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Information on EC 2.4.1.155 - alpha-1,6-mannosyl-glycoprotein 6-beta-N-acetylglucosaminyltransferase and Organism(s) Homo sapiens and UniProt Accession Q09328
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2.4.1.155 alpha-1,6-mannosyl-glycoprotein 6-beta-N-acetylglucosaminyltransferaseIUBMB Comments
Requires Mg2+. The enzyme, found in vertebrates, participates in the processing of N-glycans in the Golgi apparatus. It catalyses the addition of N-acetylglucosamine in beta 1-6 linkage to the alpha-linked mannose of biantennary N-linked oligosaccharides, and thus enables the synthesis of tri- and tetra-antennary complexes.
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Word Map
- 2.4.1.155
- n-glycans
- metastasis
- oligosaccharide
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n-linked
- glycosyltransferases
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n-glycosylation
- lectin
- udp-glcnac
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asparagine-linked
- trisaccharide
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bisect
- medicine
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beta1,6-branched
- gnt-ivs
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complex-type
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fucosyltransferase
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polylactosamine
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o-mannosylated
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tetra-antennary
- swainsonine
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leukoagglutinating
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glycomic
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glcnac-t
- diagnostics
- drug development
- pharmacology
- biotechnology
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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Synonyms
gnt-v, mgat5, n-acetylglucosaminyltransferase v, gnt-ix, gnt-vb, glcnact-v, n-acetylglucosaminyltransferase-v, gnt-va, beta1,6-n-acetylglucosaminyltransferase v, beta-1,6-n-acetylglucosaminyltransferase v, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Golgi beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase V
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N-acetylglucosaminyltransferase V
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acetylglucosaminyltransferase, uridine diphosphoacetylglucosamine-alpha-mannoside beta1-6-UDP-N-acetylglucosamine:alpha-mannoside-beta1,6 N-acetylglucosaminyltransferase
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alpha-1,3(6)-mannosylglycoprotein beta-1,6-N-acetylglucosaminyltransferase
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alpha-mannoside beta-1,6-N-acetylglucosaminyltransferase
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GnT-V
N-acetylglucosaminyltransferase V
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UDP-N-acetylglucosamine:a-mannoside beta-1,6-N-acetylglucosaminyltransferase
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GnT-V
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
hexosyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-alpha-D-glucosamine:N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)-beta-D-mannosyl-glycoprotein 6-beta-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
Requires Mg2+. The enzyme, found in vertebrates, participates in the processing of N-glycans in the Golgi apparatus. It catalyses the addition of N-acetylglucosamine in beta 1-6 linkage to the alpha-linked mannose of biantennary N-linked oligosaccharides, and thus enables the synthesis of tri- and tetra-antennary complexes.
CAS REGISTRY NUMBER
COMMENTARY
83588-90-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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]
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-
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?
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]
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-
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?
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
alpha-1-antitrypsin precursor + UDP-N-acetyl-D-glucosamine
?
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identified target protein for GnT-V in human colon cancer cell WiDr
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?
angiotensinogen preproprotein + UDP-N-acetyl-D-glucosamine
?
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identified target protein for GnT-V in human colon cancer cell WiDr
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-
?
beta-N-acetylhexosaminidase A + UDP-N-acetyl-D-glucosamine
?
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identified target protein for GnT-V in human colon cancer cell WiDr
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?
cathepsin D preproprotein + UDP-N-acetyl-D-glucosamine
?
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identified target protein for GnT-V in human colon cancer cell WiDr
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?
cathepsin X precursor + UDP-N-acetyl-D-glucosamine
?
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identified target protein for GnT-V in human colon cancer cell WiDr
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?
DDR1 variant protein + UDP-N-acetyl-D-glucosamine
?
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identified target protein for GnT-V in human colon cancer cell WiDr
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?
dipeptidyl peptidase 7 preproprotein + UDP-N-acetyl-D-glucosamine
?
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identified target protein for GnT-V in human colon cancer cell WiDr
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?
discoidin receptor tyrosine kinase + UDP-N-acetyl-D-glucosamine
?
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identified target protein for GnT-V in human colon cancer cell WiDr
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?
dystroglycan 1 precursor + UDP-N-acetyl-D-glucosamine
?
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identified target protein for GnT-V in human colon cancer cell WiDr
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?
galectin 3 binding protein + UDP-N-acetyl-D-glucosamine
?
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identified target protein for GnT-V in human colon cancer cell WiDr
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?
granulin isoform 1 precursor + UDP-N-acetyl-D-glucosamine
?
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identified target protein for GnT-V in human colon cancer cell WiDr
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?
heat shock protein 70 kDa protein 8 isoform 1 + UDP-N-acetyl-D-glucosamine
?
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identified target protein for GnT-V in human colon cancer cell WiDr
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?
heat shock protein gp96 precursor + UDP-N-acetyl-D-glucosamine
?
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identified target protein for GnT-V in human colon cancer cell WiDr
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?
heparan sulfate proteoglycan perlecan + UDP-N-acetyl-D-glucosamine
?
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identified target protein for GnT-V in human colon cancer cell WiDr
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?
hexosaminidase B preproprotein + UDP-N-acetyl-D-glucosamine
?
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identified target protein for GnT-V in human colon cancer cell WiDr
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?
human Fc binding protein + UDP-N-acetyl-D-glucosamine
?
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identified target protein for GnT-V in human colon cancer cell WiDr
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?
Ig kappa chain V-III + UDP-N-acetyl-D-glucosamine
?
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identified target protein for GnT-V in human colon cancer cell WiDr
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?
laminin gamma1 precursor + UDP-N-acetyl-D-glucosamine
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identified target protein for GnT-V in human colon cancer cell WiDr
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?
legumain preproprotein + UDP-N-acetyl-D-glucosamine
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identified target protein for GnT-V in human colon cancer cell WiDr
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?
met proto-oncogene + UDP-N-acetyl-D-glucosamine
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identified target protein for GnT-V in human colon cancer cell WiDr
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?
N-acetylgalactosamine-6-sulfatase + UDP-N-acetyl-D-glucosamine
?
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identified target protein for GnT-V in human colon cancer cell WiDr
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?
N-acetylglucosamine-6-sulfatase + UDP-N-acetyl-D-glucosamine
?
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identified target protein for GnT-V in human colon cancer cell WiDr
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?
prosaposin + UDP-N-acetyl-D-glucosamine
?
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identified target protein for GnT-V in human colon cancer cell WiDr
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?
protective protein for beta-galactosidase + UDP-N-acetyl-D-glucosamine
?
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identified target protein for GnT-V in human colon cancer cell WiDr
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?
protein tyrosine phosphatase kappa + UDP-N-acetyl-D-glucosamine
?
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identified target protein for GnT-V in human colon cancer cell WiDr
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?
protein-tyrosine kinase-related receptor PTK7 + UDP-N-acetyl-D-glucosamine
?
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identified target protein for GnT-V in human colon cancer cell WiDr
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?
ribonuclease T2 precursor + UDP-N-acetyl-D-glucosamine
?
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identified target protein for GnT-V in human colon cancer cell WiDr
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?
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 + ?
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?
tissue inhibitor of metalloproteinase-1 + UDP-N-acetyl-D-glucosamine
?
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identified target protein for GnT-V in human colon cancer cell WiDr
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?
tumor-associated calcium signal transducer 1 + UDP-N-acetyl-D-glucosamine
?
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identified target protein for GnT-V in human colon cancer cell WiDr
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?
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
?
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?
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 + ?
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?
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
?
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?
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
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?
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
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?
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
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?
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
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?
UDP-N-acetyl-D-glucosamine + GlcNAcbeta(1-2)Manalpha1-O-benzyl
UDP + GlcNAcbeta(1-2)[GlcNAcbeta(1-6)]Manalpha1-O-benzyl
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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
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
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?
Zn-alpha-2-glycoprotein + UDP-N-acetyl-D-glucosamine
?
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identified target protein for GnT-V in human colon cancer cell WiDr
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?
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
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?
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
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?
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
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?
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
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?
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
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catalyzes the formation of beta-1-6 GlcNAc branches on asparagine-linked oligosaccharides, which is directly linked to tumorigenesis
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?
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
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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
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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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?
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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best substrates are bi- and tri-antennary acceptors
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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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most active towards biantennary sugars
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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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enzyme also uses bisected oligosaccharides
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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
-
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
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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
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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
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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
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involved in biosynthesis of branched N-glycopeptides
-
-
?
additional information
?
-
synthesis of N-linked beta(1,6)-branched glykans
-
-
?
additional information
?
-
-
synthesis of N-linked beta(1,6)-branched glykans
-
-
?
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
?
-
-
ADP-glucose, CDP-glucose and GDP-glucose do not act as glycosyl donor
-
-
?
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
-
-
?
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
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 + 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-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 + 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 + 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
-
-
?
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
?
-
-
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
chitosan oligosaccharides (COS) with a degree of polymerization (DP) of 2-6 inhibit breast epithelial cell migration through downregulation of GnT-V and its products, branched N-glycans. Antimetastatic potency of COS and the underlying mechanism, overview. COS may serve as a potential therapeutic candidate for the treatment of metastatic breast cancer. Glycosyltransferase-modified N-glycan structures can modulate cell migration and thereby cancer metastasis as well
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.28 - 2.4
GlcNAc-beta(1-2)Man-alpha(1-3)(GlcNAc-beta(1-2)Man-alpha(1-4))Man-beta(1-4)GlcNAc-2-amino pyridine
0.133
GlcNAcbeta(1->2)Manalpha(1->3)-[GlcNAcbeta(1->2)Manalpha(1->6)]-Manbeta(1->4)GlcNAcbeta(1->4)GlcNAc-pyridylamine
-
-
-
0.13 - 0.23
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
1.28
GlcNAc-beta(1-2)Man-alpha(1-3)(GlcNAc-beta(1-2)Man-alpha(1-4))Man-beta(1-4)GlcNAc-2-amino pyridine
-
Hep2G cell, pH 7.0, 37°C
2.4
GlcNAc-beta(1-2)Man-alpha(1-3)(GlcNAc-beta(1-2)Man-alpha(1-4))Man-beta(1-4)GlcNAc-2-amino pyridine
-
Hep3B cell, pH 7.0, 37°C
0.13
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
-
with TDP-glucose
0.15
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
-
with UDP-N-acetylglucosamine
0.18
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
-
-
0.23
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
-
with UDP-glucose
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
immunohistochemic analysis of 313 clinical samples, overview
non-tumor tissue shows strong expression of MGAT5, immunohistochemic analysis
-
higher expression of GnT-V is correlated with a favorable prognosis for neuroblastoma patients. GnT-V may cause these tumors to regress by increasing their susceptibility to apoptosis
additional information
-
localized in the trophoblast layer. Both protein expression and the enzyme activity of GnT-V in first trimester placentas are higher than those at term. These results suggest that GnT-V would contribute to placentation in the early phase of pregnancy, possibly regulating the process of invasion of trophoblast cells
additional information
quantitative enzyme expression analysis in cancer cells, overview
additional information
CNE-2 cells express 7.5fold and 2.30fold higher levels of GnT-V mRNA and protein than HNE-1 cells, and CNE-1 cells express 1.41fold and 1.36fold higher levels of GnT-V mRNA and protein than HNE-1 cells
additional information
transcriptome analysis. Overexpression of the MGAT5 gene has been found in various tumor cells and tissues
additional information
-
transcriptome analysis. Overexpression of the MGAT5 gene has been found in various tumor cells and tissues
additional information
-
macrophage fusion hybrids with Cloudman S91 mouse melanoma cells
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
fusion with signal peptide from baculoviral protein to permit secretion into medium
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
physiological function
additional information
-
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
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
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
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
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
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
malfunction
-
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
-
enzyme down-regulation inhibits the proliferation, migration and invasion of the Hep-G2 cells
malfunction
-
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
physiological function
-
involved in the malignant potential of mucinous ovarian cancer
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
-
N-acetylglucosaminyltransferase V expression is closely associated with metastasis in vivo
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
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). MGT5A_HUMAN
741
1
84543
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
-
Golgi-resident GnT-V is cleaved mainly in the transmembrane region by gamma-secretase, followed by its secretion
glycoprotein
-
amino acids N334, N433 and N447 are glycosylated. N334 contains a biantennary structure with one or two terminating sialic acids. N433 and N447 contain structures that range from biantennary with two sialic acids to tetraantennary terminating with four sialic acids
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
enzyme downregulation in cancer cells by specific shRNA expression
additional information
generation of a stable BEL7404 Tet-on-Mgat5 cell line in which human Mgat5 can be specifically induced by doxycycline to explore functional alterations after Mgat5 overexpression
additional information
-
generation of a stable BEL7404 Tet-on-Mgat5 cell line in which human Mgat5 can be specifically induced by doxycycline to explore functional alterations after Mgat5 overexpression
additional information
GlcNAc and tet-induced Mgat5 increases the levels of many metabolites in HeLa cells, and HEK293 cells, and tet-induced Mgat5 changes in the N-glycan distributions, N-glycans profiles of transgenic HeLa and HEK-293 cells, overview. Tet-inducible Mgat5 enhances amino acid uptake and growth in nutrient-poor conditions and complex-type N-glycan branching in HEK293 Mgat5 clones. Up-regulation of Mgat5 in HEK293 cells stimulates amino acid uptake and increases metabolite levels under low Gln/Glc culture conditions
additional information
-
GlcNAc and tet-induced Mgat5 increases the levels of many metabolites in HeLa cells, and HEK293 cells, and tet-induced Mgat5 changes in the N-glycan distributions, N-glycans profiles of transgenic HeLa and HEK-293 cells, overview. Tet-inducible Mgat5 enhances amino acid uptake and growth in nutrient-poor conditions and complex-type N-glycan branching in HEK293 Mgat5 clones. Up-regulation of Mgat5 in HEK293 cells stimulates amino acid uptake and increases metabolite levels under low Gln/Glc culture conditions
additional information
GnT-V overexpression induces an aberrant E-cadherin cellular localization and alters cell morphology, GnT-V increases the stability of the cadherin/catenin complex, GnT-V leads to a reduced intercellular adhesion of gastric cells, phenotype, overview
additional information
GnT-V enzyme silencing by siRNA in Huh-7 and HepG2 cells
additional information
-
GnT-V enzyme silencing by siRNA in Huh-7 and HepG2 cells
additional information
GnT-V is used as a molecular target to further sensitize cetuximab-treated nasopharyngeal carcinoma (NPC) cells to radiation. Development of GnT-V-suppressed cell models, denoted CNE1-1564, CNE1-2224, CNE2-1564 and CNE2-2224. Lentivirus-mediated shRNA inhibits GnT-V mRNA and protein expression in NPC cell lines. The expression levels of GnTV-V mRNA in these cell models were 36.3%, 33.9%, 42% and 35.5% of the levels found in the control groups, respectively. Similarly, the GnT-V protein levels in the CNE1-1564, CNE1-2224, CNE2-1564 and CNE2-2224 cell models are decreased by 60.13%, 59.89%, 43.67% and 46.18%, respectively. GnT-V expression and depletion of GnT-V in nasopharyngeal carcinoma cells, phenotypes, overview. Changes in the radiosensitivity of CNE-1 and CNE-2 cells are also related to PI3K/Akt signaling. The total Akt level does not vary among the different groups, but the phospho-Akt and phospho-PI3K levels present differences: the phospho-Akt and phospho-PI3K levels in CNE2-1564 and CNE2-2224 cells are lower than those in CNE-2-NC, and the levels detected in CNE2-1564/cetuximab and CNE2-2224/cetuximab are lower than those found in CNE2-1564 and CNE2-2224 cells. CNE2-NC/cetuximab cells present reduced levels of phospho-Akt and phospho-PI3K compared with CNE2-NC cells. The CNE-1 cells present similar results. In brief, the irradiation-induced alteration of beta-1,6 branches on the EGFR might influence PI3K/AKT signaling
additional information
MGAT5 gene knockout in HT-29 cells using CRISPR/Cas9
additional information
-
overexpression of GnT-V, change in glycosylation of receptor protein tyrosine phosphatase kappa, decrease of cell calcium-independent adhesion, increase of tyrosine phosphorylation level of beta-catenin
additional information
-
silencing of the enzyme by expression of short hairpin RNAs specific to Gnt-V in small cell lung cancer cell lines H1688 and H146
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene expression profiling of cells is conducted by DNA microarray analysis
gene MGAT5, quantitative real-time PCR enzyme expression analysis
gene MGAT5, real-time RT-PCR enzyme expression analysis, establishing of human melanoma cell line WM-266-4 with induced stable overexpression of GnT-V, the cells show ncreased amounts of bisected and beta1-6 branched N-glycans on melanoma cell adhesion molecule MCAM/MUC18, but do not display significant differences in viability and capabilities to migrate through an endothelial layer, coexpression with MGAT3 gene, EC 2.4.1.144
gene MGAT5, recombinant expression of enzyme Gnt-V in CNE-1 and CNE-2 cells using the lentiviral transfection method
gene MGAT5, recombinant tet-inducible expression of Flag-tagged GlcNAcT-V in HeLa and HEK293 cells. Tet-induced Mgat5 HEK293 cells display a 2fold increase in tri-antennary and a 2fold increase in tetraantennary N-glycans
Huh7 and HepG2 cells are transiently transfected by both Mgat5 expression vector plasmid and empty vector plasmid as a control
stable overexpression of N-acetylglucosaminyltransferase V (GnT-V) in breast cancer MCF-10A cell line
a recombinant vector MGAT5-pCXNneo is constructed for transfection of WiDr cells
-
fusion with signal peptide from baculoviral protein to permit secretion into medium, BVVdelta73 and BVV delta188
-
gene MGAT5, quantitative real-time PCR enzyme expression analysis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
chitosan oligosaccharides (COS) inhibit the protein expression of GnT-V in a dose dependent manner
the PI3K/Akt signaling pathway is involved in regulation of GnT-V expression
during interferon-gamma-induced inflammation, the level of GnT-V in THP-1 monocytes are significantly decreased
-
high GnT-V expression correlated with FIGO surgical stage, strong immunostaining in mucinous adendocarcinoma
-
selective knockdown of GnT-Va expression, inhibition of ligand-induced downregulation of the epidermal growth factor receptor and intracellular signaling by inhibiting receptor endocytosis
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
the enzyme is useful as diagnostic marker for gastric adenocarcinomas: low intratumoral MGAT5 density is associated with poor differentiation, N classification, TNM stage, and Kiel stage, and is an independent prognosticator for poor overall survival. The combination of intratumoral MGAT5 expression and TNM or Kiel staging systems has a better predictive power for overall survival. Applying the prognostic value of intratumoral MGAT5 density to TNM stage III+IV and Kiel stage IIIB+IV groups shows a better risk stratification for overall survival in patients with late-stage gastric cancer, overview
drug development
COS may serve as a potential therapeutic candidate for the treatment of metastatic breast cancer
medicine
radiotherapy combining GnT-V down-regulation and cetuximab decelerates tumor growth
biotechnology
-
transfection of sense cDNA of enzyme results in increase in the N-acetylglucosamine-beta1,6-mannose-alpha1,3-branch of epidermal growth factor receptor. Transfection with antisense CDNA of enzyme rsults in reverse reaction. Altered expression of enzyme will change the glycan structure and function of epidermal growth factor receptor, which may modify downstream signal transduction
medicine
pharmacology
-
the work is a step toward intriguing innovative therapeutic strategies for trials currently in consider with glycosyltransferase in neurodegenerative disorders
additional information
-
an elevation of enzyme Gnt-V activity leads to radiosensitivity and migration of small cell lung cancer cells by inducing epithelial-mesenchymal transition, EMT, thereby highlighting Gnt-V as a potential therapeutic target for the prevention of EMT-associated tumour radioresistance and migration
medicine
-
link between elevated expression of enzyme and malignant transformation, macrophage fusion hybrids with Cloudman S91 mouse melanoma cells are highly metastatic in vivo, motile in vitro and express macrophage-associated traits of increased enzyme activity, beta1,6-branching and polylactosamine content
medicine
-
a selective inhibitor for this GnT-V secretion, a gamma-secretase inhibitor, could provide a useful strategy for the inhibition of tumor angiogenesis and progression
medicine
-
higher expression of GnT-V is correlated with a favorable prognosis for neuroblastoma patients. GnT-V may cause these tumors to regress by increasing their susceptibility to apoptosis
medicine
-
prognosis of thyroid carcinoma after surgery is not correlated with the expression GnT-V because the levels of expression is quite low in anaplastic (undifferentiated) carcinomas
medicine
-
a simple glycoproteomic strategy to identify the glycoproteins from breast tissue that bind to the lectin L-phytohemagglutinin is developed
medicine
-
GnT-V and beta1-6 branching N-linked oligosaccharide expressions are downregulated during carcinogenesis and progression of human testicular germ cell tumors, GnT-V may be a promising recurrence predictor for stage I non-seminomatous germ cell tumors
medicine
-
high GnT-V expression is correlated with impaired clinical outcome in endometrial cancer patients, GnT-V is an independent prognostic factor for progression-free survival
medicine
-
knowledge of the biological behavior of metalloproteinases and tissue inhibitor of metalloproteinases and the roles in various diseases have an eventual goal of therapeutic uses and clinical trials of anti-cancer agents
medicine
-
the study demonstrates the effect of down-regulating GnT-V on glucose uptake and provides a new mechanistic link between GnT-V and GLUT1, since ER stress may cause apoptosis of tumor cells, selective modulation of GLUT1 may be a useful pro-apoptotic strategy for liver or other cancers
medicine
-
GnT-V expression correlated with a poor prognosis in gastric cancer patients due to metastases
medicine
-
enzyme expression is positively related with malignancy in HCC. The enzyme is both a differentiation marker and a potential target for the treatment of hepatocellular carcinoma
medicine
-
the enzyme is a potential therapeutic target for vascular inflammatory conditions
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
J. Biochem.
113
614-619
1993
Homo sapiens
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
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
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
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
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
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
1795-1804
2004
Homo sapiens
Chakraborty, A.K.; Pawelek, J.M.
GnT-V, macrophage and cancer metastasis: a common link
Clin. Exp. Metastasis
20
365-373
2003
Homo sapiens
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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)
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
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
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
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)
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
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
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
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
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
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)
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)
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
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
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