[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/b3gat3-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/b3gat3-wikipedia\/","headline":"B3GAT3 &#8211; Wikipedia","name":"B3GAT3 &#8211; Wikipedia","description":"From Wikipedia, the free encyclopedia Protein-coding gene in the species Homo sapiens Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3 is an enzyme that in","datePublished":"2019-10-01","dateModified":"2019-10-01","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/upload.wikimedia.org\/wikipedia\/commons\/thumb\/8\/84\/PDB_1fgg_EBI.jpg\/180px-PDB_1fgg_EBI.jpg","url":"https:\/\/upload.wikimedia.org\/wikipedia\/commons\/thumb\/8\/84\/PDB_1fgg_EBI.jpg\/180px-PDB_1fgg_EBI.jpg","height":"135","width":"180"},"url":"https:\/\/wiki.edu.vn\/en\/wiki24\/b3gat3-wikipedia\/","wordCount":5087,"articleBody":"From Wikipedia, the free encyclopediaProtein-coding gene in the species Homo sapiensGalactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3 is an enzyme that in humans is encoded by the B3GAT3 gene.[5][6]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.[6]References[edit]^ a b c GRCh38: Ensembl release 89: ENSG00000149541 &#8211; Ensembl, May 2017^ a b c GRCm38: Ensembl release 89: ENSMUSG00000071649 &#8211; Ensembl, May 2017^ &#8220;Human PubMed Reference:&#8221;. National Center for Biotechnology Information, U.S. National Library of Medicine.^ &#8220;Mouse PubMed Reference:&#8221;. National Center for Biotechnology Information, U.S. National Library of Medicine.^ Kitagawa H, Tone Y, Tamura J, Neumann KW, Ogawa T, Oka S, Kawasaki T, Sugahara K (Apr 1998). &#8220;Molecular cloning and expression of glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans&#8221;. J Biol Chem. 273 (12): 6615\u20138. doi:10.1074\/jbc.273.12.6615. PMID\u00a09506957.^ a b &#8220;Entrez Gene: B3GAT3 beta-1,3-glucuronyltransferase 3 (glucuronosyltransferase I)&#8221;.External links[edit]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[edit]ul{margin-left:0}.mw-parser-output .refbegin-hanging-indents>ul>li{margin-left:0;padding-left:3.2em;text-indent:-3.2em}.mw-parser-output .refbegin-hanging-indents ul,.mw-parser-output .refbegin-hanging-indents ul li{list-style:none}@media(max-width:720px){.mw-parser-output .refbegin-hanging-indents>ul>li{padding-left:1.6em;text-indent:-1.6em}}.mw-parser-output .refbegin-columns{margin-top:0.3em}.mw-parser-output .refbegin-columns ul{margin-top:0}.mw-parser-output .refbegin-columns li{page-break-inside:avoid;break-inside:avoid-column}]]>Rual JF, Venkatesan K, Hao T,  et\u00a0al. (2005). &#8220;Towards a proteome-scale map of the human protein-protein interaction network&#8221;. Nature. 437 (7062): 1173\u20138. Bibcode:2005Natur.437.1173R. doi:10.1038\/nature04209. PMID\u00a016189514. S2CID\u00a04427026.Venkatesan N, Barr\u00e9 L, Benani A,  et\u00a0al. (2005). &#8220;Stimulation of proteoglycan synthesis by glucuronosyltransferase-I gene delivery: A strategy to promote cartilage repair&#8221;. Proc. Natl. Acad. Sci. U.S.A. 101 (52): 18087\u201392. doi:10.1073\/pnas.0404504102. PMC\u00a0535800. PMID\u00a015601778.Gulberti S, Lattard V, Fondeur M,  et\u00a0al. (2005). &#8220;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&#8221;. J. Biol. Chem. 280 (2): 1417\u201325. doi:10.1074\/jbc.M411552200. PMID\u00a015522873.Gerhard DS, Wagner L, Feingold EA,  et\u00a0al. (2004). &#8220;The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)&#8221;. Genome Res. 14 (10B): 2121\u20137. doi:10.1101\/gr.2596504. PMC\u00a0528928. PMID\u00a015489334.Gulberti S, Fournel-Gigleux S, Mulliert G,  et\u00a0al. (2003). &#8220;The functional glycosyltransferase signature sequence of the human beta 1,3-glucuronosyltransferase is a XDD motif&#8221;. J. Biol. Chem. 278 (34): 32219\u201326. doi:10.1074\/jbc.M207899200. PMID\u00a012794088.Strausberg RL, Feingold EA, Grouse LH,  et\u00a0al. (2003). &#8220;Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences&#8221;. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899\u2013903. Bibcode:2002PNAS&#8230;9916899M. doi:10.1073\/pnas.242603899. PMC\u00a0139241. PMID\u00a012477932.Kitagawa H, Taoka M, Tone Y, Sugahara K (2001). &#8220;Human glycosaminoglycan glucuronyltransferase I gene and a related processed pseudogene: genomic structure, chromosomal mapping and characterization&#8221;. Biochem. J. 358 (Pt 3): 539\u201346. doi:10.1042\/0264-6021:3580539. PMC\u00a01222090. PMID\u00a011535117.Pedersen LC, Tsuchida K, Kitagawa H,  et\u00a0al. (2000). &#8220;Heparan\/chondroitin sulfate biosynthesis. Structure and mechanism of human glucuronyltransferase I&#8221;. J. Biol. Chem. 275 (44): 34580\u20135. doi:10.1074\/jbc.M007399200. PMID\u00a010946001.Ouzzine M, Gulberti S, Netter P,  et\u00a0al. (2000). &#8220;Structure\/function of the human Ga1beta1,3-glucuronosyltransferase. Dimerization and functional activity are mediated by two crucial cysteine residues&#8221;. J. Biol. Chem. 275 (36): 28254\u201360. doi:10.1074\/jbc.M002182200. PMID\u00a010842173.Tone Y, Kitagawa H, Imiya K,  et\u00a0al. (1999). &#8220;Characterization of recombinant human glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans&#8221;. FEBS Lett. 459 (3): 415\u201320. doi:10.1016\/S0014-5793(99)01287-9. PMID\u00a010526176. S2CID\u00a07878952.Herman T, Horvitz HR (1999). &#8220;Three proteins involved in Caenorhabditis elegans vulval invagination are similar to components of a glycosylation pathway&#8221;. Proc. Natl. Acad. Sci. U.S.A. 96 (3): 974\u20139. Bibcode:1999PNAS&#8230;96..974H. doi:10.1073\/pnas.96.3.974. PMC\u00a015335. PMID\u00a09927678.li{counter-increment:listitem}.mw-parser-output .hlist ol>li::before{content:\" \"counter(listitem)\"a0 \"}.mw-parser-output .hlist dd ol>li:first-child::before,.mw-parser-output .hlist dt ol>li:first-child::before,.mw-parser-output .hlist li ol>li:first-child::before{content:\" (\"counter(listitem)\"a0 \"}]]>.navbox-abovebelow,.mw-parser-output tr+tr>.navbox-group,.mw-parser-output tr+tr>.navbox-image,.mw-parser-output tr+tr>.navbox-list{border-top:2px solid #fdfdfd}.mw-parser-output .navbox-title{background-color:#ccf}.mw-parser-output .navbox-abovebelow,.mw-parser-output .navbox-group,.mw-parser-output .navbox-subgroup .navbox-title{background-color:#ddf}.mw-parser-output .navbox-subgroup .navbox-group,.mw-parser-output .navbox-subgroup .navbox-abovebelow{background-color:#e6e6ff}.mw-parser-output .navbox-even{background-color:#f7f7f7}.mw-parser-output .navbox-odd{background-color:transparent}.mw-parser-output .navbox .hlist td dl,.mw-parser-output .navbox .hlist td ol,.mw-parser-output .navbox .hlist td ul,.mw-parser-output .navbox td.hlist dl,.mw-parser-output .navbox td.hlist ol,.mw-parser-output .navbox td.hlist ul{padding:0.125em 0}.mw-parser-output .navbox .navbar{display:block;font-size:100%}.mw-parser-output .navbox-title .navbar{float:left;text-align:left;margin-right:0.5em}]]>span,.mw-parser-output .navbar a>abbr{text-decoration:inherit}.mw-parser-output .navbar-mini abbr{font-variant:small-caps;border-bottom:none;text-decoration:none;cursor:inherit}.mw-parser-output .navbar-ct-full{font-size:114%;margin:0 7em}.mw-parser-output .navbar-ct-mini{font-size:114%;margin:0 4em}]]>PDB gallery1fgg: CRYSTAL STRUCTURE OF 1,3-GLUCURONYLTRANSFERASE I (GLCAT-I) COMPLEXED WITH GAL-GAL-XYL, UDP, AND MN2+1kws: CRYSTAL STRUCTURE OF BETA1,3-GLUCURONYLTRANSFERASE I IN COMPLEX WITH THE ACTIVE UDP-GLCUA DONOR"},{"@context":"http:\/\/schema.org\/","@type":"BreadcrumbList","itemListElement":[{"@type":"ListItem","position":1,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/#breadcrumbitem","name":"Enzyklop\u00e4die"}},{"@type":"ListItem","position":2,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/b3gat3-wikipedia\/#breadcrumbitem","name":"B3GAT3 &#8211; Wikipedia"}}]}]