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UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
-
acetylgalactosaminyltransferase, uridine diphosphoacetylgalactosamine-glycoprotein
-
-
-
-
GalNAc-transferase
-
-
-
-
glycoprotein acetylgalactosaminyltransferase
-
-
-
-
polypeptide-N-acetylgalactosamine transferase
-
-
-
-
protein-UDP acetylgalactosaminyltransferase
-
-
-
-
UDP-acetylgalactosamine-glycoprotein acetylgalactosaminyltransferase
-
-
-
-
UDP-acetylgalactosamine:peptide-N-galactosaminyltransferase
-
-
-
-
UDP-GalNAc:polypeptide N-acetylgalactosaminyl transferase
-
-
-
-
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9
-
-
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase
-
-
-
-
UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T10
-
-
UDP-N-acetylgalactosamine-glycoprotein N-acetylgalactosaminyltransferase
-
-
-
-
UDP-N-acetylgalactosamine-protein N-acetylgalactosaminyltransferase
-
-
-
-
UDP-N-acetylgalactosamine:kappa-casein polypeptide N-acetylgalactosaminyltransferase
-
-
-
-
UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferase
-
-
-
-
UDP-N-acetylgalactosamine:protein N-acetylgalactosaminyl transferase
-
-
-
-
uridine diphosphoacetylgalactosamine-glycoprotein acetylgalactosaminyltransferase
-
-
-
-
ppGaNTase-T1
-
-
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
-
-
-
-
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
-
-
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
-
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UDP-N-acetyl-D-galactosamine + PTTDSTTPAPTTK
UDP + ?
enzyme form ppGaNTase-T5
-
-
?
UDP-GalNAc + apomucin
UDP + GalNAc-mucin
apomucin is a deglycosylated bovine submaxillary mucin, mutants W328Y, W328F, W328A, W316H and W316A are inactive, mutants W316Y and W316F show 40% and 20% activity, respectively, relative to wild-type
-
-
?
UDP-GalNAc + GVVPTVVPG
UDP + GVVP(GalNAc)TVVPG
GVVPTVVPG is a synthetic peptide with threonine as acceptor site, weaker acceptor substrate for wild-type and truncated version P-T1/delta42 as PPDAATAAPL
-
-
?
UDP-GalNAc + PPDAATAAPL
UDP + PPDAA(GalNAc)TAAPL
PPDAATAAPL is a synthetic peptide with threonine as acceptor site, efficient acceptor substrate for wild-type and truncated version P-T1/delta42
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + Gly-Val-Val-Pro-Thr-Val-Val-Pro-Gly
?
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + Pro-Pro-Asp-Ala-Ala-Thr-Ala-Ala-Pro-Leu
?
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + A1 protein
UDP + N-acetyl-D-galactosaminyl-A1 protein
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + apoantifreeze glycoproteins
UDP + N-acetyl-D-galactosaminyl-apoantifreeze glycoproteins
-
apoantifreeze glycoprotein of high molecular weight accepts GalNAc much faster than apoantifreeze glycoprotein 8
-
-
?
UDP-N-acetyl-D-galactosamine + apofetuin
UDP + N-acetyl-D-galactosaminyl-apofetuin
-
lowest rate of transfer
-
-
?
UDP-N-acetyl-D-galactosamine + apomucin
UDP + N-acetyl-D-galactosaminyl-apomucin
UDP-N-acetyl-D-galactosamine + GalNAc-glycosylated peptide
UDP + N-acetyl-D-galactosaminyl-GalNAc-glucosylated peptide
UDP-N-acetyl-D-galactosamine + GTTPSPVPTTS-(O-GalNAc)T-SAP
UDP + ?
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + kappa-casein
UDP + N-acetyl-D-galactosaminyl-kappa-casein
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
UDP-N-acetyl-D-galactosamine + PTTDS-(O-GalNAc)T-TPAPTTK
UDP + ?
-
38.7% of the activity with GTTPSPVPTTS-(O-GalNAc)T-TSAP
-
-
?
UDP-N-acetyl-D-galactosamine + PTTDSTTPAPTTK
UDP + ?
additional information
?
-
UDP-N-acetyl-D-galactosamine + apomucin
UDP + N-acetyl-D-galactosaminyl-apomucin
-
enzymatically prepared apomucin accepts GalNAc much faster than chemically prepared apomucin
-
-
?
UDP-N-acetyl-D-galactosamine + apomucin
UDP + N-acetyl-D-galactosaminyl-apomucin
-
deglycosylated bovine submaxillary mucin
-
-
?
UDP-N-acetyl-D-galactosamine + apomucin
UDP + N-acetyl-D-galactosaminyl-apomucin
-
GalNAc-T1
-
-
?
UDP-N-acetyl-D-galactosamine + GalNAc-glycosylated peptide
UDP + N-acetyl-D-galactosaminyl-GalNAc-glucosylated peptide
ppGaNTase-T9: acceptors are di- and triglycosylated MUC5AC and mono-glycosylated EA2, obtained by prior action of ppGaNTase-T1, but not the unmodified peptides, formation of a tetra-glycopeptide species from MUC5AC triglycopeptide substrate, ppGaNTase-T7 forms a hexa-glycopeptide species
-
-
?
UDP-N-acetyl-D-galactosamine + GalNAc-glycosylated peptide
UDP + N-acetyl-D-galactosaminyl-GalNAc-glucosylated peptide
-
GalNAc-T1 may also specifically recognize and glycosylate partially glycosylated acceptors
-
-
?
UDP-N-acetyl-D-galactosamine + GalNAc-glycosylated peptide
UDP + N-acetyl-D-galactosaminyl-GalNAc-glucosylated peptide
ppGaNTase-T6 requires at least 2 intact GalNAc residues in the substrate, acceptor: MUC5AC-glycopeptide, obtained by the action of ppGaNTase-T1
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
GalNAc-T1: Asp-144 is the most important site for GalNAc recognition, primarily recognizes the UDP portion of UDP-GalNAc
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
only UDP-GalNAc serves as sugar donor
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
acceptors: apomucin, kappa-casein
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
acceptors: A1 protein, apofetuin, apoantifreeze glycoproteins, frequent glycosylation of the abundant serine plus threonine residues of mucins
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
ppGaNTase-T1: acceptor is MUC5AC peptide, di-glycopeptide contains GalNAc at Thr-3 and -13, tri-glycopeptide an additional one at Ser-5
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
transfer of GalNAc to a serine or threonine residue on the acceptor protein
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
transfer of GalNAc to a serine or threonine residue on the acceptor protein
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
diversely regulated ppGaNTase family may play a role in the various processes governing development
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
GalNAc-T1 glycosylates unmodified polypeptides in vivo
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
different enzyme activities are involved in the initiation of GalNAc O-glycosylation and these are differentially expressed in cells and organs
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
O-glycosylation by ppGaNTase-Ts of multisite substrates may proceed in a specific hierarchical manner
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
the enzyme is involved in the normal development of the brain through O-glycosylation of proteins in the neurons
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
UDP-N-acetyl-D-galactosamine + PTTDSTTPAPTTK
UDP + ?
enzyme form ppGaNTase-T1
-
-
?
UDP-N-acetyl-D-galactosamine + PTTDSTTPAPTTK
UDP + ?
enzyme form ppGaNTase-T3
-
-
?
UDP-N-acetyl-D-galactosamine + PTTDSTTPAPTTK
UDP + ?
enzyme form ppGaNTase-T4
-
-
?
additional information
?
-
-
not: lacto-N-fucopentaose I, ceramide dihexosides, ceramide trihexosides, globoside
-
-
?
additional information
?
-
-
contains a lectin-like repeat sequence at the C-terminus, role of GalNAc-T1 lectin domain, which is involved in glycosylation of substrates with multiple acceptor sites
-
-
?
additional information
?
-
multiple enzyme isoforms
-
-
?
additional information
?
-
multiple enzyme isoforms
-
-
?
additional information
?
-
ppGaNTase-T6: no activity with unglycosylated peptides
-
-
?
additional information
?
-
9 isoforms, ppGaNTase-T9 contains a 480-amino acid conserved region and shows no activity with non-glycosylated peptides
-
-
?
additional information
?
-
-
existence of multiple enzyme activities, differentially expressed in different organs, at least 2 distinct enzyme specificities
-
-
?
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UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
diversely regulated ppGaNTase family may play a role in the various processes governing development
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
GalNAc-T1 glycosylates unmodified polypeptides in vivo
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
different enzyme activities are involved in the initiation of GalNAc O-glycosylation and these are differentially expressed in cells and organs
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
O-glycosylation by ppGaNTase-Ts of multisite substrates may proceed in a specific hierarchical manner
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
the enzyme is involved in the normal development of the brain through O-glycosylation of proteins in the neurons
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
mucin-type O-linked glycosylation of serine or threonine residues
-
-
?
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0.113
PTTDSTTPAPTTK
enzyme form ppGaNTase-T5
0.8
Gly-Val-Val-Pro-Thr-Val-Val-Pro-Gly
-
GalNAc-T1
0.0209
GTTPSPVPTTS-(O-GalNAc)T-SAP
-
pH 7.0, 37°C
0.2
Pro-Pro-Asp-Ala-Ala-Thr-Ala-Ala-Pro-Leu
-
GalNAc-T1
0.1058
PTTDS-(O-GalNAc)T-TPAPTTK
-
pH 7.0, 37°C
0.042 - 1.02
PTTDSTTPAPTTK
0.0141
UDP-N-acetyl-D-galactosamine
-
pH 7.0, 37°C
additional information
apomucin
-
1.74
GVVPTVVPG
+/-0.3 mM, truncated wild-type P-T1/delta42
16
GVVPTVVPG
+/-0.3 mM, mutant W316Y, 9.2 times higher than wild-type
17.6
GVVPTVVPG
+/-0.5 mM, mutant W316F, 10.1 times higher than wild-type
0.35
PPDAATAAPL
+/-0.05 mM, truncated wild-type P-T1/delta42
13.5
PPDAATAAPL
+/-0.7 mM, mutant W316Y, 38.5 times higher than wild-type
15.6
PPDAATAAPL
+/-0.6 mM, mutant W316F, 44.6 times higher than wild-type
0.042
PTTDSTTPAPTTK
enzyme form ppGaNTase-1
0.229
PTTDSTTPAPTTK
enzyme form ppGaNTase-3
1.02
PTTDSTTPAPTTK
enzyme form ppGaNTase-T4
0.0417
UDP-GalNAc
-
-
3.6
UDP-GalNAc
-
GalNac-T1 mutant N465A
4
UDP-GalNAc
-
GalNac-T1 mutant G455Q
4.4
UDP-GalNAc
-
GalNac-T1 triple mutant D444A/D484A/D525A
5.1
UDP-GalNAc
-
GalNac-T1 mutants D444A and P-deltaN42
5.1
UDP-GalNAc
+/-0.8 mM, truncated wild-type P-T1/delta42
5.2
UDP-GalNAc
+/-0.1 mM, mutant Y302L
5.4
UDP-GalNAc
-
GalNac-T1 mutant F457A
6.1
UDP-GalNAc
-
GalNac-T1 mutant Q466A
6.2
UDP-GalNAc
+/-0.6 mM, mutant F325L, 1.2 times higher than wild-type
9
UDP-GalNAc
+/-0.1 mM, mutant W316Y, 1.8 times higher than wild-type
9.1
UDP-GalNAc
+/-0.7 mM, mutant W316F, 1.8 times higher than wild-type
14.2
UDP-GalNAc
+/-1.1 mM, mutant F303L, 2.8 times higher than wild-type
16
UDP-GalNAc
+/-0.3 mM, mutant Y309L, 3.2 times higher than wild-type
additional information
apomucin
13.6 +/-1.9 mg/ml, mutant F303L, 2.8 times higher than wild-type
-
additional information
apomucin
17.4 +/-3.6 mg/ml, mutant W316Y, 3.6 times higher than wild-type
-
additional information
apomucin
4.7 +/-0.1 mg/ml, truncated wild-type P-T1/delta42
-
additional information
apomucin
43.9 +/-3.8 mg/ml, mutant W316F, 9.1 times higher than wild-type
-
additional information
apomucin
5.0 +/-0.2 mg/ml, mutant Y302L
-
additional information
apomucin
6.7 +/-1.7 mg/ml, mutant F325L, 1.4 times higher than wild-type
-
additional information
apomucin
7.1 +/-0.4 mg/ml, mutant Y309L, 1.5 times higher than wild-type
-
additional information
additional information
-
-
-
additional information
additional information
-
increased values, mg/ml, for apomucin of several GalNAc-T1 mutants
-
additional information
additional information
KMs obtained using Lineweaver-Burk plot
-
additional information
additional information
the KMs for apomucin and the synthetic peptides, PPDAATAAPL and GVVPTVVPG, were measured in presence of 7.5 µM UDP-GalNAc
-
additional information
additional information
the KMs for UDP-GalNAc were measured in presence of 1.88 mg/ml apomucin
-
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D444A
-
GalNAc-T1 mutant with severely impaired apomucin glycosylation, D444A/D484A/D525A triple mutant has significantly lower activity than D444A single mutant
F303L
mutant of 40% activity relative to truncated wild-type using apomucin as acceptor substrate and of increased KM for both substrates
F325L
mutant of 60% activity relative to truncated wild-type using apomucin as acceptor substrate
F468A
-
GalNAc-T1 mutant with strongly reduced activity and decreased expression
G455Q
-
GalNAc-T1 mutant with reduced reactivity towards apomucin
P-T1-delta42
truncated GalNAc-T1 wild-type, deletion of the coding sequence for the cytoplasmic tail and the transmembrane domain, cDNA for insulin signal sequence and protein A IgG-binding domain fused to the 5-end
W316A
inactive mutant using apomucin as acceptor substrate
W316F
mutant of 20% activity relative to truncated wild-type using apomucin as acceptor substrate and of increased KMs for apomucin, UDP-GalNAc, and synthetic peptides, PPDAATAAPL and GVVPTVVPG
W316L
background level activity relative to truncated wild-type using apomucin as acceptor substrate
W316Y
mutant of 40% activity relative to truncated wild-type using apomucin as acceptor substrate and of increased KMs for apomucin, UDP-GalNAc, and synthetic peptides, PPDAATAAPL and GVVPTVVPG
W328A
inactive mutant using apomucin as acceptor substrate, low expression level
W328F
inactive mutant using apomucin as acceptor substrate
W328L
inactive mutant using apomucin as acceptor substrate
W328Y
inactive mutant using apomucin as acceptor substrate
Y302L
mutant of 80% activity relative to truncated wild-type using apomucin as acceptor substrate
Y309L
mutant of 40% activity relative to truncated wild-type using apomucin as acceptor substrate and of increased KM for both substrates
additional information
-
site-directed mutagenesis at the C-terminus and its deletion inactivates GalNAc-T1, probably caused by conformational changes in the (QXW)3 repeats, deletion of the lectin domain results in complete loss of activity
additional information
all point mutants are mutants of the truncated wild-type P-T1-delta42 and were generated by site-directed mutagenesis on pInsProAdelta42
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Sugiura, M.; Kawasaki, T.; Yamashina, I.
Purification and characterization of UDP-GalNAc:polypeptide N-acetylgalactosamine transferase from an ascites hepatoma, AH 66
J. Biol. Chem.
257
9501-9507
1982
Rattus norvegicus
brenda
Soerensen, T.; White, T.; Wandall, H.H.; Kristensen, A.K.; Roepstorff, P.; Clausen, H.
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. Identification and separation of two distinct transferase activities
J. Biol. Chem.
270
24166-24173
1995
Homo sapiens, Ovis sp., Rattus norvegicus, Sus scrofa
brenda
Ten Hagen, K.G.; Bedi, G.S.; Tetaert, D.; Kingsley, P.D.; Hagen, F.K.; Balys, M.M.; Beres, T.M.; Degand, P.; Tabak, L.A.
Cloning and characterization of a ninth member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family, ppGaNTase-T9
J. Biol. Chem.
276
17395-17404
2001
Mus musculus, Rattus norvegicus (Q925R7)
brenda
Ten Hagen, K.G.; Tetaert, D.; Hagen, F.K.; Richet, C.; Beres, T.M.; Gagnon, J.; Balys, M.M.; VanWuyckhuyse, B.; Bedi, G.S.; Degand, P.; Tabak, L.A.
Characterization of a UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase that displays glycopeptide N-acetylgalactosaminyltransferase activity
J. Biol. Chem.
274
27867-27874
1999
Mus musculus, Rattus norvegicus (Q9R0C5)
brenda
Tenno, M.; Saeki, A.; Kezdy, F.J.; Elhammer, A.P.; Kurosaka, A.
The lectin domain of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1 is involved in O-glycosylation of a polypeptide with multiple acceptor sites
J. Biol. Chem.
277
47088-47096
2002
Rattus norvegicus
brenda
Stwora-Wojczyk, M.M.; Dzierszinski, F.; Roos, D.S.; Spitalnik, S.L.; Wojczyk, B.S.
Functional characterization of a novel Toxoplasma gondii glycosyltransferase: UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T3
Arch. Biochem. Biophys.
426
231-240
2004
Mus musculus, Rattus norvegicus, Toxoplasma gondii (Q6YBY0), Toxoplasma gondii
brenda
Nakamura, N.; Toba, S.; Hirai, M.; Morishita, S.; Mikami, T.; Konishi, M.; Itoh, N.; Kurosaka, A.
Cloning and expression of a brain-specific putative UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase gene
Biol. Pharm. Bull.
28
429-433
2005
Rattus norvegicus, Homo sapiens (Q9HCQ5), Homo sapiens
brenda
Hagen, F.K.; Gregoire, C.A.; Tabak, L.A.
Cloning and sequence homology of a rat UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
Glycoconj. J.
12
901-909
1995
Rattus norvegicus (Q10473)
brenda
Ten hagen, K.G.; Hagen, F.K.; Balys, M.; Beres, T.M.; van Wuyckhuyse, B.; Tabak, L.A.
Cloning and expression of a novel, tissue specifically expressed member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family
J. Biol. Chem.
273
27749-27754
1998
Rattus norvegicus, Rattus norvegicus (O88422)
brenda
Tenno, M.; Saeki, A.; Elhammer, A.P.; Kurosaka, A.
Function of conserved aromatic residues in the Gal/GalNAc-glycosyltransferase motif of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1
FEBS J.
274
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2007
Rattus norvegicus (Q10473)
brenda