RGS10
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Regulator G-proteinske signalizacije 10 | |||||||||||
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PDB prikaz baziran na 2dlr. | |||||||||||
Dostupne strukture | |||||||||||
2DLR, 2I59, 2IHB | |||||||||||
Identifikatori | |||||||||||
Simbol | RGS10 | ||||||||||
Vanjski ID | OMIM: 602856 MGI: 1915115 HomoloGene: 37710 GeneCards: RGS10 Gene | ||||||||||
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Pregled RNK izražavanja | |||||||||||
podaci | |||||||||||
Ortolozi | |||||||||||
Vrsta | Čovek | Miš | |||||||||
Entrez | 6001 | 67865 | |||||||||
Ensembl | ENSG00000148908 | ENSMUSG00000030844 | |||||||||
UniProt | O43665 | Q9CQE5 | |||||||||
Ref. Sekv. (iRNK) | NM_001005339 | NM_026418 | |||||||||
Ref. Sekv. (protein) | NP_001005339 | NP_080694 | |||||||||
Lokacija (UCSC) | Chr 10: 121.26 - 121.3 Mb | Chr 7: 128.37 - 128.42 Mb | |||||||||
PubMed pretraga | [1] | [2] |
Regulator G-proteinske signalizacije 10 je protein koji je kod ljudi kodiran RGS10 genom.[1][2]
Članovi familje regulatora G proteinske signalizacije (RGS) su regulatorni molekuli koji deluju kao aktivirajući proteini GTPaze (GAP) za G alfa podjedinice heterotrimernih G proteina. RGS proteini imaju sposobnost deaktivacije G proteinskih podjedinica Gi alfa, Go alfa i Gq alfa podtipova. Oni dovode G proteine u njihove neaktivne, GDP-vezane forme. Regulator G proteinske signalizacije 10 pripada toj familiji. Svi RGS proteini imaju zajedničku, konzerviranu 120-aminokiselina dugu sekvencu koja se naziva RGS domen. Ovaj protein se specifično vezuje za aktivirane forme dve srodne G-proteinske podjedinice, G-alfai3 i G-alfaz, i ne formira interakcije sa strukturno i funkcionalno različitim G-alfa podjednicama. Regulator G proteinske signalizacije je lociran u jedru. Njegove dve transkriptne varijante kodiraju različiti izoforme.[2]
Poznato je da RGS10 formira interakcije sa SAP18[3] i GNAI3.[1]
- ↑ 1,0 1,1 Hunt TW, Fields TA, Casey PJ, Peralta EG (Oct 1996). „RGS10 is a selective activator of G alpha i GTPase activity”. Nature 383 (6596): 175–7. DOI:10.1038/383175a0. PMID 8774883. Greška u referenci: Nevaljana oznaka
<ref>
; naziv "pmid8774883" je zadan više puta s različitim sadržajem - ↑ 2,0 2,1 „Entrez Gene: RGS10 regulator of G-protein signalling 10”.
- ↑ Ewing, Rob M; Chu Peter, Elisma Fred, Li Hongyan, Taylor Paul, Climie Shane, McBroom-Cerajewski Linda, Robinson Mark D, O'Connor Liam, Li Michael, Taylor Rod, Dharsee Moyez, Ho Yuen, Heilbut Adrian, Moore Lynda, Zhang Shudong, Ornatsky Olga, Bukhman Yury V, Ethier Martin, Sheng Yinglun, Vasilescu Julian, Abu-Farha Mohamed, Lambert Jean-Philippe, Duewel Henry S, Stewart Ian I, Kuehl Bonnie, Hogue Kelly, Colwill Karen, Gladwish Katharine, Muskat Brenda, Kinach Robert, Adams Sally-Lin, Moran Michael F, Morin Gregg B, Topaloglou Thodoros, Figeys Daniel (2007). „Large-scale mapping of human protein-protein interactions by mass spectrometry”. Mol. Syst. Biol. (England) 3 (1): 89. DOI:10.1038/msb4100134. PMC 1847948. PMID 17353931.
- Popov S, Yu K, Kozasa T, Wilkie TM (1997). „The regulators of G protein signaling (RGS) domains of RGS4, RGS10, and GAIP retain GTPase activating protein activity in vitro.”. Proc. Natl. Acad. Sci. U.S.A. 94 (14): 7216–20. DOI:10.1073/pnas.94.14.7216. PMC 23796. PMID 9207071.
- Tu Y, Wang J, Ross EM (1997). „Inhibition of brain Gz GAP and other RGS proteins by palmitoylation of G protein alpha subunits.”. Science 278 (5340): 1132–5. DOI:10.1126/science.278.5340.1132. PMID 9353196.
- Tu Y, Popov S, Slaughter C, Ross EM (2000). „Palmitoylation of a conserved cysteine in the regulator of G protein signaling (RGS) domain modulates the GTPase-activating activity of RGS4 and RGS10.”. J. Biol. Chem. 274 (53): 38260–7. DOI:10.1074/jbc.274.53.38260. PMID 10608901.
- Popov SG, Krishna UM, Falck JR, Wilkie TM (2000). „Ca2 /Calmodulin reverses phosphatidylinositol 3,4, 5-trisphosphate-dependent inhibition of regulators of G protein-signaling GTPase-activating protein activity.”. J. Biol. Chem. 275 (25): 18962–8. DOI:10.1074/jbc.M001128200. PMID 10747990.
- Chatterjee TK, Fisher RA (2000). „Cytoplasmic, nuclear, and golgi localization of RGS proteins. Evidence for N-terminal and RGS domain sequences as intracellular targeting motifs.”. J. Biol. Chem. 275 (31): 24013–21. DOI:10.1074/jbc.M002082200. PMID 10791963.
- Burgon PG, Lee WL, Nixon AB, et al. (2001). „Phosphorylation and nuclear translocation of a regulator of G protein signaling (RGS10).”. J. Biol. Chem. 276 (35): 32828–34. DOI:10.1074/jbc.M100960200. PMID 11443111.
- Gagnon AW, Murray DL, Leadley RJ (2002). „Cloning and characterization of a novel regulator of G protein signalling in human platelets.”. Cell. Signal. 14 (7): 595–606. DOI:10.1016/S0898-6568(02)00012-8. PMID 11955952.
- Castro-Fernández C, Conn PM (2003). „Regulation of the gonadotropin-releasing hormone receptor (GnRHR) by RGS proteins: role of the GnRHR carboxyl-terminus.”. Mol. Cell. Endocrinol. 191 (2): 149–56. DOI:10.1016/S0303-7207(02)00082-5. PMID 12062898.
- 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.
- 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.
- Oh JH, Yang JO, Hahn Y, et al. (2006). „Transcriptome analysis of human gastric cancer.”. Mamm. Genome 16 (12): 942–54. DOI:10.1007/s00335-005-0075-2. PMID 16341674.
- Lee HK, Rhee KH, Kim CW, et al. (2006). „Crystallization and preliminary X-ray crystallographic analysis of human RGS10 complexed with Galphai3.”. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61 (Pt 9): 831–3. DOI:10.1107/S1744309105023602. PMC 1978115. PMID 16511171.
- Ewing RM, Chu P, Elisma F, et al. (2007). „Large-scale mapping of human protein-protein interactions by mass spectrometry.”. Mol. Syst. Biol. 3 (1): 89. DOI:10.1038/msb4100134. PMC 1847948. PMID 17353931.