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RGS10
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2DLR, 2I59, 2IHB
Identifiers
Aliases	RGS10, regulator of G protein signaling 10
External IDs	OMIM: 602856; MGI: 1915115; HomoloGene: 37710; GeneCards: RGS10; OMA:RGS10 - orthologs
Gene location (Human) Chr. Chromosome 10 (human) Band 10q26.11 Start 119,499,817 bp End 119,542,719 bp
Gene location (Mouse) Chr. Chromosome 7 (mouse) Band 7|7 F3 Start 127,975,345 bp End 128,020,482 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in monocyte thymus granulocyte muscle layer of sigmoid colon trabecular bone periodontal fiber blood lymph node appendix rectum Top expressed in blood thymus mesenteric lymph nodes spermatid spermatocyte spinal ganglia tibiofemoral joint spleen nucleus accumbens lumbar spinal ganglion More reference expression data BioGPS More reference expression data
Gene ontology Molecular function GTPase activator activity G-protein alpha-subunit binding protein binding GTPase activity Cellular component cytosol plasma membrane nucleus cytoplasm axon terminus soma dendritic spine Biological process G protein-coupled acetylcholine receptor signaling pathway positive regulation of GTPase activity negative regulation of signal transduction regulation of G protein-coupled receptor signaling pathway response to amphetamine G protein-coupled receptor signaling pathway Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6001 67865 Ensembl ENSG00000148908 ENSMUSG00000030844 UniProt O43665 Q9CQE5 RefSeq (mRNA) NM_002925 NM_001005339 NM_026418 RefSeq (protein) NP_001005339 NP_002916 NP_080694 Location (UCSC) Chr 10: 119.5 – 119.54 Mb Chr 7: 127.98 – 128.02 Mb PubMed search
Wikidata
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Regulator of G-protein signaling 10 is a protein that in humans is encoded by the RGS10 gene.

Function

Regulator of G protein signaling (RGS) family members are regulatory molecules that act as GTPase activating proteins (GAPs) for G alpha subunits of heterotrimeric G proteins. RGS proteins are able to deactivate G protein subunits of the Gi alpha, Go alpha and Gq alpha subtypes. They drive G proteins into their inactive GDP-bound forms. Regulator of G protein signaling 10 belongs to this family. All RGS proteins share a conserved 120-amino acid sequence termed the RGS domain. This protein associates specifically with the activated forms of the two related G-protein subunits, G-alphai3 and G-alphaz but fails to interact with the structurally and functionally distinct G-alpha subunits. Regulator of G protein signaling 10 protein is localized in the nucleus. Two transcript variants encoding different isoforms have been found for this gene.

Interactions

RGS10 has been shown to interact with SAP18 and GNAI3.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000148908 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000030844 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. ^ Hunt TW, Fields TA, Casey PJ, Peralta EG (Sep 1996). "RGS10 is a selective activator of G alpha i GTPase activity". Nature. 383 (6596): 175–7. Bibcode:1996Natur.383..175H. doi:10.1038/383175a0. PMID 8774883. S2CID 4318445.
6. ^ "Entrez Gene: RGS10 regulator of G-protein signalling 10".
7. Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

Further reading

• Popov S, Yu K, Kozasa T, Wilkie TM (Jul 1997). "The regulators of G protein signaling (RGS) domains of RGS4, RGS10, and GAIP retain GTPase activating protein activity in vitro". Proceedings of the National Academy of Sciences of the United States of America. 94 (14): 7216–20. Bibcode:1997PNAS...94.7216P. doi:10.1073/pnas.94.14.7216. PMC 23796. PMID 9207071.
• Tu Y, Wang J, Ross EM (Nov 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 (Dec 1999). "Palmitoylation of a conserved cysteine in the regulator of G protein signaling (RGS) domain modulates the GTPase-activating activity of RGS4 and RGS10". The Journal of Biological Chemistry. 274 (53): 38260–7. doi:10.1074/jbc.274.53.38260. PMID 10608901.
• Popov SG, Krishna UM, Falck JR, Wilkie TM (Jun 2000). "Ca2+/Calmodulin reverses phosphatidylinositol 3,4, 5-trisphosphate-dependent inhibition of regulators of G protein-signaling GTPase-activating protein activity". The Journal of Biological Chemistry. 275 (25): 18962–8. doi:10.1074/jbc.M001128200. PMID 10747990.
• Chatterjee TK, Fisher RA (Aug 2000). "Cytoplasmic, nuclear, and golgi localization of RGS proteins. Evidence for N-terminal and RGS domain sequences as intracellular targeting motifs". The Journal of Biological Chemistry. 275 (31): 24013–21. doi:10.1074/jbc.M002082200. PMID 10791963.
• Burgon PG, Lee WL, Nixon AB, Peralta EG, Casey PJ (Aug 2001). "Phosphorylation and nuclear translocation of a regulator of G protein signaling (RGS10)". The Journal of Biological Chemistry. 276 (35): 32828–34. doi:10.1074/jbc.M100960200. PMID 11443111.
• Gagnon AW, Murray DL, Leadley RJ (Jul 2002). "Cloning and characterization of a novel regulator of G protein signalling in human platelets". Cellular Signalling. 14 (7): 595–606. doi:10.1016/S0898-6568(02)00012-8. PMID 11955952.
• Castro-Fernández C, Conn PM (Jun 2002). "Regulation of the gonadotropin-releasing hormone receptor (GnRHR) by RGS proteins: role of the GnRHR carboxyl-terminus". Molecular and Cellular Endocrinology. 191 (2): 149–56. doi:10.1016/S0303-7207(02)00082-5. PMID 12062898. S2CID 36812170.
• 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 (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Oh JH, Yang JO, Hahn Y, Kim MR, Byun SS, Jeon YJ, Kim JM, Song KS, Noh SM, Kim S, Yoo HS, Kim YS, Kim NS (Dec 2005). "Transcriptome analysis of human gastric cancer". Mammalian Genome. 16 (12): 942–54. doi:10.1007/s00335-005-0075-2. PMID 16341674. S2CID 69278.
• Lee HK, Rhee KH, Kim CW, Hwang KY, Kim EE (Sep 2005). "Crystallization and preliminary X-ray crystallographic analysis of human RGS10 complexed with Galphai3". Acta Crystallographica Section F. 61 (Pt 9): 831–3. doi:10.1107/S1744309105023602. PMC 1978115. PMID 16511171.
• Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

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