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acetylgalactosaminyltransferase, uridine diphosphoacetylgalactosamine-glycoprotein
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GalNAc-transferase
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glycoprotein acetylgalactosaminyltransferase
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polypeptide GalNAc transferase
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polypeptide N-acetylgalactosaminyltransferase
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polypeptide N-acetylgalactosaminyltransferase-1
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polypeptide-N-acetylgalactosamine transferase
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protein-UDP acetylgalactosaminyltransferase
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UDP-acetylgalactosamine-glycoprotein acetylgalactosaminyltransferase
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UDP-acetylgalactosamine:peptide-N-galactosaminyltransferase
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UDP-GalNAc polypeptide:N-acetylgalactosaminyltransferase
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UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-T1
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UDP-GalNAc:polypeptide N-acetylgalactosaminyl transferase
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UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
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UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-T3
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UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase
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UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T1
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UDP-N-acetylgalactosamine-glycoprotein N-acetylgalactosaminyltransferase
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UDP-N-acetylgalactosamine-protein N-acetylgalactosaminyltransferase
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UDP-N-acetylgalactosamine:kappa-casein polypeptide N-acetylgalactosaminyltransferase
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UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferase
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UDP-N-acetylgalactosamine:protein N-acetylgalactosaminyl transferase
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uridine diphosphoacetylgalactosamine-glycoprotein acetylgalactosaminyltransferase
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additional information
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the enzyme belongs to the family of UDP-GalNAc polypeptide:N-acetylgalactosaminyltransferases, i.e. ppGalNAcTs
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UDP-GalNAc + EA2
GalNAc-EA2 + UDP
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?
UDP-GalNAc + PRFODSSSKAPPPLPSPSRLPG
GalNAc-PRFODSSSKAPPPLPSPSRLPG + UDP
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?
UDP-GalNAc + selectin
GalNAc-selectin + UDP
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reduced expression of cell surface E- and P-selectins (fourfold and fivefold) and L-selectins on immune cells of ppGalNAcT-1 deficient mice
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UDP-N-acetyl-alpha-D-galactosamine + mucin-type O-glycoprotein podoplanin
UDP + N-acetyl-alpha-D-galactosaminyl-mucin-type O-glycoprotein podoplanin
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?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide Muc10
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide Muc10
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?
UDP-N-acetyl-D-galactosamine + bone sialoprotein
UDP + UDP-N-acetyl-D-galactosaminyl-bone sialoprotein
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preferred substrate of isozyme ppGalNAcT-1, glycosylation of Thr101, Ser131, Thr199, and Ser214, glycosylation pattern, overview
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?
UDP-N-acetyl-D-galactosamine + GTTPSPVPTTS-(O-GalNAc)T-SAP
UDP + ?
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23% of the activity with P-(O-GalNAc)T-TDSTTPAPTTK
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?
UDP-N-acetyl-D-galactosamine + GTTPSPVPTTSTTSAP
UDP + ?
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73% of the activity with P-(O-GalNAc)T-TDSTTPAPTTK
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?
UDP-N-acetyl-D-galactosamine + osteopontin
UDP + N-acetyl-D-galactosaminyl-osteopontin
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preferred substrate of isozyme ppGalNAcT-1, glycosylation pattern, overview
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?
UDP-N-acetyl-D-galactosamine + P-(O-GalNAc)T-TDSTTPAPTTK
UDP + ?
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?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
UDP-N-acetyl-D-galactosamine + PTTDS-(O-GalNAc)T-TPAPTTK
UDP + ?
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4.5% of the activity with P-(O-GalNAc)T-TDSTTPAPTTK
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?
UDP-N-acetyl-D-galactosamine + PTTDSTTPAPTTK
UDP + ?
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74% of the activity with P-(O-GalNAc)T-TDSTTPAPTTK
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?
UDP-N-acetyl-D-galactosamine + VESDRSTTTTQAP
UDP + ?
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34% of the activity with P-(O-GalNAc)T-TDSTTPAPTTK
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?
additional information
?
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UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
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?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
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ppGaNTase-T1: EA2 peptide acceptor, interdependence of binding of UDP-GalNAc and acceptor substrate, enzyme undergoes a conformational change upon sugar binding, equilibrium between open and closed states may be used as a regulation mechanism of activity
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UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
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only UDP-GalNAc serves as sugar donor
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UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
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key role in O-linked glycosylation, catalyzes first step in the assembly
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UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
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initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function
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UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
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O-glycosylation by ppGaNTase-Ts of multisite substrates may proceed in a specific hierarchical manner
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UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
initiates the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine from UDP-GalNAc to Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-alpha-1-O-Ser/Thr)
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UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
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mucin-type O-linked glycosylation of serine or threonine residues
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additional information
?
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additional information
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multiple enzyme isoforms
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additional information
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multiple enzyme isoforms
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additional information
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multiple enzyme isoforms
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additional information
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enzyme structure, GT1 motif, DXD motif, Gal/GalNAc-T motif
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additional information
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UDP-GalNAc polypeptide:N-acetylgalactosaminyltransferase catalyzes the first step in the mucin-type O-glycan biosynthesis pathway by transferring GalNAc to Ser or Thr residues in a protein from the sugar donor UDP-GalNAc
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?
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UDP-N-acetyl-D-galactosamine + bone sialoprotein
UDP + UDP-N-acetyl-D-galactosaminyl-bone sialoprotein
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preferred substrate of isozyme ppGalNAcT-1, glycosylation of Thr101, Ser131, Thr199, and Ser214, glycosylation pattern, overview
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?
UDP-N-acetyl-D-galactosamine + osteopontin
UDP + N-acetyl-D-galactosaminyl-osteopontin
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preferred substrate of isozyme ppGalNAcT-1, glycosylation pattern, overview
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?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
additional information
?
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UDP-GalNAc polypeptide:N-acetylgalactosaminyltransferase catalyzes the first step in the mucin-type O-glycan biosynthesis pathway by transferring GalNAc to Ser or Thr residues in a protein from the sugar donor UDP-GalNAc
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UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
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?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
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key role in O-linked glycosylation, catalyzes first step in the assembly
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?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
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initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function
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?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
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O-glycosylation by ppGaNTase-Ts of multisite substrates may proceed in a specific hierarchical manner
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?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
initiates the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine from UDP-GalNAc to Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-alpha-1-O-Ser/Thr)
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?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
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mucin-type O-linked glycosylation of serine or threonine residues
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?
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D155N
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ppGaNTase-T1 mutant with wild type level of enzyme activity, expression in COS7 cells is markedly compromised
D156Q
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ppGaNTase-T1 mutant without enzyme activity
D209A
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ppGaNTase-T1 mutant without enzyme activity
D209E
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ppGaNTase-T1 mutant with very low enzyme activity
D209N
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ppGaNTase-T1 mutant without enzyme activity
D310N
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ppGaNTase-T1 mutant with 2% of enzyme activity
D375A
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ppGaNTase-T1 mutant with little effect on enzyme activity
D375N
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ppGaNTase-T1 mutant with little effect on enzyme activity
delta/delta
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mice homozygous for ppGalNAcT-1delta allele
E127Q
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ppGaNTase-T1 mutant with less than 1% of enzyme activity
E150Q
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ppGaNTase-T1 mutant with wild type level of enzyme activity
E213Q
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ppGaNTase-T1 mutant with less than 1% of enzyme activity
E319Q
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ppGaNTase-T1 mutant without enzyme activity
E322Q
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ppGaNTase-T1 mutant with 1% of enzyme activity
E376Q
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ppGaNTase-T1 mutant with little effect on enzyme activity
H125F
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active ppGaNTase-T1 mutant, near 3fold greater activity than wild type enzyme
H125Q
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active ppGaNTase-T1 mutant
H211D
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ppGaNTase-T1 mutant without enzyme activity
H341A
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ppGaNTase-T1 mutant with little effect on enzyme activity
H341K
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ppGaNTase-T1 mutant with little effect on enzyme activity
H341L
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ppGaNTase-T1 mutant with little effect on enzyme activity
H341R
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ppGaNTase-T1 mutant with little effect on enzyme activity
H341V
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ppGaNTase-T1 mutant with little effect on enzyme activity
N320A
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ppGaNTase-T1 mutant with little effect on enzyme activity
ppGalNAcT-1delta
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allele in transgenic mice that lacks exon 3 and enzymatic activity, crossed into C57BL/6NHsd background
wt/delta
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mice heterozygous for ppGalNAcT-1delta allele
additional information
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ppGalNAc-T13 deficient mice with decrease in Tn antigen expression in the cerebellum
additional information
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mutations in the C-terminal 128-amino acid ricin-like lectin motif of ppGaNTase-T1 do not alter its catalytic properties
additional information
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generation of Galnt1 null mice, that show reduced glycosylation of bone sialoprotein and osteopontin Ser and Thr residues speficially glycosylated by isozyme ppGalNAcT-1, overview
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Elhammer, A.; Kornfeld, S.
Purification and characterization of UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase from bovine colostrum and murine lymphoma BW5147 cells
J. Biol. Chem.
261
5249-5255
1986
Bos taurus, Mus musculus
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
Zhang, Y.; Iwasaki, H.; Wang, H.; Kudo, T.; Kalka, T.B.; Hennet, T.; Kubota, T.; Cheng, L.; Inaba, N.; Gotoh, M.; Togayachi, A.; Guo, J.; Hisatomi, H.; Nakajima, K.; Nishihara, S.; Nakamura, M.; Marth, J.D.; Narimatsu, H.
Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen
J. Biol. Chem.
278
573-584
2003
Homo sapiens, Homo sapiens (Q8IUC8), Mus musculus
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
Hagen, F.K.; Hazes, B.; Raffo, R.; deSa, D.; Tabak, L.A.
Structure-function analysis of the UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase. Essential residues lie in a predicted active site cleft resembling a lactose repressor fold
J. Biol. Chem.
274
6797-6803
1999
Mus musculus
brenda
Hagen, F.K.; Ten Hagen, K.G.; Beres, T.M.; Balys, M.M.; Van Wuyckhuyse, B.C.; Tabak, L.A.
cDNA cloning and expression of a novel UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase
J. Biol. Chem.
272
13843-13848
1997
Mus musculus
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
Zara, J.; Hagen, F.K.; Ten Hagen, K.G.; van Wuyckhuyse, B.C.; Tabak, L.A.
Cloning and expression of mouse UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-T3
Biochem. Biophys. Res. Commun.
228
38-44
1996
Mus musculus (P70419), Mus musculus
brenda
Fritz, T.A.; Hurley, J.H.; Trinh, L.B.; Shiloach, J.; Tabak, L.A.
The beginnings of mucin biosynthesis: the crystal structure of UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-T1
Proc. Natl. Acad. Sci. USA
101
15307-15312
2004
Mus musculus (O08912), Mus musculus
brenda
Tenno, M.; Ohtsubo, K.; Hagen, F.K.; Ditto, D.; Zarbock, A.; Schaerli, P.; von Andrian, U.H.; Ley, K.; Le, D.; Tabak, L.A.; Marth, J.D.
Initiation of protein O glycosylation by the polypeptide GalNAcT-1 in vascular biology and humoral immunity
Mol. Cell. Biol.
27
8783-8796
2007
Mus musculus
brenda
Miwa, H.E.; Gerken, T.A.; Jamison, O.; Tabak, L.A.
Isoform-specific O-glycosylation of osteopontin and bone sialoprotein by polypeptide N-acetylgalactosaminyltransferase-1
J. Biol. Chem.
285
1208-1219
2010
Mus musculus
brenda
Tang, J.; Zheng, H.; Chen, L.; Gao, S.; Shi, X.; Liu, J.; Xu, L.
Isoform-specific regulation of osteogenic factors by polypeptide N-acetylgalactosaminyltransferases 1 and 4
Biochem. Biophys. Res. Commun.
482
1449-1454
2017
Mus musculus (O08832), Mus musculus (O08912)
brenda
Xu, Y.; Pang, W.; Lu, J.; Shan, A.; Zhang, Y.
Polypeptide N-acetylgalactosaminyltransferase 13 contributes to neurogenesis via stabilizing the mucin-type O-glycoprotein podoplanin
J. Biol. Chem.
291
23477-23488
2016
Mus musculus (Q8CF93), Mus musculus
brenda
Peluso, G.; Tian, E.; Abusleme, L.; Munemasa, T.; Mukaibo, T.; Ten Hagen, K.G.
Loss of the disease-associated glycosyltransferase Galnt3 alters Muc10 glycosylation and the composition of the oral microbiome
J. Biol. Chem.
295
1411-1425
2020
Mus musculus (P70419)
brenda