2.4.1.313: protein O-mannose beta-1,3-N-acetylgalactosaminyltransferase
This is an abbreviated version!
For detailed information about protein O-mannose beta-1,3-N-acetylgalactosaminyltransferase, go to the full flat file.
Reaction
Synonyms
B3GALNT2, B3GalTN2, beta 1,3-N-acetylgalactosaminyltransferase2, beta-1,3-N-acetylgalactosaminyltransferase 2, beta1,3-N-acetylgalactosaminyltransferase II, beta1,3-N-acetylgalactosaminyltransferase-II, beta3GalNAc-T2, UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 2
ECTree
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General Information
General Information on EC 2.4.1.313 - protein O-mannose beta-1,3-N-acetylgalactosaminyltransferase
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malfunction
metabolism
physiological function
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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
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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
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