B3GAT3

Beta-1,3-glucuronyltransferase 3 (glucuronosyltransferase I), also known as B3GAT3, is a human gene.cite web | title = Entrez Gene: B3GAT3 beta-1,3-glucuronyltransferase 3 (glucuronosyltransferase I)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=26229| accessdate = ]

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: B3GAT3 beta-1,3-glucuronyltransferase 3 (glucuronosyltransferase I)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=26229| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Rual JF, Venkatesan K, Hao T, "et al." |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209
*cite journal | author=Venkatesan N, Barré L, Benani A, "et al." |title=Stimulation of proteoglycan synthesis by glucuronosyltransferase-I gene delivery: a strategy to promote cartilage repair. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 52 |pages= 18087–92 |year= 2005 |pmid= 15601778 |doi= 10.1073/pnas.0404504102
*cite journal | author=Gulberti S, Lattard V, Fondeur M, "et al." |title=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. |journal=J. Biol. Chem. |volume=280 |issue= 2 |pages= 1417–25 |year= 2005 |pmid= 15522873 |doi= 10.1074/jbc.M411552200
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Gulberti S, Fournel-Gigleux S, Mulliert G, "et al." |title=The functional glycosyltransferase signature sequence of the human beta 1,3-glucuronosyltransferase is a XDD motif. |journal=J. Biol. Chem. |volume=278 |issue= 34 |pages= 32219–26 |year= 2003 |pmid= 12794088 |doi= 10.1074/jbc.M207899200
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Kitagawa H, Taoka M, Tone Y, Sugahara K |title=Human glycosaminoglycan glucuronyltransferase I gene and a related processed pseudogene: genomic structure, chromosomal mapping and characterization. |journal=Biochem. J. |volume=358 |issue= Pt 3 |pages= 539–46 |year= 2001 |pmid= 11535117 |doi=
*cite journal | author=Pedersen LC, Tsuchida K, Kitagawa H, "et al." |title=Heparan/chondroitin sulfate biosynthesis. Structure and mechanism of human glucuronyltransferase I. |journal=J. Biol. Chem. |volume=275 |issue= 44 |pages= 34580–5 |year= 2000 |pmid= 10946001 |doi= 10.1074/jbc.M007399200
*cite journal | author=Ouzzine M, Gulberti S, Netter P, "et al." |title=Structure/function of the human Ga1beta1,3-glucuronosyltransferase. Dimerization and functional activity are mediated by two crucial cysteine residues. |journal=J. Biol. Chem. |volume=275 |issue= 36 |pages= 28254–60 |year= 2000 |pmid= 10842173 |doi= 10.1074/jbc.M002182200
*cite journal | author=Tone Y, Kitagawa H, Imiya K, "et al." |title=Characterization of recombinant human glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans. |journal=FEBS Lett. |volume=459 |issue= 3 |pages= 415–20 |year= 1999 |pmid= 10526176 |doi=
*cite journal | author=Herman T, Horvitz HR |title=Three proteins involved in Caenorhabditis elegans vulval invagination are similar to components of a glycosylation pathway. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 3 |pages= 974–9 |year= 1999 |pmid= 9927678 |doi=
*cite journal | author=Kitagawa H, Tone Y, Tamura J, "et al." |title=Molecular cloning and expression of glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans. |journal=J. Biol. Chem. |volume=273 |issue= 12 |pages= 6615–8 |year= 1998 |pmid= 9506957 |doi=

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