B3GAT3
B3GAT3 | |||||||||||||||||||||||||
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Identifikatori | |||||||||||||||||||||||||
Alijasi | B3GAT3 | ||||||||||||||||||||||||
Spoljašnji ID | OMIM: 606374 MGI: 1919977 HomoloGene: 56554 GeneCards: B3GAT3 | ||||||||||||||||||||||||
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Vrste | Čovek | Miš | |||||||||||||||||||||||
Entrez |
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Ensembl |
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UniProt |
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RefSeq (mRNA) |
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RefSeq (protein) |
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Location (UCSC) | n/a | Chr 19: 8.9 – 8.9 Mb | |||||||||||||||||||||||
PubMed search | [2] | [3] | |||||||||||||||||||||||
Wikidata | |||||||||||||||||||||||||
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Galaktozilgalaktozilksilozilprotein 3-beta-glukuronoziltransferaza 3 je enzim koji je kod ljudi kodiran genom B3GAT3.[4][5]
Protein kodiran ovim genom je član porodice gena glukuroniltransferaze, enzima koji pokazuju strogu specifičnost akceptora, prepoznajući nereducirajuće terminalne šećere i njihove anomerne veze. Ovaj genski proizvod katalizuje formiranje veze glikozaminoglikan-protein putem reakcije transfera glukuronila u završnom koraku biosinteze regiona veze proteoglikana.[5]
References
- ^ а б в GRCm38: Ensembl release 89: ENSMUSG00000071649 - Ensembl, May 2017
- ^ „Human PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ „Mouse PubMed Reference:”. 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 (април 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. PMID 9506957. doi:10.1074/jbc.273.12.6615
. CS1 одржавање: Формат датума (веза)
- ^ а б „Entrez Gene: B3GAT3 beta-1,3-glucuronyltransferase 3 (glucuronosyltransferase I)”.
Literatura
- 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. PMID 16189514. S2CID 4427026. doi:10.1038/nature04209.
- 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. PMC 535800
. PMID 15601778. doi:10.1073/pnas.0404504102
.
- 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. PMID 15522873. doi:10.1074/jbc.M411552200
.
- 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. PMC 528928
. PMID 15489334. doi:10.1101/gr.2596504.
- 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. PMID 12794088. doi:10.1074/jbc.M207899200
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- 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. PMC 139241
. PMID 12477932. doi:10.1073/pnas.242603899
.
- 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. PMC 1222090
. PMID 11535117. doi:10.1042/0264-6021:3580539.
- 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. PMID 10946001. doi:10.1074/jbc.M007399200
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- 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. PMID 10842173. doi:10.1074/jbc.M002182200
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- 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. PMID 10526176. S2CID 7878952. doi:10.1016/S0014-5793(99)01287-9
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- 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. PMC 15335
. PMID 9927678. doi:10.1073/pnas.96.3.974
.
Spoljašnje veze
- 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.
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PDB Galerija
- 1fgg: Kristalna struktura 1,3-glukuroniltransferaze I (GLCAT-I) u kompleksu sa GAL-GAL-XYL, UDP, i MN2+
- 1kws: Kristalna struktura beta 1,3-glukuroniltransferaze I u kompleksu sa aktivnim UDP-GLCUA donorom