ID RGS11_HUMAN Reviewed; 467 AA. AC O94810; O75883; Q4TT71; Q4TT72; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1999, sequence version 2. DT 14-DEC-2022, entry version 180. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC 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] (ISOFORMS 1 AND 3). RX 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., Chung S., RA Mangion J., Arya S., Gilman A.G., Siderovski D.P.; RT "A G protein gamma subunit-like domain shared between RGS11 and other RGS RT 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 PubMed=11157797; DOI=10.1093/hmg/10.4.339; RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.; RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of RT 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., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., 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., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., 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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP INTERACTION WITH GBETA5, AND MUTAGENESIS OF SER-245 AND TRP-274. RX 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 gamma- RT 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 their CC inactive GDP-bound form. CC -!- SUBUNIT: Heterodimer with Gbeta5. Interacts with RGS7BP, leading to CC regulate the subcellular location of the heterodimer formed with Gbeta5 CC (By similarity). {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=O94810-1; Sequence=Displayed; CC Name=2; CC IsoId=O94810-2; Sequence=VSP_023497; CC Name=3; CC IsoId=O94810-3; Sequence=VSP_046724; 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; CAI95581.1; -; Genomic_DNA. DR EMBL; AC004754; CAI95581.1; JOINED; Genomic_DNA. DR EMBL; Z69667; CAI95582.1; -; Genomic_DNA. DR EMBL; AC004754; CAI95582.1; JOINED; Genomic_DNA. DR EMBL; CH471112; EAW85839.1; -; Genomic_DNA. DR CCDS; CCDS10403.1; -. [O94810-3] DR CCDS; CCDS42088.1; -. [O94810-1] DR CCDS; CCDS66884.1; -. [O94810-2] DR RefSeq; NP_001273414.1; NM_001286485.1. [O94810-2] DR RefSeq; NP_001273415.1; NM_001286486.1. DR RefSeq; NP_003825.1; NM_003834.2. [O94810-3] DR RefSeq; NP_899180.1; NM_183337.2. [O94810-1] DR AlphaFoldDB; O94810; -. DR SMR; O94810; -. DR BioGRID; 114314; 9. DR IntAct; O94810; 4. DR STRING; 9606.ENSP00000380876; -. DR iPTMnet; O94810; -. DR PhosphoSitePlus; O94810; -. DR BioMuta; RGS11; -. DR PaxDb; O94810; -. DR PeptideAtlas; O94810; -. DR ProteomicsDB; 50449; -. [O94810-1] DR ProteomicsDB; 50450; -. [O94810-2] DR ProteomicsDB; 62260; -. DR Antibodypedia; 22598; 147 antibodies from 27 providers. DR DNASU; 8786; -. DR Ensembl; ENST00000316163.9; ENSP00000319069.5; ENSG00000076344.16. [O94810-3] DR Ensembl; ENST00000359740.6; ENSP00000352778.5; ENSG00000076344.16. [O94810-2] DR Ensembl; ENST00000397770.8; ENSP00000380876.3; ENSG00000076344.16. [O94810-1] DR GeneID; 8786; -. DR KEGG; hsa:8786; -. DR MANE-Select; ENST00000397770.8; ENSP00000380876.3; NM_183337.3; NP_899180.1. DR UCSC; uc002cgi.3; human. [O94810-1] DR AGR; HGNC:9993; -. DR CTD; 8786; -. DR DisGeNET; 8786; -. DR GeneCards; RGS11; -. DR HGNC; HGNC:9993; RGS11. DR HPA; ENSG00000076344; Tissue enhanced (brain, pituitary gland). DR MIM; 603895; gene. DR neXtProt; NX_O94810; -. DR OpenTargets; ENSG00000076344; -. DR PharmGKB; PA34363; -. DR VEuPathDB; HostDB:ENSG00000076344; -. DR eggNOG; KOG3589; Eukaryota. DR GeneTree; ENSGT00940000160198; -. DR HOGENOM; CLU_025092_0_0_1; -. DR InParanoid; O94810; -. DR OMA; RKMERMI; -. DR OrthoDB; 415625at2759; -. DR PhylomeDB; O94810; -. DR TreeFam; TF351956; -. DR PathwayCommons; O94810; -. DR Reactome; R-HSA-418594; G alpha (i) signalling events. DR Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding. DR SignaLink; O94810; -. DR BioGRID-ORCS; 8786; 17 hits in 1067 CRISPR screens. DR ChiTaRS; RGS11; human. DR GeneWiki; RGS11; -. DR GenomeRNAi; 8786; -. DR Pharos; O94810; Tbio. DR PRO; PR:O94810; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; O94810; protein. DR Bgee; ENSG00000076344; Expressed in right hemisphere of cerebellum and 123 other tissues. DR ExpressionAtlas; O94810; baseline and differential. DR Genevisible; O94810; HS. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0032991; C:protein-containing complex; IDA:MGI. DR GO; GO:0031681; F:G-protein beta-subunit binding; IPI:UniProtKB. DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central. DR GO; GO:0003924; F:GTPase activity; TAS:Reactome. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome. DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro. DR GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW. DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central. DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IBA:GO_Central. DR CDD; cd00068; GGL; 1. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 1.10.167.10; -; 1. DR Gene3D; 4.10.260.10; -; 1. DR InterPro; IPR000591; DEP_dom. DR InterPro; IPR015898; G-protein_gamma-like_dom. DR InterPro; IPR036284; GGL_sf. DR InterPro; IPR016137; RGS. DR InterPro; IPR040759; RGS_DHEX. DR InterPro; IPR036305; RGS_sf. DR InterPro; IPR044926; RGS_subdomain_2. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR Pfam; PF00610; DEP; 1. DR Pfam; PF00631; G-gamma; 1. DR Pfam; PF00615; RGS; 1. DR Pfam; PF18148; RGS_DHEX; 1. DR PRINTS; PR01301; RGSPROTEIN. DR SMART; SM00049; DEP; 1. DR SMART; SM00224; GGL; 1. DR SMART; SM00315; RGS; 1. DR SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1. DR SUPFAM; SSF48670; Transducin (heterotrimeric G protein), gamma chain; 1. DR SUPFAM; SSF46785; Winged helix DNA-binding domain; 1. DR PROSITE; PS50186; DEP; 1. DR PROSITE; PS50132; RGS; 1. PE 1: Evidence at protein level; KW Alternative splicing; Reference proteome; Signal transduction inhibitor. FT CHAIN 1..467 FT /note="Regulator of G-protein signaling 11" FT /id="PRO_0000204210" FT DOMAIN 32..107 FT /note="DEP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066" FT DOMAIN 219..282 FT /note="G protein gamma" FT DOMAIN 299..414 FT /note="RGS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171" FT REGION 440..467 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 1..21 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:9789084" FT /id="VSP_046724" FT VAR_SEQ 107..123 FT /note="TPYFWTSTLRPAAELDY -> VRLGGA (in isoform 2)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_023497" FT VARIANT 351 FT /note="V -> M (in dbSNP:rs9806942)" FT /id="VAR_061770" FT VARIANT 427 FT /note="M -> T (in dbSNP:rs739999)" FT /id="VAR_024606" FT MUTAGEN 245 FT /note="S->A: Diminishes interaction with Gbeta5." FT /evidence="ECO:0000269|PubMed:10339615" FT MUTAGEN 274 FT /note="W->F: Diminishes interaction with Gbeta5." FT /evidence="ECO:0000269|PubMed:10339615" 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 //