B3GAT3

B3GAT3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1FGG, 1KWS, 3CU0
Identifiers
Aliases	B3GAT3, GLCATI, glcUAT-I, JDSCD, beta-1,3-glucuronyltransferase 3
External IDs	MGI: 1919977 HomoloGene: 56554 GeneCards: B3GAT3
Gene ontology Molecular function • transferase activity • protein phosphatase activator activity • glucuronosyltransferase activity • metal ion binding • protein binding • galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity Cellular component • integral component of membrane • Golgi apparatus • membrane • Golgi membrane • cis-Golgi network • extracellular exosome Biological process • positive regulation of intracellular protein transport • glycosaminoglycan metabolic process • heparan sulfate proteoglycan biosynthetic process • positive regulation of catalytic activity • protein glycosylation • glycosaminoglycan biosynthetic process • chondroitin sulfate proteoglycan biosynthetic process • dermatan sulfate proteoglycan biosynthetic process • carbohydrate metabolic process • chondroitin sulfate metabolic process Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	26229	72727
Ensembl	ENSG00000149541	ENSMUSG00000071649
UniProt	O94766	P58158
RefSeq (mRNA)	NM_001288721 NM_001288722 NM_001288723 NM_012200	NM_024256
RefSeq (protein)	NP_001275652.1 NP_036332.2	NP_077218.1
Location (UCSC)	Chr 11: 62.62 – 62.62 Mb	Chr 19: 8.92 – 8.93 Mb
PubMed search	[1]	[2]
Wikidata

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Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3 is an enzyme that in humans is encoded by the B3GAT3 gene.^[3][4]

The protein encoded by this gene is a member of the glucuronyltransferase gene family, enzymes that exhibit strict acceptor specificity, recognizing nonreducing terminal sugars and their anomeric linkages. This gene product catalyzes the formation of the glycosaminoglycan-protein linkage by way of a glucuronyl transfer reaction in the final step of the biosynthesis of the linkage region of proteoglycans.^[4]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Kitagawa H, Tone Y, Tamura J, Neumann KW, Ogawa T, Oka S, Kawasaki T, Sugahara K (Apr 1998). "Molecular cloning and expression of glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans". J Biol Chem. 273 (12): 6615–8. doi:10.1074/jbc.273.12.6615. PMID 9506957.
4. "Entrez Gene: B3GAT3 beta-1,3-glucuronyltransferase 3 (glucuronosyltransferase I)".

Further reading

• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Venkatesan N, Barré L, Benani A, et al. (2005). "Stimulation of proteoglycan synthesis by glucuronosyltransferase-I gene delivery: A strategy to promote cartilage repair". Proc. Natl. Acad. Sci. U.S.A. 101 (52): 18087–92. doi:10.1073/pnas.0404504102. PMC 535800. PMID 15601778.
• Gulberti S, Lattard V, Fondeur M, et al. (2005). "Phosphorylation and sulfation of oligosaccharide substrates critically influence the activity of human beta1,4-galactosyltransferase 7 (GalT-I) and beta1,3-glucuronosyltransferase I (GlcAT-I) involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans". J. Biol. Chem. 280 (2): 1417–25. doi:10.1074/jbc.M411552200. PMID 15522873.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Gulberti S, Fournel-Gigleux S, Mulliert G, et al. (2003). "The functional glycosyltransferase signature sequence of the human beta 1,3-glucuronosyltransferase is a XDD motif". J. Biol. Chem. 278 (34): 32219–26. doi:10.1074/jbc.M207899200. PMID 12794088.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Kitagawa H, Taoka M, Tone Y, Sugahara K (2001). "Human glycosaminoglycan glucuronyltransferase I gene and a related processed pseudogene: genomic structure, chromosomal mapping and characterization". Biochem. J. 358 (Pt 3): 539–46. doi:10.1042/0264-6021:3580539. PMC 1222090. PMID 11535117.
• Pedersen LC, Tsuchida K, Kitagawa H, et al. (2000). "Heparan/chondroitin sulfate biosynthesis. Structure and mechanism of human glucuronyltransferase I". J. Biol. Chem. 275 (44): 34580–5. doi:10.1074/jbc.M007399200. PMID 10946001.
• Ouzzine M, Gulberti S, Netter P, et al. (2000). "Structure/function of the human Ga1beta1,3-glucuronosyltransferase. Dimerization and functional activity are mediated by two crucial cysteine residues". J. Biol. Chem. 275 (36): 28254–60. doi:10.1074/jbc.M002182200. PMID 10842173.
• Tone Y, Kitagawa H, Imiya K, et al. (1999). "Characterization of recombinant human glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans". FEBS Lett. 459 (3): 415–20. doi:10.1016/S0014-5793(99)01287-9. PMID 10526176.
• Herman T, Horvitz HR (1999). "Three proteins involved in Caenorhabditis elegans vulval invagination are similar to components of a glycosylation pathway". Proc. Natl. Acad. Sci. U.S.A. 96 (3): 974–9. doi:10.1073/pnas.96.3.974. PMC 15335. PMID 9927678.