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	OMIM: 606374; MGI: 1919977; HomoloGene: 56554; GeneCards: B3GAT3; OMA:B3GAT3 - orthologs
Gene location (Human) Chr. Chromosome 11 (human) Band 11q12.3 Start 62,615,296 bp End 62,622,154 bp
Gene location (Mouse) Chr. Chromosome 19 (mouse) Band 19|19 A Start 8,897,738 bp End 8,904,600 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right hemisphere of cerebellum anterior pituitary granulocyte right frontal lobe C1 segment anterior cingulate cortex prefrontal cortex nucleus accumbens caudate nucleus amygdala Top expressed in superior frontal gyrus dentate gyrus of hippocampal formation granule cell primary visual cortex ankle joint cerebellar cortex neural layer of retina granulocyte medial dorsal nucleus lateral geniculate nucleus central gray substance of midbrain More reference expression data BioGPS More reference expression data
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 cis-Golgi network extracellular exosome Golgi membrane 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 chondroitin sulfate metabolic process carbohydrate metabolic process regulation of phosphoprotein phosphatase activity Sources:Amigo / QuickGO
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_001275650 NP_001275651 NP_001275652 NP_036332 NP_077218 Location (UCSC) Chr 11: 62.62 – 62.62 Mb Chr 19: 8.9 – 8.9 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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

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.

External links

• Human B3GAT3 genome location and B3GAT3 gene details page in the UCSC Genome Browser.
• Overview of all the structural information available in the PDB for UniProt: O94766 (Human Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3 (B3GAT3)) at the PDBe-KB.

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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• 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. Bibcode:2002PNAS...9916899M. 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. Bibcode:1999FEBSL.459..415T. doi:10.1016/S0014-5793(99)01287-9. PMID 10526176. S2CID 7878952.
• 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. Bibcode:1999PNAS...96..974H. doi:10.1073/pnas.96.3.974. PMC 15335. PMID 9927678.