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Information on EC 2.4.1.102 - beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase and Organism(s) Mus musculus and UniProt Accession Q5JCT0

for references in articles please use BRENDA:EC2.4.1.102
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EC Tree
IUBMB Comments
The enzyme catalyses the addition of N-acetyl-alpha-D-glucosamine to the core 1 structure of O-glycans forming core 2.
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This record set is specific for:
Mus musculus
UNIPROT: Q5JCT0
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
+
O3-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl]-L-seryl/threonyl-[protein]
=
+
O3-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-seryl/threonyl-[protein]
Synonyms
c2gnt, gcnt3, gcnt1, c2gnt-m, c2gnt1, core 2 glcnac-t, c2glcnact-i, c2gnt-1, c2gnt-l, core 2 beta-1,6-n-acetylglucosaminyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
core 2 beta-1,6 N-acetylglucosaminyltransferase
-
mucus-type core 2 beta1,6 N-acetylglucosaminyltransferase
-
acetylglucosaminyltransferase, uridine diphosphoacetylglucosamine-mucin beta-(1-6)-
-
-
-
-
acetylglucosaminyltransferase, uridine diphosphoacetylglucosamine-mucin beta-(1-6)-, A
-
-
-
-
beta6-N-acetylglucosaminyltransferase
-
-
-
-
C2GlcNAcT-I
-
-
C2GlcNAcT-II
-
-
C2GlcNAcT-III
-
-
C2GnT
C2GnT3
-
-
C4GnT
-
-
core 2 acetylglucosaminyltransferase
-
-
-
-
core 2 beta-1,6-N-acetylglucosaminyltransferase
core 2 beta1,6-N-acetyl-glycosaminyltransferase
-
-
core 2 beta1,6-N-acetylglucosaminyltransferase
core 2 beta1,6-N-acetylglucosaminyltransferase I
-
-
core 2 GlcNAc-T
-
-
core 2 N-acetylglucosaminyltransferase
-
-
core 2beta 1,6 N-acetylglucosaminyltransferase
-
-
core 6-beta-GlcNAc-transferase A
-
-
-
-
core2 1-6-N-glucosaminyltransferase-I
-
-
gcnt4
-
-
O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase I
-
-
-
-
uridine diphosphoacetylglucosamine-mucin beta-(1-6)-acetylglucosaminyltransferase
-
-
-
-
uridine diphosphoacetylglucosamine-mucin beta-(1-6)-acetylglucosaminyltransferase A
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-glucosamine + O3-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl]-L-seryl/threonyl-[protein] = UDP + O3-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-seryl/threonyl-[protein]
show the reaction diagram
C2GnT operates through an inverting mechanism following a SN2-like reaction in which the enzyme provides a catalytic base that activates the nucleophile (in C2GnT, this is the C6 hydroxyl group from a GalNAc residue) to displace the uridine 5'-diphosphate (UDP) leaving group from the UDP-GlcNAc donor in a concerted process. It is assumed that C2GnT follows the ordered bi-bi catalytic mechanism with the UDP-GlcNAc bindings first, followed by the disaccharide acceptor binding over the nucleotide sugar. Reaction mechanism, quantum mechanical/molecular modeling, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-alpha-D-glucosamine:O3-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl]-glycoprotein 6-beta-N-acetyl-D-glucosaminyltransferase (configuration-inverting)
The enzyme catalyses the addition of N-acetyl-alpha-D-glucosamine to the core 1 structure of O-glycans forming core 2.
CAS REGISTRY NUMBER
COMMENTARY hide
87927-97-7
-
95978-15-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-alpha-D-glucosamine + beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-R
UDP + beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl-R
show the reaction diagram
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-R
UDP + beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl-R
show the reaction diagram
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-benzyl
UDP + beta-D-galactosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,6)-N-acetyl-D- galactosaminyl-benzyl
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 3-deoxy-beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-benzyl
UDP + 3-deoxy-beta-D-galactosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,6)-N-acetyl-D-galactosaminyl-benzyl
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + 4-deoxy-beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-benzyl
UDP + 4-deoxy-beta-D-galactosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,6)-N-acetyl-D-galactosaminyl-benzyl
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + asialofetuin
?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + asialoglycophorin A
?
show the reaction diagram
-
best substrate
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,3-(6-deoxy)-N-acetyl-D-galactosaminyl-benzyl
?
show the reaction diagram
-
at high concentration inhibitory
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-(CH2)8CO2Me
UDP + beta-D-galactosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,6)-N-acetyl-D-galactosaminyl-(CH2)8CO2Me
show the reaction diagram
-
synthetic disaccharide
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-benzyl
UDP + beta-D-galactosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,6)-N-acetyl-D-galactosaminyl-benzyl
show the reaction diagram
-
requirement for the 4- and 6-hydroxyls of N-acetyl-galactosamine and the hydroxyl of galactose in the acceptor substrate
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R
UDP + beta-D-galactosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,6)-N-acetyl-D-galactosaminyl-R
show the reaction diagram
UDP-N-acetyl-D-glucosamine + Galbeta(1-3)GalNAcalpha-p-nitrophenol
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Galbeta1,3GalNAc-O-p-nitrophenyl
?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + Galbeta1-3GalNAcalpha-4-nitrophenyl
?
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + p-nitrophenyl 2-acetamido-2-deoxy-3-O-(beta-D-galactopyranosyl)-alpha-D-galactopyranoside
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-alpha-D-glucosamine + beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-R
UDP + beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl-R
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-R
UDP + beta-D-galactosyl-1,3-(N-acetyl-beta-D-glucosaminyl-1,6)-N-acetyl-D-galactosaminyl-R
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
activation
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
talniflumate
selectively binds to enzyme GCNT3 via three notable hydrogen bonds between talniflumate and GCNT3. Synthesis and in silico small molecular docking simulation, overview
beta-D-galactosyl-1,3-(6-deoxy)-N-acetyl-D-galactosaminyl-benzyl
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high concentration
Cu2+
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-
Mn2+
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slight inhibition
Zn2+
-
-
additional information
-
the mutant enzyme C217S is insensitive to DTNB, iodoacetamide, NEM, HgCl2 and ZnCl2
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytokines
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induction by IL-4 and IL-12/STAT4
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additional information
-
no induction by Ag+
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
3-deoxy-beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-benzyl
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-
3.1
4-deoxy-beta-D-galactosyl-1,3-N-acetyl-D-galactosaminyl-benzyl
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-
12
beta-D-galactosyl-1,3-(6-deoxy)-N-acetyl-D-galactosaminyl-benzyl
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-
2
beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-benzyl
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-
0.11 - 0.13
Galbeta(1-3)GalNAcalpha-p-nitrophenol
1.1 - 2.8
UDP-N-acetyl-D-glucosamine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
beta-D-galactosyl-1,3-(6-deoxy)-N-acetyl-D-galactosaminyl-benzyl
-
-
0.14 - 0.26
UDP
0.23
UMP
mutant enzyme C217S, in 50 mM Tris (pH 7.5), at 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.2
-
mutant enzyme C217S
9.2
-
wild-type enzyme
additional information
-
overview: enzyme activities with several substrates
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
genetically engineered Kras-driven mouse pancreatic tumors
Manually annotated by BRENDA team
-
Panc02 cells
Manually annotated by BRENDA team
-
CD8 T cell
Manually annotated by BRENDA team
-
wild-type and transgenic CD4+ T cell lines, induction by cytokines IL-4, and IL-12/STAT4
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
the mucin-synthesizing core 2 beta-1,6 N-acetylglucosaminyltransferase (GCNT3/C2GNT) plays a significant role in mucin biosynthesis
evolution
the enzyme belongs to the GT14 family
malfunction
metabolism
-
the enzyme is required for the generation of P-selectin
physiological function
additional information
quantum mechanical/molecular modeling using enzyme crystal structures, PDB IDs 2GAK and 2GAM, as templates. C2GnT may occur in an open conformation, and a closed conformation. The location of the C2GnT-conserved Glu320 residue structurally corresponds to the catalytic base found in other glycosyltransferases with the GT-A fold. The enzyme-substrate system (C2GnT-UDP-GlcNAc-Galb1-3GalNAc ternary complex) consists of 379 amino acids, eight water molecules, donor, and acceptor, active site model
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GCNT3_MOUSE
437
1
50698
Swiss-Prot
Secretory Pathway (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
the monomer units of the observed dimer C2GnT possesses the GT-A fold and are connected by a disulfide bond between the Cys235 residues, quantum mechanical/molecular modeling using enzyme crystal structures, PDB IDs 2GAK and 2GAM, as templates. The structure of C2GnT contains two regions; the first (38-121) is composed of alpha-helices. The second region, which corresponds to the catalytic domain (122-428), is an alpha/beta/alpha structure consisting of a central six-stranded mixed beta-sheet. Four disulfide bonds are found in each monomer (Cys151-Cys199, Cys372-Cys381, Cys59-Cys413, and Cys100-Cys172), the remaining Cys217 is unpaired and located in the donor binding site. C2GnT may occur in an open conformation, and a closed conformation. The location of the C2GnT-conserved Glu320 residue structurally corresponds to the catalytic base found in other glycosyltransferases with the GT-A fold
additional information
-
in absence of dithiothreitol, one of the two free Cys residues (Cys217 and Cys235) is found to be engaged in an intermolecular bridge causing dimerization of the protein
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
both Asn58 and Asn95 are glycosylated
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
C217S mutant in complex with UDP, hanging drop vapor diffusion method, using 24% (w/v) polyethylene glycol 4000, 0.1 M glycine (pH 9.0) and 0.6 M LiCl
hanging drop vapor diffusion method, X-ray crystal structures of murine C2GnT-L in the absence and presence of the acceptor substrate Galbeta1,3GalNAc at 2.0 and 2.7 A resolution, respectively
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C217S
K401A/C217S
inactive
R378A/C217S
inactive
R378A/K401A/C217S
inactive
S158C
-
mutation reduces C2GnT activity but does not affect substrate specificity or enzyme dimerization. Mutation appears to result in haploinsufficiency of C2GnT activity. C2GnT-I haploinsufficiency is sufficient for loss of core 2 O-glycan expression and galectin-1 resistance
additional information
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
inactivation during storage may be caused by air oxidation and points to a requirement for inmodified thiols in the core protein
-
659276
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
mutant enzyme C217S can be stored at 4°C for at least 3 months without any loss of activity, wild-type enzyme loses about 95% of its activity after 4 weeks
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
IgG-Sepharose bead chromatography
pilot scale, recombinant protein A-tagged enzyme, fluidized bed system
-
recombinant
-
single-step, affinity chromatography on UDP-hexanolamine Sepharose
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene GCNT3 expression analysis in pancreatic cancer and in healthy pancreatic tissue, gene expression profiling and transcriptome analysis
the recombinant protein generated by mC2GnT-M cDNA exhibits core 2, core 4, and blood group I enzyme activities with a ratio of 1.00:0.46:1.05
expression in PC12 cells
-
HH and BW5147 cells are transfected with either wild-type or mutant human C2GnT-I cDNA. Expression of C2GnT-I makes HH cells susceptible to galectin-1
-
mutant enzymes are expressed in HEK-293T cells
overexpression in CHO cells as protein A-tagged fusion protein
-
transfection in COS-7 cells
-
transfection into CD99 or mock transfectants
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
inhibitor talniflumate alone and in combination with low-dose gefitinib reduced GCNT3 expression, leading to the disrupted production of mucins in vivo and in vitro
activation-induced enzyme up-regulation under permissive (T helper type 1) conditions is strongly reduced by cyclosporin A
-
interleukin-12 induces enzyme expression
-
no expression in normal pancreatic tissue
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
-
chemical-enzymatic synthesis of sialyl-Lex-containing hexasaccharides found on O-linked glycoproteins, process involves several enzymes of the pathway
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Oehrlein, R.; Hindsgaul, O.; Palcic, M.M.
Use of the core-2-N-acetylglucosaminyltransferase in the chemical-enzymic synthesis of a sialyl-LeX-containing hexasaccharide found on O-linked glycoproteins
Carbohydr. Res.
244
149-159
1993
Mus musculus
Manually annotated by BRENDA team
Kuhns, W.; Rutz, V.; Paulsen, H.; Matta, K.L.; Baker, M.A.; Barner, M.; Granovsky, M.; Brockhausen, I.
Processing O-glycan core 1, Galb1-3GalNAca-R. Specificities of core 2, UDP-GlcNAc: Galbeta1-3GalNAc-R(GlcNAc to GalNAc) beta6-N-acetylglucosaminyltransferase and CMP-sialic acid: Galbeta1-3GalNAc-R alpha3-sialyltransferase
Glycoconjugate J.
10
381-394
1993
Gallus gallus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Zeng, S.; Dinter, A.; Eisenkratzer, D.; Biselli, M.; Wandrey, C.; Berger, E.G.
Pilot scale expression and purification of soluble protein A tagged beta1,6N-acetylglucosaminyltransferase in CHO cells
Biochem. Biophys. Res. Commun.
237
653-658
1997
Mus musculus
Manually annotated by BRENDA team
Koya, D.; Dennis, J.W.; Warren, C.E.; Takahara, N.; Schoen, F.J.; Nishio, Y.; Nakajima, T.; Lipes, M.A.; King, G.L.
Overexpression of core 2 N-acetylglycosaminyltransferase enhances cytokine actions and induces hypertrophic myocardium in transgenic mice
FASEB J.
13
2329-2337
1999
Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Lim, Y.C.; Xie, H.; Come, C.E.; Alexander, S.I.; Grusby, M.J.; Lichtman, A.H.; Luscinskas, F.W.
IL-12, STAT4-dependent up-regulation of CD4+ T cell core 2 beta-1,6-n-acetylglucosaminyltransferase, an enzyme essential for biosynthesis of P-selectin ligands
J. Immunol.
167
4476-4484
2001
Mus musculus
Manually annotated by BRENDA team
Yen, T.Y.; Macher, B.A.; Bryson, S.; Chang, X.; Tvaroska, I.; Tse, R.; Takeshita, S.; Lew, A.M.; Datti, A.
Highly conserved cysteines of mouse core 2 beta1,6-N-acetylglucosaminyltransferase I form a network of disulfide bonds and include a thiol that affects enzyme activity
J. Biol. Chem.
278
45864-45881
2003
Mus musculus
Manually annotated by BRENDA team
Merzaban, J.S.; Zuccolo, J.; Corbel, S.Y.; Williams, M.J.; Ziltener, H.J.
An alternate core 2 beta1,6-N-acetylglucosaminyltransferase selectively contributes to P-selectin ligand formation in activated CD8 T cells
J. Immunol.
174
4051-4059
2005
Mus musculus
Manually annotated by BRENDA team
Cabrera, P.V.; Amano, M.; Mitoma, J.; Chan, J.; Said, J.; Fukuda, M.; Baum, L.G.
Haploinsufficiency of C2GnT-I glycosyltransferase renders T lymphoma cells resistant to cell death
Blood
108
2399-2406
2006
Mus musculus
Manually annotated by BRENDA team
Pak, J.E.; Arnoux, P.; Zhou, S.; Sivarajah, P.; Satkunarajah, M.; Xing, X.; Rini, J.M.
X-ray crystal structure of leukocyte type core 2 beta1,6-N-acetylglucosaminyltransferase. Evidence for a convergence of metal ion-independent glycosyltransferase mechanism
J. Biol. Chem.
281
26693-26701
2006
Mus musculus
Manually annotated by BRENDA team
Hashimoto, M.; Tan, S.; Mori, N.; Cheng, H.; Cheng, P.W.
Mucin biosynthesis: molecular cloning and expression of mouse mucus-type core 2 beta1,6 N-acetylglucosaminyltransferase
Glycobiology
17
994-1006
2007
Mus musculus (Q5JCT0), Mus musculus
Manually annotated by BRENDA team
Wang, H.; Tang, R.; Zhang, W.; Amirikian, K.; Geng, Z.; Geng, J.; Hebbel, R.P.; Xia, L.; Marth, J.D.; Fukuda, M.; Katoh, S.; Huo, Y.
Core2 1-6-N-glucosaminyltransferase-I is crucial for the formation of atherosclerotic lesions in apolipoprotein E-deficient mice
Arterioscler. Thromb. Vasc. Biol.
29
180-187
2009
Mus musculus
Manually annotated by BRENDA team
Wang, J.; Shiratori, I.; Satoh, T.; Lanier, L.L.; Arase, H.
An essential role of sialylated O-linked sugar chains in the recognition of mouse CD99 by paired Ig-like type 2 receptor (PILR)
J. Immunol.
180
1686-1693
2008
Mus musculus (Q09324), Mus musculus
Manually annotated by BRENDA team
Stone, E.L.; Ismail, M.N.; Lee, S.H.; Luu, Y.; Ramirez, K.; Haslam, S.M.; Ho, S.B.; Dell, A.; Fukuda, M.; Marth, J.D.
Glycosyltransferase function in core 2-type protein O glycosylation
Mol. Cell. Biol.
29
3770-3782
2009
Mus musculus, Mus musculus (Q5JCT0)
Manually annotated by BRENDA team
Nagaraj, S.; Neumann, J.; Winzen, B.; Frank, S.; Ziske, C.; Sievers, E.; Koch, N.; Schmidt-Wolf, I.G.
Pancreas carcinoma antigen fused to invariant chain elicits T-cell response and tumor growth inhibition
Pancreas
37
321-327
2008
Mus musculus
Manually annotated by BRENDA team
Schroeter, M.F.; Ratsch, B.A.; Lehmann, J.; Baumgrass, R.; Hamann, A.; Syrbe, U.
Differential regulation and impact of fucosyltransferase VII and core 2 beta1,6-N-acetyl-glycosaminyltransferase for generation of E- and P-selectin ligands in murine CD4+ T cells
Immunology
137
294-304
2012
Mus musculus
Manually annotated by BRENDA team
Pak, J.E.; Satkunarajah, M.; Seetharaman, J.; Rini, J.M.
Structural and mechanistic characterization of leukocyte-type core 2 ?1,6-N-acetylglucosaminyltransferase: a metal-ion-independent GT-A glycosyltransferase
J. Mol. Biol.
414
798-811
2011
Mus musculus (Q09324)
Manually annotated by BRENDA team
Rao, C.; Janakiram, N.; Madka, V.; Kumar, G.; Scott, E.; Pathuri, G.; Bryant, T.; Kutche, H.; Zhang, Y.; Biddick, L.; Gali, H.; Zhao, Y.; Lightfoot, S.; Mohammed, A.
Small-molecule inhibition of GCNT3 disrupts mucin biosynthesis and malignant cellular behaviors in pancreatic cancer
Cancer Res.
76
1965-1974
2016
Homo sapiens (O95395), Homo sapiens, Mus musculus (Q5JCT0), Mus musculus, Mus musculus C57BL/6 (Q5JCT0)
Manually annotated by BRENDA team
Tvaroska, I.; Kozmon, S.; Wimmerova, M.; Koca, J.
A QM/MM investigation of the catalytic mechanism of metal-ion-independent core 2 beta1,6-N-acetylglucosaminyltransferase
Chemistry
19
8153-8162
2013
Mus musculus (Q09324)
Manually annotated by BRENDA team