ID RGS11_HUMAN Reviewed; 467 AA. AC O94810; O75883; Q4TT71; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 2. DT 01-SEP-2009, entry version 78. DE RecName: Full=Regulator of G-protein signaling 11; DE Short=RGS11; GN Name=RGS11; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Brain, and Testis; RA Saito T., Seki N., Miyajima N.; RT "Homo sapiens regulator of G-protein signaling 11 (RGS11)."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX MEDLINE=99007310; PubMed=9789084; DOI=10.1073/pnas.95.22.13307; RA Snow B.E., Krumins A.M., Brothers G.M., Lee S.-F., Wall M.A., RA Chung S., Mangion J., Arya S., Gilman A.G., Siderovski D.P.; RT "A G protein gamma subunit-like domain shared between RGS11 and other RT RGS proteins specifies binding to Gbeta5 subunits."; RL Proc. Natl. Acad. Sci. U.S.A. 95:13307-13312(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21096910; PubMed=11157797; DOI=10.1093/hmg/10.4.339; RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., RA Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., RA Higgs D.R.; RT "Sequence, structure and pathology of the fully annotated terminal 2 RT Mb of the short arm of human chromosome 16."; RL Hum. Mol. Genet. 10:339-352(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., RA Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [5] RP INTERACTION WITH GBETA5, AND MUTAGENESIS OF SER-245 AND TRP-274. RX MEDLINE=99272721; PubMed=10339615; DOI=10.1073/pnas.96.11.6489; RA Snow B.E., Betts L., Mangion J., Sondek J., Siderovski D.P.; RT "Fidelity of G protein beta-subunit association by the G protein RT gamma-subunit-like domains of RGS6, RGS7, and RGS11."; RL Proc. Natl. Acad. Sci. U.S.A. 96:6489-6494(1999). CC -!- FUNCTION: Inhibits signal transduction by increasing the GTPase CC activity of G protein alpha subunits thereby driving them into CC their inactive GDP-bound form. CC -!- SUBUNIT: Heterodimer with Gbeta5. Interacts with RGS7BP, leading CC to regulate the subcellular location of the heterodimer formed CC with Gbeta5 (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O94810-1; Sequence=Displayed; CC Name=2; CC IsoId=O94810-2; Sequence=VSP_023497; CC -!- SIMILARITY: Contains 1 DEP domain. CC -!- SIMILARITY: Contains 1 G protein gamma domain. CC -!- SIMILARITY: Contains 1 RGS domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB016929; BAA74751.1; -; mRNA. DR EMBL; AF035153; AAC69175.1; -; mRNA. DR EMBL; AF035154; AAC69176.1; -; mRNA. DR EMBL; AE006463; AAK61221.1; -; Genomic_DNA. DR EMBL; Z69667; CAI95582.1; -; Genomic_DNA. DR EMBL; AC004754; CAI95582.1; JOINED; Genomic_DNA. DR IPI; IPI00015558; -. DR IPI; IPI00642088; -. DR RefSeq; NP_003825.1; -. DR RefSeq; NP_899180.1; -. DR UniGene; Hs.65756; -. DR HSSP; O46469; 1FQI. DR STRING; O94810; -. DR PRIDE; O94810; -. DR Ensembl; ENST00000359740; ENSP00000352778; ENSG00000076344; Homo sapiens. DR Ensembl; ENST00000397770; ENSP00000380876; ENSG00000076344; Homo sapiens. DR GeneID; 8786; -. DR KEGG; hsa:8786; -. DR UCSC; uc002cgj.1; human. DR UCSC; uc010bqs.1; human. DR CTD; 8786; -. DR GeneCards; GC16M000261; -. DR HGNC; HGNC:9993; RGS11. DR MIM; 603895; gene. DR PharmGKB; PA34363; -. DR HOVERGEN; O94810; -. DR OMA; O94810; KMERVVV. DR NextBio; 32948; -. DR ArrayExpress; O94810; -. DR Bgee; O94810; -. DR CleanEx; HS_RGS11; -. DR GermOnline; ENSG00000076344; Homo sapiens. DR GO; GO:0005834; C:heterotrimeric G-protein complex; IEA:InterPro. DR GO; GO:0005096; F:GTPase activator activity; TAS:ProtInc. DR GO; GO:0004871; F:signal transducer activity; IEA:InterPro. DR GO; GO:0007186; P:G-protein coupled receptor protein signalin...; IEA:InterPro. DR GO; GO:0007242; P:intracellular signaling cascade; IEA:InterPro. DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW. DR GO; GO:0008277; P:regulation of G-protein coupled receptor pr...; TAS:ProtInc. DR InterPro; IPR015898; G-protein_gamma-like. DR InterPro; IPR000591; Pleckstrin/G-protein_interact. DR InterPro; IPR000342; Regulat_G_prot_signal. DR InterPro; IPR011991; Wing_hlx_DNA_bd. DR Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1. DR Pfam; PF00610; DEP; 1. DR Pfam; PF00631; G-gamma; 1. DR Pfam; PF00615; RGS; 1. DR PRINTS; PR01301; RGSPROTEIN. DR ProDom; PD001580; Regl_Gprotein; 1. DR SMART; SM00049; DEP; 1. DR SMART; SM00224; GGL; 1. DR SMART; SM00315; RGS; 1. DR PROSITE; PS50186; DEP; 1. DR PROSITE; PS50058; G_PROTEIN_GAMMA; FALSE_NEG. DR PROSITE; PS50132; RGS; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Polymorphism; KW Signal transduction inhibitor. FT CHAIN 1 467 Regulator of G-protein signaling 11. FT /FTId=PRO_0000204210. FT DOMAIN 32 107 DEP. FT DOMAIN 219 282 G protein gamma. FT DOMAIN 299 414 RGS. FT VAR_SEQ 107 123 TPYFWTSTLRPAAELDY -> VRLGGA (in isoform FT 2). FT /FTId=VSP_023497. FT VARIANT 427 427 M -> T (in dbSNP:rs739999). FT /FTId=VAR_024606. FT MUTAGEN 245 245 S->A: Diminishes interaction with Gbeta5. FT MUTAGEN 274 274 W->F: Diminishes interaction with Gbeta5. SQ SEQUENCE 467 AA; 52946 MW; 46BEE11D77C2C5F7 CRC64; MAAGPAPPPG RPRAQMPHLR KMERVVVSMQ DPDQGVKMRS QRLLVTVIPH AVTGSDVVQW LAQKFCVSEE EALHLGAVLV QHGYIYPLRD PRSLMLRPDE TPYRFQTPYF WTSTLRPAAE LDYAIYLAKK NIRKRGTLVD YEKDCYDRLH KKINHAWDLV LMQAREQLRA AKQRSKGDRL VIACQEQTYW LVNRPPPGAP DVLEQGPGRG SCAASRVLMT KSADFHKREI EYFRKALGRT RVKSSVCLEA YLSFCGQRGP HDPLVSGCLP SNPWISDNDA YWVMNAPTVA APTKLRVERW GFSFRELLED PVGRAHFMDF LGKEFSGENL SFWEACEELR YGAQAQVPTL VDAVYEQFLA PGAAHWVNID SRTMEQTLEG LRQPHRYVLD DAQLHIYMLM KKDSYPRFLK SDMYKALLAE AGIPLEMKRR VFPFTWRPRH SSPSPALLPT PVEPTAACGP GGGDGVA //