Any feedback?
Information on EC 2.4.1.313 - protein O-mannose beta-1,3-N-acetylgalactosaminyltransferase and Organism(s) Homo sapiens and UniProt Accession Q8NCR0
for references in articles please use BRENDA:EC2.4.1.313Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.4.1.313 protein O-mannose beta-1,3-N-acetylgalactosaminyltransferaseIUBMB Comments
The human protein is specific for UDP-N-acetyl-alpha-D-galactosamine as donor . The enzyme is involved in the formation of a phosphorylated trisaccharide on a threonine residue of alpha-dystroglycan, an extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains.
Specify your search results
Word Map
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
Synonyms
b3galnt2, beta3galnac-t2, beta1,3-n-acetylgalactosaminyltransferase-ii, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
B3GALNT2
B3GALNT2
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-alpha-D-galactosamine:N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl-threonyl-[protein] 3-beta-N-acetyl-D-galactosaminyltransferase
The human protein is specific for UDP-N-acetyl-alpha-D-galactosamine as donor [1]. The enzyme is involved in the formation of a phosphorylated trisaccharide on a threonine residue of alpha-dystroglycan, an extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains.
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-galactosamine + 3-O-N-acetyl-beta-D-glucosaminyl-[Ser347 of human casein kinase II peptide]
UDP + 3-O-[N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl]-[Ser347 of human casein kinase II peptide]
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + 3-O-[N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl]-L-threonyl-[protein]
UDP + 3-O-[N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl]-L-threonyl-[protein]
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + 4-nitrophenyl-beta-D-glucose
?
2% activity compared to GlcNAc-beta-benzyl
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + calf fetuin
?
the enzyme efficiently transfers GalNAc to N-glycans of fetal calf fetuin, which is treated with neuraminidase and beta-galactosidase
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + Gal-beta(1->3)(GlcNAcbeta(1->6))GalNAcalpha1-O-4-nitrophenyl
?
best acceptor substrate, 185% activity compared to GlcNAc-beta-benzyl
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + Glc-NAcbeta(1->6)GalNAcalpha1-O-4-nitrophenyl
?
19% activity compared to GlcNAc-beta-benzyl
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + GlcNAc-beta-benzyl
?
100% activity
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + GlcNAcbeta(1->3)GalNAcalpha-4-nitrophenyl
UDP + GalNAcbeta(1->3)GlcNAcbeta(1->3)GalNAcalpha-4-nitrophenyl
8% activity compared to GlcNAc-beta-benzyl
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + GlcNAcbeta(1->4)GlcNAcbeta1-O-benzyl
?
29% activity compared to GlcNAc-beta-benzyl
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + 3-O-[N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl]-L-threonyl-[protein]
UDP + 3-O-[N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl]-L-threonyl-[protein]
UDP-N-acetyl-alpha-D-galactosamine + 3-O-[N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl]-L-threonyl-[protein]
UDP + 3-O-[N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl]-L-threonyl-[protein]
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + 3-O-[N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl]-L-threonyl-[protein]
UDP + 3-O-[N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl]-L-threonyl-[protein]
-
-
-
?
additional information
?
-
the enzyme shows no activity toward any glycolipid, Gal-beta-4-mitrophenyl, Gal-beta-O-4-nitrophenyl, Gal-NAc-alpha-benzyl, GalNAc-beta-4-nitrophenyl, Glc-alpha-4-nitrophenyl, GlcA-beta-4-nitrophenyl, Fuc-alpha-4-nitrophenyl, Xyl-alpha-4-nitrophenyl, Xyl-beta-4-nitrophenyl, Man-alpha-4-nitrophenyl, lactoside-benzyl, lactosylceramide, galactocenebroside type 1, paragloboside, globoside, Galbeta(1->4)GalNAc-alpha-4-nitrophenyl, Galbeta(1->3)GlcNAc-beta-4-nitrophenyl, and Galbeta(1->3)GalNAcalpha(core1)-4-nitrophenyl
-
-
?
additional information
?
-
-
the enzyme shows no activity toward any glycolipid, Gal-beta-4-mitrophenyl, Gal-beta-O-4-nitrophenyl, Gal-NAc-alpha-benzyl, GalNAc-beta-4-nitrophenyl, Glc-alpha-4-nitrophenyl, GlcA-beta-4-nitrophenyl, Fuc-alpha-4-nitrophenyl, Xyl-alpha-4-nitrophenyl, Xyl-beta-4-nitrophenyl, Man-alpha-4-nitrophenyl, lactoside-benzyl, lactosylceramide, galactocenebroside type 1, paragloboside, globoside, Galbeta(1->4)GalNAc-alpha-4-nitrophenyl, Galbeta(1->3)GlcNAc-beta-4-nitrophenyl, and Galbeta(1->3)GalNAcalpha(core1)-4-nitrophenyl
-
-
?
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-galactosamine + 3-O-[N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl]-L-threonyl-[protein]
UDP + 3-O-[N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl]-L-threonyl-[protein]
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + 3-O-[N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl]-L-threonyl-[protein]
UDP + 3-O-[N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl]-L-threonyl-[protein]
UDP-N-acetyl-alpha-D-galactosamine + 3-O-[N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl]-L-threonyl-[protein]
UDP + 3-O-[N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl]-L-threonyl-[protein]
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + 3-O-[N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl]-L-threonyl-[protein]
UDP + 3-O-[N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl]-L-threonyl-[protein]
-
-
-
?
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
malfunction
metabolism
-
the enzyme is involved in the functional glycosylation of alpha-dystroglycan
physiological function
beta-1,3-N-acetylgalactosaminyltransferase2 B3GALNT2 and protein O-mannose beta-1,4-Nacetylglucosaminyltransferase GTDC2 act coordinately on O-mannose to synthesize the O-mannosyl glycan GalNAc-beta-3-GlcNAc-beta-4-Man present in alpha-dystroglycan. Kinase SGK196 phosphorylates the 6-position of O-mannose using ATP
physiological function
inhibition of Golgi-resident glycosyltransferase increases the abundance of B3GALNT2-synthesized type-I LacdiNAc structures. Most of the identified glycoproteins modified by B3GalTN2 localize to intracellular organelles, particularly to the endoplasmic reticulum. Whereas B4GALNT3 and B4GALNT4 synthesize LDN on extracellular glycoproteins, B3GALNT2 primarily transfers LacdiNAc to intracellular glycoproteins
malfunction
-
knockdown of B3GALNT2 expression attenuates cell growth and induced apoptosis in breast cancer cells
malfunction
-
mutations in B3GALNT2 cause congenital muscular dystrophy and hypoglycosylation of alpha-dystroglycan
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). B3GL2_HUMAN
500
0
56704
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
the enzyme is N-glycosylated on both Asn-116 and Asn-174. This modification is necessary for its secretion in breast cancer cells
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
detection and/or imaging of O-GlcNAc as well as potential sites for O-GlcNAc modification on biological samples. Occupied modification sites are detected using in vitro incorporation of azido-GalNAc by B3GALNT2, and unoccupied sites are detected by in vitro incorporation of azido-GlcNAc by O-GlcNAc transferase (OGT), via click chemistry
medicine
medicine
a 5-year-old patient heterozygous for a one-base duplication and a missense mutation in the gene B3GALNT2 patient shows psychomotor retardation, ataxia, spasticity, muscle weakness and increased serum creatine kinase levels. The skeletal muscle displays reduced glycosylated alpha-dystroglycan. The brain at 3.5 years of age shows increased T2 signal from supratentorial and infratentorial white matter, a hypoplastic pons and subcortical cerebellar cysts. The patient shows a milder phenotype than previously described patients with mutations in the B3GALNT2 gene
medicine
mutations in GTDC2, beta-1,3-N-acetylgalactosaminyltransferase 2B3GALNT2, and kinase SGK196 disrupt dystroglycan receptor function and lead to congenital muscular dystrophy
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Stevens, E.; Carss, K.J.; Cirak, S.; Foley, A.R.; Torelli, S.; Willer, T.; Tambunan, D.E.; Yau, S.; Brodd, L.; Sewry, C.A.; Feng, L.; Haliloglu, G.; Orhan, D.; Dobyns, W.B.; Enns, G.M.; Manning, M.; Krause, A.; Salih, M.A.; Walsh, C.A.; Hurles, M.; Campbell, K.P.; Manzini, M.C.; Manzini, M.C.; Stemple, D.; Lin, Y.Y.
Mutations in B3GALNT2 cause congenital muscular dystrophy and hypoglycosylation of alpha-dystroglycan
Am. J. Hum. Genet.
92
354-365
2013
Danio rerio, Homo sapiens
Matsuo, T.; Komatsu, M.; Yoshimaru, T.; Kiyotani, K.; Miyoshi, Y.; Sasa, M.; Katagiri, T.
Involvement of B3GALNT2 overexpression in the cell growth of breast cancer
Int. J. Oncol.
44
427-434
2014
Homo sapiens
Hiruma, T.; Togayachi, A.; Okamura, K.; Sato, T.; Kikuchi, N.; Kwon, Y.; Nakamura, A.; Fujimura, K.; Gotoh, M.; Tachibana, K.; Ishizuka, Y.; Noce, T.; Nakanishi, H.; Narimatsu, H.
A novel human beta1,3-N-acetylgalactosaminyltransferase that synthesizes a unique carbohydrate structure, GalNAcbeta1-3GlcNAc
J. Biol. Chem.
279
14087-14095
2004
Homo sapiens (Q8NCR0), Homo sapiens
Yoshida-Moriguchi, T.; Willer, T.; Anderson, M.E.; Venzke, D.; Whyte, T.; Muntoni, F.; Lee, H.; Nelson, S.F.; Yu, L.; Campbell, K.P.
SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function
Science
341
896-899
2013
Homo sapiens, Homo sapiens (Q8NCR0)
Hedberg, C.; Oldfors, A.; Darin, N.
B3GALNT2 is a gene associated with congenital muscular dystrophy with brain malformations
Eur. J. Hum. Genet.
22
707-710
2014
Homo sapiens (Q8NCR0), Homo sapiens
Wu, Z.L.; Tatge, T.J.; Grill, A.E.; Zou, Y.
Detecting and imaging O-GlcNAc sites using glycosyltransferases a systematic approach to study O-GlcNAc
Cell Chem. Biol.
25
1428-1435
2018
Homo sapiens (Q8NCR0)
Nakane, T.; Angata, K.; Sato, T.; Kaji, H.; Narimatsu, H.
Identification of mammalian glycoproteins with type-I LacdiNAc structures synthesized by the glycosyltransferase B3GALNT2
J. Biol. Chem.
294
7433-7444
2019
Cricetulus griseus (A0A3L7H411), Cricetulus griseus, Homo sapiens (Q8NCR0)
EXTERNAL LINKS (specific for EC-Number 2.4.1.313)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
