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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]
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?
UDP-N-acetyl-alpha-D-galactosamine + 3-O-[N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl]-L-threonyl-[low-density lipoprotein receptor-related protein 1]
UDP + 3-O-[N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl]-L-threonyl-[low-density lipoprotein receptor-related protein 1]
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?
UDP-N-acetyl-alpha-D-galactosamine + 3-O-[N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl]-L-threonyl-[nicastrin]
UDP + 3-O-[N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl]-L-threonyl-[nicastrin]
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?
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
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?
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
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?
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
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?
UDP-N-acetyl-alpha-D-galactosamine + Glc-NAcbeta(1->6)GalNAcalpha1-O-4-nitrophenyl
?
19% activity compared to GlcNAc-beta-benzyl
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?
UDP-N-acetyl-alpha-D-galactosamine + GlcNAc-beta-benzyl
?
100% activity
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?
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
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?
UDP-N-acetyl-alpha-D-galactosamine + GlcNAcbeta(1->4)GlcNAcbeta1-O-benzyl
?
29% activity compared to GlcNAc-beta-benzyl
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?
additional information
?
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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]
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?
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]
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?
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]
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?
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]
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?
additional information
?
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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
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?
additional information
?
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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
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?
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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]
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?
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]
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?
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]
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?
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]
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?
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Breast Neoplasms
Involvement of B3GALNT2 overexpression in the cell growth of breast cancer.
Carcinoma, Hepatocellular
Increased B3GALNT2 in hepatocellular carcinoma promotes macrophage recruitment via reducing acetoacetate secretion and elevating MIF activity.
Hydrocephalus
A nonsense mutation in B3GALNT2 is concordant with hydrocephalus in Friesian horses.
Hydrocephalus
Congenital hydrocephalus in a Belgian draft horse associated with a nonsense mutation in B3GALNT2.
Intellectual Disability
B3GALNT2 mutations associated with non-syndromic autosomal recessive intellectual disability reveal a lack of genotype-phenotype associations in the muscular dystrophy-dystroglycanopathies.
Muscular Dystrophies
B3GALNT2 is a gene associated with congenital muscular dystrophy with brain malformations.
Muscular Dystrophies
B3GALNT2-Related Dystroglycanopathy: Expansion of the Phenotype with Novel Mutation Associated with Muscle-Eye-Brain Disease, Walker-Warburg Syndrome, Epileptic Encephalopathy-West Syndrome, and Sensorineural Hearing Loss.
Muscular Dystrophies
Integrative data mining highlights candidate genes for monogenic myopathies.
Muscular Dystrophies
Mutations in B3GALNT2 Cause Congenital Muscular Dystrophy and Hypoglycosylation of ?-Dystroglycan.
Muscular Dystrophies
Serial prenatal and postnatal MRI of dystroglycanopathy in a patient with familial B3GALNT2 mutation.
Muscular Dystrophies
SGK196 is a glycosylation-specific O-mannose kinase required for dystroglycan function.
Neoplasms
Increased B3GALNT2 in hepatocellular carcinoma promotes macrophage recruitment via reducing acetoacetate secretion and elevating MIF activity.
Seizures
B3GALNT2 mutations associated with non-syndromic autosomal recessive intellectual disability reveal a lack of genotype-phenotype associations in the muscular dystrophy-dystroglycanopathies.
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malfunction
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knockdown of B3GALNT2 expression attenuates cell growth and induced apoptosis in breast cancer cells
malfunction
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knockdown of b3galnt2 in zebrafish recapitulates the human congenital muscular dystrophy phenotype with reduced motility, brain abnormalities, and disordered muscle fibers with evidence of damage to both the myosepta and the sarcolemma. Functional dystroglycan glycosylation is also reduced
malfunction
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mutations in B3GALNT2 cause congenital muscular dystrophy and hypoglycosylation of alpha-dystroglycan
metabolism
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the enzyme is involved in the functional glycosylation of alpha-dystroglycan
metabolism
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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. LacdiNAc presence on low-density lipoprotein receptor-related protein 1 and nicastrin depends on B3GALNT2. 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
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
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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
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
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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
brenda
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
brenda
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
brenda
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)
brenda
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
brenda
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)
brenda
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)
brenda