La KHDRBS3 (pour « KH domain-containing, RNA-binding, signal transduction-associated protein 3 » en anglais) est une protéine codée par le gèneKHDRBS3, présent sur le chromosome 8 humain et le chromosome 15 de la souris[4],[5],[6].
Interaction
La KHDRBS3 interagit avec la protéine SIAH1 (en)[7],[8].
Notes et références
(en) Cet article est partiellement ou en totalité issu de l’article de Wikipédia en anglais intitulé « KHDRBS3 » (voir la liste des auteurs).
↑ ab et cGRCm38: Ensembl release 89: ENSMUSG00000022332 - Ensembl, May 2017
↑« Publications PubMed pour l'Homme », sur National Center for Biotechnology Information, U.S. National Library of Medicine
↑« Publications PubMed pour la Souris », sur National Center for Biotechnology Information, U.S. National Library of Medicine
↑(en) Venables JP, Vernet C, Chew SL, Elliott DJ, Cowmeadow RB, Wu J, Cooke HJ, Artzt K, Eperon IC, « T-STAR/ETOILE: a novel relative of SAM68 that interacts with an RNA-binding protein implicated in spermatogenesis », Hum Mol Genet, vol. 8, no 6, , p. 959–69 (PMID10332027, DOI10.1093/hmg/8.6.959).
↑(en) Lee J, Burr JG, « Salpalpha and Salpbeta, growth-arresting homologs of Sam68 », Gene, vol. 240, no 1, , p. 133–47 (PMID10564820, DOI10.1016/S0378-1119(99)00421-7).
↑(en) Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M, « Towards a proteome-scale map of the human protein-protein interaction network », Nature, vol. 437, no 7062, , p. 1173–8 (PMID16189514, DOI10.1038/nature04209).
↑(en) Venables JP, Dalgliesh C, Paronetto MP, Skitt L, Thornton JK, Saunders PT, Sette C, Jones KT, Elliott DJ, « SIAH1 targets the alternative splicing factor T-STAR for degradation by the proteasome », Hum. Mol. Genet., vol. 13, no 14, , p. 1525–34 (PMID15163637, DOI10.1093/hmg/ddh165).
Bibliographie
(en) Di Fruscio M, Chen T, Richard S, « Characterization of Sam68-like mammalian proteins SLM-1 and SLM-2: SLM-1 is a Src substrate during mitosis. », Proc. Natl. Acad. Sci. U.S.A., vol. 96, no 6, , p. 2710–5 (PMID10077576, PMCID15834, DOI10.1073/pnas.96.6.2710)
(en) Venables JP, Elliott DJ, Makarova OV, Makarov EM, Cooke HJ, Eperon IC, « RBMY, a probable human spermatogenesis factor, and other hnRNP G proteins interact with Tra2beta and affect splicing. », Hum. Mol. Genet., vol. 9, no 5, , p. 685–94 (PMID10749975, DOI10.1093/hmg/9.5.685)
(en) Stoss O, Olbrich M, Hartmann AM, Konig H, Memmott J, Andreadis A, Stamm S, « The STAR/GSG family protein rSLM-2 regulates the selection of alternative splice sites. », J. Biol. Chem., vol. 276, no 12, , p. 8665–73 (PMID11118435, DOI10.1074/jbc.M006851200)
(en) Sugimoto Y, Morita R, Amano K, Shah PU, Pascual-Castroviejo I, Khan S, Delgado-Escueta AV, Yamakawa K, « T-STAR gene: fine mapping in the candidate region for childhood absence epilepsy on 8q24 and mutational analysis in patients. », Epilepsy Res., vol. 46, no 2, , p. 139–44 (PMID11463515, DOI10.1016/S0920-1211(01)00274-1)
(en) Kool J, van Zaane W, van der Eb AJ, Terleth C, « Down-regulation of T-STAR, a growth inhibitory protein, after SV40-mediated immortalization. », Cell Growth Differ., vol. 12, no 11, , p. 535–41 (PMID11714634)
(en) Reddy TR, Suhasini M, Xu W, Yeh LY, Yang JP, Wu J, Artzt K, Wong-Staal F, « A role for KH domain proteins (Sam68-like mammalian proteins and quaking proteins) in the post-transcriptional regulation of HIV replication. », J. Biol. Chem., vol. 277, no 8, , p. 5778–84 (PMID11741900, DOI10.1074/jbc.M106836200)
(en) Côté J, Boisvert FM, Boulanger MC, Bedford MT, Richard S, « Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1. », Mol. Biol. Cell, vol. 14, no 1, , p. 274–87 (PMID12529443, PMCID140244, DOI10.1091/mbc.E02-08-0484)
(en) Venables JP, Dalgliesh C, Paronetto MP, Skitt L, Thornton JK, Saunders PT, Sette C, Jones KT, Elliott DJ, « SIAH1 targets the alternative splicing factor T-STAR for degradation by the proteasome. », Hum. Mol. Genet., vol. 13, no 14, , p. 1525–34 (PMID15163637, DOI10.1093/hmg/ddh165)
(en) Cohen CD, Doran PP, Blattner SM, Merkle M, Wang GQ, Schmid H, Mathieson PW, Saleem MA, Henger A, Rastaldi MP, Kretzler M, « Sam68-like mammalian protein 2, identified by digital differential display as expressed by podocytes, is induced in proteinuria and involved in splice site selection of vascular endothelial growth factor. », J. Am. Soc. Nephrol., vol. 16, no 7, , p. 1958–65 (PMID15901763, DOI10.1681/ASN.2005020204)
(en) Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M, « Towards a proteome-scale map of the human protein-protein interaction network. », Nature, vol. 437, no 7062, , p. 1173–8 (PMID16189514, DOI10.1038/nature04209)
(en) Zhang L, Guo L, Peng Y, Chen B, « Expression of T-STAR gene is associated with regulation of telomerase activity in human colon cancer cell line HCT-116. », World J. Gastroenterol., vol. 12, no 25, , p. 4056–60 (PMID16810759)
(en) Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M, « Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. », Cell, vol. 127, no 3, , p. 635–48 (PMID17081983, DOI10.1016/j.cell.2006.09.026)
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