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B3GAT3








B3GAT3


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B3GAT3
Protein B3GAT3 PDB 1fgg.png







Available structures
PDB Ortholog search: PDBe RCSB



Identifiers
Aliases
B3GAT3, GLCATI, glcUAT-I, JDSCD, beta-1,3-glucuronyltransferase 3
External IDs MGI: 1919977 HomoloGene: 56554 GeneCards: B3GAT3


















Gene location (Human)
Chromosome 11 (human)
Chr. Chromosome 11 (human)[1]

Chromosome 11 (human)
Genomic location for B3GAT3

Genomic location for B3GAT3

Band 11q12.3 Start 62,615,296 bp[1]
End 62,622,175 bp[1]























RNA expression pattern

PBB GE B3GAT3 35179 at fs.png

PBB GE B3GAT3 203452 at fs.png
More reference expression data















Orthologs
Species Human Mouse
Entrez





Ensembl





UniProt





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: 8.92 – 8.93 Mb

PubMed search
[3] [4]
Wikidata



View/Edit Human View/Edit Mouse

Galactosylgalactosylxylosylprotein 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]





  1. ^ abc GRCh38: Ensembl release 89: ENSG00000149541 - Ensembl, May 2017


  2. ^ abc GRCm38: Ensembl release 89: ENSMUSG00000071649 - Ensembl, May 2017


  3. ^ "Human PubMed Reference:"..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output q{quotes:"""""""'""'"}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/6/65/Lock-green.svg/9px-Lock-green.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-limited a,.mw-parser-output .cs1-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Lock-gray-alt-2.svg/9px-Lock-gray-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Lock-red-alt-2.svg/9px-Lock-red-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{font-size:100%}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}


  4. ^ "Mouse PubMed Reference:".


  5. ^ 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.


  6. ^ ab "Entrez Gene: B3GAT3 beta-1,3-glucuronyltransferase 3 (glucuronosyltransferase I)".




External links[edit]


  • Human B3GAT3 genome location and B3GAT3 gene details page in the UCSC Genome Browser.


Further reading[edit]


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  • 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.

















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