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Information on EC 2.4.1.41 - polypeptide N-acetylgalactosaminyltransferase and Organism(s) Mus musculus

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.41 polypeptide N-acetylgalactosaminyltransferase
IUBMB Comments
Requires both Mn2+ and Ca2+. The glycosyl residue is transferred to threonine or serine hydroxy groups on the polypeptide core of submaxillary mucin, kappa-casein, apofetuin and some other acceptors of high molecular mass.
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This record set is specific for:
Mus musculus
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Word Map
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
galnt3, n-acetylgalactosaminyltransferase, galnt2, galnac-t3, galnac-t, galnt14, galnac-transferase, galnac transferase, galnac-t2, galnac-t1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylgalactosaminyltransferase, uridine diphosphoacetylgalactosamine-glycoprotein
-
-
-
-
GalNAc-T13
-
GalNAc-transferase
-
-
-
-
glycoprotein acetylgalactosaminyltransferase
-
-
-
-
polypeptide GalNAc transferase
-
-
polypeptide GalNAcT
-
-
polypeptide N-acetylgalactosaminyltransferase
-
-
polypeptide N-acetylgalactosaminyltransferase-1
-
-
polypeptide-N-acetylgalactosamine transferase
-
-
-
-
pp-GaNTase
-
ppGalNAc-T
-
-
-
-
ppGalNAc-T1
-
-
ppGalNAcT
-
-
ppGaNTase
-
-
-
-
ppGaNTase-T1
-
ppGaNTase-T3
-
ppGaNTase-T4
-
-
protein-UDP acetylgalactosaminyltransferase
-
-
-
-
UDP-acetylgalactosamine-glycoprotein acetylgalactosaminyltransferase
-
-
-
-
UDP-acetylgalactosamine:peptide-N-galactosaminyltransferase
-
-
-
-
UDP-GalNAc polypeptide:N-acetylgalactosaminyltransferase
-
-
UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-T1
-
UDP-GalNAc:polypeptide N-acetylgalactosaminyl transferase
-
-
-
-
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
-
-
-
-
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-T3
-
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase
-
-
-
-
UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T1
-
-
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
-
-
-
-
additional information
-
the enzyme belongs to the family of UDP-GalNAc polypeptide:N-acetylgalactosaminyltransferases, i.e. ppGalNAcTs
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyl-transferase
Requires both Mn2+ and Ca2+. The glycosyl residue is transferred to threonine or serine hydroxy groups on the polypeptide core of submaxillary mucin, kappa-casein, apofetuin and some other acceptors of high molecular mass.
CAS REGISTRY NUMBER
COMMENTARY hide
9075-15-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-GalNAc + EA2
GalNAc-EA2 + UDP
show the reaction diagram
-
-
-
-
?
UDP-GalNAc + PRFODSSSKAPPPLPSPSRLPG
GalNAc-PRFODSSSKAPPPLPSPSRLPG + UDP
show the reaction diagram
-
-
-
-
?
UDP-GalNAc + selectin
GalNAc-selectin + UDP
show the reaction diagram
-
-
reduced expression of cell surface E- and P-selectins (fourfold and fivefold) and L-selectins on immune cells of ppGalNAcT-1 deficient mice
-
?
UDP-N-acetyl-alpha-D-galactosamine + mucin-type O-glycoprotein podoplanin
UDP + N-acetyl-alpha-D-galactosaminyl-mucin-type O-glycoprotein podoplanin
show the reaction diagram
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + polypeptide Muc10
UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide Muc10
show the reaction diagram
-
-
-
?
UDP-N-acetyl-D-galactosamine + bone sialoprotein
UDP + UDP-N-acetyl-D-galactosaminyl-bone sialoprotein
show the reaction diagram
-
preferred substrate of isozyme ppGalNAcT-1, glycosylation of Thr101, Ser131, Thr199, and Ser214, glycosylation pattern, overview
-
-
?
UDP-N-acetyl-D-galactosamine + GTTPSPVPTTS-(O-GalNAc)T-SAP
UDP + ?
show the reaction diagram
-
23% of the activity with P-(O-GalNAc)T-TDSTTPAPTTK
-
-
?
UDP-N-acetyl-D-galactosamine + GTTPSPVPTTSTTSAP
UDP + ?
show the reaction diagram
-
73% of the activity with P-(O-GalNAc)T-TDSTTPAPTTK
-
-
?
UDP-N-acetyl-D-galactosamine + osteopontin
UDP + N-acetyl-D-galactosaminyl-osteopontin
show the reaction diagram
-
preferred substrate of isozyme ppGalNAcT-1, glycosylation pattern, overview
-
-
?
UDP-N-acetyl-D-galactosamine + P-(O-GalNAc)T-TDSTTPAPTTK
UDP + ?
show the reaction diagram
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
UDP-N-acetyl-D-galactosamine + PTTDS-(O-GalNAc)T-TPAPTTK
UDP + ?
show the reaction diagram
-
4.5% of the activity with P-(O-GalNAc)T-TDSTTPAPTTK
-
-
?
UDP-N-acetyl-D-galactosamine + PTTDSTTPAPTTK
UDP + ?
show the reaction diagram
-
74% of the activity with P-(O-GalNAc)T-TDSTTPAPTTK
-
-
?
UDP-N-acetyl-D-galactosamine + VESDRSTTTTQAP
UDP + ?
show the reaction diagram
-
34% of the activity with P-(O-GalNAc)T-TDSTTPAPTTK
-
-
?
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-D-galactosamine + bone sialoprotein
UDP + UDP-N-acetyl-D-galactosaminyl-bone sialoprotein
show the reaction diagram
-
preferred substrate of isozyme ppGalNAcT-1, glycosylation of Thr101, Ser131, Thr199, and Ser214, glycosylation pattern, overview
-
-
?
UDP-N-acetyl-D-galactosamine + osteopontin
UDP + N-acetyl-D-galactosaminyl-osteopontin
show the reaction diagram
-
preferred substrate of isozyme ppGalNAcT-1, glycosylation pattern, overview
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
show the reaction diagram
additional information
?
-
-
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
metal-dependent enzyme
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0259
GTTPSPVPTTSTTSAP
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pH 7.0, 37°C
0.198
PTTDS-(O-GalNAc)T-TPAPTTK
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pH 7.0, 37°C
0.0788
UDP-N-acetyl-D-galactosamine
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pH 7.0, 37°C
additional information
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.15
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
isozymes ppGalNAcT-1, ppGalNAcT-2, and ppGalNAcT-3, expression patterns, overview. Expression of isozyme ppGalNAcT-1 especially in calvaria and tibia
Manually annotated by BRENDA team
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lymphoma cells
Manually annotated by BRENDA team
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ppGalNacT-1 activity is essential for O-glycosylation in germinal center (GC) B cells within the white pulp of the spleen and lymph nodes upon immunization, increased apoptosis of IgG bearing GC B cells and reduced IgG abundance in the absence of ppGalNAcT-1
Manually annotated by BRENDA team
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ppGalNAcT-1 mediated O-glycosylation contributes to innate immune inflammatory response among activated endothelial cells by expression of cell surface selectin ligands on neutrophils
Manually annotated by BRENDA team
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low level of isozyme T4
Manually annotated by BRENDA team
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mostly inguinal lymph nodes, not Peyer’s patch tissue, ppGalNAcT-1 activity regulates L-selectin ligand level in high endothelial venules that is responsible for lymph node cellularity and B- and T-cell homing
Manually annotated by BRENDA team
Galnt3 is the major O-glycosyltransferase expressed in the secretory cells of salivary glands
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GALT2_MOUSE
570
1
64514
Swiss-Prot
Secretory Pathway (Reliability: 2)
GALT3_MOUSE
633
1
72932
Swiss-Prot
Secretory Pathway (Reliability: 4)
GALT4_MOUSE
578
1
66555
Swiss-Prot
Secretory Pathway (Reliability: 1)
GALT5_MOUSE
930
1
105780
Swiss-Prot
Secretory Pathway (Reliability: 3)
GALT1_MOUSE
559
1
64255
Swiss-Prot
Secretory Pathway (Reliability: 1)
GLT10_MOUSE
603
1
69116
Swiss-Prot
Secretory Pathway (Reliability: 1)
GLT11_MOUSE
608
1
69201
Swiss-Prot
Secretory Pathway (Reliability: 1)
GLT12_MOUSE
576
1
66541
Swiss-Prot
Secretory Pathway (Reliability: 5)
GLT13_MOUSE
556
1
63983
Swiss-Prot
Secretory Pathway (Reliability: 1)
GLT14_MOUSE
550
1
63989
Swiss-Prot
Secretory Pathway (Reliability: 2)
GLT15_MOUSE
638
1
72321
Swiss-Prot
Secretory Pathway (Reliability: 2)
GLT16_MOUSE
558
1
62875
Swiss-Prot
Secretory Pathway (Reliability: 3)
GLT17_MOUSE
598
1
67691
Swiss-Prot
Secretory Pathway (Reliability: 3)
GALT6_MOUSE
622
0
71537
Swiss-Prot
Mitochondrion (Reliability: 5)
GALT7_MOUSE
657
1
75419
Swiss-Prot
Secretory Pathway (Reliability: 1)
GLT18_MOUSE
622
1
71096
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57000
-
x * 57000, recombinant isozyme ppGalNAcT-1, SDS-PAGE, x * 60000, recombinant isozyme ppGalNAcT-2, SDS-PAGE
60000
-
x * 57000, recombinant isozyme ppGalNAcT-1, SDS-PAGE, x * 60000, recombinant isozyme ppGalNAcT-2, SDS-PAGE
70000
-
1 * 70000, SDS-PAGE
71500
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 57000, recombinant isozyme ppGalNAcT-1, SDS-PAGE, x * 60000, recombinant isozyme ppGalNAcT-2, SDS-PAGE
monomer
-
1 * 70000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of mppGaNTase-T1 (without maltose-binding protein) are grown by hanging drop vapor diffusion at room temperature
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D155N
-
ppGaNTase-T1 mutant with wild type level of enzyme activity, expression in COS7 cells is markedly compromised
D156Q
-
ppGaNTase-T1 mutant without enzyme activity
D209A
-
ppGaNTase-T1 mutant without enzyme activity
D209E
-
ppGaNTase-T1 mutant with very low enzyme activity
D209N
-
ppGaNTase-T1 mutant without enzyme activity
D310N
-
ppGaNTase-T1 mutant with 2% of enzyme activity
D375A
-
ppGaNTase-T1 mutant with little effect on enzyme activity
D375N
-
ppGaNTase-T1 mutant with little effect on enzyme activity
delta/delta
-
mice homozygous for ppGalNAcT-1delta allele
E127Q
-
ppGaNTase-T1 mutant with less than 1% of enzyme activity
E150Q
-
ppGaNTase-T1 mutant with wild type level of enzyme activity
E213Q
-
ppGaNTase-T1 mutant with less than 1% of enzyme activity
E319Q
-
ppGaNTase-T1 mutant without enzyme activity
E322Q
-
ppGaNTase-T1 mutant with 1% of enzyme activity
E376Q
-
ppGaNTase-T1 mutant with little effect on enzyme activity
H125F
-
active ppGaNTase-T1 mutant, near 3fold greater activity than wild type enzyme
H125Q
-
active ppGaNTase-T1 mutant
H211D
-
ppGaNTase-T1 mutant without enzyme activity
H341A
-
ppGaNTase-T1 mutant with little effect on enzyme activity
H341K
-
ppGaNTase-T1 mutant with little effect on enzyme activity
H341L
-
ppGaNTase-T1 mutant with little effect on enzyme activity
H341R
-
ppGaNTase-T1 mutant with little effect on enzyme activity
H341V
-
ppGaNTase-T1 mutant with little effect on enzyme activity
N320A
-
ppGaNTase-T1 mutant with little effect on enzyme activity
ppGalNAcT-1delta
-
allele in transgenic mice that lacks exon 3 and enzymatic activity, crossed into C57BL/6NHsd background
wt/delta
-
mice heterozygous for ppGalNAcT-1delta allele
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2500fold
-
recombinant His-tagged isozymes ppGalNAcT-1 and ppGalNAcT-2 from Pichia pastoris medium by nickel affinity chromatography, the tag is cleaved off by TEV protease, recombinant isozyme ppGalNAcT-3t from medium of COS-7 cells
-
recombinant ppGaNTases expressed in COS7 cells
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
amino acid sequences of ppGaNTase-T3 and –T4
-
isozymes ppGalNAcT-1, ppGalNAcT-2, and ppGalNAcT-3, recombinant expression of the His-tagged isozymes ppGalNAcT-1, ppGalNAcT-2 in Pichia pastoris and of isozyme ppGalNAcT-3 in COS-7 cells, secretion of the recombinant proteins
-
pIMKF3 for expression in COS7 cells
-
ppGalNAc-T13 and -T1 are localized to chromosome 2 and 18, ppGalNAc-T13 is cloned and sequenced, 556-amino acid protein
-
ppGaNTase-T1 (mppGaNTase-T1) is expressed as a fusion protein with maltose-binding protein at the N terminus and residues 42–559 of mppGaNTase-T1 at the C terminus separated by a tobacco etch virus protease recognition sequence. The fusion protein is expressed in Pichia pastoris
ppGaNTase-T1 is cloned from kidney RNA, amino acid sequence, expression of ppGaNTases as secreted forms in COS7 cells
-
ppGaNTase-T4 from spleen cDNA library, transient expression in COS7 cellsas secreted soluble and functional enzyme
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of GalNAc-T13 is dramatically upregulated during early neurogenesis in mouse embryonic brains
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
isoform Galnt3-deficient mice serve as a model for the disease hyperphosphatemic familial tumoral calcinosis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team