RGS11_HUMAN
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 03-AUG-2022, entry version 178.
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;
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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 PRIDE; O94810; -.
DR ProteomicsDB; 50449; -. [O94810-1]
DR ProteomicsDB; 50450; -. [O94810-2]
DR ProteomicsDB; 62260; -.
DR Antibodypedia; 22598; 147 antibodies from 28 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 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; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR SUPFAM; SSF48670; SSF48670; 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
