V overexpression induces an aberrant E-cadherin cellular localization and alters cell morphology, fibroblastoid cells exhibit a remarkable decrease of E-cadherin membranar expression with punctual E-cadherin staining in focal areas of cell-cell contacts
malfunction
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inhibition of enzyme Gnt-V increases the radiosensitivity of cancer cells. Increased enzyme activity leads to the radiosensitivity and migration of small cell lung cancer cells by inducing epithelial-mesenchymal transition. Overexpression of Gnt-V leads to a further increase in the relative viable cell number and survival fraction with a decrease in apoptosis rate and Bax/Bcl-2 ratio, when the cells are treated with irradiation. Downregulation of Gnt-V increased E-cadherin but suppressed ZEB2, vimentin and N-cadherin expression, while upregulation of enzyme levels leads to the downregulation of E-cadherin and upregulation of ZEB2, vimentin and N-cadherin at both the protein and mRNA levels
malfunction
Mgat5 overexpression increases p21-activated kinase 1 (PAK1) expression and upregulated beta-1-6-GlcNAc branched N-glycosylation. Mgat5 overexpression promotes anchorage-independent growth and inhibits anoikis in hepatoma cells. shRNA-mediated PAK1 knockdown and kinase inactivation with kinase dead mutant PAK1 K299R coexpression or allosteric inhibitor P21-activated kinase inhibitor III (IPA3) treatment reverses anoikis resistance in Mgat5-overexpressed hepatoma cells. Knockdown of Mgat5 reduces EGFR/PAK1-dependent anoikis resistance, which can be reversed by PAK1 T423E
malfunction
GnT-V overexpression greatly promotes cell migration in the transfectants by using wound healing assay. But the induction in the cell migration is significantly suppressed by an addition of chitosan oligosaccharides (COS)
malfunction
inhibition of N-acetylglucosaminyltransferase V enhances the cetuximab-induced radiosensitivity of nasopharyngeal carcinoma (NPC) cells likely through EGFR N-glycan alterations. Cetuximab is an epidermal growth factor receptor (EGFR) inhibitor used as a radiosensitizer in the treatment of NPC. The half-maximal inhibitory concentration (IC50) of cetuximab in CNE-1 and CNE-2 cells is 0.717 and 1.244 mg/ml, respectively
malfunction
interruption of beta1,6-GlcNAc glycan modification of CD147/basigin decreases matrix metalloproteinase (MMP) expression in HCC cell lines and affects the interaction of CD147/basigin with integrin beta1, mechanism modeling, overview. Real-time PCR shows that MMP-1, MMP-2, and MMP-9 are reduced in cells treated with mutant CD147/basigin (defective beta1,6-branched N-glycosylation) compared with cells treated with wild-type, suggesting that GnT-V-mediated glycosylation increases CD147/basigin-mediated HCC cell invasion. Overexpression of GnT-V increases the level of CD147/basigin-beta1,6-branching and the induction of MMPs
malfunction
overexpression of N-acetylglucosaminyltransferase V protects detached cancer cells from apoptotic death, and suppression or knockout of the gene sensitized cancer cells to the apoptotic death. The gene overexpression also stimulates anchorage-dependent as well as anchorage-independent colony formation of cancer cells following anoikis stress treatments
metabolism
-
part of N-glycan pathway
metabolism
existence of a bi-directional cross-talk between E-cadherin and two major N-glycan processing enzymes, N-acetylglucosaminyltransferase-III or -V (GnT-III or GnT-V). Molecular mechanisms underlying E-cadherin regulation in gastric cancer, overview
metabolism
the enzyme is involved in the N-glycan-branching pathway, regulation of cellular metabolite levels by Mgat5, overview
metabolism
activation of the PI3K/Akt pathway is involved in the regulation of GnT-V expression and deletion of GnT-V-mediated N-glycosylation impairs the PI3K/Akt pathway
physiological function
-
involved in the malignant potential of mucinous ovarian cancer
physiological function
-
tumor progression
physiological function
-
a high enzyme expression in keratinocytes contributes to heparin-binding epidermal growth factor-like growth factor-mediated epidermal hyperproliferation by inhibiting endocytosis of epidermal growth factor receptors bearing beta1,6 N-acetylglucosamine on their N-glycans. The enzyme plays a role in epidermal homoeostasis, particularly in hyperproliferative conditions
physiological function
-
concomitant overexpression of tissue inhibitor of metalloproteinase-1 and N-acetylglucosaminyltransferase V directs accelerated tumor growth and cancer progression in vivo and in vitro. Cells with high enzyme expression show higher collagenolytic activity, compared with the mock cells. Membrane type-1-matrix metalloproteinase expression is induced by N-acetylglucosaminyltransferase V overexpression
physiological function
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enzyme overexpression of in cancer cells enhances the signaling of growth factors such as epidermal growth factor by increasing galectin-3 binding to polylactosamine structures on receptor N-glycans. Enzyme overexpression in Mv1Lu cells enhances the migration of these cells to scratch wounds. GnT-V maintains skin homeostasis by regulating the proliferation of keratinocytes through epidermal growth factor-R signaling
physiological function
-
GnT-V is involved in synthesizing branched O-mannosyl glycans in brain
physiological function
-
N-acetylglucosaminyltransferase V (GnT-V) regulates transforming growth factor-beta1 response in hepatic stellate cells and the progression of steatohepatitis through modulating lymphocyte and hepatic stellate cell functions. Excess expression of GnT-V enhances beta1-6GlcNAc branching of N-glycans in transgenic hepatic stellate cells. GnT-V enhances transforming growth factor-beta signaling but decreases collagen I expression in transgenic hepatic stellate cells
physiological function
-
N-acetylglucosaminyltransferase V expression is closely associated with metastasis in vivo
physiological function
elevated expression and activity of N-acetylglucosaminyltransferase V in hepatocellular carcinoma is a common early event involved in tumor invasion during hepatocarcinogenesis. EGFR/PAK1 signaling dominates Mgat5-induced resistance of hepatoma cells to anoikis
physiological function
enzyme expression is involved in the development of various cancers and their progression, through altering N-glycan branching, associations between MGAT5 expression and clinicopathologic features, overview. Kaplan-Meier survival analysis indicates that the overall survival of gastric cancer patients with low intratumoral MGAT5 expression is significantly poorer than those patients with high MGAT5 intratumoral expression
physiological function
enzyme that catalyzes the formation of a beta1,6-N-acetylglucosamine side chain to a core mannosyl residue in N-linked glycoproteins. Besides its direct function of producing aberrant glycoproteins, it promotes cancer progression by its involvement in the stimulation of oncoproteins. Enzyme GnT-V guides the transcriptional activation of membrane-type matrix metalloproteinase-1 (MT1-MMP) in cancer cells. The activated MT1-MMP expression has dual effects on cancer progression. It not only promotes proteolytic activity for cancer cells per se, but also leads to the activation of MMP-2. Consequently, the activation of the two MMPs triggered by GnT-V intensifies the invasive potential. Cancer invasion is stimulated by GnT-V-induced activation of both MT1-MMP and MMP-2
physiological function
-
expression of enzyme Gnt-V correlates with the N stage in patients with small cell lung cancer. Increased enzyme activity leads to the radiosensitivity and migration of small cell lung cancer cells by inducing epithelial-mesenchymal transition. Gnt-V regulates the expression of epithelial and mesenchymal markers in SCLC cells
physiological function
GnT-V promotes the destabilization of E-cadherin at the cell membrane leading to its mislocalization and unstable adherens-junctions with impairment of cellcell adhesion. Role pf the enzyme GnT-V in E-cadherin-mediated tumor invasion. GnT-V catalyzes the addition of ?1,6 GlcNAc branching N-glycans and is associated to increased metastasis. E-cadherin is specifically modified with bisecting GlcNAc or beta1,6 GlcNAc branched structures
physiological function
N-acetylglucosaminyltransferase V catalyzes the synthesis of the beta1-6 bond between the sugar residue of the donor and alpha1,6-linked mannose of the core of N-glycan. Subsequently, the beta1-6 branch is formed and antennae are initiated
physiological function
alterations in glycosylation patterns regulate cancer development and progression, serve as important biomarkers, and provide a set of specific targets for diagnosis and therapeutic intervention. The modifications most often associated with cancer include sialylation, beta1,6-GlcNAc-branched N-glycans, and core fucosylation. Increased GlcNAc-branched N-glycan levels result from increased activity of N-acetylglucosaminyltransferase V (GnT-V) encoded by the mannoside acetylglucosaminyltransferase 5 (MGAT5) gene and are closely associated with cancer metastasis. N-acetylglucosaminyltransferase V (GnT-V) regulates cancer processes and cancer cell migration. GnT-V-mediated N-glycosylation of CD147/basigin, a tumor-associated glycoprotein that carries beta1,6-N-acetylglucosamine (beta1,6-GlcNAc) glycans, is upregulated during TGF-beta1-induced epithelial-to-mesenchymal transition (EMT), which correlates with tumor metastasis in patients with hepatocellular carcinoma (HCC). The PI3K/Akt signaling pathway is involved in the regulation of GnT-V expression
physiological function
N-acetylglucosaminyltransferase V (GnT-V) catalyzes the formation of the N-linked beta-1-6 branching of oligosaccharides adding GlcNAc to beta-1,6-linked branches
physiological function
N-acetylglucosaminyltransferase V (GnT-V) is a Golgi-located enzyme that catalyzes the branching of the beta1,6-N-acetylglucosamine side chain to the core mannosyl residue of N-linked glycan. N-acetylglucosaminyltransferase V confers anoikis resistance to colon cancer cells during hematogenous metastasis. This resistance is abolished by the lectin from Sambucus sieboldiana, treatment with the lectin significantly sensitizes anoikis-induced cancer cell deaths in vitro as well as in vivo. Anoikis is a form of anchorage-dependent apoptosis, and cancer cells adopt anokis-resistance molecular machinery to conduct metastasis. The MGAT5 gene is a key modulator of anoikis resistance, MGAT5-stimulated anoikis resistance is validated in clinical specimens by correlating the MGAT5 mRNA levels to the cancer stage. MGAT5 potentiates anchorage-dependent and -independent growth following anoikis stress. Glycan profiling identifies unique N-glycan structural features involved in anoikis resistance
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Schachter, H.; Brockhausen, I.; Hull, E.
High-performance liquid chromatography assays for N-acetylglucosaminyltransferases involved in N- and O-glycan synthesis
Methods Enzymol.
179
351-397
1989
Gallus gallus, Homo sapiens, Mesocricetus auratus, Mus musculus
brenda
Taniguchi, N.; Nishikawa, A.; Fujii, S.; Gu, J.
Glycosyltransferase assays using pyridylaminated acceptors: N-acetylglucosaminyltransferase III, IV, and V
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179
397-408
1989
Rattus norvegicus
brenda
Cummings, R.D.; Trowbridge, I.S.; Kornfeld, S.
A mouse lymphoma cell line resistant to the leukoagglutinating lectin from Phaseolus vulgaris is deficient in UDP-GlcNAc: alpha-D-mannoside beta 1,6 N-acetylglucosaminyltransferase
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1982
Mus musculus
brenda
Gu, J.; Nishikawa, A.; Tsuruoka, N.; Ohno, M.; Yamaguchi, N.; Kangawa, K.; Taniguchi, N.
Purification and characterization of UDP-N-acetylglucosamine: alpha-6-D-mannoside beta 1-6N-acetylglucosaminyltransferase (N-acetylglucosaminyltransferase V) from a human lung cancer cell line
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113
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1993
Homo sapiens
brenda
Palcic, M.M.; Ripka, J.; Kaur, K.J.; Shoreibah, M.; Hindsgaul, O.; Pierce, M.
Regulation of N-acetylglucosaminyltransferase V activity. Kinetic comparisons of parental, Rous sarcoma virus-transformed BHK, and L-phytohemagglutinin-resistant BHK cells using synthetic substrates and an inhibitory substrate analog
J. Biol. Chem.
265
6759-6769
1990
Mesocricetus auratus
brenda
Khan, S.H.; Crawley, S.C.; Kanie, O.; Hindsgaul, O.
A trisaccharide acceptor analog for N-acetylglucosaminyltransferase V which binds to the enzyme but sterically precludes the transfer reaction
J. Biol. Chem.
268
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1993
Mesocricetus auratus
brenda
Hindsgaul, O.; Kaur, K.J.; Srivastava, G.; Blaszcyk-Thurin, M.; Crawley, S.C.; Heerze, L.D.; Palcic, M.M.
Evaluation of deoxygenated oligosaccharide acceptor analogs as specific inhibitors of glycosyltransferases
J. Biol. Chem.
266
17858-17862
1991
Mesocricetus auratus
brenda
Shoreibah, M.; Hindsgaul, O.; Pierce, M.
Purification and characterization of rat kidney UDP-N-acetylglucosamine: alpha-6-D-mannoside beta-1,6-N-acetylglucosaminyltransferase
J. Biol. Chem.
267
2920-2927
1992
Rattus norvegicus
brenda
Granovsky, M.; Fode, C.; Warren, C.E.; Campbell, R.M.; Marth, J.D.; Pierce, M.; Fregien, N.; Dennis, J.W.
GlcNAc-transferase V and core 2 GlcNAc-transferase expression in the developing mouse embryo
Glycobiology
5
797-806
1995
Mus musculus
brenda
Khan, S.H.; Duus, J.O.; Crawley, S.C.; Palcic, M.M.; Hindsgaul, O.
Acceptor-substrate recognition by N-acetylglucosaminyltransferase-V: role of the mannose residue in beta-DGlcNAc(1->2)alpha-DMan(1->6)beta-DGlcOR
Tetrahedron
5
2415-2435
1994
Mesocricetus auratus
-
brenda
Korczak, B.; Le, T.; Elowe, S.; Datti, A.; Dennis, J.W.
Minimal catalytic domain of N-acetylglucosaminyltransferase V
Glycobiology
10
595-599
2000
Mus musculus
brenda
Park, C.; Jin, U.H.; Lee, Y.C.; Cho, T.J.; Kim, C.H.
Characterization of UDP-N-acetylglucosamine:alpha-6-D-mannoside beta-1,6-N-Acetylglucosaminyltransferase V from a Human Hepatoma Cell Line Hep3B
Arch. Biochem. Biophys.
367
281-288
1999
Homo sapiens
brenda
Saito, T.; Miyoshi, E.; Sasai, K.; Nakano, N.; Eguchi, H.; Honke, K.; Taniguchi, N.
A secreted type of beta 1,6-N-acetylglucosaminyltransferase V (GnT-V) induces tumor angiogenesis without mediation of glycosylation: a novel function of GnT-V distinct from the original glycosyltransferase activity
J. Biol. Chem.
277
17002-17008
2002
Homo sapiens
brenda
Sasai, K.; Ikeda, Y.; Eguchi, H.; Tsuda, T.; Honke, K.; Taniguchi, N.
The action of N-acetylglucosaminyltransferase-V is prevented by the bisecting GlcNAc residue at the catalytic step
FEBS Lett.
522
151-155
2002
Homo sapiens
brenda
Sasai, K.; Ikeda, Y.; Fujii, T.; Tsuda, T.; Taniguchi, N.
UDP-GlcNAc concentration is an important factor in the biosynthesis of beta1,6-branched oligosaccharides: Regulation based on the kinetic properties of N-acetylglucosaminyltransferase V
Glycobiology
12
119-127
2002
Homo sapiens
brenda
Takamatsu, S.; Inoue, N.; Katsumata, T.; Nakamura, K.; Fujibayashi, Y.; Takeuchi, M.
The relationship between the branch-forming glycosyltransferases and cell surface sugar chain structures
Biochemistry
44
6343-6349
2005
Homo sapiens
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Guo, P.; Wang, Q.Y.; Guo, H.B.; Shen, Z.H.; Chen, H.L.
N-acetylglucosaminyltransferase V modifies the signaling pathway of epidermal growth factor receptor
Cell. Mol. Life Sci.
61
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2004
Homo sapiens
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Chakraborty, A.K.; Pawelek, J.M.
GnT-V, macrophage and cancer metastasis: a common link
Clin. Exp. Metastasis
20
365-373
2003
Homo sapiens
brenda
Kaneko, M.; Alvarez-Manilla, G.; Kamar, M.; Lee, I.; Lee, J.K.; Troupe, K.; Zhang, W.; Osawa, M.; Pierce, M.
A novel beta(1,6)-N-acetylglucosaminyltransferase V (GnT-VB)(1)
FEBS Lett.
554
515-519
2003
Homo sapiens (Q09328), Homo sapiens
brenda
Kamar, M.; Alvarez-Manilla, G.; Abney, T.; Azadi, P.; Kumar Kolli, V.S.; Orlando, R.; Pierce, M.
Analysis of the site-specific N-glycosylation of beta1,6 N-acetylglucosaminyltransferase V
Glycobiology
14
583-592
2004
Homo sapiens
brenda
Dawson, G.; Moskal, J.R.; Dawson, S.A.
Transfection of 2,6 and 2,3-sialyltransferase genes and GlcNAc-transferase genes into human glioma cell line U-373 MG affects glycoconjugate expression and enhances cell death
J. Neurochem.
89
1436-1444
2004
Homo sapiens
brenda
Tomiie, M.; Isaka, S.; Miyoshi, E.; Taniguchi, N.; Kimura, T.; Ogita, K.; Tsutsui, T.; Shimoya, K.; Nakagawa, T.; Kondo, A.; Koyama, M.; Murata, Y.
Elevated expression of N-acetylglucosaminyltransferase V in first trimester human placenta
Biochem. Biophys. Res. Commun.
330
999-1004
2005
Homo sapiens
brenda
Fang, H.; Huang, W.; Xu, Y.Y.; Shen, Z.H.; Wu, C.Q.; Qiao, S.Y.; Xu, Y.; Yu, L.; Chen, H.L.
Blocking of N-acetylglucosaminyltransferase V induces cellular endoplasmic reticulum stress in human hepatocarcinoma 7721 cells
Cell Res.
16
82-92
2006
Homo sapiens
brenda
Nakahara, S.; Saito, T.; Kondo, N.; Moriwaki, K.; Noda, K.; Ihara, S.; Takahashi, M.; Ide, Y.; Gu, J.; Inohara, H.; Katayama, T.; Tohyama, M.; Kubo, T.; Taniguchi, N.; Miyoshi, E.
A secreted type of beta1,6 N-acetylglucosaminyltransferase V (GnT-V), a novel angiogenesis inducer, is regulated by gamma-secretase
FASEB J.
20
2451-2459
2006
Homo sapiens
brenda
Inamori, K.; Gu, J.; Ohira, M.; Kawasaki, A.; Nakamura, Y.; Nakagawa, T.; Kondo, A.; Miyoshi, E.; Nakagawara, A.; Taniguchi, N.
High expression of N-acetylglucosaminyltransferase V in favorable neuroblastomas: Involvement of its effect on apoptosis
FEBS Lett.
580
627-632
2006
Homo sapiens
brenda
Ito, Y.; Akinaga, A.; Yamanaka, K.; Nakagawa, T.; Kondo, A.; Dickson, R.B.; Lin, C.Y.; Miyauchi, A.; Taniguchi, N.; Miyoshi, E.
Co-expression of matriptase and N-acetylglucosaminyltransferase V in thyroid cancer tissues - its possible role in prolonged stability in vivo by aberrant glycosylation
Glycobiology
16
368-374
2006
Homo sapiens
brenda
Zhao, Y.; Nakagawa, T.; Itoh, S.; Inamori, K.; Isaji, T.; Kariya, Y.; Kondo, A.; Miyoshi, E.; Miyazaki, K.; Kawasaki, N.; Taniguchi, N.; Gu, J.
N-acetylglucosaminyltransferase III antagonizes the effect of N-acetylglucosaminyltransferase V on alpha3beta1 integrin-mediated cell migration
J. Biol. Chem.
281
32122-32130
2006
Homo sapiens
brenda
Macnaughtan, M.A.; Kamar, M.; Alvarez-Manilla, G.; Venot, A.; Glushka, J.; Pierce, J.M.; Prestegard, J.H.
NMR structural characterization of substrates bound to N-acetylglucosaminyltransferase V
J. Mol. Biol.
366
1266-1281
2007
Homo sapiens
brenda
Guo, P.; Chen, H.J.; Wang, Q.Y.; Chen, H.L.
Down regulation of N-acetylglucosaminyltransferase V facilitates all-transretinoic acid to induce apoptosis of human hepatocarcinoma cells
Mol. Cell. Biochem.
284
103-110
2006
Homo sapiens
brenda
Chakraborty, A.K.; Pawelek, J.
beta1,6-Branched oligosaccharides regulate melanin content and motility in macrophage-melanoma fusion hybrids
Melanoma Res.
17
9-16
2007
Mus musculus
brenda
Tsui, K.H.; Chang, P.L.; Feng, T.H.; Chung, L.C.; Sung, H.C.; Juang, H.H.
Evaluating the function of matriptase and N-acetylglucosaminyltransferase V in prostate cancer metastasis
Anticancer Res.
28
1993-1999
2008
Homo sapiens
brenda
Li, J.; Wang, X.M.; Wang, Q.; Yang, M.; Feng, X.C.; Shen, Z.H.
Down-regulation of N-acetylglucosaminyltransferase-V induces ER stress by changing glycosylation and function of GLUT1
Arch. Biochem. Biophys.
463
102-109
2007
Homo sapiens
brenda
Yamamoto, E.; Ino, K.; Miyoshi, E.; Shibata, K.; Takahashi, N.; Kajiyama, H.; Nawa, A.; Nomura, S.; Nagasaka, T.; Kikkawa, F.
Expression of N-acetylglucosaminyltransferase V in endometrial cancer correlates with poor prognosis
Br. J. Cancer
97
1538-1544
2007
Homo sapiens
brenda
Yang, X.; Li, J.; Geng, M.
N-acetylglucosaminyltransferase V modifies TrKA protein, regulates the receptor function
Cell. Mol. Neurobiol.
28
663-670
2008
Homo sapiens
brenda
Yamamoto, E.; Ino, K.; Miyoshi, E.; Inamori, K.I.; Abe, A.; Sumigama, S.; Iwase, A.; Kajiyama, H.; Shibata, K.; Nawa, A.; Kikkawa, F.
N-acetylglucosaminyltransferase V regulates extravillous trophoblast invasion through glycosylation of alpha5beta1 integrin
Endocrinology
150
990-999
2009
Homo sapiens
brenda
Cheung, P.; Pawling, J.; Partridge, E.A.; Sukhu, B.; Grynpas, M.; Dennis, J.W.
Metabolic homeostasis and tissue renewal are dependent on beta1,6GlcNAc-branched N-glycans
Glycobiology
17
828-837
2007
Mus musculus
brenda
Kyan, A.; Kamimura, N.; Hagisawa, S.; Hatakeyama, S.; Koie, T.; Yoneyama, T.; Arai, Y.; Nakagawa, H.; Nishimura, S.; Miyoshi, E.; Hashimoto, Y.; Ohyama, C.
Positive expressions of N-acetylglucosaminyltransferase-V (GnT-V) and beta1-6 branching N-linked oligosaccharides in human testicular germ cells diminish during malignant transformation and progression
Int. J. Oncol.
32
129-134
2008
Homo sapiens
brenda
Abbott, K.L.; Aoki, K.; Lim, J.M.; Porterfield, M.; Johnson, R.; ORegan, R.M.; Wells, L.; Tiemeyer, M.; Pierce, M.
Targeted glycoproteomic identification of biomarkers for human breast carcinoma
J. Proteome Res.
7
1470-1480
2008
Homo sapiens
brenda
Chakraborty, D.; Chakraborty, A.K.
Evidence for tyrosinase as a beta1,6 branch containing glycoprotein: substrate of GnT-V
Life Sci.
83
260-263
2008
Mus musculus
brenda
Zhao, Y.; Li, J.; Xing, Y.; Wang, J.; Lu, C.; Xin, X.; Geng, M.
N-acetylglucosaminyltransferase V mediates cell migration and invasion of mouse mammary tumor cells 4TO7 via RhoA and Rac1 signaling pathway
Mol. Cell. Biochem.
309
199-208
2008
Mus musculus
brenda
Kim, Y.S.; Hwang, S.Y.; Kang, H.Y.; Sohn, H.; Oh, S.; Kim, J.Y.; Yoo, J.S.; Kim, Y.H.; Kim, C.H.; Jeon, J.H.; Lee, J.M.; Kang, H.A.; Miyoshi, E.; Taniguchi, N.; Yoo, H.S.; Ko, J.H.
Functional proteomics study reveals that N-acetylglucosaminyltransferase V reinforces the invasive/metastatic potential of colon cancer through aberrant glycosylation on tissue inhibitor of metalloproteinase-1
Mol. Cell. Proteomics
7
1-14
2008
Homo sapiens
brenda
Guo, H.B.; Nairn, A.; Harris, K.; Randolph, M.; Alvarez-Manilla, G.; Moremen, K.; Pierce, M.
Loss of expression of N-acetylglucosaminyltransferase Va results in altered gene expression of glycosyltransferases and galectins
FEBS Lett.
582
527-535
2008
Mus musculus
brenda
Soleimani, L.; Roder, J.; Dennis, J.; Lipina, T.
Beta N-acetylglucosaminyltransferase V (Mgat5) deficiency reduces the depression-like phenotype in mice
Genes Brain Behav.
7
334-343
2008
Mus musculus
brenda
Guo, H.B.; Johnson, H.; Randolph, M.; Lee, I.; Pierce, M.
Knockdown of GnT-Va expression inhibits ligand-induced downregulation of the epidermal growth factor receptor and intracellular signaling by inhibiting receptor endocytosis
Glycobiology
19
547-559
2009
Homo sapiens
brenda
Alvarez-Manilla, G.; Troupe, K.; Fleming, M.; Martinez-Uribe, E.; Pierce, M.
Comparison of the substrate specificities and catalytic properties of the sister N-acetylglucosaminyltransferases, GnT-V and GnT-Vb (IX)
Glycobiology
20
166-174
2010
Homo sapiens
brenda
Kasuya, T.; Jung, J.; Kadoya, H.; Matsuzaki, T.; Tatemastu, K.; Okajima, T.; Miyoshi, E.; Tanizawa, K.; Kuroda, S.
In vivo delivery of bio-nanocapsules displaying L4-PHA isolectin to malignant tumors overexpressing N-acetylglucosaminyltransferase V
Hum. Gene Ther.
19
887-895
2008
Homo sapiens
brenda
Pinho, S.S.; Reis, C.A.; Paredes, J.; Magalhaes, A.M.; Ferreira, A.C.; Figueiredo, J.; Xiaogang, W.; Carneiro, F.; Gaertner, F.; Seruca, R.
The role of N-acetylglucosaminyltransferase III and V in the post-transcriptional modifications of E-cadherin
Hum. Mol. Genet.
18
2599-2608
2009
Homo sapiens
brenda
Chen, H.L.; Li, C.F.; Grigorian, A.; Tian, W.; Demetriou, M.
T cell receptor signaling co-regulates multiple Golgi genes to enhance N-glycan branching
J. Biol. Chem.
284
32454-32461
2009
Homo sapiens
brenda
Wang, C.; Li, Z.; Yang, Z.; Zhao, H.; Yang, Y.; Chen, K.; Cai, X.; Wang, L.; Shi, Y.; Qiu, S.; Fan, J.; Zha, X.
The effect of receptor protein tyrosine phosphatase kappa on the change of cell adhesion and proliferation induced by N-acetylglucosaminyltransferase V
J. Cell. Biochem.
109
113-123
2010
Homo sapiens
brenda
Xu, Y.Y.; Guan, D.Y.; Yang, M.; Wang, H.; Shen, Z.H.
All-trans-retinoic acid intensifies endoplasmic reticulum stress in N-acetylglucosaminyltransferase V repressed human hepatocarcinoma cells by perturbing homocysteine metabolism
J. Cell. Biochem.
109
468-477
2010
Homo sapiens
brenda
Takahashi, N.; Yamamoto, E.; Ino, K.; Miyoshi, E.; Nagasaka, T.; Kajiyama, H.; Shibata, K.; Nawa, A.; Kikkawa, F.
High expression of N-acetylglucosaminyltransferase V in mucinous tumors of the ovary
Oncol. Rep.
22
1027-1032
2009
Homo sapiens
brenda
Tian, H.; Miyoshi, E.; Kawaguchi, N.; Shaker, M.; Ito, Y.; Taniguchi, N.; Tsujimoto, M.; Matsuura, N.
The implication of N-acetylglucosaminyltransferase V expression in gastric cancer
Pathobiology
75
288-294
2008
Homo sapiens
brenda
Pinho, S.S.; Figueiredo, J.; Cabral, J.; Carvalho, S.; Dourado, J.; Magalhaes, A.; Gaertner, F.; Mendonca, A.M.; Isaji, T.; Gu, J.; Carneiro, F.; Seruca, R.; Taniguchi, N.; Reis, C.A.
E-cadherin and adherens-junctions stability in gastric carcinoma: Functional implications of glycosyltransferases involving N-glycan branching biosynthesis, N-acetylglucosaminyltransferases III and V
Biochim. Biophys. Acta
1830
2690-2700
2012
Homo sapiens (Q09328)
brenda
Miyoshi, E.; Terao, M.; Kamada, Y.
Physiological roles of N-acetylglucosaminyltransferase V (GnT-V) in mice
BMB Rep.
45
554-559
2012
Mus musculus
brenda
Kimura, A.; Terao, M.; Kato, A.; Hanafusa, T.; Murota, H.; Katayama, I.; Miyoshi, E.
Upregulation of N-acetylglucosaminyltransferase-V by heparin-binding EGF-like growth factor induces keratinocyte proliferation and epidermal hyperplasia
Exp. Dermatol.
21
515-519
2012
Mus musculus
brenda
Wei, T.; Liu, Q.; He, F.; Zhu, W.; Hu, L.; Guo, L.; Zhang, J.
The role of N-acetylglucosaminyltransferases V in the malignancy of human hepatocellular carcinoma
Exp. Mol. Pathol.
93
8-17
2012
Homo sapiens
brenda
Kamada, Y.; Mori, K.; Matsumoto, H.; Kiso, S.; Yoshida, Y.; Shinzaki, S.; Hiramatsu, N.; Ishii, M.; Moriwaki, K.; Kawada, N.; Takehara, T.; Miyoshi, E.
N-Acetylglucosaminyltransferase V regulates TGF-beta response in hepatic stellate cells and the progression of steatohepatitis
Glycobiology
22
778-787
2012
Mus musculus
brenda
Yang, H.M.; Yu, C.; Yang, Z.
N-Acetylglucosaminyltransferase V negatively regulates integrin alpha5beta1-mediated monocyte adhesion and transmigration through vascular endothelium
Int. J. Oncol.
41
589-598
2012
Homo sapiens
brenda
Lee, J.K.; Matthews, R.T.; Lim, J.M.; Swanier, K.; Wells, L.; Pierce, J.M.
Developmental expression of the neuron-specific N-acetylglucosaminyltransferase Vb (GnT-Vb/IX) and identification of its in vivo glycan products in comparison with those of its paralog, GnT-V
J. Biol. Chem.
287
28526-28536
2012
Mus musculus
brenda
Kim, Y.S.; Ahn, Y.H.; Song, K.J.; Kang, J.G.; Lee, J.H.; Jeon, S.K.; Kim, H.C.; Yoo, J.S.; Ko, J.H.
Overexpression and beta-1,6-N-acetylglucosaminylation-initiated aberrant glycosylation of TIMP-1: a double whammy strategy in colon cancer progression
J. Biol. Chem.
287
32467-32478
2012
Homo sapiens
brenda
Lee, J.H.; Kang, J.G.; Song, K.J.; Jeon, S.K.; Oh, S.; Kim, Y.S.; Ko, J.H.
N-Acetylglucosaminyltransferase V triggers overexpression of MT1-MMP and reinforces the invasive/metastatic potential of cancer cells
Biochem. Biophys. Res. Commun.
431
658-663
2013
Homo sapiens (Q09328)
brenda
Bubka, M.; Link-Lenczowski, P.; Janik, M.; Pochec, E.; Litynska, A.
Overexpression of N-acetylglucosaminyltransferases III and V in human melanoma cells. Implications for MCAM N-glycosylation
Biochimie
103
37-49
2014
Homo sapiens (Q09328), Homo sapiens
brenda
Wang, X.; He, H.; Zhang, H.; Chen, W.; Ji, Y.; Tang, Z.; Fang, Y.; Wang, C.; Liu, F.; Shen, Z.; Qin, J.; Zhu, Y.; Liu, H.; Xu, J.; Gu, J.; Qin, X.; Sun, Y.
Clinical and prognostic implications of beta1,6-N-acetylglucosaminyltransferase V in patients with gastric cancer
Cancer Sci.
104
185-193
2013
Homo sapiens (Q09328), Homo sapiens
brenda
Huang, C.; Huang, M.; Chen, W.; Zhu, W.; Meng, H.; Guo, L.; Wei, T.; Zhang, J.
N-acetylglucosaminyltransferase V modulates radiosensitivity and migration of small cell lung cancer through epithelial-mesenchymal transition
FEBS J.
282
4295-4306
2015
Homo sapiens
brenda
Liu, J.; Liu, H.; Zhang, W.; Wu, Q.; Liu, W.; Liu, Y.; Pan, D.; Xu, J.; Gu, J.
N-acetylglucosaminyltransferase V confers hepatoma cells with resistance to anoikis through EGFR/PAK1 activation
Glycobiology
23
1097-1109
2013
Homo sapiens (Q09328), Homo sapiens
brenda
Abdel Rahman, A.; Ryczko, M.; Nakano, M.; Pawling, J.; Rodrigues, T.; Johswich, A.; Taniguchi, N.; Dennis, J.
Golgi N-glycan branching N-acetylglucosaminyltransferases I, V and VI promote nutrient uptake and metabolism
Glycobiology
25
225-240
2015
Homo sapiens (Q09328), Homo sapiens
brenda
Dong, Z.; Zuber, C.; Pierce, M.; Stanley, P.; Roth, J.
Reduction in Golgi apparatus dimension in the absence of a residential protein, N-acetylglucosaminyltransferase V
Histochem. Cell Biol.
141
153-164
2014
Cricetulus griseus (P97259), Cricetulus griseus, Rattus norvegicus (Q08834)
brenda
Xu, Q.; Wang, W.; Qu, C.; Gu, J.; Yin, H.; Jia, Z.; Song, L.; Du, Y.
Chitosan oligosaccharides inhibit epithelial cell migration through blockade of N-acetylglucosaminyltransferase V and branched GlcNAc structure
Carbohydr. Polym.
170
241-246
2017
Homo sapiens (Q09328)
brenda
Huang, X.; Liu, T.; Wang, Q.; Zhu, W.; Meng, H.; Guo, L.; Wei, T.; Zhang, J.
Inhibition of N-acetylglucosaminyltransferase V enhances the cetuximab-induced radiosensitivity of nasopharyngeal carcinoma cells likely through EGFR N-glycan alterations
Glycobiology
27
713-725
2017
Homo sapiens (Q09328)
brenda
Cui, J.; Huang, W.; Wu, B.; Jin, J.; Jing, L.; Shi, W.P.; Liu, Z.Y.; Yuan, L.; Luo, D.; Li, L.; Chen, Z.N.; Jiang, J.L.
N-glycosylation by N-acetylglucosaminyltransferase V enhances the interaction of CD147/basigin with integrin beta1 and promotes HCC metastasis
J. Pathol.
245
41-52
2018
Homo sapiens (Q09328), Homo sapiens
brenda
Song, K.J.; Jeon, S.K.; Moon, S.B.; Park, J.S.; Kim, J.S.; Kim, J.; Kim, S.; An, H.J.; Ko, J.H.; Kim, Y.S.
Lectin from Sambucus sieboldiana abrogates the anoikis resistance of colon cancer cells conferred by N-acetylglucosaminyltransferase V during hematogenous metastasis
Oncotarget
8
42238-42251
2017
Homo sapiens (Q09328), Homo sapiens
brenda