B3GAT3

B3GAT3
Available structures
PDBPretraga ortologa: PDBe RCSB
List of PDB id codes

1FGG, 1KWS, 3CU0

Identifikatori
AlijasiB3GAT3
Spoljašnji IDOMIM: 606374 MGI: 1919977 HomoloGene: 56554 GeneCards: B3GAT3
Genska lokacija (miš)
Chromosome 19 (mouse)
Hr.Chromosome 19 (mouse)[1]
Chromosome 19 (mouse)
Genomska lokacija za B3GAT3
Genomska lokacija za B3GAT3
Band19|19 AStart8,897,738 bp[1]
Kraj8,904,600 bp[1]
Obrazac RNK izražavanja


More reference expression data
Genska ontologija
Molecular function transferase activity
protein phosphatase activator activity
glucuronosyltransferase activity
metal ion binding
GO:0001948, GO:0016582 везивање за протеине плазме
galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity
Cellular component саставни део мембране
Голџијев апарат
мембрана
cis-Golgi network
extracellular exosome
Golgi membrane
Biological process positive regulation of intracellular protein transport
glycosaminoglycan metabolic process
heparan sulfate proteoglycan biosynthetic process
GO:0048554 positive regulation of catalytic activity
GO:0033578, GO:0033577, GO:0033575, GO:0033576 protein glycosylation
glycosaminoglycan biosynthetic process
chondroitin sulfate proteoglycan biosynthetic process
dermatan sulfate proteoglycan biosynthetic process
chondroitin sulfate metabolic process
Метаболизам угљених хидрата
regulation of phosphoprotein phosphatase activity
Sources:Amigo / QuickGO
Ortolozi
VrsteČovekMiš
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)n/aChr 19: 8.9 – 8.9 Mb
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

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

  1. ^ а б в GRCm38: Ensembl release 89: ENSMUSG00000071649 - Ensembl, May 2017
  2. ^ „Human PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine. 
  3. ^ „Mouse PubMed Reference:”. National Center for Biotechnology Information, U.S. National Library of Medicine. 
  4. ^ 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 Слободан приступ. CS1 одржавање: Формат датума (веза)
  5. ^ 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 Слободан приступ. PMID 15601778. doi:10.1073/pnas.0404504102 Слободан приступ. 
  • 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 Слободан приступ. 
  • 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 Слободан приступ. 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 Слободан приступ. 
  • 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 Слободан приступ. PMID 12477932. doi:10.1073/pnas.242603899 Слободан приступ. 
  • 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 Слободан приступ. 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 Слободан приступ. 
  • 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 Слободан приступ. 
  • 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 Слободан приступ. 
  • 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 Слободан приступ. PMID 9927678. doi:10.1073/pnas.96.3.974 Слободан приступ. 

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+
    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
    1kws: Kristalna struktura beta 1,3-glukuroniltransferaze I u kompleksu sa aktivnim UDP-GLCUA donorom
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2.4.1: Heksozil-
transferaze
Glukozil-
Galaktozil-
Glukuronozil-
Fukozil-
Manozil-
2.4.2: Pentozil-
transferaze
Riboza
ADP-riboziltransferaza
Fosforiboziltransferaza
Drugi
Drugi
2.4.99: Sijalil
transferaze